Query Ver_Hs_NP_057092.2_Lic3 Command /cluster/toolkit/production/bioprogs/hhpred/hhsearch -cpu 4 -v 1 -i /cluster/toolkit/production/tmp/production/96187/c_NP_057092.hhm -d /cluster/toolkit/production/databases/hhpred/new_dbs/pfam_18Apr07/db//pfam.hhm /cluster/toolkit/production/databases/hhpred/new_dbs/smart_18Apr07/db/smart.hhm /cluster/toolkit/production/databases/hhpred/new_dbs/KOG_18Apr07/db/KOG.hhm /cluster/toolkit/production/databases/hhpred/new_dbs/COG_18Apr07/db/COG.hhm /cluster/toolkit/production/databases/hhpred/new_dbs/cd_18Apr07/db/cd.hhm -o /cluster/toolkit/production/tmp/production/96187/c_NP_057092.hhr -p 20 -P 20 -Z 100 -B 100 -seq 1 -aliw 80 -local -ssm 2 -norealign -sc 1 No Hit Prob E-value P-value Score SS Cols Query HMM Template HMM 1 KOG3929 Uncharacterized conser 100.0 0 0 799.8 18.2 345 1-351 10-363 (363) 2 KOG3905 Dynein light intermedi 100.0 0 0 318.5 19.2 254 4-269 31-320 (473) 3 pfam05783 DLIC Dynein light in 100.0 1.4E-45 0 303.7 18.2 254 4-269 26-315 (475) 4 cd04128 Spg1 Spg1p. Spg1p (se 99.6 3.2E-15 1.5E-19 114.3 12.6 177 34-255 3-182 (182) 5 cd01860 Rab5_related Rab5-rela 99.5 4.1E-14 2E-18 107.3 9.8 153 34-238 4-159 (163) 6 cd04106 Rab23_lke Rab23-like s 99.5 7.7E-14 3.7E-18 105.6 10.9 155 34-238 3-159 (162) 7 cd01867 Rab8_Rab10_Rab13_like 99.5 6.7E-14 3.2E-18 106.0 10.3 154 34-238 6-161 (167) 8 cd00154 Rab Rab family. Rab G 99.5 7.3E-14 3.5E-18 105.8 10.5 154 34-238 3-158 (159) 9 cd04110 Rab35 Rab35 subfamily. 99.5 1E-13 4.8E-18 104.9 11.2 153 34-238 9-163 (199) 10 cd00876 Ras Ras family. The R 99.5 7.6E-14 3.6E-18 105.7 10.4 154 34-238 2-157 (160) 11 cd04109 Rab28 Rab28 subfamily. 99.5 2.2E-13 1.1E-17 102.7 11.8 158 34-238 3-162 (215) 12 cd01865 Rab3 Rab3 subfamily. 99.5 2.6E-13 1.2E-17 102.3 11.9 154 34-238 4-159 (165) 13 cd01869 Rab1_Ypt1 Rab1/Ypt1 su 99.5 1.3E-13 6.3E-18 104.2 10.4 154 34-238 5-160 (166) 14 cd04107 Rab32_Rab38 Rab38/Rab3 99.5 3.6E-13 1.7E-17 101.4 12.4 181 34-258 3-188 (201) 15 cd01866 Rab2 Rab2 subfamily. 99.5 3E-13 1.4E-17 101.9 11.8 154 34-238 7-162 (168) 16 cd04119 RJL RJL (RabJ-Like) su 99.5 2.1E-13 1E-17 102.8 10.9 159 34-238 3-163 (168) 17 cd01868 Rab11_like Rab11-like. 99.5 2.5E-13 1.2E-17 102.4 11.1 154 34-238 6-161 (165) 18 cd04120 Rab12 Rab12 subfamily. 99.5 3.8E-13 1.8E-17 101.3 11.9 172 34-254 3-184 (202) 19 cd04114 Rab30 Rab30 subfamily. 99.5 2.6E-13 1.2E-17 102.3 10.8 154 34-238 10-165 (169) 20 cd04122 Rab14 Rab14 subfamily. 99.5 3.2E-13 1.5E-17 101.8 11.2 153 34-238 5-160 (166) 21 cd04112 Rab26 Rab26 subfamily. 99.5 2.3E-13 1.1E-17 102.6 10.4 154 34-238 3-159 (191) 22 cd04124 RabL2 RabL2 subfamily. 99.5 5.6E-13 2.7E-17 100.2 12.4 152 34-238 3-158 (161) 23 cd04125 RabA_like RabA-like su 99.5 2.8E-13 1.3E-17 102.1 10.4 154 34-238 3-158 (188) 24 cd01861 Rab6 Rab6 subfamily. 99.5 2.3E-13 1.1E-17 102.7 9.9 154 34-238 3-158 (161) 25 cd04117 Rab15 Rab15 subfamily. 99.5 6.7E-13 3.2E-17 99.7 12.1 154 34-238 3-158 (161) 26 pfam00071 Ras Ras family. Incl 99.5 3.3E-13 1.6E-17 101.6 10.5 154 34-238 2-157 (162) 27 cd04118 Rab24 Rab24 subfamily. 99.5 1.7E-13 8.3E-18 103.4 9.0 157 34-238 3-162 (193) 28 cd01864 Rab19 Rab19 subfamily. 99.5 3.5E-13 1.7E-17 101.5 10.5 154 34-238 6-162 (165) 29 cd04175 Rap1 Rap1 subgroup. T 99.5 7.8E-13 3.7E-17 99.3 12.0 154 34-238 4-159 (164) 30 cd00157 Rho Rho (Ras homology) 99.4 4.1E-13 2E-17 101.1 9.9 158 34-238 3-169 (171) 31 smart00174 RHO Rho (Ras homolo 99.4 2.4E-13 1.1E-17 102.6 8.5 158 34-238 1-168 (174) 32 cd04132 Rho4_like Rho4-like su 99.4 4.7E-13 2.3E-17 100.7 9.3 160 32-238 1-163 (187) 33 cd04116 Rab9 Rab9 subfamily. 99.4 2.5E-12 1.2E-16 96.1 13.0 157 34-238 8-167 (170) 34 cd04108 Rab36_Rab34 Rab34/Rab3 99.4 1.2E-12 5.9E-17 98.0 11.4 157 34-238 3-161 (170) 35 cd01862 Rab7 Rab7 subfamily. 99.4 1.5E-12 7E-17 97.6 11.6 160 34-238 3-167 (172) 36 cd01863 Rab18 Rab18 subfamily. 99.4 1.6E-12 7.6E-17 97.4 11.6 154 34-238 3-158 (161) 37 cd04176 Rap2 Rap2 subgroup. T 99.4 1.6E-12 7.4E-17 97.4 11.2 154 34-238 4-159 (163) 38 cd04113 Rab4 Rab4 subfamily. 99.4 1.4E-12 6.8E-17 97.7 10.8 154 34-238 3-158 (161) 39 smart00175 RAB Rab subfamily o 99.4 1.2E-12 5.7E-17 98.2 10.0 154 34-238 3-158 (164) 40 cd04141 Rit_Rin_Ric Rit/Rin/Ri 99.4 2E-12 9.7E-17 96.7 11.1 154 34-238 5-160 (172) 41 cd04136 Rap_like Rap-like subf 99.4 2.2E-12 1E-16 96.5 10.7 154 34-238 4-159 (163) 42 cd04123 Rab21 Rab21 subfamily. 99.4 2.8E-12 1.3E-16 95.8 11.0 154 34-238 3-158 (162) 43 cd04140 ARHI_like ARHI subfami 99.4 3.8E-12 1.8E-16 95.0 11.6 157 34-237 4-164 (165) 44 cd04152 Arl4_Arl7 Arl4/Arl7 su 99.4 9.6E-12 4.6E-16 92.5 13.6 160 33-238 5-166 (183) 45 cd04137 RheB Rheb (Ras Homolog 99.4 3.3E-12 1.6E-16 95.4 11.2 156 32-238 2-159 (180) 46 cd04139 RalA_RalB RalA/RalB su 99.4 3.6E-12 1.7E-16 95.2 11.3 154 34-238 3-158 (164) 47 cd04101 RabL4 RabL4 (Rab-like4 99.4 2E-12 9.4E-17 96.8 9.9 154 34-238 3-160 (164) 48 cd04133 Rop_like Rop subfamily 99.4 1.6E-12 7.5E-17 97.4 9.1 158 34-238 4-169 (176) 49 cd01870 RhoA_like RhoA-like su 99.4 1.6E-12 7.8E-17 97.3 9.2 158 34-238 4-171 (175) 50 cd04121 Rab40 Rab40 subfamily. 99.4 2.4E-12 1.2E-16 96.2 10.0 153 34-238 9-163 (235) 51 cd04135 Tc10 TC10 subfamily. 99.4 1.7E-12 7.9E-17 97.2 9.1 157 34-237 3-169 (174) 52 cd04131 Rnd Rnd subfamily. Th 99.4 1.6E-12 7.4E-17 97.4 8.5 143 34-221 4-156 (178) 53 cd04143 Rhes_like Rhes_like su 99.4 2.1E-11 1E-15 90.3 13.8 182 34-255 3-192 (247) 54 cd00877 Ran Ran (Ras-related n 99.4 6.5E-12 3.1E-16 93.5 11.0 151 34-238 3-155 (166) 55 cd04129 Rho2 Rho2 subfamily. 99.4 4.5E-12 2.1E-16 94.6 10.1 160 34-238 4-173 (187) 56 cd04102 RabL3 RabL3 (Rab-like3 99.4 1.5E-12 6.9E-17 97.6 7.5 158 34-215 3-165 (202) 57 cd04111 Rab39 Rab39 subfamily. 99.4 1.1E-11 5.2E-16 92.1 12.0 156 34-238 5-162 (211) 58 cd04127 Rab27A Rab27a subfamil 99.3 8.2E-12 3.9E-16 92.9 11.2 157 34-238 7-173 (180) 59 cd01892 Miro2 Miro2 subfamily. 99.3 4.3E-12 2E-16 94.7 9.5 152 34-238 7-162 (169) 60 smart00173 RAS Ras subfamily o 99.3 9.2E-12 4.4E-16 92.6 10.9 154 34-238 5-160 (166) 61 cd01875 RhoG RhoG subfamily. 99.3 1.3E-11 6.3E-16 91.6 11.4 168 34-246 6-185 (191) 62 cd04138 H_N_K_Ras_like H-Ras/N 99.3 1.2E-11 5.7E-16 91.9 10.8 153 34-238 4-158 (162) 63 KOG1673 Ras GTPases [General f 99.3 4.5E-12 2.2E-16 94.5 8.5 179 34-257 23-204 (205) 64 cd04115 Rab33B_Rab33A Rab33B/R 99.3 2.1E-11 9.8E-16 90.4 11.5 155 34-237 5-168 (170) 65 cd04134 Rho3 Rho3 subfamily. 99.3 2.4E-11 1.2E-15 89.9 11.9 170 32-246 1-182 (189) 66 cd04177 RSR1 RSR1 subgroup. R 99.3 1.3E-11 6E-16 91.7 10.1 154 34-238 4-160 (168) 67 cd04172 Rnd3_RhoE_Rho8 Rnd3/Rh 99.3 6E-12 2.8E-16 93.8 8.4 155 34-235 8-173 (182) 68 cd04146 RERG_RasL11_like RERG/ 99.3 3.2E-11 1.5E-15 89.2 12.0 155 34-238 2-160 (165) 69 smart00176 RAN Ran (Ras-relate 99.3 1.7E-11 8.2E-16 90.9 10.5 146 37-235 1-155 (200) 70 cd04156 ARLTS1 ARLTS1 subfamil 99.3 5.7E-11 2.7E-15 87.6 13.0 156 34-238 2-158 (160) 71 cd01874 Cdc42 Cdc42 subfamily. 99.3 1.1E-11 5.3E-16 92.1 9.1 158 34-238 4-171 (175) 72 cd04144 Ras2 Ras2 subfamily. 99.3 4.5E-11 2.1E-15 88.3 12.2 156 34-238 2-159 (190) 73 cd04159 Arl10_like Arl10-like 99.3 5.5E-11 2.6E-15 87.7 12.4 154 34-238 2-157 (159) 74 cd04145 M_R_Ras_like M-Ras/R-R 99.3 1.7E-11 8E-16 91.0 9.8 154 34-238 5-160 (164) 75 cd04151 Arl1 Arl1 subfamily. 99.3 1E-10 4.8E-15 86.1 13.3 153 34-238 2-156 (158) 76 cd04130 Wrch_1 Wrch-1 subfamil 99.3 1.4E-11 6.4E-16 91.6 8.7 157 34-237 3-169 (173) 77 pfam00025 Arf ADP-ribosylation 99.3 5.2E-11 2.5E-15 87.9 11.6 155 34-238 18-173 (176) 78 cd04173 Rnd2_Rho7 Rnd2/Rho7 su 99.3 3.7E-11 1.8E-15 88.8 10.3 152 34-233 4-167 (222) 79 cd04126 Rab20 Rab20 subfamily. 99.3 4.2E-11 2E-15 88.5 10.4 155 34-238 3-186 (220) 80 cd04160 Arfrp1 Arfrp1 subfamil 99.2 1.4E-10 6.8E-15 85.2 12.7 157 33-238 1-165 (167) 81 cd04174 Rnd1_Rho6 Rnd1/Rho6 su 99.2 2.7E-11 1.3E-15 89.7 8.5 142 34-221 16-168 (232) 82 cd01893 Miro1 Miro1 subfamily. 99.2 1E-10 4.8E-15 86.1 11.2 156 34-238 3-160 (166) 83 KOG0078 GTP-binding protein SE 99.2 3.5E-11 1.7E-15 88.9 8.7 154 34-238 15-170 (207) 84 cd00878 Arf_Arl Arf (ADP-ribos 99.2 3E-11 1.4E-15 89.4 8.2 110 34-190 2-112 (158) 85 cd04154 Arl2 Arl2 subfamily. 99.2 5.9E-11 2.8E-15 87.5 9.6 136 31-213 14-150 (173) 86 cd04142 RRP22 RRP22 subfamily. 99.2 1.5E-10 7.1E-15 85.0 11.3 157 34-237 3-173 (198) 87 cd01871 Rac1_like Rac1-like su 99.2 1.4E-10 6.6E-15 85.2 9.8 158 34-238 4-171 (174) 88 cd04147 Ras_dva Ras-dva subfam 99.2 3.2E-10 1.5E-14 83.0 11.2 156 34-237 2-162 (198) 89 smart00177 ARF ARF-like small 99.1 2.5E-10 1.2E-14 83.6 9.4 121 31-198 17-138 (181) 90 cd04149 Arf6 Arf6 subfamily. 99.1 1.4E-10 6.6E-15 85.2 7.8 113 31-190 9-122 (168) 91 cd04157 Arl6 Arl6 subfamily. 99.1 1.6E-10 7.7E-15 84.8 8.0 113 33-190 1-116 (162) 92 cd04150 Arf1_5_like Arf1-Arf5- 99.1 2.6E-10 1.3E-14 83.5 8.7 118 34-198 3-121 (159) 93 cd04158 ARD1 ARD1 subfamily. 99.1 1.1E-09 5E-14 79.7 11.3 140 34-221 2-142 (169) 94 cd04155 Arl3 Arl3 subfamily. 99.1 5.4E-10 2.6E-14 81.5 9.3 121 31-198 14-135 (173) 95 cd04153 Arl5_Arl8 Arl5/Arl8 su 99.1 3.4E-10 1.6E-14 82.8 8.1 113 31-190 15-128 (174) 96 cd01873 RhoBTB RhoBTB subfamil 99.0 4.5E-09 2.2E-13 75.7 11.4 154 34-233 5-187 (195) 97 KOG0094 GTPase Rab6/YPT6/Ryh1, 99.0 3.7E-09 1.8E-13 76.3 10.9 174 34-258 25-203 (221) 98 cd04103 Centaurin_gamma Centau 99.0 5E-09 2.4E-13 75.4 11.2 151 34-238 3-155 (158) 99 cd04162 Arl9_Arfrp2_like Arl9/ 99.0 1.4E-09 6.8E-14 78.9 8.3 108 34-190 2-111 (164) 100 cd00879 Sar1 Sar1 subfamily. 99.0 1.6E-09 7.7E-14 78.5 8.5 120 31-198 19-140 (190) No 1 >KOG3929 Uncharacterized conserved protein [Function unknown] Probab=100.00 E-value=0 Score=799.78 Aligned_columns=345 Identities=88% Q ss_pred CCCCCHHHHHHHHHHHCCCCCCCCCHHHC-----CCCEEEEEECCCCCHHHHHHHHCCCCCCC-CCCCCCCHHHHHHHCC Q ss_conf 98741889999876522576661101112-----57458998659886377777552766788-8753100022111015 Q Ver_Hs_NP_0570 1 MPSETLWEIAKAEVEKRGINGSEGDGAEI-----AEKFVFFIGSKNGGKTTIILRCLDRDEPP-KPTLALEYTYGRRAKG 74 (351) Q Consensus 1 ~~~~~lw~~~~~ev~~~~~~~~~~~~~~~-----~ek~v~~vGsk~~GKTTli~Rfl~r~e~~-KPTlALeYtygRra~~ 74 (351) ||-+++|.++.++++.+..++++++---. -|.|++|.|+++- ||+|++|++|++.+ .||+|||||||||++| T Consensus 10 m~Ve~~~~~a~a~~~~~DinG~~~deqL~e~~~~~E~~I~~~Gn~~~--tt~I~~~FdR~e~~~~ptlaLEYtygRR~~g 87 (363) T KOG3929 10 MPVETLWEIAKAEVEKRDINGSEGDEQLAEIAEKFEFFIGSKGNGGK--TTIILRCFDRDEPPKPPTLALEYTYGRRAKG 87 (363) T ss_pred HHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHCCHHCEEEEECCCCE--EEEEEECCCCCCCCCCCCEEEEEHHHHHHCC T ss_conf 55555433454101244312321378999850300205677338850--6653300576567899721221012344147 Q ss_pred CCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHH Q ss_conf 78711178889715785420211000042351206778887369846899999999999999999999998526953789 Q Ver_Hs_NP_0570 75 HNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVS 154 (351) Q Consensus 75 ~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~ 154 (351) |+ +||||||||||||+++.+|++||||.+||++|++|+|||||+|+++|+|||+.++++|++|++++++|.+..+++.+ T Consensus 88 ~~-~kdiaN~WELGgg~~~~~LLsVPit~~~l~~~slIL~LDls~p~~~W~t~E~~~~~~R~~vd~~~~~~~k~~~~L~E 166 (363) T KOG3929 88 HN-PKDIANFWELGGGTSLLDLLSVPITGDTLRTFSLILVLDLSKPNDLWPTMENLLQATRSHVDKVIMKLGKTNAKLVE 166 (363) T ss_pred CC-CHHHHHHHHCCCCCCHHHHHHCCCCCCCHHHHHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHH T ss_conf 88-51456555326732468886055455628775666765115624432579999999998999999987414889999 Q ss_pred HHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCCCCCHHHHHHHHHHHHHHHHHCCCEE-EEEECHHHHHHHHHHH Q ss_conf 999999984146677600111068877997121000158876678999999999998609468-8851203456789998 Q Ver_Hs_NP_0570 155 EMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQDFESEKRKVICKTLRFVAHYYGASL-MFTSKSEALLLKIRGV 233 (351) Q Consensus 155 ~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~~~D~e~rK~i~r~LR~iAH~yGA~L-~FtSk~e~l~~r~r~~ 233 (351) +|+||.|+|+|+||+|.++++|||||++|||+|||+||+||||+|||+||||||+||+|||+| ||+|++++++..+|++ T Consensus 167 ~mrqR~~~rvgqd~~d~e~~dP~P~PV~IVgsKYDvFq~FesekRkH~C~~LRf~Ah~yGaaLlmfSskMe~l~K~ir~~ 246 (363) T KOG3929 167 EMRQRIWNRVGQDHPDHELIDPFPVPVVIVGSKYDVFQDFESEKRKHICKTLRFVAHYYGAALLMFSSKMEALLKKIRGV 246 (363) T ss_pred HHHHHHHHHHCCCCCCCCCCCCCCCCEEEECCCCHHHCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH T ss_conf 99999998621468740002778853478535200012663678999999999999997789999888789999998777 Q ss_pred HHHHHCCCCCCCEEEEECCCCEEEECCCCCHHHCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHCCCCCCCHHHHHH--CC Q ss_conf 8875057777730575067757870587636566887556531022245423678999998637897531234532--66 Q Ver_Hs_NP_0570 234 INQLAFGIDKSKSICVDQNKPLFITAGLDSFGQIGSPPVPENDIGKLHAHSPMELWKKVYEKLFPPKSINTLKDIK--DP 311 (351) Q Consensus 234 inhl~FG~~~~k~~~~D~~kPl~I~aG~DS~~~IG~P~~~~~~~g~~~~~~~ldlwk~~~~~~fP~k~~~~~k~~~--DP 311 (351) ||||+||++++++++||||+|+||+||+|||++||.||+++|++| |++|+++|+++|.+.||+++.+.+++.+ || T Consensus 247 i~HlaFG~~~~~s~~vD~NkPlfi~~G~DS~~~IG~pp~~~nd~G---a~sp~elw~~~F~~l~PQk~~~~~kd~kttDP 323 (363) T KOG3929 247 INHLAFGIDKSKSICVDQNKPLFITAGLDSFGQIGSPPVPENDIG---AHSPMELWKKVFEKLFPQKSINTLKDIKTTDP 323 (363) T ss_pred HHHHHCCCCCCCCEEEECCCCEEEEECCCCHHHCCCCCCCCCCCC---CCCHHHHHHHHHHHHCCCHHHHHHHHHHHCCC T ss_conf 775404765766545307874589855532233378888743345---43337899999986334123455555430153 Q ss_pred CCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCC Q ss_conf 7788888358899999999999999876765654102469 Q Ver_Hs_NP_0570 312 ARDPQYAENEVDEMRIQKDLELEQYKRSSSKSWKQIELDS 351 (351) Q Consensus 312 ~~dp~f~E~~ID~lR~qKd~ELeqy~r~~~~~~~~~~~~~ 351 (351) ++||+|+|++||+||.||++||+||+|+..++||+-++++ T Consensus 324 a~DP~FKE~~IDe~r~qK~~EL~~~~Rs~~~R~k~E~~~~ 363 (363) T KOG3929 324 ARDPQFKENEIDEMRIQKDLELEQYKRSSSKRWKQEELDS 363 (363) T ss_pred CCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC T ss_conf 3266655520678998888999888765766666665219 No 2 >KOG3905 Dynein light intermediate chain [Cell motility] Probab=100.00 E-value=0 Score=318.49 Aligned_columns=254 Identities=25% Q ss_pred CCHHHHHHHHHHHCCCCCCCCCHHHCCCCEEEEEECCCCCHHHHHHHHCCCCCCCCCCCCCCHHHHHHHCCCCCCCEEEE Q ss_conf 41889999876522576661101112574589986598863777775527667888753100022111015787111788 Q Ver_Hs_NP_0570 4 ETLWEIAKAEVEKRGINGSEGDGAEIAEKFVFFIGSKNGGKTTIILRCLDRDEPPKPTLALEYTYGRRAKGHNTPKDIAH 83 (351) Q Consensus 4 ~~lw~~~~~ev~~~~~~~~~~~~~~~~ek~v~~vGsk~~GKTTli~Rfl~r~e~~KPTlALeYtygRra~~~~~~KdvaH 83 (351) ++||.+|++||++|.+++.+ +.|+|+++|..++|||||| +-|+..|.+|+..+|||-|....+..++....|+ T Consensus 31 qnlWs~iLsev~T~~~sklp------sgk~VlvlGdn~sGKtsLi-~klqg~e~~KkgsgLeY~yl~V~de~RDd~tr~~ 103 (473) T KOG3905 31 QNLWSEILSEVSTRTRSKLP------SGKNVLVLGDNGSGKTSLI-SKLQGSETVKKGSGLEYLYLHVHDEDRDDLTRCN 103 (473) T ss_pred HHHHHHHHHHHHHCCCCCCC------CCCEEEEEECCCCCHHHHH-HHHHCCCCCCCCCCCEEEEEEECCCCHHHHHHCC T ss_conf 89999998654201234477------8865799705887457898-8763024567765312678862131004465487 Q ss_pred EEEECCCCCHHHCEEEEECCCCCCEEEEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHH Q ss_conf 89715785420211000042351206778887369846899999999999999999999998526953789999999984 Q Ver_Hs_NP_0570 84 FWELGGGTSLLDLISIPITGDTLRTFSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNN 163 (351) Q Consensus 84 ~WELGgg~~ls~Li~ipit~~~l~~~~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~ 163 (351) +|.|.|...+..|+...+.+.++....||+++|||+||.+.++|..|.++++.|+|++ +.+++.+++++|+.... T Consensus 104 VWiLDGd~~h~~LLk~al~ats~aetlviltasms~Pw~~lesLqkWa~Vl~ehidkl-----~i~~ee~ka~rqk~~k~ 178 (473) T KOG3905 104 VWILDGDLYHKGLLKFALPATSLAETLVILTASMSNPWTLLESLQKWASVLREHIDKL-----KIPPEEMKAGRQKLEKD 178 (473) T ss_pred CEEECCCHHHHHHHHHCCCCCCCCCEEEEEEEECCCCHHHHHHHHHHHHHHHHHHHHH-----CCCHHHHHHHHHHHHHH T ss_conf 1487187555212432046556154589899865750358999999999999989862-----58989999999998888 Q ss_pred CC--------------------CCCCCCCCCCC---------CCCCEEEECCEECCC------CCCCHHHHHHHHHHHHH Q ss_conf 14--------------------66776001110---------688779971210001------58876678999999999 Q Ver_Hs_NP_0570 164 MP--------------------KDHPDHELIDP---------FPVPLVIIGSKYDVF------QDFESEKRKVICKTLRF 208 (351) Q Consensus 164 ~~--------------------~dhpD~~~v~p---------~piPlvIVg~KYD~F------~~~D~e~rK~i~r~LR~ 208 (351) .+ ...-|-+.+-| ||||+++||+|+|+. ++|..|+..+|.+.||- T Consensus 179 wQeYvep~e~~pgsp~~r~t~~~~~~de~~llPL~~dtLt~NlGi~vlVV~TK~D~~s~leke~eyrDehfdfiq~~lRk 258 (473) T KOG3905 179 WQEYVEPGEDQPGSPQRRTTVVGSSADEHVLLPLGQDTLTHNLGIPVLVVCTKCDAVSVLEKEHEYRDEHFDFIQSHLRK 258 (473) T ss_pred HHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHCCCCCEEEEEECCCHHHHHHHCCCCCHHHHHHHHHHHHH T ss_conf 89760512478888620343335655311112267762000068747999842430334552010016789999999999 Q ss_pred HHHHCCCEEEEEECHHHHHHH-HHHHHHHHHCCCCCCCEEEEECCCCEEEECCCCCHHHCCC Q ss_conf 998609468885120345678-9998887505777773057506775787058763656688 Q Ver_Hs_NP_0570 209 VAHYYGASLMFTSKSEALLLK-IRGVINQLAFGIDKSKSICVDQNKPLFITAGLDSFGQIGS 269 (351) Q Consensus 209 iAH~yGA~L~FtSk~e~l~~r-~r~~inhl~FG~~~~k~~~~D~~kPl~I~aG~DS~~~IG~ 269 (351) +|..|||+|+|||.+|.++.. ++.+|.|-.||+++.-.+++.+...||||||||+.++|+. T Consensus 259 FCLr~GaaLiyTSvKE~KNidllyKYivhr~yG~~fttpAlVVEkdaVfIPAGWD~eKKI~I 320 (473) T KOG3905 259 FCLRYGAALIYTSVKETKNIDLLYKYIVHRSYGFPFTTPALVVEKDAVFIPAGWDNEKKIDI 320 (473) T ss_pred HHHHCCCEEEEEECCCCCCHHHHHHHHHHHHCCCCCCCHHHEEECCEEEECCCCCCCCHHHH T ss_conf 99860630255411124556888888887641553135001232031463046686300221 No 3 >pfam05783 DLIC Dynein light intermediate chain (DLIC). This family consists of several eukaryotic dynein light intermediate chain proteins. The light intermediate chains (LICs) of cytoplasmic dynein consist of multiple isoforms, which undergo post-translational modification to produce a large number of species. DLIC1 is known to be involved in assembly, organisation, and function of centrosomes and mitotic spindles when bound to pericentrin. DLIC2 is a subunit of cytoplasmic dynein 2 that may play a role in maintaining Golgi organisation by binding cytoplasmic dynein 2 to its Golgi-associated cargo. Probab=100.00 E-value=1.4e-45 Score=303.67 Aligned_columns=254 Identities=24% Q ss_pred CCHHHHHHHHHHHCCCCCCCCCHHHCCCCEEEEEECCCCCHHHHHHHHCCCCCCCCCCCCCCHHHHHHHCCCCCCCEEEE Q ss_conf 41889999876522576661101112574589986598863777775527667888753100022111015787111788 Q Ver_Hs_NP_0570 4 ETLWEIAKAEVEKRGINGSEGDGAEIAEKFVFFIGSKNGGKTTIILRCLDRDEPPKPTLALEYTYGRRAKGHNTPKDIAH 83 (351) Q Consensus 4 ~~lw~~~~~ev~~~~~~~~~~~~~~~~ek~v~~vGsk~~GKTTli~Rfl~r~e~~KPTlALeYtygRra~~~~~~KdvaH 83 (351) ++||..|+.+|.++.+++.+ .+|+|+++|..++|||||| .-|+..+.+|..-||+|+|-...+.+++..-.+| T Consensus 26 ~nLWsSIL~~V~t~~r~Klp------~~KniLVLG~~~~GKttLl-~~Lqg~~~~kkg~aL~Y~YldV~DeD~Dd~~R~~ 98 (475) T pfam05783 26 QNLWSEILSEVSTRTRSKLP------SGKNVLVLGDNGSGKTSLI-SRLQGSERTKKGRGLEYLYLHVHDEDRDDLTRCN 98 (475) T ss_pred HHHHHHHHHHHHCCCCCCCC------CCCEEEEEECCCCCHHHHH-HHHHCCCCCCCCCCCCEEEECCCCCCHHHHCCCC T ss_conf 24789888653025333477------7664788508997557899-9750577667863101346323220303221542 Q ss_pred EEEECCCCCHHHCEEEEECCCCCCEEEEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHH Q ss_conf 89715785420211000042351206778887369846899999999999999999999998526953789999999984 Q Ver_Hs_NP_0570 84 FWELGGGTSLLDLISIPITGDTLRTFSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNN 163 (351) Q Consensus 84 ~WELGgg~~ls~Li~ipit~~~l~~~~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~ 163 (351) +|-|.|..+++.||...++++|+.++.|+||||||+||.+.+.|..|+++++.|++++ +.+++...+|++++... T Consensus 99 vwiLd~~~~~~~LLK~aL~~~si~~TlViI~lDms~PW~~i~qL~~Wi~VLrehi~~L-----~i~~ee~~el~e~l~~~ 173 (475) T pfam05783 99 VWILDGDLYHKGLLKFALPATSLAETLVILTASMSNPWTLLESLQKWASVLREHIDKL-----KIPPEEMKAGRQKLEKD 173 (475) T ss_pred EEECCCCCCCCCCCCCCCCCCCHHHHHEHHHHHHHHHHHHHHHHHHHHHHHHHHHHHC-----CCCHHHHHHHHHHHHHH T ss_conf 4760875152223212577231422012001212013489999999999999999713-----89988999999999999 Q ss_pred CCC--------------------CCCCCCCCCC---------CCCCEEEECCEECCCC------CCCHHHHHHHHHHHHH Q ss_conf 146--------------------6776001110---------6887799712100015------8876678999999999 Q Ver_Hs_NP_0570 164 MPK--------------------DHPDHELIDP---------FPVPLVIIGSKYDVFQ------DFESEKRKVICKTLRF 208 (351) Q Consensus 164 ~~~--------------------dhpD~~~v~p---------~piPlvIVg~KYD~F~------~~D~e~rK~i~r~LR~ 208 (351) .+. ...|.++..| +|||+|+||+|.|... ++.-|+..+|.+.||- T Consensus 174 wqeY~epg~~~d~s~~r~t~~~~~~~~~~v~lPLgeg~Lt~NLGiPiiVVctKsD~ie~LEKe~~ykeE~fDfIqq~LR~ 253 (475) T pfam05783 174 WQEYVEPGEDLDGSPQRRTSVVGSFDEEHVLLPLGQDTLTHNLGLPVLVVCTKCDAMSVLEKEHDYRDEHFDFIQSHLRK 253 (475) T ss_pred HHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEECCCCEEEEEEEECCCHHHHHHCCCCCCHHHHHHHHHHHHH T ss_conf 99860553467877632456656534445657788763412788269998617621333320156643679999999999 Q ss_pred HHHHCCCEEEEEECHHHHHHH-HHHHHHHHHCCCCCCCEEEEECCCCEEEECCCCCHHHCCC Q ss_conf 998609468885120345678-9998887505777773057506775787058763656688 Q Ver_Hs_NP_0570 209 VAHYYGASLMFTSKSEALLLK-IRGVINQLAFGIDKSKSICVDQNKPLFITAGLDSFGQIGS 269 (351) Q Consensus 209 iAH~yGA~L~FtSk~e~l~~r-~r~~inhl~FG~~~~k~~~~D~~kPl~I~aG~DS~~~IG~ 269 (351) +|-.|||+|+|||-++..+.. .+.+|-|-+||+++.-..++.....||||+|||+|.+|+. T Consensus 254 ~cLqYGAsLiYTS~ke~kNldlLykYl~HrlYgfpf~~~a~VvekDaIfIPsGWDn~kKI~I 315 (475) T pfam05783 254 FCLQYGAALIYTSVKETKNIDLLYKYIVHRSYGFPFTTPALVVEKDAVFIPAGWDNEKKIDI 315 (475) T ss_pred HHHHCCCEEEEECCCCCCCHHHHHHHHHHHHHCCCCCCCCCEEEHHEEEECCCCCCHHHHHH T ss_conf 99870975898547764238999999998860765456220010000340588881455675 No 4 >cd04128 Spg1 Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are Probab=99.64 E-value=3.2e-15 Score=114.28 Aligned_columns=177 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||++||+.. .+.+.||.+++|.--.-...++.. ..++|..+|--.+..+...-.+ ....+ T Consensus 3 ivliGd~~VGKTsLi~r~~~~~F~~~y~~TiG~~~~~k~i~v~~~~v--~l~iwDtaGqE~f~~~~~~y~~----~a~~~ 76 (182) T cd04128 3 IGLLGDAQIGKTSLMVKYVEGEFDEDYIQTLGVNFMEKTISIRGTEI--TFSIWDLGGQREFINMLPLVCN----DAVAI 76 (182) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEECCEEE--EEEEEECCCCCCCHHHHHHHCC----CCCEE T ss_conf 89981698438888777643712776355034467898999889689--9887316888310127786403----77768 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..|++.++.+... ++| ++||+|+|+. T Consensus 77 ilVfDit~~~Sf-~~i~~W~~~i~~~~~~-------------------------------------~~~-ILVGNK~DL~ 117 (182) T cd04128 77 LFMFDLTRKSTL-NSIKEWYRQARGFNKT-------------------------------------AIP-ILVGTKYDLF 117 (182) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCE-EEEECCCCCC T ss_conf 999865997899-9999999999862799-------------------------------------608-9983274310 Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHH-HHHHHHHHHCCCCCCCEEEEECCCCE Q ss_conf 58876678999999999998609468885120345678-99988875057777730575067757 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLK-IRGVINQLAFGIDKSKSICVDQNKPL 255 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r-~r~~inhl~FG~~~~k~~~~D~~kPl 255 (351) .+.+++.+..+..-.+-.|-.+|+.++++|-+...... .=..+-..+|..+...+-.+.--.|+ T Consensus 118 ~~~~~~~~~~~~~~~~~~a~~~~~~~~etSAktg~nV~e~Fe~l~~ki~~~~~~~~~~~~~~~~~ 182 (182) T cd04128 118 ADLPPEEQEEITKQARKYAKAMKAPLIFCSTSHSINVQKIFKIVLAKAFDLPLTIPEILTVGEPI 182 (182) T ss_pred CCCCHHHHHHHHHHHHHHHHHCCCCEEEEECCCCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCCC T ss_conf 01442456778899999999729959999724798878999999999853788877668888899 No 5 >cd01860 Rab5_related Rab5-related subfamily. This subfamily includes Rab5 and Rab22 of mammals, Ypt51/Ypt52/Ypt53 of yeast, and RabF of plants. The members of this subfamily are involved in endocytosis and endocytic-sorting pathways. In mammals, Rab5 GTPases localize to early endosomes and regulate fusion of clathrin-coated vesicles to early endosomes and fusion between early endosomes. In yeast, Ypt51p family members similarly regulate membrane trafficking through prevacuolar compartments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence mo Probab=99.53 E-value=4.1e-14 Score=107.31 Aligned_columns=153 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEE-EEEEECCCCCHHHCEEEEECCCCCCEEE Q ss_conf 899865988637777755276--6788875310002211101578711178-8897157854202110000423512067 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIA-HFWELGGGTSLLDLISIPITGDTLRTFS 110 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~Kdva-H~WELGgg~~ls~Li~ipit~~~l~~~~ 110 (351) |++||+.|+||||||.||+.. .+.+.||++.+| +...-....+.+- ++|..+|...+..|...-++. .-. T Consensus 4 i~iiG~~gvGKTsli~r~~~~~f~~~~~pTig~~~---~~k~i~~~~~~v~l~i~Dt~G~e~~~~l~~~~~~~----a~~ 76 (163) T cd01860 4 LVLLGDSSVGKSSLVLRFVKNEFSENQESTIGAAF---LTQTVNLDDTTVKFEIWDTAGQERYRSLAPMYYRG----AAA 76 (163) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEE---EEEEEEECCEEEEEEEECCCCCHHHHHHHHHHHCC----CCE T ss_conf 99981699658999998862833755351013225---68899888879999970489831245666765138----884 Q ss_pred EEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 78887369846899999999999999999999998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 111 LVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 111 viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) ++||.|++.+.++=. +..|++.++++... .+|++|||+|.|. T Consensus 77 ~ilvydit~~~Sf~~-i~~w~~~i~~~~~~-------------------------------------~~~iilVgNK~Dl 118 (163) T cd01860 77 AIVVYDITSEESFEK-AKSWVKELQRNASP-------------------------------------NIIIALVGNKADL 118 (163) T ss_pred EEEEEECCCHHHHHH-HHHHHHHHHHHCCC-------------------------------------CCEEEEEECCHHH T ss_conf 999986599789999-99988765530699-------------------------------------9589998322105 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 158876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 191 FQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 191 F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+--.-.+.+|-.+|+..+.+|-++. ..+..+..+++ T Consensus 119 -----~~~r~v~~~e~~~~a~~~~~~~~e~SAk~~--~nI~~~F~~l~ 159 (163) T cd01860 119 -----ESKRQVSTEEAQEYADENGLLFFETSAKTG--ENVNELFTEIA 159 (163) T ss_pred -----HHCCCCCHHHHHHHHHHCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf -----430588789999999965992999971489--88889999999 No 6 >cd04106 Rab23_lke Rab23-like subfamily. Rab23 is a member of the Rab family of small GTPases. In mouse, Rab23 has been shown to function as a negative regulator in the sonic hedgehog (Shh) signalling pathway. Rab23 mediates the activity of Gli2 and Gli3, transcription factors that regulate Shh signaling in the spinal cord, primarily by preventing Gli2 activation in the absence of Shh ligand. Rab23 also regulates a step in the cytoplasmic signal transduction pathway that mediates the effect of Smoothened (one of two integral membrane proteins that are essential components of the Shh signaling pathway in vertebrates). In humans, Rab23 is expressed in the retina. Mice contain an isoform that shares 93% sequence identity with the human Rab23 and an alternative splicing isoform that is specific to the brain. This isoform causes the murine open brain phenotype, indicating it may have a role in the development of the central nervous system. GTPase activating proteins (GAPs) interact with G Probab=99.52 E-value=7.7e-14 Score=105.61 Aligned_columns=155 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.|.|||||+.||+.. .+.+.||++.+|.--......+...=-.++|..+|.-.+..+...-++..+ .+ T Consensus 3 i~~iGd~~vGKTsli~r~~~~~f~~~~~~Tig~~~~~k~v~v~~~~~~v~l~iwDt~g~e~~~~~~~~~~~~~~----~~ 78 (162) T cd04106 3 VIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIGVDFLEKQIFLRQSDEDVRLMLWDTAGQEEFDAITKAYYRGAQ----AC 78 (162) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEEEECCEEEEEEEECCCCCCHHHHHHHHHCCCCC----EE T ss_conf 89980798448999999862822755564101046777899700884799998718888003455376414897----89 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.++++ +.++.|++.++..... +|+++||+|.|.. T Consensus 79 llvydvt~~~Sf-~~i~~w~~~i~~~~~~--------------------------------------~p~ilVGNK~Dl~ 119 (162) T cd04106 79 ILVFSTTDRESF-EAIESWKEKVEAECGD--------------------------------------IPMVLVQTKIDLL 119 (162) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 999866997899-9999999999985499--------------------------------------3799982142321 Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .+ |.+.-+-.+.+|..+|+..+.+|-++. ..+..+..+|+ T Consensus 120 ~~-----~~vs~~~~~~~a~~~~~~~~E~SAk~~--~nV~e~F~~la 159 (162) T cd04106 120 DQ-----AVITNEEAEALAKRLQLPLFRTSVKDD--FNVTELFEYLA 159 (162) T ss_pred CC-----CCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf 24-----658989999999966995999971589--88789999998 No 7 >cd01867 Rab8_Rab10_Rab13_like Rab8/Sec4/Ypt2. Rab8/Sec4/Ypt2 are known or suspected to be involved in post-Golgi transport to the plasma membrane. It is likely that these Rabs have functions that are specific to the mammalian lineage and have no orthologs in plants. Rab8 modulates polarized membrane transport through reorganization of actin and microtubules, induces the formation of new surface extensions, and has an important role in directed membrane transport to cell surfaces. The Ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the Ypt/Rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian Rab8. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhi Probab=99.52 E-value=6.7e-14 Score=106.00 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.||||||.||+.. .+.+.||.+.+|..-.....+... -.++|..+|--.+..+-...++.-+ .+ T Consensus 6 i~liGd~~vGKTsli~r~~~~~f~~~~~~Tig~~~~~k~v~~~~~~v--~l~iwDt~G~e~~~~~~~~~~~~a~----~~ 79 (167) T cd01867 6 LLLIGDSGVGKSCLLLRFSEDSFNPSFISTIGIDFKIRTIELDGKKI--KLQIWDTAGQERFRTITTAYYRGAM----GI 79 (167) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEECCEEE--EEEEEECCCCCHHHHHHHHHCCCCC----EE T ss_conf 99982698438999988763810765564121256788999889499--9999866898002345375436998----89 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.++.|++.++++..+ -+|++|||+|.|+ T Consensus 80 iivfDit~~~Sf-~~i~~w~~~i~~~~~~-------------------------------------~~~~ilVGNK~DL- 120 (167) T cd01867 80 ILVYDITDEKSF-ENIRNWMRNIEEHASE-------------------------------------DVERMLVGNKCDM- 120 (167) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEEECCCC- T ss_conf 999856984678-9999999999852699-------------------------------------9389999404675- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +++|.+-..-.+-+|-.+|+..+.+|-+.. ..+..+..+++ T Consensus 121 ----~~~r~v~~~~~~~~a~~~~~~~~e~SAk~~--~nv~~~F~~l~ 161 (167) T cd01867 121 ----EEKRVVSKEEGEALADEYGIKFLETSAKAN--INVEEAFFTLA 161 (167) T ss_pred ----CCCCCCCHHHHHHHHHHCCCCEEEEEECCC--CCHHHHHHHHH T ss_conf ----222466989999999964995999970489--78789999999 No 8 >cd00154 Rab Rab family. Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide di Probab=99.52 E-value=7.3e-14 Score=105.76 Aligned_columns=154 Identities=23% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |.+||+.|.||||||+|++.. .+.+.||++.+|..-.-...+... -..+|..+|...+..|.+..++. .-.+ T Consensus 3 i~ivG~~~vGKTsli~~~~~~~f~~~~~~Ti~~~~~~k~i~~~~~~~--~~~i~Dt~g~e~~~~~~~~~~~~----~d~~ 76 (159) T cd00154 3 IVLIGDSGVGKTSLLLRFVDGKFDENYKSTIGVDFKSKTIEIDGKTV--KLQIWDTAGQERFRSITPSYYRG----AHGA 76 (159) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEECCEEE--EEEEEECCCCHHHHHHHHHHCCC----CCEE T ss_conf 89982699668999999863824744465310036888998889599--99998659971456777875148----9869 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|+|++++.++ ..++.|++.++++... .+|++|||+|+|+ T Consensus 77 iiv~d~~~~~Sf-~~i~~~~~~i~~~~~~-------------------------------------~~piiivgnK~Dl- 117 (159) T cd00154 77 ILVYDITNRESF-ENLDKWLKELKEYAPE-------------------------------------NIPIILVGNKIDL- 117 (159) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEECCCCH- T ss_conf 999866997899-9999999999982699-------------------------------------9789998413100- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .+++.+...-.+.+|..+++..+.+|-+.. ..+..+...++ T Consensus 118 ----~~~~~v~~~~~~~~~~~~~~~~~e~Sa~~~--~~i~~~F~~i~ 158 (159) T cd00154 118 ----EDQRQVSTEEAQQFAKENGLLFFETSAKTG--ENVEELFQSLA 158 (159) T ss_pred ----HHHCCCCHHHHHHHHHHCCCCEEEEEECCC--CCHHHHHHHHC T ss_conf ----010265688999999965996999970479--88789999970 No 9 >cd04110 Rab35 Rab35 subfamily. Rab35 is one of several Rab proteins to be found to participate in the regulation of osteoclast cells in rats. In addition, Rab35 has been identified as a protein that interacts with nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) in human cells. Overexpression of NPM-ALK is a key oncogenic event in some anaplastic large-cell lymphomas; since Rab35 interacts with N|PM-ALK, it may provide a target for cancer treatments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is Probab=99.52 E-value=1e-13 Score=104.91 Aligned_columns=153 Identities=24% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.|.||||||.||+.. .+.+.||++.+|..-.-.-.+... ..++|..+|-..+..|...-++. .-.+ T Consensus 9 vv~iGd~~VGKTsli~r~~~~~F~~~y~~Tig~~~~~k~v~i~~~~~--~l~iwDtaGqe~~~~l~~~y~~~----a~~~ 82 (199) T cd04110 9 LLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEINGERV--KLQIWDTAGQERFRTITSTYYRG----THGV 82 (199) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCEEEEEEEEEEEECCEEE--EEEEEECCCCCHHHHHHHHHCCC----CCEE T ss_conf 99982698438999988761800766465112235788899858399--99998669970356776765038----9879 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.++++ +.+..|++.+++..+. +|+++||+|.| T Consensus 83 ilVydit~~~Sf-~~i~~w~~~i~~~~~~--------------------------------------~~~iLVGNK~D-- 121 (199) T cd04110 83 IVVYDVTNGESF-VNVKRWLQEIEQNCDD--------------------------------------VCKVLVGNKND-- 121 (199) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC--------------------------------------CCEEEEEECCC-- T ss_conf 999877997799-9999999999851256--------------------------------------73699840336-- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .+++|.+.-.-.+.+|-.+|+..+.+|-+.. ..+-.+...++ T Consensus 122 ---l~~~r~v~~ee~~~~a~~~~~~f~EtSAktg--~nV~e~F~~i~ 163 (199) T cd04110 122 ---DPERKVVETEDAYKFAGQMGISLFETSAKEN--INVEEMFNCIT 163 (199) T ss_pred ---CHHHCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ---3112265689999999966995999971589--88889999999 No 10 >cd00876 Ras Ras family. The Ras family of the Ras superfamily includes classical N-Ras, H-Ras, and K-Ras, as well as R-Ras, Rap, Ral, Rheb, Rhes, ARHI, RERG, Rin/Rit, RSR1, RRP22, Ras2, Ras-dva, and RGK proteins. Ras proteins regulate cell growth, proliferation and differentiation. Ras is activated by guanine nucleotide exchange factors (GEFs) that release GDP and allow GTP binding. Many RasGEFs have been identified. These are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active GTP-bound Ras interacts with several effector proteins: among the best characterized are the Raf kinases, phosphatidylinositol 3-kinase (PI3K), RalGEFs and NORE/MST1. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of m Probab=99.52 E-value=7.6e-14 Score=105.66 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|+||||||+||+.. .+...||++-.|.--..-.+++- ..++|..+|.-.+..+...-++.-. .+ T Consensus 2 i~~iGd~~vGKTsli~r~~~~~f~~~~~~ti~~~~~k~~~~~~~~~---~l~i~Dt~G~e~~~~~~~~~~~~a~----~~ 74 (160) T cd00876 2 VVVLGAGGVGKSAITIQFVKGTFVEEYDPTIEDSYRKTIVVDGETY---TLDILDTAGQEEFSAMRDLYIRQGD----GF 74 (160) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCHHHEEEEEEEECCEEE---EEEEEECCCCHHHHHHHHHHHCCCC----EE T ss_conf 7888079966899999987281067535420022677888848289---9998635884133468887640461----78 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||+|++.+.+ ++.+..|++.+++.... -.+|+++||+|+|+ T Consensus 75 iivfdi~~~~S-f~~i~~w~~~i~~~~~~------------------------------------~~~piilvgNK~Dl- 116 (160) T cd00876 75 ILVYSITDRES-FEEIKGYREQILRVKDD------------------------------------EDIPIVLVGNKCDL- 116 (160) T ss_pred EEEEECCCHHH-HHHHHHHHHHHHHHCCC------------------------------------CCCEEEEEECCCCC- T ss_conf 99986699779-99999999999985389------------------------------------99679998213263- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) ++.|++...-.+.+|+.+|+..+.+|-+.. ..+..+..+++ T Consensus 117 ----~~~r~v~~~e~~~~a~~~~~~~~e~Sak~~--~nV~~~F~~i~ 157 (160) T cd00876 117 ----ENERQVSKEEGKALAKEWGCPFIETSAKDN--INIDEVFKLLV 157 (160) T ss_pred ----HHHCCCCHHHHHHHHHHCCCCEEEEEECCC--CCHHHHHHHHH T ss_conf ----001167688999999964996999970489--88889999999 No 11 >cd04109 Rab28 Rab28 subfamily. First identified in maize, Rab28 has been shown to be a late embryogenesis-abundant (Lea) protein that is regulated by the plant hormone abcisic acid (ABA). In Arabidopsis, Rab28 is expressed during embryo development and is generally restricted to provascular tissues in mature embryos. Unlike maize Rab28, it is not ABA-inducible. Characterization of the human Rab28 homolog revealed two isoforms, which differ by a 95-base pair insertion, producing an alternative sequence for the 30 amino acids at the C-terminus. The two human isoforms are presumbly the result of alternative splicing. Since they differ at the C-terminus but not in the GTP-binding region, they are predicted to be targeted to different cellular locations. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs Probab=99.50 E-value=2.2e-13 Score=102.73 Aligned_columns=158 Identities=20% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.|||||+.||+.. .+.+.||+++|| |-+...-....+-..++|..+|-.....+.+..+...+ .+ T Consensus 3 VvliGd~~VGKTSLi~rf~~~~F~~~y~~Tig~d~-~~k~i~i~~~~~v~l~iwDtaGqe~~~~~~~~y~~~a~----~~ 77 (215) T cd04109 3 IVVLGDGAVGKTSLCRRFAKEGFGKSYKQTIGLDF-FSKRVTLPGNLNVTLQVWDIGGQSIGGKMLDKYIYGAH----AV 77 (215) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEE-EEEEEEECCCCEEEEEEEECCCCCHHHHHHHHHHCCCC----EE T ss_conf 89982698538999988770721776465145678-78999975860589999864773023688998705998----48 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+ .=++.++.|++.+++.... ...++|++|||+|.|+ T Consensus 78 ilVYdIt~~-~SF~~i~~W~~~i~~~~~~----------------------------------~~~~~~iiLVGNK~DL- 121 (215) T cd04109 78 FLVYDVTNS-QSFENLEDWYSMVRKVLKS----------------------------------SETQPLVVLVGNKTDL- 121 (215) T ss_pred EEEEECCCH-HHHHHHHHHHHHHHHHHHC----------------------------------CCCCCEEEEECCCCCH- T ss_conf 999753897-6899999999999987310----------------------------------5898189996054240- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .+.|.+-..--+.+|-.+|+..+++|-+.. .++..+-.+++ T Consensus 122 ----~~~R~Vs~ee~~~~A~~~~~~f~EvSAktg--~nV~elF~~la 162 (215) T cd04109 122 ----EHNRTVKDDKHARFAQANGMESCLVSAKTG--DRVNLLFQQLA 162 (215) T ss_pred ----HHCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----120667989999999964995999962679--88889999999 No 12 >cd01865 Rab3 Rab3 subfamily. The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promot Probab=99.50 E-value=2.6e-13 Score=102.33 Aligned_columns=154 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||.||++. .+.+.||++.+|..-.-...+... -.++|..+|.-.+..+.....+.-. .+ T Consensus 4 iilvGd~~VGKTsli~rf~~~~f~~~y~~Ti~~~~~~k~i~~~~~~v--~l~iwDt~G~e~~~~~~~~~~~~~~----~~ 77 (165) T cd01865 4 LLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFRNDKRV--KLQIWDTAGQERYRTITTAYYRGAM----GF 77 (165) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCEEEEEEEEEEEECCEEE--EEEEEECCCCCHHHHHHHHHCCCCC----EE T ss_conf 99980799538998887644810666343036567899998779389--9999745887013456564336998----89 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ ..++.|++.+++.... .+|+++||+|.|+ T Consensus 78 iivfd~t~~~Sf-~~i~~w~~~i~~~~~~-------------------------------------~~~iilVGNK~Dl- 118 (165) T cd01865 78 ILMYDITNEESF-NAVQDWSTQIKTYSWD-------------------------------------NAQVILVGNKCDM- 118 (165) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CEEEEEEECCCCH- T ss_conf 999866986689-9999999999860699-------------------------------------6089997217772- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+-..-.+-+|-.+|...+.+|-+.. .++..+..+++ T Consensus 119 ----~~~r~v~~~~~~~~a~~~~~~y~EtSAk~~--~nV~e~F~~l~ 159 (165) T cd01865 119 ----EDERVVSSERGRQLADQLGFEFFEASAKEN--INVKQVFERLV 159 (165) T ss_pred ----HHHHHHHHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----465531388999999965994999971589--88789999999 No 13 >cd01869 Rab1_Ypt1 Rab1/Ypt1 subfamily. Rab1 is found in every eukaryote and is a key regulatory component for the transport of vesicles from the ER to the Golgi apparatus. Studies on mutations of Ypt1, the yeast homolog of Rab1, showed that this protein is necessary for the budding of vesicles of the ER as well as for their transport to, and fusion with, the Golgi apparatus. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to t Probab=99.50 E-value=1.3e-13 Score=104.16 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.|.||||||.||+.. .+.+.||++-+|..-.-...+... -.++|..+|......|.+.-+. ..-.+ T Consensus 5 iv~vGd~~vGKTsli~r~~~~~f~~~y~~Tig~~~~~k~i~~~~~~v--~l~iwDt~G~e~~~~l~~~~~~----~a~~~ 78 (166) T cd01869 5 LLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTI--KLQIWDTAGQERFRTITSSYYR----GAHGI 78 (166) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEECCEEE--EEEEEECCCCHHHHHHHHHHCC----CCCEE T ss_conf 99982699548999998753800666576012356788999989589--9998626886011231121226----89889 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||+|++...++=. +..|++.+++.... .+|.+|||+|+|+ T Consensus 79 iivfdit~~~Sf~~-i~~w~~~i~~~~~~-------------------------------------~~~~ilVGNK~Dl- 119 (166) T cd01869 79 IIVYDVTDQESFNN-VKQWLQEIDRYASE-------------------------------------NVNKLLVGNKCDL- 119 (166) T ss_pred EEEEECCCHHHHHH-HHHHHHHHHHHCCC-------------------------------------CCEEEEEEECCCC- T ss_conf 99986798568999-99999999872599-------------------------------------8279998503333- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+-..--+-+|-.+|+..+.+|-+.. ..+..+...++ T Consensus 120 ----~~~r~V~~~~~~~~a~~~~~~~~E~Sak~g--~~V~e~F~~la 160 (166) T cd01869 120 ----TDKRVVDYSEAQEFADELGIPFLETSAKNA--TNVEQAFMTMA 160 (166) T ss_pred ----CCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----324557989999999965995999971489--88789999999 No 14 >cd04107 Rab32_Rab38 Rab38/Rab32 subfamily. Rab32 and Rab38 are members of the Rab family of small GTPases. Human Rab32 was first identified in platelets but it is expressed in a variety of cell types, where it functions as an A-kinase anchoring protein (AKAP). Rab38 has been shown to be melanocyte-specific. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Probab=99.49 E-value=3.6e-13 Score=101.45 Aligned_columns=181 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.||||||.||+.. .+.+.||++.||..-.-...++..= -.++|..+|--.+..|...-.+... .+ T Consensus 3 IvliGd~~VGKTsli~r~~~~~F~~~~~~Tig~d~~~k~i~~~~~~~v-~l~iwDtaGqe~f~~l~~~y~r~a~----~~ 77 (201) T cd04107 3 VLVIGDLGVGKTSIIKRYVHGIFSQHYKATIGVDFALKVIEWDPNTVV-RLQLWDIAGQERFGGMTRVYYRGAV----GA 77 (201) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEECCCEEE-EEEEECCCCCHHHHHHHHHHCCCCC----EE T ss_conf 899816995489999997718006765650344677889987697689-9986227884245566565427987----69 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..|++.+++.+. .-..-++|++|||+|+|+ T Consensus 78 ilvyDit~~~SF-~~i~~W~~~i~~~~~---------------------------------~~~~~~ipiilVGNK~DL- 122 (201) T cd04107 78 IIVFDVTRPSTF-EAVLKWKADLDSKVT---------------------------------LPNGEPIPCLLLANKCDL- 122 (201) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHHH---------------------------------CCCCCCCEEEEEECCCCC- T ss_conf 999873897789-999999999998740---------------------------------368997289997058873- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHH--HHHHHHHHHCCCCCCCEEEEECCCCEEEE Q ss_conf 5887667899999999999860946888-5120345678--99988875057777730575067757870 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLK--IRGVINQLAFGIDKSKSICVDQNKPLFIT 258 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r--~r~~inhl~FG~~~~k~~~~D~~kPl~I~ 258 (351) .+.|.+...-..-.|-.+|..-+| +|-....... |..++.+..=+....+...+..+.++... T Consensus 123 ----~~~~~v~~~e~~~~a~~~~~~~~fEtSAktg~nV~e~F~~l~~~i~~~~~~~~~~~~~~~~~~~~~ 188 (201) T cd04107 123 ----KKRLAKDGEQMDQFCKENGFIGWFETSAKEGINIEEAMRFLVKNILANDKNLQQAETPEDGSVIDL 188 (201) T ss_pred ----HHHCCCCHHHHHHHHHHCCCCCEEEEECCCCCCHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCC T ss_conf ----000447989999999963998268875048978789999999999974112466566656721132 No 15 >cd01866 Rab2 Rab2 subfamily. Rab2 is localized on cis-Golgi membranes and interacts with Golgi matrix proteins. Rab2 is also implicated in the maturation of vesicular tubular clusters (VTCs), which are microtubule-associated intermediates in transport between the ER and Golgi apparatus. In plants, Rab2 regulates vesicle trafficking between the ER and the Golgi bodies and is important to pollen tube growth. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key featur Probab=99.49 E-value=3e-13 Score=101.88 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.|.||||||.||+.. .+...||++.||.--.-...+... -.++|..+|.-.+..|...-+...+ .+ T Consensus 7 ivliGd~~VGKTsli~r~~~~~f~~~~~~Ti~~~~~~k~i~~~~~~v--~l~iwDt~G~e~~~~l~~~~~~~a~----~~ 80 (168) T cd01866 7 YIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQI--KLQIWDTAGQESFRSITRSYYRGAA----GA 80 (168) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEECCCCCCEE--EEEEEECCCCCCHHHHHHHHCCCCC----EE T ss_conf 99981698438999999854825754453000000123214678428--9998753888411245365347997----79 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.++.|++.++.+... .+|+++||+|.|+ T Consensus 81 iivfdvt~~~Sf-~~i~~w~~~~~~~~~~-------------------------------------~~piilVGnK~DL- 121 (168) T cd01866 81 LLVYDITRRETF-NHLTSWLEDARQHSNS-------------------------------------NMTIMLIGNKCDL- 121 (168) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEECCHHH- T ss_conf 999766997789-9999999999973699-------------------------------------9689998332012- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) ..+|.+.-.-.+.+|-.+|+..+-+|-+.. .++..+-.+++ T Consensus 122 ----~~~r~v~~~e~~~~a~~~~~~~~E~SAkt~--~nV~~~F~~la 162 (168) T cd01866 122 ----ESRREVSYEEGEAFAKEHGLIFMETSAKTA--SNVEEAFINTA 162 (168) T ss_pred ----HHHCCCCHHHHHHHHHHCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf ----330477688999999965984999861579--88789999999 No 16 >cd04119 RJL RJL (RabJ-Like) subfamily. RJLs are found in many protists and as chimeras with C-terminal DNAJ domains in deuterostome metazoa. They are not found in plants, fungi, and protostome metazoa, suggesting a horizontal gene transfer between protists and deuterostome metazoa. RJLs lack any known membrane targeting signal and contain a degenerate phosphate/magnesium-binding 3 (PM3) motif, suggesting an impaired ability to hydrolyze GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Probab=99.49 E-value=2.1e-13 Score=102.84 Aligned_columns=159 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||+.||++. .+.+.||++.+|..-.-...+... ..++|..+|.-.+..+....++.-+ .+ T Consensus 3 ivivGd~~vGKTsli~r~~~~~f~~~y~~Tig~~~~~k~i~~~~~~~--~l~iwDtaG~e~~~~~~~~~~~~a~----~~ 76 (168) T cd04119 3 VISMGNSGVGKSCIIKRYCEGRFVSKYLPTIGIDYGVKKVSVRNKEV--RVNFFDLSGHPEYLEVRNEFYKDTQ----GV 76 (168) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEECCEEE--EEEEEECCCCHHHHHHHHHHHCCCC----EE T ss_conf 89980798548999988771801665365035555567888879489--9998606898125788788723999----38 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|.|+++++++=. +.+|++.++++... .-..-.+|+++||+|+|+ T Consensus 77 ilvydit~~~Sf~~-i~~w~~~~~~~~~~--------------------------------~~~~~~~~iilvGNK~Dl- 122 (168) T cd04119 77 LLVYDVTDRQSFEA-LDSWLKEMKQEGGP--------------------------------HGNMENIVVVVCANKIDL- 122 (168) T ss_pred EEEEECCCHHHHHH-HHHHHHHHHHHCCC--------------------------------CCCCCCCEEEEEECCCCC- T ss_conf 99985699778999-99999999986055--------------------------------566687479997053233- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +++|.+-..--+-+|..+|+..+.+|-+.. ..+..+.+.++ T Consensus 123 ----~~~r~V~~~~~~~~a~~~~~~~~E~SAk~~--~nV~e~F~~l~ 163 (168) T cd04119 123 ----TKHRAVSEDEGRLWAESKGFKYFETSACTG--EGVNEMFQTLF 163 (168) T ss_pred ----CCCCCCCHHHHHHHHHHCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf ----235767989999999964991999971589--78789999999 No 17 >cd01868 Rab11_like Rab11-like. Rab11a, Rab11b, and Rab25 are closely related, evolutionary conserved Rab proteins that are differentially expressed. Rab11a is ubiquitously synthesized, Rab11b is enriched in brain and heart and Rab25 is only found in epithelia. Rab11/25 proteins seem to regulate recycling pathways from endosomes to the plasma membrane and to the trans-Golgi network. Furthermore, Rab11a is thought to function in the histamine-induced fusion of tubulovesicles containing H+, K+ ATPase with the plasma membrane in gastric parietal cells and in insulin-stimulated insertion of GLUT4 in the plasma membrane of cardiomyocytes. Overexpression of Rab25 has recently been observed in ovarian cancer and breast cancer, and has been correlated with worsened outcomes in both diseases. In addition, Rab25 overexpression has also been observed in prostate cancer, transitional cell carcinoma of the bladder, and invasive breast tumor cells. GTPase activating proteins (GAPs) interact with GTP Probab=99.49 E-value=2.5e-13 Score=102.37 Aligned_columns=154 Identities=23% Q ss_pred EEEEECCCCCHHHHHHHHCCCC--CCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 8998659886377777552766--78887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDRD--EPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r~--e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||.||+... +...||++.||. .+..--+..+=-.++|-.+|.-.+..+...-+...+ .+ T Consensus 6 i~~iG~~~VGKTsli~r~~~~~F~~~~~~Tig~~~~--~k~v~~~~~~~~l~iwDtaG~e~~~~~~~~~~~~a~----~~ 79 (165) T cd01868 6 IVLIGDSGVGKSNLLSRFTRNEFNLDSKSTIGVEFA--TRSIQIDGKTIKAQIWDTAGQERYRAITSAYYRGAV----GA 79 (165) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEE--EEEEEECCEEEEEEEECCCCCHHHHHHHHHHHCCCC----EE T ss_conf 999826996589999998638567455641001246--889864890899998538986124577676504886----79 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|.|++.+.++ +.++.|++.++.+... .+|++|||+|.|+ T Consensus 80 iivyDit~~~Sf-~~i~~w~~~i~~~~~~-------------------------------------~~piilVGNK~DL- 120 (165) T cd01868 80 LLVYDITKKQTF-ENVERWLKELRDHADS-------------------------------------NIVIMLVGNKSDL- 120 (165) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEECCCCH- T ss_conf 999746997789-9999999999983289-------------------------------------9379998216562- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+.-.-.+.+|-.+|+..+.+|-+.. ..+..+..+++ T Consensus 121 ----~~~r~v~~~e~~~~a~~~~~~~~e~Sak~g--~ni~~~F~~l~ 161 (165) T cd01868 121 ----RHLRAVPTEEAKAFAEKNGLSFIETSALDG--TNVEEAFKQLL 161 (165) T ss_pred ----HHCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----120377688999999965994999971479--88889999999 No 18 >cd04120 Rab12 Rab12 subfamily. Rab12 was first identified in canine cells, where it was localized to the Golgi complex. The specific function of Rab12 remains unknown, and inconsistent results about its cellular localization have been reported. More recent studies have identified Rab12 associated with post-Golgi vesicles, or with other small vesicle-like structures but not with the Golgi complex. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic Probab=99.49 E-value=3.8e-13 Score=101.28 Aligned_columns=172 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.|||||++||.+. .+.+.||++.||.--.-.-.+... -.++|..+|--.+..|.+.-.+... .+ T Consensus 3 IvliGd~~VGKTsli~rf~~~~F~~~y~~Tig~df~~k~i~i~g~~i--~lqIwDTaGqE~f~~l~~~y~r~a~----g~ 76 (202) T cd04120 3 VIIIGSRGVGKTSLMRRFTDDTFCEACKSGVGVDFKIKTVELRGKKI--RLQIWDTAGQERFNSITSAYYRSAK----GI 76 (202) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEECCEEE--EEEEEECCCCCHHHHHHHHHHCCCC----EE T ss_conf 89980798428999999763811666565123578899999879189--9998756886035788777632898----79 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..|++.++++..+ .+|+++||+|.|+ T Consensus 77 ilVyDit~~~SF-~~l~~W~~~i~~~~~~-------------------------------------~~~iiLVGNK~DL- 117 (202) T cd04120 77 ILVYDITKKETF-DDLPKWMKMIDKYASE-------------------------------------DAELLLVGNKLDC- 117 (202) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CEEEEEEECCCCH- T ss_conf 999766984578-9999999999972499-------------------------------------3489997122212- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEE-EE------CHHHHHHHHHHHHHHHHCCCCCC-CEEEEECCCC Q ss_conf 5887667899999999999860946888-51------20345678999888750577777-3057506775 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMF-TS------KSEALLLKIRGVINQLAFGIDKS-KSICVDQNKP 254 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tS------k~e~l~~r~r~~inhl~FG~~~~-k~~~~D~~kP 254 (351) ..+|.+-..--+-+|..+++..+| +| -.|.+..-+|.++.+........ ..-.++..+| T Consensus 118 ----~~~R~Vs~~e~~~~A~~~~~~~f~EtSAk~~~NV~e~F~~l~~~i~~~~~~~~~~~~~~~~~~~~~~ 184 (202) T cd04120 118 ----ETDREISRQQGEKFAQQITGMRFCEASAKDNFNVDEIFLKLVDDILKKMPLDILRNELSNSILSLQP 184 (202) T ss_pred ----HHHCCCCHHHHHHHHHHHCCCEEEEEECCCCCCHHHHHHHHHHHHHHHCCCCCCCCCCCCCEEECCC T ss_conf ----1020236799999999708970899851489888899999999999734310035666872110587 No 19 >cd04114 Rab30 Rab30 subfamily. Rab30 appears to be associated with the Golgi stack. It is expressed in a wide variety of tissue types and in humans maps to chromosome 11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Probab=99.48 E-value=2.6e-13 Score=102.29 Aligned_columns=154 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||.||+.. .+...||.+.+|.--...-++... -.++|..+|......|.....+... .+ T Consensus 10 ivliGd~~VGKTsli~rf~~~~f~~~~~~Ti~~~~~~k~~~~~~~~v--~l~iwDtaG~e~~~~~~~~~~~~a~----~~ 83 (169) T cd04114 10 IVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEIKGEKI--KLQIWDTAGQERFRSITQSYYRSAN----AL 83 (169) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEECCEEE--EEEEEECCCCHHHHHHHHHHHCCCC----EE T ss_conf 99982698448999999862867854331122114788998889599--9999865898024677687604888----38 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..|++.++++... .+|++|||+|.|+ T Consensus 84 iivydit~~~Sf-~~i~~w~~~i~~~~~~-------------------------------------~~~iilVGNK~Dl- 124 (169) T cd04114 84 ILTYDITCEESF-RCLPEWLREIEQYANN-------------------------------------KVITILVGNKIDL- 124 (169) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHHCC-------------------------------------CCEEEEEECCCCC- T ss_conf 999655984688-9999999999874069-------------------------------------9418998114321- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+--.-.+-+|..+|...+-+|-+.. ..+..+..+++ T Consensus 125 ----~~~r~v~~~~~~~~a~~~~~~~~e~SAktg--~nV~~~F~~la 165 (169) T cd04114 125 ----AERREVSQQRAEEFSDAQDMYYLETSAKES--DNVEKLFLDLA 165 (169) T ss_pred ----CCCCCCCHHHHHHHHHHCCCEEEEEEECCC--CCHHHHHHHHH T ss_conf ----102365878999999964983999970379--88889999999 No 20 >cd04122 Rab14 Rab14 subfamily. Rab14 GTPases are localized to biosynthetic compartments, including the rough ER, the Golgi complex, and the trans-Golgi network, and to endosomal compartments, including early endosomal vacuoles and associated vesicles. Rab14 is believed to function in both the biosynthetic and recycling pathways between the Golgi and endosomal compartments. Rab14 has also been identified on GLUT4 vesicles, and has been suggested to help regulate GLUT4 translocation. In addition, Rab14 is believed to play a role in the regulation of phagocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GT Probab=99.48 E-value=3.2e-13 Score=101.75 Aligned_columns=153 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEE-EEEEECCCCCHHHCEEEEECCCCCCEEE Q ss_conf 899865988637777755276--6788875310002211101578711178-8897157854202110000423512067 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIA-HFWELGGGTSLLDLISIPITGDTLRTFS 110 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~Kdva-H~WELGgg~~ls~Li~ipit~~~l~~~~ 110 (351) |+++|+.|.||||||.||++. .+...||++.+| ....-....+++- ++|..+|-..+..+...-++..+. T Consensus 5 ivviGd~~VGKTsli~r~~~~~f~~~~~~Ti~~~~---~~k~i~~~~~~v~l~i~Dt~G~e~~~~~~~~~~~~a~~---- 77 (166) T cd04122 5 YIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEF---GTRIIEVNGQKIKLQIWDTAGQERFRAVTRSYYRGAAG---- 77 (166) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEE---EEEEEEECCEEEEEEEEECCCCHHHHHHHHHHCCCCCE---- T ss_conf 99982699558999988763843644562102214---67888528908999986358860234553864269875---- Q ss_pred EEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 78887369846899999999999999999999998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 111 LVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 111 viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) ++||.|++.+.++ ..++.|++.++++... .+|+++||+|+|+ T Consensus 78 ~ilvydit~~~Sf-~~i~~w~~~~~~~~~~-------------------------------------~~~iilVGNK~DL 119 (166) T cd04122 78 ALMVYDITRRSTY-NHLSSWLTDARNLTNP-------------------------------------NTVIFLIGNKADL 119 (166) T ss_pred EEEEEECCCHHHH-HHHHHHHHHHHHCCCC-------------------------------------CCEEEEECCHHHH T ss_conf 9998207998789-9999999999740489-------------------------------------9579996372544 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 158876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 191 FQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 191 F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+--.-..-+|..+|+..+.+|-++. .++..+-.+++ T Consensus 120 -----~~~r~v~~~e~~~~a~~~~~~~~E~SAk~~--~nV~e~F~~l~ 160 (166) T cd04122 120 -----EAQRDVTYEEAKQFADENGLLFLECSAKTG--ENVEDAFLETA 160 (166) T ss_pred -----HHHCCCCHHHHHHHHHHCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf -----430354178999999964991999971589--88789999999 No 21 >cd04112 Rab26 Rab26 subfamily. First identified in rat pancreatic acinar cells, Rab26 is believed to play a role in recruiting mature granules to the plasma membrane upon beta-adrenergic stimulation. Rab26 belongs to the Rab functional group III, which are considered key regulators of intracellular vesicle transport during exocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Probab=99.48 E-value=2.3e-13 Score=102.63 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC---CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEE Q ss_conf 899865988637777755276---67888753100022111015787111788897157854202110000423512067 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR---DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFS 110 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r---~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~ 110 (351) |++||+.+.||||||.||+.. .+.+.||++.+|..-.-...+... -.++|..+|.-.+..|...-++.-. . T Consensus 3 Iv~iGd~~VGKTsli~r~~~~~f~~~~~~~Tig~~~~~k~i~~~~~~i--~l~iwDtaGqe~~~~l~~~yy~~a~----~ 76 (191) T cd04112 3 VMLLGDSGVGKTCLLVRFKDGAFLNGNFIATVGIDFRNKVVTVDGVKV--KLQIWDTAGQERFRSVTHAYYRDAH----A 76 (191) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEECCEEE--EEEEEECCCCHHHHHHHHHHHCCCC----E T ss_conf 899826995489999887628225876342111003677898879389--9998755887012455366613897----7 Q ss_pred EEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 78887369846899999999999999999999998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 111 LVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 111 viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) ++||.|++.+.+ ++.+..|++.++++..+ .+|++|||+|.|+ T Consensus 77 ~iivyDit~~~S-f~~i~~w~~~i~~~~~~-------------------------------------~~~ivlVGNK~DL 118 (191) T cd04112 77 LLLLYDITNKAS-FDNIRAWLTEIKEYAQE-------------------------------------DVVIMLLGNKADM 118 (191) T ss_pred EEEEEECCCHHH-HHHHHHHHHHHHHHCCC-------------------------------------CCEEEEEEECCCC T ss_conf 999987799789-99999999988852699-------------------------------------9489998632776 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 158876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 191 FQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 191 F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+-..-.+.+|-.+|+..+.||-+++ ..+-.+...++ T Consensus 119 -----~~~r~V~~~e~~~~a~~~~~~~~EtSAk~~--~nI~e~F~~l~ 159 (191) T cd04112 119 -----SGERVVKREDGERLAKEYGVPFMETSAKTG--LNVELAFTAVA 159 (191) T ss_pred -----CCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf -----322553889999999966995999962589--88889999999 No 22 >cd04124 RabL2 RabL2 subfamily. RabL2 (Rab-like2) subfamily. RabL2s are novel Rab proteins identified recently which display features that are distinct from other Rabs, and have been termed Rab-like. RabL2 contains RabL2a and RabL2b, two very similar Rab proteins that share 98% sequence identity in humans. RabL2b maps to the subtelomeric region of chromosome 22q13.3 and RabL2a maps to 2q13, a region that suggests it is also a subtelomeric gene. Both genes are believed to be expressed ubiquitously, suggesting that RabL2s are the first example of duplicated genes in human proximal subtelomeric regions that are both expressed actively. Like other Rab-like proteins, RabL2s lack a prenylation site at the C-terminus. The specific functions of RabL2a and RabL2b remain unknown. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-b Probab=99.48 E-value=5.6e-13 Score=100.22 Aligned_columns=152 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |.++|+.+.|||||++||+.. ++.+.||.++++ |-+....+...= ..++|..+|.-.+..+.+.-++..+ .+ T Consensus 3 iiliGd~~VGKTsli~r~~~~~f~~~~~~t~~~~~-~~k~~~~~~~~v-~l~iwDt~G~e~~~~~~~~~~~~a~----~~ 76 (161) T cd04124 3 IILLGDSAVGKSKLVERFLMDGYEPQQLSTYALTL-YKHNAKFEGKTI-LVDFWDTAGQERFQTMHASYYHKAH----AC 76 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEE-EEEEEEECCEEE-EEEEEECCCCCHHHHHHHHHCCCCC----EE T ss_conf 89980699448898878653863766235325678-999999988699-9999745784110356674302478----58 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..|++.++++..+ +|+++||+|.|+ T Consensus 77 ilvfDit~~~Sf-~~l~~W~~~i~~~~~~--------------------------------------~p~ilVGNK~Dl- 116 (161) T cd04124 77 ILVFDVTRKITY-KNLSKWYEELREYRPE--------------------------------------IPCIVVANKIDL- 116 (161) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCC- T ss_conf 999866996688-9999999999984699--------------------------------------379998237656- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHH--HHHHHHHHH Q ss_conf 58876678999999999998609468885120345678--999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLK--IRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r--~r~~inhl~ 238 (351) +++ +..--+-+|..+++..+.+|-+...... +..++...+ T Consensus 117 ---~~~----~~~~~~~~a~~~~~~~fetSAk~g~nV~e~F~~~~~~~i 158 (161) T cd04124 117 ---DPS----VTQKKFNFAEKHNLPLYYVSAADGTNVVKLFQDAIKLAV 158 (161) T ss_pred ---CHH----HHHHHHHHHHHCCCCEEEEECCCCCCHHHHHHHHHHHHH T ss_conf ---435----689999999965991999972689887899999999998 No 23 >cd04125 RabA_like RabA-like subfamily. RabA was first identified in D. discoideum, where its expression levels were compared to other Rabs in growing and developing cells. The RabA mRNA levels were below the level of detection by Northern blot analysis, suggesting a very low level of expression. The function of RabA remains unknown. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Probab=99.47 E-value=2.8e-13 Score=102.13 Aligned_columns=154 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||.||+.. .+.+.||++.||..-.-...+... -.++|..+|...+..|...-+.. .-.+ T Consensus 3 IvviGd~~VGKTsli~r~~~~~f~~~~~~Tig~d~~~k~i~~~~~~v--~l~iwDtaGqe~~~~l~~~~~~~----a~~~ 76 (188) T cd04125 3 VVIIGDYGVGKSSLLKRFTEDEFSESTKSTIGVDFKIKTVYIENKII--KLQIWDTNGQERFRSLNNSYYRG----AHGY 76 (188) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEECCEEE--EEEEEECCCCCHHHHHHHHHHCC----CCEE T ss_conf 89982699548999998762801776467302125788999868499--99987569982025676876308----9859 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.++.|+..+++...+ .+|++|||+|+|+. T Consensus 77 ilvyDit~~~Sf-~~i~~w~~~i~~~~~~-------------------------------------~~~~ilvgNK~DL~ 118 (188) T cd04125 77 LLVYDVTDQESF-ENLKFWINEINRYARE-------------------------------------NVIKVIVANKSDLV 118 (188) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEEECCCCH T ss_conf 999866997899-9999999999861699-------------------------------------96899985135230 Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +.|.+--.-.+.+|..+|+..+.+|-... ..+..+...++ T Consensus 119 -----~~r~V~~~~~~~~a~~~~~~~fEtSAktg--~nV~e~F~~l~ 158 (188) T cd04125 119 -----NNKVVDSNIAKSFCDSLNIPFFETSAKQS--INVEEAFILLV 158 (188) T ss_pred -----HHCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf -----12336999999999856992999962589--88889999999 No 24 >cd01861 Rab6 Rab6 subfamily. Rab6 is involved in microtubule-dependent transport pathways through the Golgi and from endosomes to the Golgi. Rab6A of mammals is implicated in retrograde transport through the Golgi stack, and is also required for a slow, COPI-independent, retrograde transport pathway from the Golgi to the endoplasmic reticulum (ER). This pathway may allow Golgi residents to be recycled through the ER for scrutiny by ER quality-control systems. Yeast Ypt6p, the homolog of the mammalian Rab6 GTPase, is not essential for cell viability. Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde transport, and possibly also in Golgi-to-ER trafficking. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Probab=99.47 E-value=2.3e-13 Score=102.66 Aligned_columns=154 Identities=23% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.||||||.||+.. .+.+.||++.+|.--.....+... -..+|..+|.-.+..|...-++..+ .+ T Consensus 3 I~~iG~~~vGKTsli~r~~~~~f~~~~~~Tig~~~~~k~i~~~~~~v--~l~i~Dt~G~e~~~~l~~~~~~~~~----~~ 76 (161) T cd01861 3 LVFLGDQSVGKTSIITRFMYDTFDNQYQATIGIDFLSKTMYLEDKTV--RLQLWDTAGQERFRSLIPSYIRDSS----VA 76 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEECCEEE--EEEEECCCCCHHHHHHHHHHCCCCC----CE T ss_conf 89981798558999998863812665574343368888998879399--9998517884257788898603888----17 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|.|++.+.++ +.+..|++.+++.... .+|++|||+|+|+ T Consensus 77 ilvyd~t~~~Sf-~~~~~w~~~i~~~~~~-------------------------------------~~~iilVgNK~Dl- 117 (161) T cd01861 77 VVVYDITNRQSF-DNTDKWIDDVRDERGN-------------------------------------DVIIVLVGNKTDL- 117 (161) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEECCCCH- T ss_conf 999853987689-9999999888862399-------------------------------------9789997155332- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+--.-.+.+|-.+|+..+-+|-+.. ..+..+...++ T Consensus 118 ----~~~~~v~~~~~~~~a~~~~~~~~E~Sak~~--~nV~e~F~~ia 158 (161) T cd01861 118 ----SDKRQVSTEEGEKKAKELNAMFIETSAKAG--HNVKELFRKIA 158 (161) T ss_pred ----HHCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----121367688999999965993999971489--78789999999 No 25 >cd04117 Rab15 Rab15 subfamily. Rab15 colocalizes with the transferrin receptor in early endosome compartments, but not with late endosomal markers. It codistributes with Rab4 and Rab5 on early/sorting endosomes, and with Rab11 on pericentriolar recycling endosomes. It is believed to function as an inhibitory GTPase that regulates distinct steps in early endocytic trafficking. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to Probab=99.47 E-value=6.7e-13 Score=99.73 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.|||||+.||++. .+.+.||++.||..-.-...+... -.++|..+|.-.+..|.+......+ .+ T Consensus 3 IiliGd~~VGKTsli~rf~~~~F~~~~~~Tig~~~~~k~i~~~~~~i--~l~iwDtaG~e~~~~l~~~~~~~a~----~~ 76 (161) T cd04117 3 LLLIGDSGVGKTCLLCRFTDNEFHSSHISTIGVDFKMKTIEVDGIKV--RIQIWDTAGQERYQTITKQYYRRAQ----GI 76 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEEEEEEEEECCEEE--EEEEEECCCCHHHHHHHHHHCCCCC----EE T ss_conf 89982698448999998754821754344221114678998989699--9998746987235667686446998----89 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++++.++ +.+..|++.+++...+ .+|+++||+|.| T Consensus 77 ilvydit~~~Sf-~~i~~w~~~i~~~~~~-------------------------------------~~~~ilVgnK~D-- 116 (161) T cd04117 77 FLVYDISSERSY-QHIMKWVSDVDEYAPE-------------------------------------GVQKILIGNKAD-- 116 (161) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEECCCC-- T ss_conf 999865997899-9999999999972579-------------------------------------946999811578-- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) ..++|.+...-.+.+|-.+|+..+.+|-+.+ ..+..+..+++ T Consensus 117 ---l~~~r~v~~~e~~~~a~~~~~~~~E~SAk~~--~nV~e~F~~la 158 (161) T cd04117 117 ---EEQKRQVGDEQGNKLAKEYGMDFFETSACTN--SNIKESFTRLT 158 (161) T ss_pred ---HHHHHHHHHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ---0231114689999999965996999971589--88789999999 No 26 >pfam00071 Ras Ras family. Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices. Probab=99.47 E-value=3.3e-13 Score=101.63 Aligned_columns=154 Identities=23% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|+||||||.|++.. .+...||++.++.--.-.-.+... -..+|..+|......+....+.. .-++ T Consensus 2 i~viG~~~vGKTsli~r~~~~~f~~~~~~Ti~~~~~~k~v~~~~~~~--~l~i~Dt~g~e~~~~~~~~~~~~----ad~~ 75 (162) T pfam00071 2 LVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIGVDFYTKTIEVDGKTV--KLQIWDTAGQERFRSLRPAYYRG----AQGF 75 (162) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEECCEEE--EEEEEECCCCCHHHHHHHHHCCC----CCEE T ss_conf 78881799668999999863832765442010157899998736799--99998669980135675865048----9889 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|+|++...++ +.++.|++.+++...+ ++|++|||+|.|+ T Consensus 76 ilvfd~~~~~Sf-~~i~~w~~~i~~~~~~-------------------------------------~~piilvgnK~Dl- 116 (162) T pfam00071 76 LLVYDITSRDSF-ENVKKWLEEILRHADE-------------------------------------NVPIVLVGNKCDL- 116 (162) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEEECCHH- T ss_conf 999877997899-9999999999984599-------------------------------------9489998504201- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +++|.+...-.+-+|-.+++..+.+|-+.. ..+..+...++ T Consensus 117 ----~~~~~i~~~e~~~~~~~~~~~y~e~Sak~g--~gI~e~F~~l~ 157 (162) T pfam00071 117 ----EDQRVVSTEEGEALAKELGLPFMETSAKTN--TNVEEAFEELA 157 (162) T ss_pred ----HHHCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----121167688999999964995999971479--88889999999 No 27 >cd04118 Rab24 Rab24 subfamily. Rab24 is distinct from other Rabs in several ways. It exists primarily in the GTP-bound state, having a low intrinsic GTPase activity; it is not efficiently geranyl-geranylated at the C-terminus; it does not form a detectable complex with Rab GDP-dissociation inhibitors (GDIs); and it has recently been shown to undergo tyrosine phosphorylation when overexpressed in vitro. The specific function of Rab24 still remains unknown. It is found in a transport route between ER-cis-Golgi and late endocytic compartments. It is putatively involved in an autophagic pathway, possibly directing misfolded proteins in the ER to degradative pathways. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilita Probab=99.47 E-value=1.7e-13 Score=103.39 Aligned_columns=157 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCC---CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEE Q ss_conf 899865988637777755276---67888753100022111015787111788897157854202110000423512067 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR---DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFS 110 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r---~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~ 110 (351) |++||+.+.|||||++||+.. ++.+.||++.+|.--+-..++... ..++|..+|--.+..|...-.+..+ . T Consensus 3 vvliGd~~VGKTsli~r~~~~~F~~~~y~~Tig~~f~~k~i~~~~~~v--~l~iwDtaGqe~~~~l~~~~yr~a~----~ 76 (193) T cd04118 3 VVMLGKESVGKTSLVERYVHHRFLVGPYQNTIGAAFVAKRMVVGERVV--TLGIWDTAGSERYEAMSRIYYRGAK----A 76 (193) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEECCCEEE--EEEEECCCCCHHHHHHHHHHHCCCC----E T ss_conf 899807983289998887527316887466133235888864387579--9998638875357898987612887----3 Q ss_pred EEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 78887369846899999999999999999999998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 111 LVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 111 viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) ++||.|++++.++ +.++.|++.+++..+. +|++|||+|.|+ T Consensus 77 ~ilvydit~~~SF-~~l~~w~~~i~~~~~~--------------------------------------~~iilVGNK~DL 117 (193) T cd04118 77 AIVCYDLTDSSSF-ERAKFWVKELQNLEEH--------------------------------------CKIYLCGTKSDL 117 (193) T ss_pred EEEEEECCCCHHH-HHHHHHHHHHHHCCCC--------------------------------------CEEEEEECCCCH T ss_conf 8999874881017-8999999998621899--------------------------------------789998414221 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 158876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 191 FQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 191 F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) -+. +...|.+--.-.+-+|-.+|+..+.+|-+.. ..+..+-..++ T Consensus 118 ~~~-~~~~r~V~~ee~~~~A~~~~~~~fEtSAktg--~nV~elF~~ia 162 (193) T cd04118 118 IEQ-DRSLRQVDFHDVQDFADEIKAQHFETSSKTG--QNVDELFQKVA 162 (193) T ss_pred HHC-CCCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf 120-6664446889999999966995999962589--88889999999 No 28 >cd01864 Rab19 Rab19 subfamily. Rab19 proteins are associated with Golgi stacks. Similarity analysis indicated that Rab41 is closely related to Rab19. However, the function of these Rabs is not yet chracterized. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Probab=99.46 E-value=3.5e-13 Score=101.46 Aligned_columns=154 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||.||+.. .+.+.||.+.+|+.-...-.+... ...+|..+|...+..|...-++.-. .+ T Consensus 6 ivivGd~~vGKTsli~rf~~~~F~~~~~~tig~~~~~k~i~~~~~~v--~l~iwDt~G~e~~~~l~~~~~~~~~----~~ 79 (165) T cd01864 6 IILIGDSNVGKTCVVQRFKSGTFSERQGNTIGVDFTMKTLEIEGKRV--KLQIWDTAGQERFRTITQSYYRSAN----GA 79 (165) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEECCEEE--EEEEEECCCCCHHHHHHHHHCCCCC----EE T ss_conf 99980799448999998762820776677112577899999889589--9999754887013577686426998----79 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=. +..|+..++.+... .+|+++||+|.|+ T Consensus 80 ilvydit~~~Sf~~-l~~w~~~i~~~~~~-------------------------------------~~~ivlVGNK~Dl- 120 (165) T cd01864 80 IIAYDITRRSSFES-VPHWIEEVEKYGAS-------------------------------------NVVLLLIGNKCDL- 120 (165) T ss_pred EEEEECCCHHHHHH-HHHHHHHHHHCCCC-------------------------------------CCEEEEEECCCCC- T ss_conf 99987599779999-99988889851698-------------------------------------9579997242110- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 5887667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) .++|.+.-.-.+-+|..+|+.-+| +|-++. ..+..+-.+++ T Consensus 121 ----~~~r~V~~~~~~~~a~~~~~~~~~E~SAk~~--~nv~e~F~~la 162 (165) T cd01864 121 ----EEQREVLFEEACTLAEKNGMLAVLETSAKES--QNVEEAFLLMA 162 (165) T ss_pred ----CCCCCCCHHHHHHHHHHCCCCEEEEEEECCC--CCHHHHHHHHH T ss_conf ----0035545789999999649948999740489--89889999999 No 29 >cd04175 Rap1 Rap1 subgroup. The Rap1 subgroup is part of the Rap subfamily of the Ras family. It can be further divided into the Rap1a and Rap1b isoforms. In humans, Rap1a and Rap1b share 95% sequence homology, but are products of two different genes located on chromosomes 1 and 12, respectively. Rap1a is sometimes called smg p21 or Krev1 in the older literature. Rap1 proteins are believed to perform different cellular functions, depending on the isoform, its subcellular localization, and the effector proteins it binds. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and the microsomal membrane of pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. High expression of Rap1 has been observed in the n Probab=99.46 E-value=7.8e-13 Score=99.30 Aligned_columns=154 Identities=20% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||.||+.. .+.+.||++-.| ++.---...+-...+|..+|.-.+..+.+.-.+. .-.+ T Consensus 4 ivlvGd~~VGKTsli~r~~~~~f~~~y~~Ti~~~~---~k~i~~~~~~~~l~iwDtaG~e~~~~~~~~~~~~----a~~~ 76 (164) T cd04175 4 LVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSY---RKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKN----GQGF 76 (164) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEE---EEEEEECCEEEEEEEEECCCCCHHHHHHHHHCCC----CCEE T ss_conf 89980798538999999862800665575312136---8999888948999987279982023576755058----9879 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..|+..+.+..+ .-.+|+++||+|.|+ T Consensus 77 ilvydit~~~Sf-~~i~~~~~~i~~~~~------------------------------------~~~ip~vlvGNK~DL- 118 (164) T cd04175 77 VLVYSITAQSTF-NDLQDLREQILRVKD------------------------------------TEDVPMILVGNKCDL- 118 (164) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCC------------------------------------CCCCEEEEEECCCCC- T ss_conf 999866997788-999999888886408------------------------------------998579998125653- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .+.|.+--.-...+|..+|+..+-+|-+.+ ..+..+...++ T Consensus 119 ----~~~r~V~~~~~~~~a~~~~~~~~E~Sak~~--~nV~e~F~~l~ 159 (164) T cd04175 119 ----EDERVVGKEQGQNLARQWGCAFLETSAKAK--INVNEIFYDLV 159 (164) T ss_pred ----CCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----000334078999999965993899971479--88789999999 No 30 >cd00157 Rho Rho (Ras homology) family. Members of the Rho family include RhoA, Cdc42, Rac, Rnd, Wrch1, RhoBTB, and Rop. There are 22 human Rho family members identified currently. These proteins are all involved in the reorganization of the actin cytoskeleton in response to external stimuli. They also have roles in cell transformation by Ras in cytokinesis, in focal adhesion formation and in the stimulation of stress-activated kinase. These various functions are controlled through distinct effector proteins and mediated through a GTP-binding/GTPase cycle involving three classes of regulating proteins: GAPs (GTPase-activating proteins), GEFs (guanine nucleotide exchange factors), and GDIs (guanine nucleotide dissociation inhibitors). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho protein Probab=99.45 E-value=4.1e-13 Score=101.06 Aligned_columns=158 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.|||||+.||... .+.+.||+.-.| ++.-......--.++|..+|...+..|...-++.-+. + T Consensus 3 i~liGd~~VGKTsli~r~~~~~f~~~~~~Ti~~~~---~~~i~~~~~~~~l~iwDt~G~e~~~~l~~~~~~~a~~----~ 75 (171) T cd00157 3 IVVVGDGAVGKTCLLISYTTGKFPTEYVPTVFDNY---SATVTVDGKQVNLGLWDTAGQEEYDRLRPLSYPNTDV----F 75 (171) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEE---EEEEEECCEEEEEEEEECCCCHHHHHHHHHHHCCCCE----E T ss_conf 89980799548999999863831665343265214---5578755679999996067743467898987328985----8 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=.-.++|++.++..... +|++|||+|.|+- T Consensus 76 ilvydit~~~Sf~~~~~~w~~~i~~~~~~--------------------------------------~piilVgnK~DL~ 117 (171) T cd00157 76 LICFSVDSPSSFENVKTKWIPEIRHYCPN--------------------------------------VPIILVGTKIDLR 117 (171) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 99971688658999999989999984689--------------------------------------5699985374421 Q ss_pred CCCC------HHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 5887------667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 192 QDFE------SEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D------~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) .+.. ..+|.+--.-.+-+|-.+|+..+| +|-+.. .++..+...++ T Consensus 118 ~~~~~~~~~~~~~r~Vs~~e~~~~a~~~~~~~f~EtSAktg--~nV~e~F~~l~ 169 (171) T cd00157 118 DDENTLKKLEKGKEPITPEEGEKLAKEIGAIGYMECSALTQ--EGVKEVFEEAI 169 (171) T ss_pred CCHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 21122322101357789899999999739952788750489--88789999996 No 31 >smart00174 RHO Rho (Ras homology) subfamily of Ras-like small GTPases; Members of this subfamily of Ras-like small GTPases include Cdc42 and Rac, as well as Rho isoforms. Probab=99.45 E-value=2.4e-13 Score=102.57 Aligned_columns=158 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.|.|||||+.||+.. .+.+.||..-.|+.--..++..- -.++|..+|.-.+..|.....+. .-.+ T Consensus 1 ivliGd~~VGKTsli~rf~~~~f~~~~~pTi~~~~~~~i~~~~~~v---~l~iwDtaGqe~~~~l~~~~y~~----a~~~ 73 (174) T smart00174 1 LVVVGDGAVGKTCLLISYTTNAFPEDYVPTVFENYSADVEVDGKPV---ELGLWDTAGQEDYDRLRPLSYPD----TDVF 73 (174) T ss_pred CEEECCCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCEEE---EEEECCCCCCCHHHHHHHHHHCC----CCEE T ss_conf 6787159833899999986182266625515432467555778679---99864666662235666876438----8368 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=.-.+.|++.++++... +|+++||+|.|+- T Consensus 74 ilvydit~~~Sf~~l~~~W~~~i~~~~~~--------------------------------------~piiLVGnK~DL~ 115 (174) T smart00174 74 LICFSVDSPASFENVKEKWYPEVKHFCPN--------------------------------------VPIILVGTKLDLR 115 (174) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 99986388657899999889999984789--------------------------------------6699971565632 Q ss_pred CCCC-------HHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 5887-------667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 192 QDFE-------SEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D-------~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) .+-. .+++.+-..-.+.+|..+|+-.+| ||-+.. ..+..+..+++ T Consensus 116 ~~~~~~~~~~~~~~~~vs~~e~~~~a~~~~~~~y~EtSAktg--~nV~e~F~~l~ 168 (174) T smart00174 116 NDEDTLEELSKKKQEPVTYEQGEALAKRIGAVKYIECSALTQ--EGVREVFEEAI 168 (174) T ss_pred CHHHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 013455554310135688889999999718941688750488--78789999999 No 32 >cd04132 Rho4_like Rho4-like subfamily. Rho4 is a GTPase that controls septum degradation by regulating secretion of Eng1 or Agn1 during cytokinesis. Rho4 also plays a role in cell morphogenesis. Rho4 regulates septation and cell morphology by controlling the actin cytoskeleton and cytoplasmic microtubules. The localization of Rho4 is modulated by Rdi1, which may function as a GDI, and by Rga9, which is believed to function as a GAP. In S. pombe, both Rho4 deletion and Rho4 overexpression result in a defective cell wall, suggesting a role for Rho4 in maintaining cell wall integrity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Probab=99.43 E-value=4.7e-13 Score=100.68 Aligned_columns=160 Identities=19% Q ss_pred CEEEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 45899865988637777755276--6788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 32 KFVFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 32 k~v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) |-|+++|+.+.|||||++||... .+.+.||++-+|..-.....+... -.++|..+|.-.+..|...-.+ ..- T Consensus 1 ~KVvliGd~~VGKTsli~r~~~~~F~~~~~~Ti~~~~~~~~~~~~~~~v--~l~iwDtaGqe~f~~l~~~~~~----~a~ 74 (187) T cd04132 1 KKIVVVGDGGCGKTCLLIVYSQGKFPEEYVPTVFENYVTNIQGPNGKII--ELALWDTAGQEEYDRLRPLSYP----DVD 74 (187) T ss_pred CEEEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCCEEE--EEEEECCCCCHHHHHHHHHHHC----CCC T ss_conf 9689981798328999988761822676465157678999997388189--9986148775245778887724----897 Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .++||.|++.|.++=.-.+.|+..+++.... +|++|||+|.| T Consensus 75 ~~ilvyDit~~~Sf~~~~~~W~~~i~~~~~~--------------------------------------~piilVGNK~D 116 (187) T cd04132 75 VLLICYAVDNPTSLDNVEDKWFPEVNHFCPG--------------------------------------TPIMLVGLKTD 116 (187) T ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCC T ss_conf 5899986599789999998778999984589--------------------------------------77999841675 Q ss_pred CCCCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 015887667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 190 VFQDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 190 ~F~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) +..+ ....|.+--.-.+.+|-..|+..+| +|-+.. ..+-.+...++ T Consensus 117 L~~~-~~~~r~V~~~e~~~~a~~~~~~~y~EtSAk~g--~nV~e~F~~l~ 163 (187) T cd04132 117 LRKD-KNLDRKVTPAQAESVAKKQGAFAYLECSAKTM--ENVEEVFDTAI 163 (187) T ss_pred CHHH-HCCCCCCCHHHHHHHHHHCCCCEEEEEEECCC--CCHHHHHHHHH T ss_conf 1223-11136789889999999738932689861278--88789999999 No 33 >cd04116 Rab9 Rab9 subfamily. Rab9 is found in late endosomes, together with mannose 6-phosphate receptors (MPRs) and the tail-interacting protein of 47 kD (TIP47). Rab9 is a key mediator of vesicular transport from late endosomes to the trans-Golgi network (TGN) by redirecting the MPRs. Rab9 has been identified as a key component for the replication of several viruses, including HIV1, Ebola, Marburg, and measles, making it a potential target for inhibiting a variety of viruses. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CX Probab=99.43 E-value=2.5e-12 Score=96.13 Aligned_columns=157 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.||||||.||+.. ++.+.||++.+|..-.....+... -.++|..+|.-.+..|....++..+ .+ T Consensus 8 ivliGd~~vGKTsLi~rf~~~~f~~~~~~tig~~~~~k~i~~~~~~~--~l~i~Dtag~e~~~~l~~~~~~~~~----~~ 81 (170) T cd04116 8 VILLGDGGVGKSSLMNRYVTNKFDTQLFHTIGVEFLNKDLEVDGHFV--TLQIWDTAGQERFRSLRTPFYRGSD----CC 81 (170) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCEEECCEEEECCCCCCEE--EEEEECCCCCCHHHHHHHHHHCCCC----EE T ss_conf 99980799548999988753811777347323110220000479648--9998707898101231157631898----48 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|+++++++=. +..|++.+.++.+ .-.+-.+|++|||+|.|+ T Consensus 82 iivydit~~~Sf~~-i~~w~~e~~~~~~---------------------------------~~~~~~ipiilVGNK~DL- 126 (170) T cd04116 82 LLTFAVDDSQSFQN-LSNWKKEFIYYAD---------------------------------VKEPESFPFVVLGNKNDI- 126 (170) T ss_pred EEEEECCCHHHHHH-HHHHHHHHHHHCC---------------------------------CCCCCCCEEEEEECCCCC- T ss_conf 99985499768999-9999999998603---------------------------------577897079998354220- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 5887667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) +.|.+...-.+.+|..+|...+| +|-+.+ .++..+-..++ T Consensus 127 -----~~r~V~~~e~~~~~~~~~~~~~~E~SAk~g--~nv~~~F~~l~ 167 (170) T cd04116 127 -----PERQVSTEEAQAWCRENGDYPYFETSAKDA--TNVAAAFEEAV 167 (170) T ss_pred -----HHHCCHHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf -----111011789999999707971789860489--88789999998 No 34 >cd04108 Rab36_Rab34 Rab34/Rab36 subfamily. Rab34, found primarily in the Golgi, interacts with its effector, Rab-interacting lysosomal protein (RILP). This enables its participation in microtubular dynenin-dynactin-mediated repositioning of lysosomes from the cell periphery to the Golgi. A Rab34 (Rah) isoform that lacks the consensus GTP-binding region has been identified in mice. This isoform is associated with membrane ruffles and promotes macropinosome formation. Rab36 has been mapped to human chromosome 22q11.2, a region that is homozygously deleted in malignant rhabdoid tumors (MRTs). However, experimental assessments do not implicate Rab36 as a tumor suppressor that would enable tumor formation through a loss-of-function mechanism. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further re Probab=99.43 E-value=1.2e-12 Score=98.05 Aligned_columns=157 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.|||||+.||... .+.+.||++.+|.--+....+... -.++|..+|--.+..+.+.-....+. + T Consensus 3 ivliGd~~VGKTsli~rf~~~~f~~~y~~Tig~d~~~k~~~~~~~~i--~l~iwDtaG~e~~~~~~~~~~~~a~~----~ 76 (170) T cd04108 3 VIVVGDLSVGKTCLINRFCKDVFDKNYKATIGVDFEMERFEILGVPF--SLQLWDTAGQERFKCIASTYYRGAQA----I 76 (170) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEECCEEE--EEEEEECCCCHHHHHHHHHHCCCCCE----E T ss_conf 89981698548998888762822786244256678899875188379--99985368860245666754048880----8 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||+|+++++++ +.+..|++.+.+... |-.+|+++||+|+|+. T Consensus 77 ilvyDit~~~Sf-~~~~~w~~~~~~~~~------------------------------------~~~~~i~LVGnK~DL~ 119 (170) T cd04108 77 IIVFDLTDVASL-EHTRQWLEDALKEND------------------------------------PSSVLLFLVGTKKDLS 119 (170) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHHC------------------------------------CCCCEEEEEECCCCCC T ss_conf 999754986578-999999999987407------------------------------------9996899983560104 Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +..++..+-+--+-+|..+|+..+.+|-+.. .++..+-.+++ T Consensus 120 ---~~~~~~~~~~~~~~~a~~~~~~~fEtSAktg--~nV~e~F~~ia 161 (170) T cd04108 120 ---SPAQYALMEQDAIKLAAEMQAEYWSVSALSG--ENVREFFFRVA 161 (170) T ss_pred ---CCCCCEECHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ---5311200378999999965995999972588--78789999999 No 35 >cd01862 Rab7 Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C- Probab=99.43 E-value=1.5e-12 Score=97.57 Aligned_columns=160 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.||||||.||+.. .+.+.||++.+|.--.-.-.+... ..++|..+|.-.+..|...-++. .-.+ T Consensus 3 ivliGd~~vGKTsli~r~~~~~f~~~y~~Tig~~~~~k~i~~~~~~~--~l~i~Dt~G~e~~~~l~~~~~~~----a~~~ 76 (172) T cd01862 3 VIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVTVDDKLV--TLQIWDTAGQERFQSLGVAFYRG----ADCC 76 (172) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEECCEEE--EEEEEECCCCCCHHHHHHHHHCC----CCEE T ss_conf 89981798448999999862810665355200157788999988799--99998668993003577887238----9679 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.++++=.- ..|++.+..+.. .-.+-.+|++|||+|.|+ T Consensus 77 ilvydit~~~Sf~~i-~~w~~e~~~~~~---------------------------------~~~~~~iP~ilVGnK~Dl- 121 (172) T cd01862 77 VLVYDVTNPKSFESL-DSWRDEFLIQAS---------------------------------PSDPENFPFVVLGNKIDL- 121 (172) T ss_pred EEEEECCCHHHHHHH-HHHHHHHHHHCC---------------------------------CCCCCCCEEEEECCCCCH- T ss_conf 999856985578999-999999998638---------------------------------777886079997141000- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHH--HHHHHHHHH Q ss_conf 5887667899999999999860946888-5120345678--999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLK--IRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r--~r~~inhl~ 238 (351) .++|.+--.-.+-+|-.+|...+| +|-+...... |..++..+. T Consensus 122 ----~~~r~v~~~e~~~~a~~~~~~~~~e~SAk~~~nV~e~F~~l~~~~~ 167 (172) T cd01862 122 ----EEKRQVSTKKAQQWCQSNGNIPYFETSAKEAINVEQAFETIARKAL 167 (172) T ss_pred ----HHHCCCCHHHHHHHHHHHCCCEEEEEEECCCCCHHHHHHHHHHHHH T ss_conf ----1211531789999999707960799860489787899999999999 No 36 >cd01863 Rab18 Rab18 subfamily. Mammalian Rab18 is implicated in endocytic transport and is expressed most highly in polarized epithelial cells. However, trypanosomal Rab, TbRAB18, is upregulated in the BSF (Blood Stream Form) stage and localized predominantly to elements of the Golgi complex. In human and mouse cells, Rab18 has been identified in lipid droplets, organelles that store neutral lipids. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of mos Probab=99.43 E-value=1.6e-12 Score=97.37 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.||||||.||+.. .+.+.||++.||. .+.-.-+..+=-..+|..+|--.+..|.+...+.-+ .+ T Consensus 3 iv~iG~~~VGKTsli~r~~~~~f~~~~~~Ti~~~~~--~k~i~~~~~~~~l~iwDt~G~e~~~~l~~~~~~~~~----~~ 76 (161) T cd01863 3 ILLIGDSGVGKSSLLLRFTDDTFDPDLAATIGVDFK--VKTLTVDGKKVKLAIWDTAGQERFRTLTSSYYRGAQ----GV 76 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEE--EEEEEECCEEEEEEEEECCCCCHHHHHHHHHCCCCC----EE T ss_conf 899807996589999998628207765651000245--889989896999999754887101245475435998----79 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|.|++.+.++=. +..|++.++.+... -.+|++|||+|+|. T Consensus 77 i~vfd~t~~~Sf~~-i~~w~~~i~~~~~~------------------------------------~~~~~ilvGNK~Dl- 118 (161) T cd01863 77 ILVYDVTRRDTFTN-LETWLNELETYSTN------------------------------------NDIVKMLVGNKIDK- 118 (161) T ss_pred EEEEECCCHHHHHH-HHHHHHHHHHHCCC------------------------------------CCCEEEEECCCCCC- T ss_conf 99985698679999-99999999973389------------------------------------99389996123343- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +.|.+...-.+-+|-.+|+..+.+|-+.. ..+..+..+++ T Consensus 119 -----~~r~v~~~e~~~~a~~~~~~~~e~SAk~~--~nv~e~F~~l~ 158 (161) T cd01863 119 -----ENREVTREEGLKFARKHNMLFIETSAKTR--DGVQQAFEELV 158 (161) T ss_pred -----CCCCCCHHHHHHHHHHCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf -----00048888999999966992999970589--78789999999 No 37 >cd04176 Rap2 Rap2 subgroup. The Rap2 subgroup is part of the Rap subfamily of the Ras family. It consists of Rap2a, Rap2b, and Rap2c. Both isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK) are putative effectors of Rap2 in mediating the activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton. In human platelets, Rap2 was shown to interact with the cytoskeleton by binding the actin filaments. In embryonic Xenopus development, Rap2 is necessary for the Wnt/beta-catenin signaling pathway. The Rap2 interacting protein 9 (RPIP9) is highly expressed in human breast carcinomas and correlates with a poor prognosis, suggesting a role for Rap2 in breast cancer oncogenesis. Rap2b, but not Rap2a, Rap2c, Rap1a, or Rap1b, is expressed in human red blood cells, where it is believed to be involved in vesiculation. A number of additional effector proteins for Rap2 have been identified, incl Probab=99.42 E-value=1.6e-12 Score=97.43 Aligned_columns=154 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||+||+.. .+.+.||++ |+.--+-...+... ..++|..+|...+..|...-++.. -.+ T Consensus 4 IvvvGd~~VGKTsli~rf~~~~f~~~y~~Ti~-~~~~k~i~~~~~~~--~l~i~Dt~G~e~~~~~~~~~~~~a----~~~ 76 (163) T cd04176 4 VVVLGSGGVGKSALTVQFVSGTFIEKYDPTIE-DFYRKEIEVDSSPS--VLEILDTAGTEQFASMRDLYIKNG----QGF 76 (163) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCCC-CEEEEEEEECCEEE--EEEEEECCCCCHHHHHHHHHCCCC----CEE T ss_conf 89970798548999988763800776563100-00478998889689--999874688712456777425799----869 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.+ ++.++.|++.+.+... +-++|++|||+|.|+ T Consensus 77 ilvydi~~~~S-f~~i~~~~~~i~~~~~------------------------------------~~~~piilvGnK~Dl- 118 (163) T cd04176 77 IVVYSLVNQQT-FQDIKPMRDQIVRVKG------------------------------------YEKVPIILVGNKVDL- 118 (163) T ss_pred EEEEECCCHHH-HHHHHHHHHHHHHHCC------------------------------------CCCCEEEEEECCCCH- T ss_conf 99976699768-8999998765675318------------------------------------998289997332001- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) ...|++--.-...+|-.+|+..+.+|-+.+ .++..+...++ T Consensus 119 ----~~~r~V~~~e~~~~a~~~~~~y~E~SAk~~--~nV~e~F~~l~ 159 (163) T cd04176 119 ----ESEREVSSAEGRALAEEWGCPFMETSAKSK--TMVNELFAEIV 159 (163) T ss_pred ----HHHCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----111024637899999963995899970479--88789999999 No 38 >cd04113 Rab4 Rab4 subfamily. Rab4 has been implicated in numerous functions within the cell. It helps regulate endocytosis through the sorting, recycling, and degradation of early endosomes. Mammalian Rab4 is involved in the regulation of many surface proteins including G-protein-coupled receptors, transferrin receptor, integrins, and surfactant protein A. Experimental data implicate Rab4 in regulation of the recycling of internalized receptors back to the plasma membrane. It is also believed to influence receptor-mediated antigen processing in B-lymphocytes, in calcium-dependent exocytosis in platelets, in alpha-amylase secretion in pancreatic cells, and in insulin-induced translocation of Glut4 from internal vesicles to the cell surface. Rab4 is known to share effector proteins with Rab5 and Rab11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to p Probab=99.42 E-value=1.4e-12 Score=97.66 Aligned_columns=154 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.||||||.||+.. .+.+.||++.+|.--.-.-.+... ...+|-.+|-.....|...-....+ .+ T Consensus 3 iviiGd~~VGKTsli~~~~~~~f~~~~~~Tig~~~~~~~i~~~~~~~--~l~i~Dt~G~e~~~~l~~~~~~~a~----~~ 76 (161) T cd04113 3 FIIIGSSGTGKSCLLHRFVENKFKEDSQHTIGVEFGSKIIRVGGKRV--KLQIWDTAGQERFRSVTRSYYRGAA----GA 76 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCCEEEEEEEECCEEE--EEEEEECCCCCHHHHHHHHHCCCCC----EE T ss_conf 89982698558999999862810666564101201358998889699--9998325887013455586426997----79 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|.|++.+.++ +.++.|++.+|..... .+|++|||+|.|+ T Consensus 77 iivydi~~~~Sf-~~i~~w~~~~~~~~~~-------------------------------------~~~iilvgNK~DL- 117 (161) T cd04113 77 LLVYDITNRTSF-EALPTWLSDARALASP-------------------------------------NIVVILVGNKSDL- 117 (161) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEECCCCC- T ss_conf 999855986689-9999999999872489-------------------------------------9689998324564- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+--.-.+-+|-.+|...+.+|-++. ..+..+-.+++ T Consensus 118 ----~~~r~v~~~e~~~~a~~~~~~~~e~Sak~~--~ni~e~F~~la 158 (161) T cd04113 118 ----ADQREVTFLEASRFAQENGLLFLETSALTG--ENVEEAFLKCA 158 (161) T ss_pred ----CCCCCCCHHHHHHHHHHCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf ----213345889999999965990999971589--88889999999 No 39 >smart00175 RAB Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking. Probab=99.41 E-value=1.2e-12 Score=98.15 Aligned_columns=154 Identities=23% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||+.||+.. .+.+.||++.||..-...-.+... ...+|..+|...+..|....++.-+. + T Consensus 3 iviiG~~~vGKTsii~~~~~~~f~~~~~~Ti~~~~~~k~v~~~~~~~--~l~i~Dt~g~e~~~~~~~~~~~~~d~----~ 76 (164) T smart00175 3 IILIGDSGVGKSSLLSRFTDGKFSEDSKSTIGVDFKTKTIEVDGKRV--KLQIWDTAGQERFRSITSSYYRGAVG----A 76 (164) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEECCEEE--EEEEEECCCCHHHHHHHHHHHCCCCE----E T ss_conf 89982699648999999862810665565022367789999989699--99986469871467777875048976----9 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|+|++.+.++ +.++.|++.++.+... .+|++|||+|.|. T Consensus 77 iivfdi~~~~Sf-~~i~~w~~~i~~~~~~-------------------------------------~~piilvgNK~Dl- 117 (164) T smart00175 77 LLVYDITNRDSF-ENLENWLKELREYADP-------------------------------------NVVIMLVGNKSDL- 117 (164) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEEECCCC- T ss_conf 999327987799-9999999999972699-------------------------------------9589998511022- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) ..+|.+--.-.+.+|-.+|+..+-+|-+.. ..+..+..+++ T Consensus 118 ----~~~~~i~~~e~~~~a~~~~~~y~E~Sak~~--~~i~e~F~~l~ 158 (164) T smart00175 118 ----EEQRQVSTEEAQKFAEEHGLLFIETSAKTN--TNVEEAFEELA 158 (164) T ss_pred ----CCCCCCCHHHHHHHHHHCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf ----000258989999999964982999970479--88789999999 No 40 >cd04141 Rit_Rin_Ric Rit/Rin/Ric subfamily. Rit (Ras-like protein in all tissues), Rin (Ras-like protein in neurons) and Ric (Ras-related protein which interacts with calmodulin) form a subfamily with several unique structural and functional characteristics. These proteins all lack a the C-terminal CaaX lipid-binding motif typical of Ras family proteins, and Rin and Ric contain calmodulin-binding domains. Rin, which is expressed only in neurons, induces neurite outgrowth in rat pheochromocytoma cells through its association with calmodulin and its activation of endogenous Rac/cdc42. Rit, which is ubiquitously expressed in mammals, inhibits growth-factor withdrawl-mediated apoptosis and induces neurite extension in pheochromocytoma cells. Rit and Rin are both able to form a ternary complex with PAR6, a cell polarity-regulating protein, and Rac/cdc42. This ternary complex is proposed to have physiological function in processes such as tumorigenesis. Activated Ric is likely to sign Probab=99.41 E-value=2e-12 Score=96.71 Aligned_columns=154 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCCC--CCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 8998659886377777552766--78887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDRD--EPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r~--e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.||||||+||+... +.+.||++-.|+---..++..- .+.+|..+|--.+..|.+.-.+... .+ T Consensus 5 i~liGd~~VGKTsli~rf~~~~F~~~y~pTi~~~~~~~i~~~~~~v---~l~iwDtaGqe~~~~l~~~~~~~a~----~~ 77 (172) T cd04141 5 IVMLGAGGVGKSAVTMQFISHSFPDYHDPTIEDAYKQQARIDNEPA---LLDILDTAGQAEFTAMRDQYMRCGE----GF 77 (172) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCEEEEEEEEEECCEEE---EEEEECCCCCHHHHHHHHHHCCCCC----EE T ss_conf 9997079843899999987282277656630000478998979589---9986227762135567687514997----38 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..| -+.+.+..... .+|++|||+|.|+ T Consensus 78 ilVyditd~~Sf-~~i~~w--------~~~i~~~~~~~----------------------------~~pivlvgNK~DL- 119 (172) T cd04141 78 IICYSVTDRHSF-QEASEF--------KKLITRVRLTE----------------------------DIPLVLVGNKVDL- 119 (172) T ss_pred EEEEECCCHHHH-HHHHHH--------HHHHHHHCCCC----------------------------CCEEEEEECCCHH- T ss_conf 998542897689-999999--------99999740799----------------------------9779998156016- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .+.|.+.-.--+.+|-.+|+..+-+|-+.+ .++..+...++ T Consensus 120 ----~~~r~V~~~e~~~~a~~~~~~f~EtSAk~~--~nV~~~F~~l~ 160 (172) T cd04141 120 ----ESQRQVTTEEGRNLAREFNCPFFETSAALR--HYIDDAFHGLV 160 (172) T ss_pred ----HHCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----541566778999999965996999970589--88789999999 No 41 >cd04136 Rap_like Rap-like subfamily. The Rap subfamily consists of the Rap1, Rap2, and RSR1. Rap subfamily proteins perform different cellular functions, depending on the isoform and its subcellular localization. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and microsomal membrane of the pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. Rap1 localizes in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Probab=99.40 E-value=2.2e-12 Score=96.53 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.||||||+||+.. .+.+.||++-.| .+.---....-..++|..+|.-.+..|.+.-++. .-.+ T Consensus 4 iilvGd~~VGKTsli~r~~~~~f~~~~~~ti~~~~---~k~i~v~~~~~~l~iwDtaG~e~~~~l~~~~~~~----a~~~ 76 (163) T cd04136 4 VVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSY---RKQIEVDGQQCMLEILDTAGTEQFTAMRDLYIKN----GQGF 76 (163) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCCCCCE---EEEEEECCEEEEEEEEECCCCHHHHHHHHHHHCC----CCEE T ss_conf 89970798438999998862800676565100012---6889888968999988479980356888875116----8828 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..|++.+.+..+. -++|++|||+|.|+ T Consensus 77 ilvfdvt~~~Sf-~~i~~~~~~i~~~~~~------------------------------------~~ip~ilVGNK~DL- 118 (163) T cd04136 77 VLVYSITSQSSF-NDLQDLREQILRVKDT------------------------------------ENVPMVLVGNKCDL- 118 (163) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC------------------------------------CCCEEEEECCCCCC- T ss_conf 999756997888-9999999999974089------------------------------------99389997244676- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .+.|.+.-.-...+|..+|+..+.+|-+.+ .++..+...++ T Consensus 119 ----~~~r~v~~~~~~~~a~~~~~~~~E~Sak~~--~nv~e~F~~l~ 159 (163) T cd04136 119 ----EDERVVSREEGQALARQWGCPFYETSAKSK--INVDEVFADLV 159 (163) T ss_pred ----CCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----465637989999999966995999971479--78789999999 No 42 >cd04123 Rab21 Rab21 subfamily. The localization and function of Rab21 are not clearly defined, with conflicting data reported. Rab21 has been reported to localize in the ER in human intestinal epithelial cells, with partial colocalization with alpha-glucosidase, a late endosomal/lysosomal marker. More recently, Rab21 was shown to colocalize with and affect the morphology of early endosomes. In Dictyostelium, GTP-bound Rab21, together with two novel LIM domain proteins, LimF and ChLim, has been shown to regulate phagocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site Probab=99.39 E-value=2.8e-12 Score=95.85 Aligned_columns=154 Identities=25% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.++||||||.||+.. .+.+.||++.+|..-.-...+... -.++|..+|...+..+...-++. .-.+ T Consensus 3 i~~iGd~~vGKTsli~r~~~~~f~~~~~~ti~~~~~~k~i~~~~~~~--~l~iwDt~G~~~~~~~~~~~~~~----a~~~ 76 (162) T cd04123 3 VVLLGEGRVGKTSLVLRYVENKFNEKHESTTQASFFQKTVNIGGKRI--DLAIWDTAGQERYHALGPIYYRD----ADGA 76 (162) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCCCEEEEEECCCCEE--EEEEEECCCCHHHHHHHHHHHCC----CCEE T ss_conf 89982699658999999862811776454112441355331599389--99973078750235665766148----9868 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|.|++. .+=++.+..|++.+++...+ .+|++|||+|.|+ T Consensus 77 ilvydit~-~~Sf~~i~~w~~~i~~~~~~-------------------------------------~~piilVGNK~Dl- 117 (162) T cd04123 77 ILVYDITD-ADSFQKVKKWIKELKQMRGN-------------------------------------NISLVIVGNKIDL- 117 (162) T ss_pred EEEEECCC-HHHHHHHHHHHHHHHHHCCC-------------------------------------CCEEEEEEEHHHH- T ss_conf 99942798-77899999999989973189-------------------------------------9659998400231- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +++|.+-..-.+.+|-.+|+..+.+|-+.. ..+..+...++ T Consensus 118 ----~~~r~V~~~~~~~~a~~~~~~~~E~Sak~~--~nv~e~F~~l~ 158 (162) T cd04123 118 ----ERQRVVSKSEAEEYAKSVGAKHFETSAKTG--KGIEELFLSLA 158 (162) T ss_pred ----HHHCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----210254778999999964993899971589--78789999999 No 43 >cd04140 ARHI_like ARHI subfamily. ARHI (A Ras homolog member I) is a member of the Ras family with several unique structural and functional properties. ARHI is expressed in normal human ovarian and breast tissue, but its expression is decreased or eliminated in breast and ovarian cancer. ARHI contains an N-terminal extension of 34 residues (human) that is required to retain its tumor suppressive activity. Unlike most other Ras family members, ARHI is maintained in the constitutively active (GTP-bound) state in resting cells and has modest GTPase activity. ARHI inhibits STAT3 (signal transducers and activators of transcription 3), a latent transcription factor whose abnormal activation plays a critical role in oncogenesis. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to Probab=99.39 E-value=3.8e-12 Score=94.98 Aligned_columns=157 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||.||+.. .+.+.||++-.| ++...-+...=-.++|..+|.-.+..|....+...+ .+ T Consensus 4 IvliGd~~VGKTsli~r~~~~~F~~~y~~ti~~~~---~~~i~~~~~~~~l~i~Dt~G~e~~~~l~~~~~~~a~----~~ 76 (165) T cd04140 4 VVVFGAGGVGKSSLVLRFVKGTFRESYIPTIEDTY---RQVISCSKNICTLQITDTTGSHQFPAMQRLSISKGH----AF 76 (165) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEECEE---EEEEEECCCEEEEEEECCCCCCCHHHHHHHHHCCCC----EE T ss_conf 89980799658999988762820665454200115---778863694899997037763102356688621898----58 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..|+..+++.... .+-.+|+++||+|.| T Consensus 77 ilvydit~~~Sf-~~i~~~~~~i~~~~~~----------------------------------~~~~ipiilvGNK~D-- 119 (165) T cd04140 77 ILVYSVTSKQSL-EELKPIYELICEIKGN----------------------------------NIEKIPIMLVGNKCD-- 119 (165) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHHCC----------------------------------CCCCCEEEEEECCCC-- T ss_conf 999875997788-9999999999986224----------------------------------889857999503114-- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHH--HHHHHHHH Q ss_conf 58876678999999999998609468885120345678--99988875 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLK--IRGVINQL 237 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r--~r~~inhl 237 (351) ....|.+--.-.+.+|-.+|+..+.+|-+...... ++.++|-+ T Consensus 120 ---l~~~r~V~~~e~~~~a~~~~~~~~E~SAk~~~nv~~~F~~l~~l~ 164 (165) T cd04140 120 ---ESHKREVSSNEGAACATEWNCAFMETSAKTNHNVQELFQELLNLE 164 (165) T ss_pred ---CCCCCCCCHHHHHHHHHHCCCCEEEEECCCCCCHHHHHHHHHHHC T ss_conf ---010466898999999995699589997148988789999999851 No 44 >cd04152 Arl4_Arl7 Arl4/Arl7 subfamily. Arl4 (Arf-like 4) is highly expressed in testicular germ cells, and is found in the nucleus and nucleolus. In mice, Arl4 is developmentally expressed during embryogenesis, and a role in somite formation and central nervous system differentiation has been proposed. Arl7 has been identified as the only Arf/Arl protein to be induced by agonists of liver X-receptor and retinoid X-receptor and by cholesterol loading in human macrophages. Arl7 is proposed to play a role in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily. Probab=99.39 E-value=9.6e-12 Score=92.49 Aligned_columns=160 Identities=19% Q ss_pred EEEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEE-EEEEEECCCCCHHHCEEEEECCCCCCEEE Q ss_conf 58998659886377777552-76678887531000221110157871117-88897157854202110000423512067 Q Ver_Hs_NP_0570 33 FVFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDI-AHFWELGGGTSLLDLISIPITGDTLRTFS 110 (351) Q Consensus 33 ~v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~Kdv-aH~WELGgg~~ls~Li~ipit~~~l~~~~ 110 (351) .|+++|..++|||||++|+. +......||.+..+..-.-..+++ ++| .++|++||.-.+-.|...-.+. .-. T Consensus 5 kIvilG~~~~GKTsil~r~~~~~~~~~~pT~g~~~~~~~~~~~~~--~~v~l~iwD~aGqe~~r~l~~~yy~~----a~g 78 (183) T cd04152 5 HIVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEKIKVSLGNS--KGITFHFWDVGGQEKLRPLWKSYTRC----TDG 78 (183) T ss_pred EEEEEECCCCCHHHHHHHHHCCCCCCEECCEEEEEEEEEEEECCC--CEEEEEEEECCCCHHHHHHHHHHCCC----CCE T ss_conf 999985089868998887644821110022033478898750477--42799998648850256755311368----867 Q ss_pred EEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 78887369846899999999999999999999998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 111 LVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 111 viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) +|+|+|.|...++=...++| +++.+.....+ +|++|+|+|.|. T Consensus 79 iI~V~D~sd~~~~~~~~~~l--------~~i~~~~~~~~-----------------------------~piLi~~NK~Dl 121 (183) T cd04152 79 IVFVVDSVDVERMEEAKTEL--------HKITRFSENQG-----------------------------VPVLVLANKQDL 121 (183) T ss_pred EEEEEECCCHHHHHHHHHHH--------HHHHHCCCCCC-----------------------------CEEEEEECCCCC T ss_conf 99998537834689999999--------99971126789-----------------------------789999616787 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 158876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 191 FQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 191 F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) -.....+...-.. .|+-++..++..+.-+|-... ..+...+..|+ T Consensus 122 ~~~~~~~e~~~~~-~l~~~~~~~~~~~~~~SA~tG--~Gi~e~f~~L~ 166 (183) T cd04152 122 PNALSVSEVEKLL-ALHELSASTPWHVQPACAIIG--EGLQEGLEKLY 166 (183) T ss_pred CCCCCHHHHHHHH-HHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 6467889999998-889998518967987404678--78889999999 No 45 >cd04137 RheB Rheb (Ras Homolog Enriched in Brain) subfamily. Rheb was initially identified in rat brain, where its expression is elevated by seizures or by long-term potentiation. It is expressed ubiquitously, with elevated levels in muscle and brain. Rheb functions as an important mediator between the tuberous sclerosis complex proteins, TSC1 and TSC2, and the mammalian target of rapamycin (TOR) kinase to stimulate cell growth. TOR kinase regulates cell growth by controlling nutrient availability, growth factors, and the energy status of the cell. TSC1 and TSC2 form a dimeric complex that has tumor suppressor activity, and TSC2 is a GTPase activating protein (GAP) for Rheb. The TSC1/TSC2 complex inhibits the activation of TOR kinase through Rheb. Rheb has also been shown to induce the formation of large cytoplasmic vacuoles in a process that is dependent on the GTPase cycle of Rheb, but independent of the TOR kinase, suggesting Rheb plays a role in endocytic trafficking that le Probab=99.39 E-value=3.3e-12 Score=95.38 Aligned_columns=156 Identities=21% Q ss_pred CEEEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 45899865988637777755276--6788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 32 KFVFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 32 k~v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) +-|++||+.|.|||||+.||+.. .+.+.||++-+| .+..--+...=-..+|..+|--.+..|...-.+.-+ T Consensus 2 ~KIvliGd~~VGKTsli~rf~~~~f~~~y~~Ti~~~~---~k~i~v~~~~~~l~iwDtaGqe~~~~l~~~~~~~a~---- 74 (180) T cd04137 2 RKIAVLGSRSVGKSSLTVQFVEGHFVESYYPTIENTF---SKIIRYKGQDYHLEIVDTAGQDEYSILPQKYSIGIH---- 74 (180) T ss_pred EEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCEECCC---CCCEEECCEEEEEEECCCCCCCCCHHHHHHHCCCCC---- T ss_conf 0789970798438999999861800776466100031---200356682689987478873200023366504887---- Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .++||+|++.+.++ +.++.|++.+.+.... -.+|++|||+|.| T Consensus 75 ~~ilvfdit~~~Sf-~~i~~~~~~i~~~~~~------------------------------------~~ipiiLvGNK~D 117 (180) T cd04137 75 GYILVYSVTSRKSF-EVVKVIYDKILDMLGK------------------------------------ESVPIVLVGNKSD 117 (180) T ss_pred EEEEEEECCCHHHH-HHHHHHHHHHHHHHCC------------------------------------CCCEEEEEEECCC T ss_conf 38998544897678-9999999999986189------------------------------------9848999420168 Q ss_pred CCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 0158876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 190 VFQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 190 ~F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) + +..|.+--.-..-+|..+|+..+.+|-+.. ..+..+...++ T Consensus 118 l-----~~~r~V~~~e~~~~a~~~~~~~~E~SAk~~--~nV~e~F~~l~ 159 (180) T cd04137 118 L-----HTQRQVSTEEGKELAESWGAAFLESSAREN--ENVEEAFELLI 159 (180) T ss_pred C-----CCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf 5-----123657989999999965997899861579--88889999999 No 46 >cd04139 RalA_RalB RalA/RalB subfamily. The Ral (Ras-like) subfamily consists of the highly homologous RalA and RalB. Ral proteins are believed to play a crucial role in tumorigenesis, metastasis, endocytosis, and actin cytoskeleton dynamics. Despite their high sequence similarity (80% sequence identity), nonoverlapping and opposing functions have been assigned to RalA and RalBs in tumor migration. In human bladder and prostate cancer cells, RalB promotes migration while RalA inhibits it. A Ral-specific set of GEFs has been identified that are activated by Ras binding. This RalGEF activity is enhanced by Ras binding to another of its target proteins, phosphatidylinositol 3-kinase (PI3K). Ral effectors include RLIP76/RalBP1, a Rac/cdc42 GAP, and the exocyst (Sec6/8) complex, a heterooctomeric protein complex that is involved in tethering vesicles to specific sites on the plasma membrane prior to exocytosis. In rat kidney cells, RalB is required for functional assembly of the exo Probab=99.39 E-value=3.6e-12 Score=95.17 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.||||||.||+.. .+.+.||++..|+---.-++... -.++|..+|...+..|...-++... .+ T Consensus 3 ivliGd~~VGKTsli~r~~~~~f~~~~~~Ti~~~~~~~i~~~~~~v---~l~iwDt~Gqe~~~~l~~~~~~~a~----~~ 75 (164) T cd04139 3 VIVVGAGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEDV---QLNILDTAGQEDYAAIRDNYHRSGE----GF 75 (164) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEEEEEEEECCCEE---EEEEEECCCCHHHHHHHHHHCCCCC----EE T ss_conf 8998179854899999987182076544322321468998859389---9998427887135788887525898----79 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.+..|...+.++.+ +-.+|++|||+|.|+ T Consensus 76 ilvydit~~~Sf-~~i~~~~~~~~~~~~------------------------------------~~~ip~ilvGNK~Dl- 117 (164) T cd04139 76 LLVFSITDMESF-TATAEFREQILRVKD------------------------------------DDNVPLLLVGNKCDL- 117 (164) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHHC------------------------------------CCCCEEEEECCCHHH- T ss_conf 999752885578-899999999998617------------------------------------997279997240132- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+...-.+.+|..+|+..+.+|-+.. .++..+..+++ T Consensus 118 ----~~~r~v~~~e~~~~a~~~~~~~~E~SAk~g--~ni~e~F~~l~ 158 (164) T cd04139 118 ----EDKRQVSSEEAANLARQWGVPYVETSAKTR--QNVEKAFYDLV 158 (164) T ss_pred ----HHHCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----231167489999999965995999971589--88789999999 No 47 >cd04101 RabL4 RabL4 (Rab-like4) subfamily. RabL4s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL4 lacks a prenylation site at the C-terminus. The specific function of RabL4 remains unknown. Probab=99.39 E-value=2e-12 Score=96.78 Aligned_columns=154 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHCCC----CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 899865988637777755276----6788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR----DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r----~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) |++||+.|.|||||++||++. .+.+.||++.||..-.-. -++...--..+|..+|...+..+...-++ ..- T Consensus 3 vv~iGd~~VGKTsli~~~~~~~~~f~~~y~~T~~~~~~~~~~~-i~~~~~~~l~i~DtaGqe~~~~~~~~~~~----~a~ 77 (164) T cd04101 3 CAVVGDPAVGKTAFVQMFHSNGAVFPKNYLMTTGCDFVVKEVP-VDTDNTVELFIFDSAGQELYSDMVSNYWE----SPS 77 (164) T ss_pred EEEEECCCCCHHHHHHHHHHCCCEECCCCCCCEEEEEEEEEEE-ECCCCEEEEEEEECCCCHHHHHHHHHHCC----CCC T ss_conf 8998079821898888776168441666543112456799999-77996799999603872246788787424----997 Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .++||.|++.+.++ +.+..|+..++..-.. +|++|||+|+| T Consensus 78 ~~ilvydit~~~Sf-~~i~~w~~~i~~~~~~--------------------------------------~p~ilVGNK~D 118 (164) T cd04101 78 VFILVYDVSNKASF-ENCSRWVNKVRTASKH--------------------------------------MPGVLVGNKMD 118 (164) T ss_pred EEEEEEECCCHHHH-HHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCC T ss_conf 69999417997689-9999999999984499--------------------------------------73999821434 Q ss_pred CCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 0158876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 190 VFQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 190 ~F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) + .++|++--.--+.+|-.+|+..+.+|-++. .++..+...++ T Consensus 119 L-----~~~r~V~~~~~~~~a~~~~~~~~e~SAktg--~nV~e~F~~la 160 (164) T cd04101 119 L-----ADKAEVTDAQAQAFAQANQLKFFKTSALRG--VGYEEPFESLA 160 (164) T ss_pred C-----CCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf 0-----011678989999999963994999971689--88789999999 No 48 >cd04133 Rop_like Rop subfamily. The Rop (Rho-related protein from plants) subfamily plays a role in diverse cellular processes, including cytoskeletal organization, pollen and vegetative cell growth, hormone responses, stress responses, and pathogen resistance. Rops are able to regulate several downstream pathways to amplify a specific signal by acting as master switches early in the signaling cascade. They transmit a variety of extracellular and intracellular signals. Rops are involved in establishing cell polarity in root-hair development, root-hair elongation, pollen-tube growth, cell-shape formation, responses to hormones such as abscisic acid (ABA) and auxin, responses to abiotic stresses such as oxygen deprivation, and disease resistance and disease susceptibility. An individual Rop can have a unique function or an overlapping function shared with other Rop proteins; in addition, a given Rop-regulated function can be controlled by one or multiple Rop proteins. For example, Probab=99.38 E-value=1.6e-12 Score=97.41 Aligned_columns=158 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||+.||.+. .+.+.||++-+|+.--..+++.- ..++|.-+|.-.+..|...-++ ..-.+ T Consensus 4 iv~iGd~~VGKTsLi~rf~~~~F~~~~~pTi~~~~~~~i~~~~~~v---~l~IwDTaGqe~~~~l~~~~~r----~a~~~ 76 (176) T cd04133 4 CVTVGDGAVGKTCMLICYTSNKFPTDYIPTVFDNFSANVSVDGNTV---NLGLWDTAGQEDYNRLRPLSYR----GADVF 76 (176) T ss_pred EEEECCCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEECCEEE---EEEEEECCCCHHHHHHHHHHCC----CCCEE T ss_conf 9997179844899888875380168635335311136788889489---9998756887146788887411----44726 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++-.-++.|+..+++.... +|++|||+|.|+= T Consensus 77 ilvydvt~~~Sf~~~~~~w~~~~~~~~~~--------------------------------------~piiLVGNK~DL~ 118 (176) T cd04133 77 VLAFSLISRASYENVLKKWVPELRHYAPN--------------------------------------VPIVLVGTKLDLR 118 (176) T ss_pred EEEEECCCCHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCH T ss_conf 99974487220799999989999972799--------------------------------------4899970575511 Q ss_pred CCCC-----HHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 5887-----667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 192 QDFE-----SEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D-----~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) ++-. ++.+-+...--.-+|..+|+.++| +|-+.. .++..+-..++ T Consensus 119 ~~r~~~~~~~~~~~v~~~e~~~~a~~~~~~~y~EtSAktg--~nV~e~F~~~~ 169 (176) T cd04133 119 DDKQYLADHPGASPITTAQGEELRKQIGAAAYIECSSKTQ--QNVKAVFDAAI 169 (176) T ss_pred HHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 1245665301335436789999999639974899751378--78789999999 No 49 >cd01870 RhoA_like RhoA-like subfamily. The RhoA subfamily consists of RhoA, RhoB, and RhoC. RhoA promotes the formation of stress fibers and focal adhesions, regulating cell shape, attachment, and motility. RhoA can bind to multiple effector proteins, thereby triggering different downstream responses. In many cell types, RhoA mediates local assembly of the contractile ring, which is necessary for cytokinesis. RhoA is vital for muscle contraction; in vascular smooth muscle cells, RhoA plays a key role in cell contraction, differentiation, migration, and proliferation. RhoA activities appear to be elaborately regulated in a time- and space-dependent manner to control cytoskeletal changes. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. RhoA and RhoC are observed only in geranyl Probab=99.38 E-value=1.6e-12 Score=97.29 Aligned_columns=158 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.|||||+.||... .+.+.||+.-+|+.--..++... ..++|..+|--.+..|...-.+..+ .+ T Consensus 4 iiliGd~~VGKTsli~r~~~~~F~~~~~pTi~~~~~~~i~i~~~~v---~l~iwDtaGqe~~~~l~~~~~~~a~----~~ 76 (175) T cd01870 4 LVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQV---ELALWDTAGQEDYDRLRPLSYPDTD----VI 76 (175) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCEEE---EEEEECCCCHHHHHHHHHHHHCCCC----EE T ss_conf 8998269843899999986382366525402213689998989699---9987058620246677787504898----48 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=.-.++|+..+++.... +|+++||+|+|+- T Consensus 77 ilvydi~~~~Sf~~i~~~W~~~~~~~~~~--------------------------------------~piiLvgnK~DL~ 118 (175) T cd01870 77 LMCFSIDSPDSLENIPEKWTPEVKHFCPN--------------------------------------VPIILVGNKKDLR 118 (175) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 99976686557899999889999972589--------------------------------------5299985154433 Q ss_pred CCCC-------HHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 5887-------667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 192 QDFE-------SEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D-------~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) .+.. ..+|.+...--+-+|..+|+..+| +|-+.. ..+..+...++ T Consensus 119 ~~~~~~~~~~~~~~~~v~~~eg~~~a~~~~~~~y~E~SAktg--~nV~e~Fe~~~ 171 (175) T cd01870 119 NDEHTRRELAKMKQEPVKPEEGRDMANKIGAFGYMECSAKTK--EGVREVFEMAT 171 (175) T ss_pred CCHHHHHHHHHHCCCCCCHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 431467766541046779899999999739972898741488--88789999999 No 50 >cd04121 Rab40 Rab40 subfamily. This subfamily contains Rab40a, Rab40b, and Rab40c, which are all highly homologous. In rat, Rab40c is localized to the perinuclear recycling compartment (PRC), and is distributed in a tissue-specific manor, with high expression in brain, heart, kidney, and testis, low expression in lung and liver, and no expression in spleen and skeletal muscle. Rab40c is highly expressed in differentiated oligodendrocytes but minimally expressed in oligodendrocyte progenitors, suggesting a role in the vesicular transport of myelin components. Unlike most other Ras-superfamily proteins, Rab40c was shown to have a much lower affinity for GTP, and an affinity for GDP that is lower than for GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide d Probab=99.38 E-value=2.4e-12 Score=96.22 Aligned_columns=153 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHC--CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 8998659886377777552--76678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL--DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl--~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||+.||. .-.+.+.||++.+|..-.-...+... ..++|.-+|--.+..+...-.+. .-.+ T Consensus 9 IVliGd~~VGKTSLi~rf~~~~f~~~y~~TiG~d~~~k~i~vdg~~v--~L~IWDTAGqE~f~sl~~~y~r~----A~gv 82 (235) T cd04121 9 FLLVGDSDVGKGEILASLQDGSTESPYGYNMGIDYKTTTILLDGRRV--KLQLWDTSGQGRFCTIFRSYSRG----AQGI 82 (235) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEECCCEE--EEEEEECCCCCHHHCCCHHHHCC----CCCE T ss_conf 99981698447888776425810676343024467899998858289--99987466410011000233214----7717 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|+++.+++=. ++.|++.++++... +|+++||+|.|+ T Consensus 83 ILVYDIT~r~SF~~-i~~W~~ei~~~~~~--------------------------------------ipiILVGNK~DL- 122 (235) T cd04121 83 ILVYDITNRWSFDG-IDRWIKEIDEHAPG--------------------------------------VPKILVGNRLHL- 122 (235) T ss_pred EEEEECCCHHHHHH-HHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCH- T ss_conf 99987699778999-99999999863289--------------------------------------659997032240- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+-..--+.+|..+|+.-+-+|-+++ .++..+-++++ T Consensus 123 ----~~~R~Vs~eEg~~~A~~~~~~FfEtSAKtn--~NV~E~F~ela 163 (235) T cd04121 123 ----AFKRQVATEQAQAYAERNGMTFFEVSPLCN--FNITESFTELA 163 (235) T ss_pred ----HHCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----023777989999999966995999853689--98889999999 No 51 >cd04135 Tc10 TC10 subfamily. TC10 is a Rho family protein that has been shown to induce microspike formation and neurite outgrowth in vitro. Its expression changes dramatically after peripheral nerve injury, suggesting an important role in promoting axonal outgrowth and regeneration. TC10 regulates translocation of insulin-stimulated GLUT4 in adipocytes and has also been shown to bind directly to Golgi COPI coat proteins. GTP-bound TC10 in vitro can bind numerous potential effectors. Depending on its subcellular localization and distinct functional domains, TC10 can differentially regulate two types of filamentous actin in adipocytes. TC10 mRNAs are highly expressed in three types of mouse muscle tissues: leg skeletal muscle, cardiac muscle, and uterus; they were also present in brain, with higher levels in adults than in newborns. TC10 has also been shown to play a role in regulating the expression of cystic fibrosis transmembrane conductance regulator (CFTR) through interacti Probab=99.38 E-value=1.7e-12 Score=97.24 Aligned_columns=157 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.|||||+.||+.. .+.+.||+.-.|+---..++... ..++|.-+|.-.+..+.....+..+ .+ T Consensus 3 ivliGd~~VGKTsLi~~~~~~~F~~~~~~Ti~~~~~~~i~i~~~~~---~l~iwDtaGqe~~~~~~~~~~~~a~----~~ 75 (174) T cd04135 3 CVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQY---LLGLYDTAGQEDYDRLRPLSYPMTD----VF 75 (174) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEECCCCEEEECCEEE---EEEEECCCCCHHHHHHHHHHCCCCC----EE T ss_conf 8997079843899999876183167645514403320035688689---9987168887026778897548998----79 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC- Q ss_conf 8887369846899999999999999999999998526953789999999984146677600111068877997121000- Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV- 190 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~- 190 (351) +||.|++.+.++=.--+.|++.++++.+. +|+++||+|.|+ T Consensus 76 ilvydit~~~Sf~~i~~~w~~~~~~~~~~--------------------------------------~piilVGnK~DL~ 117 (174) T cd04135 76 LICFSVVNPASFQNVKEEWVPELKEYAPN--------------------------------------VPYLLVGTQIDLR 117 (174) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 99965586324899999989999861799--------------------------------------5489973563331 Q ss_pred ------CCCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHH Q ss_conf ------15887667899999999999860946888-512034567899988875 Q Ver_Hs_NP_0570 191 ------FQDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQL 237 (351) Q Consensus 191 ------F~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl 237 (351) =+-.+..+|.+-..--+-+|..+|+.++| +|-+.. ..+..+..++ T Consensus 118 ~~~~~~~~~~~~~~r~Vs~eeg~~~a~~~~~~~f~EtSAkt~--~~V~e~F~~~ 169 (174) T cd04135 118 DDPKTLARLNDMKEKPVTVEQGQKLAKEIGAHCYVECSALTQ--KGLKTVFDEA 169 (174) T ss_pred CCHHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHH T ss_conf 214677665420267789899999999808924688741467--7778999999 No 52 >cd04131 Rnd Rnd subfamily. The Rnd subfamily contains Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. These novel Rho family proteins have substantial structural differences compared to other Rho members, including N- and C-terminal extensions relative to other Rhos. Rnd3/RhoE is farnesylated at the C-terminal prenylation site, unlike most other Rho proteins that are geranylgeranylated. In addition, Rnd members are unable to hydrolyze GTP and are resistant to GAP activity. They are believed to exist only in the GTP-bound conformation, and are antagonists of RhoA activity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Probab=99.37 E-value=1.6e-12 Score=97.44 Aligned_columns=143 Identities=20% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||++||... .+.+.||++-.|+-.-..+++.- -.++|..+|.-.+..|...-.+ ..-.+ T Consensus 4 ivlvGd~~VGKTsli~r~~~~~F~~~~~~Ti~~~~~~~~~v~~~~v---~l~iWDTaGqe~f~~l~~~~y~----~a~~~ 76 (178) T cd04131 4 IVVVGDVQCGKTALLQVFAKDCYPETYVPTVFENYTASFEIDEQRI---ELSLWDTSGSPYYDNVRPLCYP----DSDAV 76 (178) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCEEE---EEEEEECCCCCHHHHHHHHHCC----CCCEE T ss_conf 8998269844899999975383376624136645789998868489---9998756888033557687627----99679 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||+|++.|.++=.-+..|+..++++... +|+++||+|.|+= T Consensus 77 ilvfdit~~~Sf~~v~~~W~~ei~~~~~~--------------------------------------~~iiLVGnK~DLr 118 (178) T cd04131 77 LICFDISRPETLDSVLKKWRGEIQEFCPN--------------------------------------TKVLLVGCKTDLR 118 (178) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 99975688557789999999999984598--------------------------------------5399960421221 Q ss_pred CCCC-------HHHHHHHHHHHHHHHHHCCCEEEE-EE Q ss_conf 5887-------667899999999999860946888-51 Q Ver_Hs_NP_0570 192 QDFE-------SEKRKVICKTLRFVAHYYGASLMF-TS 221 (351) Q Consensus 192 ~~~D-------~e~rK~i~r~LR~iAH~yGA~L~F-tS 221 (351) .+.. ..++.+-.--=.-+|..+||.++| +| T Consensus 119 ~~~~~~~~l~~~~~~~Vs~eeg~~~A~~~~a~~y~E~S 156 (178) T cd04131 119 TDLSTLMELSHQRQAPVSYEQGCAIAKQLGAEIYLECS 156 (178) T ss_pred CCHHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEE T ss_conf 21567888763578778989999999982992577530 No 53 >cd04143 Rhes_like Rhes_like subfamily. This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression l Probab=99.36 E-value=2.1e-11 Score=90.33 Aligned_columns=182 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.|||||++||+.. .+.+.||++ .|.++.-.-....--.++|.-+|--.+..|...-+...+ .+ T Consensus 3 IVllGd~~VGKTSLi~Rf~~~~F~e~y~pTI~---df~~K~i~idg~~v~L~IwDTAGqE~f~sl~~~~~~~ad----~~ 75 (247) T cd04143 3 MVVLGASKVGKTAIVSRFLGGRFEEQYTPTIE---DFHRKLYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGD----VF 75 (247) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCCC---CEEEEEEEECCEEEEEEEECCCCCCCCCCCCCCCCCCCC----EE T ss_conf 89982698318889887653832676234210---005789988792899997225446545543402103887----89 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.+ ++.++.|++.++..-.....+..... .+|++|||+|.|. T Consensus 76 ILVyDIT~r~S-Fe~v~~w~~eI~e~k~~~~~~~~~~~----------------------------~vpiILVGNK~DL- 125 (247) T cd04143 76 ILVFSLDNRES-FEEVCRLREQILETKSCLKNKTKENV----------------------------KIPMVICGNKADR- 125 (247) T ss_pred EEEEECCCHHH-HHHHHHHHHHHHHHHHHHCCCCCCCC----------------------------CCEEEEEECCCCC- T ss_conf 99975699789-99999999999986311002345788----------------------------7279997055673- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHH--HHHHHHHHHC----CCCCCCEEEEECCCCE Q ss_conf 58876678999999999998609468885120345678--9998887505----7777730575067757 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLK--IRGVINQLAF----GIDKSKSICVDQNKPL 255 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r--~r~~inhl~F----G~~~~k~~~~D~~kPl 255 (351) +.+..-..-.+.+++|-.+|+..+-+|-+.+..+. |+.|..+... .-..++-+++.+-.|+ T Consensus 126 ---~~~R~Vs~eEa~q~~A~~~~~~ffEtSAKtg~NVdE~F~~L~~~~~l~~~~~p~~~~~~~~~~~~~~ 192 (247) T cd04143 126 ---DFPREVQRDEVEQLVGGDENCAYFEVSAKKNSNLDEMFRALFSLAKLPNEMSPSLHRKISVQYGDAL 192 (247) T ss_pred ---CCCCCCCHHHHHHHHHHHCCCCEEEEECCCCCCHHHHHHHHHHHCCCCCCCCCCHHEEEEEEECCCC T ss_conf ---2257338899999999827982899852589888999999998648732268204103232215534 No 54 >cd00877 Ran Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases. Ran GTPase is involved in diverse biological functions, such as nuclear transport, spindle formation during mitosis, DNA replication, and cell division. Among the Ras superfamily, Ran is a unique small G protein. It does not have a lipid modification motif at the C-terminus to bind to the membrane, which is often observed within the Ras superfamily. Ran may therefore interact with a wide range of proteins in various intracellular locations. Like other GTPases, Ran exists in GTP- and GDP-bound conformations that interact differently with effectors. Conversion between these forms and the assembly or disassembly of effector complexes requires the interaction of regulator proteins. The intrinsic GTPase activity of Ran is very low, but it is greatly stimulated by a GTPase-activating protein (RanGAP1) located in the cytoplasm. By contrast, RCC1, a guanine nucleotide exchange factor that generates RanGTP, is Probab=99.36 E-value=6.5e-12 Score=93.53 Aligned_columns=151 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |.++|+.+.|||||+.||++. .+.+.||.+.++..-.-...+... -.++|..+|--.+..|.+.-++ ..-.+ T Consensus 3 IvliGd~~VGKTsli~r~~~~~F~~~y~~Tig~~~~~~~~~~~~~~i--~l~iwDtaG~e~f~~l~~~y~~----~a~~~ 76 (166) T cd00877 3 LVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLDFHTNRGKI--RFNVWDTAGQEKFGGLRDGYYI----GGQCA 76 (166) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEECCCEE--EEEEEECCCCCCCCCCCCCCCC----CCCEE T ss_conf 89982698448999888763811666453464488899999879479--9998845785213545512000----26758 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.++++=. +..|++.+++..+. +|++|||+|.|+ T Consensus 77 ilvfDit~~~Sf~~-i~~w~~~i~~~~~~--------------------------------------ipivlVGNK~Dl- 116 (166) T cd00877 77 IIMFDVTSRVTYKN-VPNWHRDLVRVCGN--------------------------------------IPIVLCGNKVDI- 116 (166) T ss_pred EEEEECCCHHHHHH-HHHHHHHHHHHCCC--------------------------------------CCEEEEECCCCC- T ss_conf 99986699789898-98899999864599--------------------------------------658999326773- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +.++...+...+.... |+..+.+|-++. .++..+..+++ T Consensus 117 -----~~~~~~~~~~~~~~~~-~~~~~EtSAk~g--~NV~e~F~~la 155 (166) T cd00877 117 -----KDRKVKAKQITFHRKK-NLQYYEISAKSN--YNFEKPFLWLA 155 (166) T ss_pred -----CCCCCCHHHHHHHHHC-CCCEEEEECCCC--CCHHHHHHHHH T ss_conf -----2011248999999957-994999970489--89889999999 No 55 >cd04129 Rho2 Rho2 subfamily. Rho2 is a fungal GTPase that plays a role in cell morphogenesis, control of cell wall integrity, control of growth polarity, and maintenance of growth direction. Rho2 activates the protein kinase C homolog Pck2, and Pck2 controls Mok1, the major (1-3) alpha-D-glucan synthase. Together with Rho1 (RhoA), Rho2 regulates the construction of the cell wall. Unlike Rho1, Rho2 is not an essential protein, but its overexpression is lethal. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for proper intracellular localization via membrane attachment. As with other Rho family GTPases, the GDP/GTP cycling is regulated by GEFs (guanine nucleotide exchange factors), GAPs (GTPase-activating proteins) and GDIs (guanine nucleotide dissociation inhibitors). Probab=99.35 E-value=4.5e-12 Score=94.56 Aligned_columns=160 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||+.||... .+.+.||.+-+|.---..++..- ...+|..+|--.+..|.+.-....+ .+ T Consensus 4 ivliGd~~VGKTsL~~r~~~~~F~~~~~pTi~~~~~~~i~v~~~~v---~l~iwDTaGqe~~~~l~~~~~~~a~----~~ 76 (187) T cd04129 4 LVIVGDGACGKTSLLSVFTLGEFPEEYHPTVFENYVTDCRVDGKPV---QLALWDTAGQEEYERLRPLSYSKAH----VI 76 (187) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEECCEEE---EEEEEECCCCCHHHHHHHHHHCCCC----EE T ss_conf 8998259843899999986173277636603665677446778689---9988655765215789998706997----89 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC- Q ss_conf 8887369846899999999999999999999998526953789999999984146677600111068877997121000- Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV- 190 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~- 190 (351) +||.|++.+.++-.--++|+..++++..+ +|+++||+|.|+ T Consensus 77 ilvydi~~~~Sf~~i~~~w~~~~~~~~~~--------------------------------------~piiLvGnK~DL~ 118 (187) T cd04129 77 LIGFAVDTPDSLENVRTKWIEEVRRYCPN--------------------------------------VPVILVGLKKDLR 118 (187) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCH T ss_conf 99963388567888889889999983689--------------------------------------4499983588711 Q ss_pred ----CCCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHH--HHHHHHHHH Q ss_conf ----15887667899999999999860946888-5120345678--999888750 Q Ver_Hs_NP_0570 191 ----FQDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLK--IRGVINQLA 238 (351) Q Consensus 191 ----F~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r--~r~~inhl~ 238 (351) ......++|.+--.--+.+|...|+--+| +|-+...... |..+....+ T Consensus 119 ~~~~~~~~~~~~r~v~~~e~~~~a~~~~~~~y~EtSAktg~nV~e~Fe~~~r~aL 173 (187) T cd04129 119 QDAVAKEEYRTQRFVPIQQGKRVAKEIGAKKYMECSALTGEGVDDVFEAATRAAL 173 (187) T ss_pred HHHHHHHHHHHCCCCCHHHHHHHHHHCCCCEEEEEECCCCCCHHHHHHHHHHHHH T ss_conf 2344321011105689899999999728954788633578787899999999984 No 56 >cd04102 RabL3 RabL3 (Rab-like3) subfamily. RabL3s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL3 lacks a prenylation site at the C-terminus. The specific function of RabL3 remains unknown. Probab=99.35 E-value=1.5e-12 Score=97.62 Aligned_columns=158 Identities=20% Q ss_pred EEEEECCCCCHHHHHHHHC--CCCCCCCCCCCCCHHHHHHHCCCCCCCEE---EEEEEECCCCCHHHCEEEEECCCCCCE Q ss_conf 8998659886377777552--76678887531000221110157871117---888971578542021100004235120 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL--DRDEPPKPTLALEYTYGRRAKGHNTPKDI---AHFWELGGGTSLLDLISIPITGDTLRT 108 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl--~r~e~~KPTlALeYtygRra~~~~~~Kdv---aH~WELGgg~~ls~Li~ipit~~~l~~ 108 (351) |++||+.|.|||||++||. +=.+.|.||.+.++.+-.-.-....+.+- .++|..+|--.+..|.+.-.+ .. T Consensus 3 IvliGDsgVGKTSLi~r~~~~~f~~~~~~TIG~~v~~k~~~~~~~~~~~k~~~lqlWDTAGQEryrsl~~~yYr----~a 78 (202) T cd04102 3 VLVVGDSGVGKSSLVHLICKNQVLGRPSWTVGCSVDVKHHTYKEGTPEEKTFFVELWDVGGSESVKSTRAVFYN----QV 78 (202) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEECCCCCCCEEEEEEEEECCCCHHHHHHHHHHHC----CC T ss_conf 89982598558999888653711688575166899999998406776640799999853897135667888852----89 Q ss_pred EEEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEE Q ss_conf 67788873698468999999999999999999999985269537899999999841466776001110688779971210 Q Ver_Hs_NP_0570 109 FSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKY 188 (351) Q Consensus 109 ~~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KY 188 (351) -.++||.|++...++ +.++.|+..+...-. .-+....+-..-|.....-.+||+++||+|. T Consensus 79 ~gvILVyDITnr~SF-enL~~Wl~Eil~k~~------------------~~~~~~~~~~~~~~~~~~~~~ip~lvvGnK~ 139 (202) T cd04102 79 NGIILVHDLTNRKSS-QNLQRWSLEALNKDT------------------FPTGLLVTNGDYDSEQFGGNQIPLLVIGTKL 139 (202) T ss_pred CEEEEEEECCCHHHH-HHHHHHHHHHHCCCC------------------CCCCCCCCCCCCCHHHCCCCCCEEEEECCCC T ss_conf 879999757997899-999999999741465------------------4445666555443012278972089972640 Q ss_pred CCCCCCCHHHHHHHHHHHHHHHHHCCC Q ss_conf 001588766789999999999986094 Q Ver_Hs_NP_0570 189 DVFQDFESEKRKVICKTLRFVAHYYGA 215 (351) Q Consensus 189 D~F~~~D~e~rK~i~r~LR~iAH~yGA 215 (351) |.-.+-.+....+..++ -+|||.-|| T Consensus 140 D~~~~~~~~~~~~~~~~-~~i~~~~~~ 165 (202) T cd04102 140 DQIPEKESSGNLVLTAR-GFVAEQGNA 165 (202) T ss_pred CHHCCCCCCCCCHHHHC-CCHHHHCCC T ss_conf 01103675654000000-013544385 No 57 >cd04111 Rab39 Rab39 subfamily. Found in eukaryotes, Rab39 is mainly found in epithelial cell lines, but is distributed widely in various human tissues and cell lines. It is believed to be a novel Rab protein involved in regulating Golgi-associated vesicular transport during cellular endocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Probab=99.35 E-value=1.1e-11 Score=92.12 Aligned_columns=156 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.|||||++||++. .+.+.||++.|| |.+...-....+--.++|-.+|--.+..+...-.+ ....+ T Consensus 5 IviiGd~~VGKTsli~rf~~~~F~~~~~~Tig~df-~~k~v~i~dgk~v~L~IwDTaGqE~f~si~~~yyr----~a~g~ 79 (211) T cd04111 5 LIVIGDSTVGKSSLLKRFTEGRFAEVSDPTVGVDF-FSRLIEIEPGVRIKLQLWDTAGQERFRSITRSYYR----NSVGV 79 (211) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCEEEEE-EEEEEEECCCCEEEEEEEECCCCHHHHHHHHHHHC----CCCEE T ss_conf 99982698548999988770821676565024688-89999961784799998636997156888888601----89889 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+. =++.+..|++.++.+.+ |.-+|+++||+|.|+ T Consensus 80 ilVyDit~~~-SFe~i~~w~~ei~~~~~------------------------------------~~~~~~iLVGNK~DL- 121 (211) T cd04111 80 LLVFDITNRE-SFEHVHDWLEEARSHIQ------------------------------------PHRPVFILVGHKCDL- 121 (211) T ss_pred EEEEECCCHH-HHHHHHHHHHHHHHHCC------------------------------------CCCCEEEEECCCCCH- T ss_conf 9998669977-89999999999998518------------------------------------998589997165341- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .+.|.+--.--+.+|-.+|+..+-||-+.. .++..+-..++ T Consensus 122 ----~~~R~Vs~eea~~~A~~~~~~f~EtSAktg--~nV~e~F~~la 162 (211) T cd04111 122 ----ESQRQVTREEAEKLAKDLGMKYIETSARTG--DNVEEAFELLT 162 (211) T ss_pred ----HHHHCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----333012489999999966996999963589--88899999999 No 58 >cd04127 Rab27A Rab27a subfamily. The Rab27a subfamily consists of Rab27a and its highly homologous isoform, Rab27b. Unlike most Rab proteins whose functions remain poorly defined, Rab27a has many known functions. Rab27a has multiple effector proteins, and depending on which effector it binds, Rab27a has different functions as well as tissue distribution and/or cellular localization. Putative functions have been assigned to Rab27a when associated with the effector proteins Slp1, Slp2, Slp3, Slp4, Slp5, DmSlp, rabphilin, Dm/Ce-rabphilin, Slac2-a, Slac2-b, Slac2-c, Noc2, JFC1, and Munc13-4. Rab27a has been associated with several human diseases, including hemophagocytic syndrome (Griscelli syndrome or GS), Hermansky-Pudlak syndrome, and choroidermia. In the case of GS, a rare, autosomal recessive disease, a Rab27a mutation is directly responsible for the disorder. When Rab27a is localized to the secretory granules of pancreatic beta cells, it is believed to mediate glucose-stimulated Probab=99.35 E-value=8.2e-12 Score=92.91 Aligned_columns=157 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEE--------EEEEEECCCCCHHHCEEEEECC Q ss_conf 899865988637777755276--678887531000221110157871117--------8889715785420211000042 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDI--------AHFWELGGGTSLLDLISIPITG 103 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~Kdv--------aH~WELGgg~~ls~Li~ipit~ 103 (351) |+++|+.+.||||||.||+.. .+.+.||.++++.--+-...+..+... ..+|..+|...+..|.....+. T Consensus 7 ivviGd~~vGKTsli~r~~~~~f~~~~~~Tig~~~~~k~i~~~~~~~~~~~~~~~~v~l~iwDtaGqe~~~~l~~~~~~~ 86 (180) T cd04127 7 FLALGDSGVGKTSFLYQYTDNKFNPKFITTVGIDFREKRVVYNSSGPGGTLGRGQRIHLQLWDTAGQERFRSLTTAFFRD 86 (180) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEEECCCCCCCCCCCCEEEEEEEECCCCCHHHHHHHHHCCC T ss_conf 99980698438999888763832776354011135577999712554332457727999997247762145676886049 Q ss_pred CCCCEEEEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEE Q ss_conf 35120677888736984689999999999999999999999852695378999999998414667760011106887799 Q Ver_Hs_NP_0570 104 DTLRTFSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVI 183 (351) Q Consensus 104 ~~l~~~~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvI 183 (351) .. .++||.|++.++++=. +..|++.++.+.. ..++ |+++ T Consensus 87 a~----~~ilvydit~~~Sf~~-~~~w~~~i~~~~~-------~~~~-----------------------------~ivl 125 (180) T cd04127 87 AM----GFLLIFDLTNEQSFLN-VRNWMSQLQTHAY-------CENP-----------------------------DIVL 125 (180) T ss_pred CC----EEEEEEECCCHHHHHH-HHHHHHHHHHHCC-------CCCC-----------------------------EEEE T ss_conf 98----8999974689668899-9999999986136-------7875-----------------------------0788 Q ss_pred ECCEECCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 7121000158876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 184 IGSKYDVFQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 184 Vg~KYD~F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) ||+|+| -.++|.+--.-.+-+|..+|+..+++|-+.. ..+..+...|+ T Consensus 126 VgNK~D-----l~~~r~Vs~~e~~~~a~~~~~~~~e~SAk~~--~nV~e~F~~l~ 173 (180) T cd04127 126 CGNKAD-----LEDQRQVSEEQAKALADKYGIPYFETSAATG--TNVEKAVERLL 173 (180) T ss_pred EECCCC-----CCCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf 720235-----5211224878999999965995999971479--88789999999 No 59 >cd01892 Miro2 Miro2 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the putative GTPase domain in the C terminus of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature. Probab=99.34 E-value=4.3e-12 Score=94.68 Aligned_columns=152 Identities=20% Q ss_pred EEEEECCCCCHHHHHHHHCCC---CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEE Q ss_conf 899865988637777755276---67888753100022111015787111788897157854202110000423512067 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR---DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFS 110 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r---~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~ 110 (351) |+++|+.|.|||||++||..+ ++.++||++.+|. .+...-...+-..++|..||.-...-|...-.+...+ T Consensus 7 ~~vlGd~gVGKTsll~rfv~~~F~~~~y~~Tig~~f~--~k~v~v~g~~~~l~l~Dtagqe~~~~l~~~~~~~a~~---- 80 (169) T cd01892 7 CFVLGAKGSGKSALLRAFLGRSFSLNAYSPTIKPRYA--VNTVEVYGQEKYLILREVGEDEVAILLNDAELAACDV---- 80 (169) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCCCCCEEE--EEEEEECCEEEEEEEECCCCHHHHHHHHHHHCCCCCE---- T ss_conf 9998089964899999985687466621152023167--9888876747899851157303454431322058878---- Q ss_pred EEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 78887369846899999999999999999999998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 111 LVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 111 viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) ++||.|.++|.++ +++.++..+....+. ||+++||+|.|+ T Consensus 81 ~ilVYDit~~~SF------------~~i~~~~~~~~~~~~----------------------------ipiilVGNK~DL 120 (169) T cd01892 81 ACLVYDSSDPKSF------------SYCAEVYKKYFMLGE----------------------------IPCLFVAAKADL 120 (169) T ss_pred EEEEEECCCHHHH------------HHHHHHHHHCCCCCC----------------------------CEEEEEECCCCC T ss_conf 9999867997899------------999999986048999----------------------------559998303677 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHCCCEE-EEEECHHHHHHHHHHHHHHHH Q ss_conf 158876678999999999998609468-885120345678999888750 Q Ver_Hs_NP_0570 191 FQDFESEKRKVICKTLRFVAHYYGASL-MFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 191 F~~~D~e~rK~i~r~LR~iAH~yGA~L-~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|.+--.-=.-+|+.+|..- +.+|-+.. .++..+-..++ T Consensus 121 -----~~~RqVs~~e~~~~a~~~g~~~~~e~SAKtg--~nV~e~F~~la 162 (169) T cd01892 121 -----DEQQQRYEVQPDEFCRKLGLPPPLHFSSKLG--DSSNELFTKLA 162 (169) T ss_pred -----CCCCCCCCCCHHHHHHHCCCCCCEEEEECCC--CCHHHHHHHHH T ss_conf -----5556336337689999629996368870179--99899999999 No 60 >smart00173 RAS Ras subfamily of RAS small GTPases; Similar in fold and function to the bacterial EF-Tu GTPase. p21Ras couples receptor Tyr kinases and G protein receptors to protein kinase cascades Probab=99.34 E-value=9.2e-12 Score=92.60 Aligned_columns=154 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||.||++. .+.+.||++-.|+---..++..- ..++|..+|.-.+..|...-++..+ .+ T Consensus 5 iiliGd~~vGKTsli~r~~~~~f~~~y~~ti~~~~~k~~~i~~~~~---~l~iwDtaG~e~~~~~~~~~~~~a~----~~ 77 (166) T smart00173 5 LVVLGSGGVGKSALTIQFVQGIFVDDYDPTIEDSYRKQIEIDGEVC---LLDILDTAGQEEFSAMRDQYMRTGE----GF 77 (166) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCCEEEEEEECCEEE---EEEEEECCCCCCHHHHHHHHHCCCC----CE T ss_conf 9998079964899999987280277545521212257898989799---9998627998512367788740799----35 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=.--.+| +.+.+.....+ +|++|||+|.|. T Consensus 78 iivydit~~~Sf~~~~~w~--------~~i~~~~~~~~-----------------------------ip~vlvgNK~Dl- 119 (166) T smart00173 78 LLVYSITDRQSFEEIKKFR--------EQILRVKDRDD-----------------------------VPIVLVGNKCDL- 119 (166) T ss_pred EEEEECCCHHHHHHHHHHH--------HHHHHHCCCCC-----------------------------CEEEEEECCCCC- T ss_conf 9999749978999998998--------99987428999-----------------------------579998114651- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +++|.+.-.-..-+|..+|+..+.+|-+.. ..+..+..+++ T Consensus 120 ----~~~r~v~~~~~~~~a~~~~~~~~E~SAk~~--~nV~e~F~~l~ 160 (166) T smart00173 120 ----ENERQVSTEEGKELARQWNCPFLETSAKER--INVDEAFYDLV 160 (166) T ss_pred ----CCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----000457678999999966996999972589--88889999999 No 61 >cd01875 RhoG RhoG subfamily. RhoG is a GTPase with high sequence similarity to members of the Rac subfamily, including the regions involved in effector recognition and binding. However, RhoG does not bind to known Rac1 and Cdc42 effectors, including proteins containing a Cdc42/Rac interacting binding (CRIB) motif. Instead, RhoG interacts directly with Elmo, an upstream regulator of Rac1, in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. Thus RhoG activates Rac1 through Elmo and Dock180 to control cell morphology. RhoG has also been shown to play a role in caveolar trafficking and has a novel role in signaling the neutrophil respiratory burst stimulated by G protein-coupled receptor (GPCR) agonists. Most Rho proteins contain a lipid modification site at the C-termin Probab=99.33 E-value=1.3e-11 Score=91.60 Aligned_columns=168 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.|||||+.||... .+.+.||+.-.|+.--..++..- ..++|.-+|--.+..|...-.+..+. + T Consensus 6 vvliGd~~VGKTsli~r~~~~~F~~~~~pTi~~~~~~~~~~~~~~v---~l~iwDTaGqe~~~~l~~~~~~~a~~----~ 78 (191) T cd01875 6 CVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQTAVDGRTV---SLNLWDTAGQEEYDRLRTLSYPQTNV----F 78 (191) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCCEE---EEEEECCCCCHHHHHHHHHHHCCCCE----E T ss_conf 9987079842899988875284266535504554688666517279---99851488854467787876238986----9 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=.--+.|+..++.+... +|++|||+|.|+- T Consensus 79 iivyditd~~Sf~~i~~~w~~~i~~~~~~--------------------------------------vpiiLVGNK~DL~ 120 (191) T cd01875 79 IICFSIASPSSYENVRHKWHPEVCHHCPN--------------------------------------VPILLVGTKKDLR 120 (191) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 99986488678899999889999972689--------------------------------------6799983476631 Q ss_pred CCCCHHHHH-------HHHHHHHHHHHHCCCEEEE-EECHHHHHHH--HHHHHHHHHCCCCCCCE Q ss_conf 588766789-------9999999999860946888-5120345678--99988875057777730 Q Ver_Hs_NP_0570 192 QDFESEKRK-------VICKTLRFVAHYYGASLMF-TSKSEALLLK--IRGVINQLAFGIDKSKS 246 (351) Q Consensus 192 ~~~D~e~rK-------~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r--~r~~inhl~FG~~~~k~ 246 (351) .+-+..++- +...--+.+|..+|+-.+| +|-+...... |..++...+..+|.... T Consensus 121 ~~~~~~~~~~e~~~~~Vs~eeg~~~a~~~~~~~y~EtSAktg~nV~e~F~~l~r~vl~~~p~~~~ 185 (191) T cd01875 121 NDADTLKKLKEQGQAPITPQQGGALAKQIHAVKYLECSALNQDGVKEVFAEAVRAVLNPTPIKDT 185 (191) T ss_pred CCHHHHHHHHHHHCCCCCHHHHHHHHHHCCCCEEEEEECCCCCCHHHHHHHHHHHHHCCCCCCCC T ss_conf 12688888875102466889999999980895068864047778789999999998478898878 No 62 >cd04138 H_N_K_Ras_like H-Ras/N-Ras/K-Ras subfamily. H-Ras, N-Ras, and K-Ras4A/4B are the prototypical members of the Ras family. These isoforms generate distinct signal outputs despite interacting with a common set of activators and effectors, and are strongly associated with oncogenic progression in tumor initiation. Mutated versions of Ras that are insensitive to GAP stimulation (and are therefore constitutively active) are found in a significant fraction of human cancers. Many Ras guanine nucleotide exchange factors (GEFs) have been identified. They are sequestered in the cytosol until activation by growth factors triggers recruitment to the plasma membrane or Golgi, where the GEF colocalizes with Ras. Active (GTP-bound) Ras interacts with several effector proteins that stimulate a variety of diverse cytoplasmic signaling activities. Some are known to positively mediate the oncogenic properties of Ras, including Raf, phosphatidylinositol 3-kinase (PI3K), RalGEFs, and Tiam1. Probab=99.32 E-value=1.2e-11 Score=91.87 Aligned_columns=153 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHCCCC--CCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 8998659886377777552766--78887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDRD--EPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r~--e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.|.||||||+||++.. +.+.||.+-.| ++..--+...-..|+|..+|.-.+..+...-++ ..-.+ T Consensus 4 vvliGd~~VGKTSli~~~~~~~f~~~y~~Ti~~~~---~k~v~i~~~~~~l~i~Dt~G~e~~~~~~~~~~~----~a~~~ 76 (162) T cd04138 4 LVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSY---RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMR----TGEGF 76 (162) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCEEEE---EEEEEECCEEEEEEEEECCCCHHHHHHHHHHHC----CCCEE T ss_conf 89981799548999999861801676565100147---889999895899998746885013466487523----89769 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++++.++ +.+..|+..+++..+. -.+|++|||+|.|+ T Consensus 77 ilvydv~~~~Sf-~~i~~w~~~i~~~~~~------------------------------------~~~piilvgNK~Dl- 118 (162) T cd04138 77 LCVFAINSRKSF-EDIHTYREQIKRVKDS------------------------------------DDVPMVLVGNKCDL- 118 (162) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCCC------------------------------------CCCEEEEEEEECCC- T ss_conf 999866997899-9999999999874189------------------------------------99489998300475- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +.|++--.-.+.+|..+|+.-+-+|-+.. ..+..+...++ T Consensus 119 -----~~r~v~~~e~~~~a~~~~~~~~E~SAkt~--~nV~e~F~~l~ 158 (162) T cd04138 119 -----AARTVSSRQGQDLAKSYGIPYIETSAKTR--QGVEEAFYTLV 158 (162) T ss_pred -----CCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf -----33258989999999966995999970489--78789999999 No 63 >KOG1673 Ras GTPases [General function prediction only] Probab=99.32 E-value=4.5e-12 Score=94.52 Aligned_columns=179 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHC--CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 8998659886377777552--76678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL--DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl--~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |=++|+..-||||++-+.. +.+|..--|+++...=-.-.-++... .--+|+|||--.+-..|.+. ..-..++ T Consensus 23 v~llGD~qiGKTs~mvkYV~~~~de~~~q~~GvN~mdkt~~i~~t~I--sfSIwdlgG~~~~~n~lPia----c~dsvaI 96 (205) T KOG1673 23 VGLLGDAQIGKTSLMVKYVQNEYDEEYTQTLGVNFMDKTVSIRGTDI--SFSIWDLGGQREFINMLPIA----CKDSVAI 96 (205) T ss_pred EEEEECCCCCCCEEEEEEHHCCCHHHHHHHHCCCEEEEEEEEECEEE--EEEEEECCCHHHHHHCCCEE----ECCCEEE T ss_conf 87630665461101221110410456788742200000578611079--99843035303554147612----3372879 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +.|+||+.+..+ .+.-.|+++.|..-+..+ -++||+|||.| T Consensus 97 lFmFDLt~r~TL-nSi~~WY~QAr~~NktAi--------------------------------------PilvGTKyD~f 137 (205) T KOG1673 97 LFMFDLTRRSTL-NSIKEWYRQARGLNKTAI--------------------------------------PILVGTKYDLF 137 (205) T ss_pred EEEEECCCHHHH-HHHHHHHHHHCCCCCCCC--------------------------------------EEEEECCHHHH T ss_conf 876415780246-789999998504786434--------------------------------------05761552441 Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHH-HHHHHHHHHCCCCCCCEEEEECCCCEEE Q ss_conf 58876678999999999998609468885120345678-9998887505777773057506775787 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLK-IRGVINQLAFGIDKSKSICVDQNKPLFI 257 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r-~r~~inhl~FG~~~~k~~~~D~~kPl~I 257 (351) -+++||....|.+.-|.-|....|+|+|.|-.-+.+.. +-..+--.+|-.+....-...--.|++. T Consensus 138 i~lp~e~Q~~I~~qar~YAk~mnAsL~F~Sts~sINv~KIFK~vlAklFnL~~ti~~~~~iGdPild 204 (205) T KOG1673 138 IDLPPELQETISRQARKYAKVMNASLFFCSTSHSINVQKIFKIVLAKLFNLPWTIPEILTIGDPILD 204 (205) T ss_pred EECCHHHHHHHHHHHHHHHHHHCCCEEEEECCCCCCHHHHHHHHHHHHHCCCCCCHHHCCCCCCCCC T ss_conf 0078136899999999888874462467412242229999999988883572241322025650005 No 64 >cd04115 Rab33B_Rab33A Rab33B/Rab33A subfamily. Rab33B is ubiquitously expressed in mouse tissues and cells, where it is localized to the medial Golgi cisternae. It colocalizes with alpha-mannose II. Together with the other cisternal Rabs, Rab6A and Rab6A', it is believed to regulate the Golgi response to stress and is likely a molecular target in stress-activated signaling pathways. Rab33A (previously known as S10) is expressed primarily in the brain and immune system cells. In humans, it is located on the X chromosome at Xq26 and its expression is down-regulated in tuberculosis patients. Experimental evidence suggests that Rab33A is a novel CD8+ T cell factor that likely plays a role in tuberculosis disease processes. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine Probab=99.31 E-value=2.1e-11 Score=90.40 Aligned_columns=155 Identities=23% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEE-EEEEECCCCCH-HHCEEEEECCCCCCEE Q ss_conf 899865988637777755276--6788875310002211101578711178-88971578542-0211000042351206 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIA-HFWELGGGTSL-LDLISIPITGDTLRTF 109 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~Kdva-H~WELGgg~~l-s~Li~ipit~~~l~~~ 109 (351) |+++|+.+.|||||+.||+.. .+.+.||+++|| ....-....+.+- ++|-.+|--.+ ..|++.-....+ T Consensus 5 ivliGd~~VGKTsli~r~~~~~F~~~~~~Tig~d~---~~k~i~~~~~~v~l~iwDtaGqe~f~~~l~~~y~~~a~---- 77 (170) T cd04115 5 IIVIGDSNVGKTCLTYRFCAGRFPERTEATIGVDF---RERTVEIDGERIKVQLWDTAGQERFRKSMVQHYYRNVH---- 77 (170) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEE---EEEEEEECCEEEEEEEECCCCCHHHHHHHHHHHCCCCC---- T ss_conf 99980799658999999862855754453122035---78999988958999982278733567777654304898---- Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .+++|.|++.+.++ +.+..|++.++++.. +-.+|+++||+|.| T Consensus 78 ~~ilvydit~~~SF-~~i~~w~~~i~~~~~------------------------------------~~~~p~iLVGNK~D 120 (170) T cd04115 78 AVVFVYDVTNMASF-HSLPSWIEECEQHSL------------------------------------PNEVPRILVGNKCD 120 (170) T ss_pred EEEEEEECCCHHHH-HHHHHHHHHHHHHCC------------------------------------CCCCEEEEEECCCC T ss_conf 48999876997788-999999999997259------------------------------------98617999802135 Q ss_pred CCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECH---HHHHHH--HHHHHHHH Q ss_conf 0158876678999999999998609468885120---345678--99988875 Q Ver_Hs_NP_0570 190 VFQDFESEKRKVICKTLRFVAHYYGASLMFTSKS---EALLLK--IRGVINQL 237 (351) Q Consensus 190 ~F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~---e~l~~r--~r~~inhl 237 (351) + .++|.+-..--+-+|-.+|+..+-+|-+ ++.... +..+-+.+ T Consensus 121 L-----~~~r~Vs~~e~~~~A~~~~~~~fE~SAK~~~~~~nV~~~F~~la~~l 168 (170) T cd04115 121 L-----REQIQVPTDLAQRFADAHSMPLFETSAKDPSENDHVEAIFMTLAHKL 168 (170) T ss_pred C-----HHHCCCCHHHHHHHHHHCCCCEEEEECCCCCCCCCHHHHHHHHHHHH T ss_conf 0-----12136798999999996699599986267888868789999999996 No 65 >cd04134 Rho3 Rho3 subfamily. Rho3 is a member of the Rho family found only in fungi. Rho3 is believed to regulate cell polarity by interacting with the diaphanous/formin family protein For3 to control both the actin cytoskeleton and microtubules. Rho3 is also believed to have a direct role in exocytosis that is independent of its role in regulating actin polarity. The function in exocytosis may be two-pronged: first, in the transport of post-Golgi vesicles from the mother cell to the bud, mediated by myosin (Myo2); second, in the docking and fusion of vesicles to the plasma membrane, mediated by an exocyst (Exo70) protein. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Probab=99.31 E-value=2.4e-11 Score=89.94 Aligned_columns=170 Identities=17% Q ss_pred CEEEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 45899865988637777755276--6788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 32 KFVFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 32 k~v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) +-|++||+.+.|||||++||... .+.+.||.+-+|+.--..++..- -.++|.-+|--.+..|.+.-....+ T Consensus 1 ~KiiliGd~~VGKTsLi~rf~~~~F~~~~~~Ti~~~~~~~i~vd~~~v---~l~iwDTaGqE~f~~l~~~~y~~a~---- 73 (189) T cd04134 1 RKVVVLGDGACGKTSLLNVFTRGYFPQVYEPTVFENYVHDIFVDGLHI---ELSLWDTAGQEEFDRLRSLSYADTD---- 73 (189) T ss_pred CEEEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCEEE---EEEEECCCCCHHHHHHHHHHHCCCC---- T ss_conf 968998269833899998876380067516616775678667779489---9998627787145778887733898---- Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .++||.|++.+.++=.-...|+..++++... +|+++||+|+| T Consensus 74 ~~ilvydit~~~Sf~~i~~~W~~ei~~~~~~--------------------------------------v~iiLVGnK~D 115 (189) T cd04134 74 VIMLCFSVDSPDSLENVESKWLGEIREHCPG--------------------------------------VKLVLVALKCD 115 (189) T ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEEECCC T ss_conf 7899986688446689999889999983589--------------------------------------55999850467 Q ss_pred CCCCCCHHHHH-------HHHHHHHHHHHHCCCEEEE-EECHHHHHHH--HHHHHHHHHCCCCCCCE Q ss_conf 01588766789-------9999999999860946888-5120345678--99988875057777730 Q Ver_Hs_NP_0570 190 VFQDFESEKRK-------VICKTLRFVAHYYGASLMF-TSKSEALLLK--IRGVINQLAFGIDKSKS 246 (351) Q Consensus 190 ~F~~~D~e~rK-------~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r--~r~~inhl~FG~~~~k~ 246 (351) +=.+-.+.... +-..--..+|..+||-.+| +|-+...... |..+....+-..|+++. T Consensus 116 L~~~~~~~~~~~~~~~~~vs~~e~~~~a~~~~~~~y~EtSAKt~~nV~e~F~~lar~~L~~~~~~~~ 182 (189) T cd04134 116 LREARNERDDLQRYGKHTISYEEGLAVAKRINALRYLECSAKLNRGVNEAFTEAARVALNVRPPHPH 182 (189) T ss_pred CCCCHHHHHHHHHHHCCCCCHHHHHHHHHHCCCCEEEEEECCCCCCHHHHHHHHHHHHHCCCCCCCC T ss_conf 6553134566765313677989999999980895068864257878789999999998278877887 No 66 >cd04177 RSR1 RSR1 subgroup. RSR1/Bud1p is a member of the Rap subfamily of the Ras family that is found in fungi. In budding yeasts, RSR1 is involved in selecting a site for bud growth on the cell cortex, which directs the establishment of cell polarization. The Rho family GTPase cdc42 and its GEF, cdc24, then establish an axis of polarized growth by organizing the actin cytoskeleton and secretory apparatus at the bud site. It is believed that cdc42 interacts directly with RSR1 in vivo. In filamentous fungi, polar growth occurs at the tips of hypha and at novel growth sites along the extending hypha. In Ashbya gossypii, RSR1 is a key regulator of hyphal growth, localizing at the tip region and regulating in apical polarization of the actin cytoskeleton. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key featu Probab=99.31 E-value=1.3e-11 Score=91.73 Aligned_columns=154 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.|.||||||+||+.. .+.+.||++-.| ++.--=+...--.++|..+|--.+..|.+.-++.-+. + T Consensus 4 iiliGd~~VGKTsli~r~~~~~F~~~~~~Ti~~~~---~k~i~v~~~~~~l~iwDtaG~e~~~~l~~~~~~~a~~----~ 76 (168) T cd04177 4 IVVLGAGGVGKSALTVQFVQNVFIESYDPTIEDSY---RKQVEIDGRQCDLEILDTAGTEQFTAMRELYIKSGQG----F 76 (168) T ss_pred EEEECCCCCCHHHHHHHHHCCEECCCCCCCCCCCE---EEEEEECCEEEEEEEEECCCCCHHHHHHHHHCCCCCE----E T ss_conf 89980799548999998871800676454101103---5789898969999987279871245687875359985----8 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.+ ++.+..|.+.+.+..+. -.+|++|||+|+|+ T Consensus 77 ilvydit~~~S-f~~l~~~~~~i~~~~~~------------------------------------~~~piilvGNK~DL- 118 (168) T cd04177 77 LLVYSVTSEAS-LNELGELREQVLRIKDS------------------------------------DNVPMVLVGNKADL- 118 (168) T ss_pred EEEEECCCHHH-HHHHHHHHHHHHHHCCC------------------------------------CCCEEEEECCCCCC- T ss_conf 99985699789-99999999999863189------------------------------------99589998024784- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 5887667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) .+.|.+--.-.+.+|..+|..-+| +|-+.. ..+..+..+++ T Consensus 119 ----~~~r~v~~~e~~~~a~~~~~~~~~E~SAk~g--~nV~e~F~~l~ 160 (168) T cd04177 119 ----EDDRQVSREDGVSLSQQWGNVPFYETSARKR--TNVDEVFIDLV 160 (168) T ss_pred ----CCCCCCCHHHHHHHHHHHCCCCEEEEEECCC--CCHHHHHHHHH T ss_conf ----3357689899999999816983588860489--88789999999 No 67 >cd04172 Rnd3_RhoE_Rho8 Rnd3/RhoE/Rho8 subfamily. Rnd3/RhoE/Rho8 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd2/Rho7. Rnd3/RhoE is known to bind the serine-threonine kinase ROCK I. Unphosphorylated Rnd3/RhoE associates primarily with membranes, but ROCK I-phosphorylated Rnd3/RhoE localizes in the cytosol. Phosphorylation of Rnd3/RhoE correlates with its activity in disrupting RhoA-induced stress fibers and inhibiting Ras-induced fibroblast transformation. In cells that lack stress fibers, such as macrophages and monocytes, Rnd3/RhoE induces a redistribution of actin, causing morphological changes in the cell. In addition, Rnd3/RhoE has been shown to inhibit cell cycle progression in G1 phase at a point upstream of the pRb family pocket protein checkpoint. Rnd3/RhoE has also been shown to inhibit Ras- and Raf-induced fibroblast transformation. In mammary epithelial tumor cells, Rnd3/RhoE regulates the assembly of the apical junction complex and tight Probab=99.30 E-value=6e-12 Score=93.78 Aligned_columns=155 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.||||||+||.+. .+.+.||++-+|+--=..++..- -.++|.-+|--.+..|.+.-.. ..-.+ T Consensus 8 ivlvGd~~VGKTsli~r~~~~~F~~~~~~Ti~~~~~~~~~i~~~~v---~l~iwDTaGqe~~~~l~~~~y~----~a~~~ 80 (182) T cd04172 8 IVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRI---ELSLWDTSGSPYYDNVRPLSYP----DSDAV 80 (182) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCEEE---EEEEECCCCCHHHHHHHHHHCC----CCCEE T ss_conf 9998369854889988875380157612057753689998878599---9998507887456666476526----99879 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC- Q ss_conf 8887369846899999999999999999999998526953789999999984146677600111068877997121000- Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV- 190 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~- 190 (351) +||.|++++.++=.-+++|+..++.+... +|+++||+|.|+ T Consensus 81 ilvfdit~~~Sf~~v~~~W~~ei~~~~~~--------------------------------------~~iiLVGnK~DL~ 122 (182) T cd04172 81 LICFDISRPETLDSVLKKWKGEIQEFCPN--------------------------------------TKMLLVGCKSDLR 122 (182) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 99986588557899999989999984689--------------------------------------6699985487653 Q ss_pred ------CCCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHH-HHHHHH Q ss_conf ------15887667899999999999860946888-5120345678-999888 Q Ver_Hs_NP_0570 191 ------FQDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLK-IRGVIN 235 (351) Q Consensus 191 ------F~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r-~r~~in 235 (351) .+-.+..++.+--.--.-+|..+||..+| +|-..+ .+ ++.+.. T Consensus 123 ~~~~~~~~l~~~~q~~Vs~eeg~~~A~~~~a~~y~EtSAk~~--~n~v~~~F~ 173 (182) T cd04172 123 TDLTTLVELSNHRQTPVSYDQGANMAKQIGAATYIECSALQS--ENSVRDIFH 173 (182) T ss_pred CHHHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEEECCC--CCHHHHHHH T ss_conf 205778767634687679899999999718950688751268--841899999 No 68 >cd04146 RERG_RasL11_like RERG/RasL11-like subfamily. RERG (Ras-related and Estrogen- Regulated Growth inhibitor) and Ras-like 11 are members of a novel subfamily of Ras that were identified based on their behavior in breast and prostate tumors, respectively. RERG expression was decreased or lost in a significant fraction of primary human breast tumors that lack estrogen receptor and are correlated with poor clinical prognosis. Elevated RERG expression correlated with favorable patient outcome in a breast tumor subtype that is positive for estrogen receptor expression. In contrast to most Ras proteins, RERG overexpression inhibited the growth of breast tumor cells in vitro and in vivo. RasL11 was found to be ubiquitously expressed in human tissue, but down-regulated in prostate tumors. Both RERG and RasL11 lack the C-terminal CaaX prenylation motif, where a = an aliphatic amino acid and X = any amino acid, and are localized primarily in the cytoplasm. Both are believed to have tu Probab=99.30 E-value=3.2e-11 Score=89.22 Aligned_columns=155 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHC-EEEEECCCCCCEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021-10000423512067 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDL-ISIPITGDTLRTFS 110 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~L-i~ipit~~~l~~~~ 110 (351) |+++|+.+.||||||.||++. .+.+.||++-.|+---.-++..- ..++|..+|.-....+ ....+...+ . T Consensus 2 Iv~iGd~~vGKTsLi~r~~~~~F~~~y~~ti~~~~~k~~~v~~~~v---~l~i~DtaG~e~~~~~~~~~~~~~ad----~ 74 (165) T cd04146 2 IAVLGASGVGKSALVVRFLTKRFIGEYDPNLESLYSRQVTIDGEQV---SLEILDTAGQQQADTEQLERSIRWAD----G 74 (165) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCHHHHHEEEEEECCCEE---EEEEECCCCCHHHHHHCCCCCCCCCC----E T ss_conf 7888179832899999986174477546301211100002259448---99972277720110000013546888----7 Q ss_pred EEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 78887369846899999999999999999999998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 111 LVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 111 viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) ++||.|++.+.++ +.+..|++.++.+... +-.+|++|||+|+|+ T Consensus 75 ~ilvydit~~~SF-~~i~~~~~~i~~~~~~-----------------------------------~~~~piilVGNK~DL 118 (165) T cd04146 75 FVLVYSITDRSSF-DEISQLKQLIREIKKR-----------------------------------DREIPVILVGNKADL 118 (165) T ss_pred EEEEEECCCHHHH-HHHHHHHHHHHHHCCC-----------------------------------CCCCEEEEECCCCCC T ss_conf 9999766985368-9999999999975147-----------------------------------998279997233360 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHH-HHHHHHHHHH Q ss_conf 15887667899999999999860946888512034567-8999888750 Q Ver_Hs_NP_0570 191 FQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLL-KIRGVINQLA 238 (351) Q Consensus 191 F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~-r~r~~inhl~ 238 (351) ++.|.+--.-.+-+|-.+|+..+.+|-+.+ . .+..+-.+++ T Consensus 119 -----~~~r~V~~ee~~~~a~~~~~~~~E~SAk~~--~~~V~e~F~~l~ 160 (165) T cd04146 119 -----LHYRQVSTEEGEKLASELGCLFFEVSAAED--YDGVHSVFHELC 160 (165) T ss_pred -----HHCCCCCHHHHHHHHHHCCCCEEEEEECCC--CCHHHHHHHHHH T ss_conf -----010546989999999965995899860458--802799999999 No 69 >smart00176 RAN Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the active transport of proteins through nuclear pores. Probab=99.30 E-value=1.7e-11 Score=90.90 Aligned_columns=146 Identities=24% Q ss_pred EECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEE-EEEEECCCCCHHHCEEEEECCCCCCEEEEEE Q ss_conf 865988637777755276--6788875310002211101578711178-8897157854202110000423512067788 Q Ver_Hs_NP_0570 37 IGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIA-HFWELGGGTSLLDLISIPITGDTLRTFSLVL 113 (351) Q Consensus 37 vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~Kdva-H~WELGgg~~ls~Li~ipit~~~l~~~~vii 113 (351) ||+.|.|||||++||+.. .+.+.||++.|| +...-+...+.|- ++|..+|--.+..|.....+... .++| T Consensus 1 VGDsgVGKTsli~R~~~~~F~~~y~~TIGvd~---~~k~i~~~~~~I~l~IWDTAGQE~f~sl~~~yyr~a~----g~il 73 (200) T smart00176 1 VGDGGTGKTTFVKRHLTGEFEKKYVATLGVEV---HPLVFHTNRGPIKFNVWDTAGQEKFGGLEDGYYIQAQ----CAII 73 (200) T ss_pred CCCCCCCHHHHHHHHHCCEECCCCCCEEEEEE---EEEEEEECCCEEEEEEEECCCCCCCCCCCHHHHCCCC----EEEE T ss_conf 98874127888777644700676355466678---8999987185799988751565211000212305884----7999 Q ss_pred EEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCCC Q ss_conf 87369846899999999999999999999998526953789999999984146677600111068877997121000158 Q Ver_Hs_NP_0570 114 VLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQD 193 (351) Q Consensus 114 vlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~~ 193 (351) |+|++.+.++=. ++.|++.+.+..+. +|+++||+|+|+ ++ T Consensus 74 VfDVT~~~SF~n-i~~W~~ei~~~~~~--------------------------------------ipivLvGNK~DL-~~ 113 (200) T smart00176 74 MFDVTSRVTYKN-VPNWHRDLVRVCEN--------------------------------------IPIVLCGNKVDI-KD 113 (200) T ss_pred EEECCCHHHHHH-HHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCC-CC T ss_conf 976699778888-98899999986489--------------------------------------779998124353-32 Q ss_pred CCHHHHHHHHHHHHHHHHHCCCEEEEEE------CHHHHHHHHHHHHH Q ss_conf 8766789999999999986094688851------20345678999888 Q Ver_Hs_NP_0570 194 FESEKRKVICKTLRFVAHYYGASLMFTS------KSEALLLKIRGVIN 235 (351) Q Consensus 194 ~D~e~rK~i~r~LR~iAH~yGA~L~FtS------k~e~l~~r~r~~in 235 (351) |++..+... +|-.+|..-+-+| -.++++-..|.+++ T Consensus 114 -----r~v~~e~~~-fa~~~~~~y~EtSAKt~~NVee~F~~Larkl~~ 155 (200) T smart00176 114 -----RKVKAKSIV-FHRKKNLQYYDISAKSNYNFEKPFLWLARKLIG 155 (200) T ss_pred -----CCCHHHHHH-HHHHCCCCEEEEEECCCCCHHHHHHHHHHHHHC T ss_conf -----435489999-999668958998734787776889999999854 No 70 >cd04156 ARLTS1 ARLTS1 subfamily. ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in h Probab=99.30 E-value=5.7e-11 Score=87.62 Aligned_columns=156 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEE Q ss_conf 8998659886377777552-766788875310002211101578711178889715785420211000042351206778 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLV 112 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~vi 112 (351) |+++|..|+|||||++|+. ++.....||++ |......-..+. -.++|++||...+..+-+.-.....- +| T Consensus 2 IlilG~~~sGKTsll~rl~~~~~~~~~pTig--~~~~~~~~~~~v---~l~iwD~~G~e~~r~~~~~y~~~a~~----iI 72 (160) T cd04156 2 VLLLGLDSAGKSTLLYKLKHAELVTTIPTVG--FNVEMLQLEKHL---SLTVWDVGGQEKMRTVWKCYLENTDG----LV 72 (160) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCEEEEEC--EEEEEEEECCEE---EEEEEECCCCHHHHHHHHHHCCCCCE----EE T ss_conf 7899508986899888774586230220001--048899876837---99987458740346666764057637----99 Q ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCC Q ss_conf 88736984689999999999999999999999852695378999999998414667760011106887799712100015 Q Ver_Hs_NP_0570 113 LVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQ 192 (351) Q Consensus 113 ivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~ 192 (351) +|+|.|++.++=+..++| +++++.-.-.+ +|++|||+|-|. + T Consensus 73 ~V~D~sd~~~~~~~~~~l--------~~~l~~~~~~~-----------------------------~p~liv~NK~Dl-~ 114 (160) T cd04156 73 YVVDSSDEARLDESQKEL--------KHILKNEHIKG-----------------------------VPVVLLANKQDL-P 114 (160) T ss_pred EEEECCCHHHHHHHHHHH--------HHHHHHHCCCC-----------------------------CEEEEEEECCCC-C T ss_conf 997257834689999999--------98852001279-----------------------------759999605588-5 Q ss_pred CCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 8876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 193 DFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 193 ~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) +--+...-.-.-.|.-++...+..++.+|-... ..+...-.+++ T Consensus 115 ~~~~~~ei~~~l~l~~~~~~~~~~i~~~SA~tG--~gi~e~F~~lA 158 (160) T cd04156 115 GALTAEEITRRFKLKKYCSDRDWYVQPCSAVTG--EGLAEAFRKLA 158 (160) T ss_pred CCCCHHHHHHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 457889999899899998608938999731468--57789999984 No 71 >cd01874 Cdc42 Cdc42 subfamily. Cdc42 is an essential GTPase that belongs to the Rho family of Ras-like GTPases. These proteins act as molecular switches by responding to exogenous and/or endogenous signals and relaying those signals to activate downstream components of a biological pathway. Cdc42 transduces signals to the actin cytoskeleton to initiate and maintain polarized growth and to mitogen-activated protein morphogenesis. In the budding yeast Saccharomyces cerevisiae, Cdc42 plays an important role in multiple actin-dependent morphogenetic events such as bud emergence, mating-projection formation, and pseudohyphal growth. In mammalian cells, Cdc42 regulates a variety of actin-dependent events and induces the JNK/SAPK protein kinase cascade, which leads to the activation of transcription factors within the nucleus. Cdc42 mediates these processes through interactions with a myriad of downstream effectors, whose number and regulation we are just starting to understand. In addi Probab=99.29 E-value=1.1e-11 Score=92.10 Aligned_columns=158 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||+.||... .+.+.||++-.|+.--..++..- ..++|.-+|.-.+..|...-.+ ..-.+ T Consensus 4 vvlvGd~~VGKTsli~r~~~~~F~~~~~~Ti~~~~~~~i~i~~~~~---~l~iwDTaGqe~~~~l~~~~~r----~a~~~ 76 (175) T cd01874 4 CVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPY---TLGLFDTAGQEDYDRLRPLSYP----QTDVF 76 (175) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCEEE---EEEEEECCCCCHHHHHHHHHCC----CCCEE T ss_conf 9998179832789888865282266524235301679999989589---9998636776024566686505----99879 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|+..+.++=.-.++|+..++.+... +|+++||+|.|+= T Consensus 77 iivydit~~~SF~~i~~~w~~~~~~~~~~--------------------------------------~p~ilVGnK~DL~ 118 (175) T cd01874 77 LVCFSVVSPSSFENVKEKWVPEITHHCPK--------------------------------------TPFLLVGTQIDLR 118 (175) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 99975786424899999889999972589--------------------------------------6499971675643 Q ss_pred CCCC-------HHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 5887-------667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 192 QDFE-------SEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D-------~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) .+-. ...|-+...--+-+|..+|+-.+| +|-+.. ..+..+-.++. T Consensus 119 ~~~~~~~~~~~~~~r~Vs~eeg~~~A~~~~~~~y~EtSAktg--~~V~e~F~~ai 171 (175) T cd01874 119 DDPSTIEKLAKNKQKPITPETGEKLARDLKAVKYVECSALTQ--KGLKNVFDEAI 171 (175) T ss_pred CCHHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 415788876521367768899999999728950798751467--66789999999 No 72 >cd04144 Ras2 Ras2 subfamily. The Ras2 subfamily, found exclusively in fungi, was first identified in Ustilago maydis. In U. maydis, Ras2 is regulated by Sql2, a protein that is homologous to GEFs (guanine nucleotide exchange factors) of the CDC25 family. Ras2 has been shown to induce filamentous growth, but the signaling cascade through which Ras2 and Sql2 regulate cell morphology is not known. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Probab=99.29 E-value=4.5e-11 Score=88.29 Aligned_columns=156 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.||||||.||+.. .+.+.||++-.| ++..--+..+-..++|.-+|.-.+..|...-+ -..-.+ T Consensus 2 ivliGd~gVGKTsLi~rf~~~~F~~~y~pTi~~~~---~~~~~i~~~~~~l~iwDTaGqe~~~~l~~~~~----r~a~~~ 74 (190) T cd04144 2 LVVLGDGGVGKTALTIQLCLNHFVETYDPTIEDSY---RKQVVVDGQPCMLEVLDTAGQEEYTALRDQWI----REGEGF 74 (190) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCEEEE---EEEEEECCEEEEEEEEECCCCCHHHHHHHHHH----CCCCEE T ss_conf 78881798428999999870810776466401114---78898715479999974798602468878753----056078 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=. ++.|++.+.+..+. .+-.+|++|||+|.|.. T Consensus 75 ilVyditd~~SF~~-i~~w~~~i~~~~~~----------------------------------~~~~~piilVGNK~DL~ 119 (190) T cd04144 75 ILVYSITSRSTFER-VERFREQIQRVKDE----------------------------------SAADVPIMIVGNKCDKV 119 (190) T ss_pred EEEEECCCHHHHHH-HHHHHHHHHHHHHH----------------------------------CCCCCEEEEEECCCCCC T ss_conf 99987599778999-99999999987420----------------------------------69997899970565333 Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .. |.+--.--+.+|+.+|+..+-+|-+.. .++..+...++ T Consensus 120 ~~-----r~V~~ee~~~~a~~~~~~y~E~SAk~~--~nV~e~F~~l~ 159 (190) T cd04144 120 YE-----REVSTEEGAALARRLGCEFIEASAKTN--VNVERAFYTLV 159 (190) T ss_pred CC-----CCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf 44-----667989999999966991999861589--88789999999 No 73 >cd04159 Arl10_like Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved. Probab=99.29 E-value=5.5e-11 Score=87.71 Aligned_columns=154 Identities=23% Q ss_pred EEEEECCCCCHHHHHHHHCCCC--CCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 8998659886377777552766--78887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDRD--EPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r~--e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|..|+|||||++|+.+.. +.+.||++.++ ++....+. -.++|.+||--.+..+.+.-...-+ .+ T Consensus 2 IvivG~~~vGKTsl~~~~~~~~f~~~~~~Tig~~~---~~i~~~~~---~l~iwDtaGqe~~~~~~~~y~~~a~----~i 71 (159) T cd04159 2 ITLVGLQNSGKTTLVNVIAGGQFSEDTIPTVGFNM---RKVTKGNV---TLKVWDLGGQPRFRSMWERYCRGVN----AI 71 (159) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCEEEEEEEEE---EEEEECCE---EEEEEECCCCHHHHHHHHHHHHCCC----CE T ss_conf 78994289868999998754941653230000279---99884778---9999855873135788987631048----51 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|+|.|.+.++=...++| ++++....-.+ +|++|+|+|.|+- T Consensus 72 i~V~D~td~~s~~~~~~~l--------~~ll~~~~~~~-----------------------------ipili~gNK~Dl~ 114 (159) T cd04159 72 VYVVDAADRTALEAAKNEL--------HDLLEKPSLEG-----------------------------IPLLVLGNKNDLP 114 (159) T ss_pred EEEEECCCHHHHHHHHHHH--------HHHHHCCCCCC-----------------------------CEEEEEECCCCCC T ss_conf 7998548866789999999--------98751037799-----------------------------5799981246842 Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .....+. ++...--..+....-+.+-+|-... ..+-.++..|. T Consensus 115 ~~~~~~e--~~~~~~~~~~~~~~~~~~~~SAktg--~gI~e~f~wL~ 157 (159) T cd04159 115 GALSVDE--LIEQMNLKSITDREVSCYSISCKEK--TNIDIVLDWLI 157 (159) T ss_pred CCCCHHH--HHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 1258889--9999989998518945899861479--88899999985 No 74 >cd04145 M_R_Ras_like M-Ras/R-Ras-like subfamily. This subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, and related members of the Ras family. M-Ras is expressed in lympho-hematopoetic cells. It interacts with some of the known Ras effectors, but appears to also have its own effectors. Expression of mutated M-Ras leads to transformation of several types of cell lines, including hematopoietic cells, mammary epithelial cells, and fibroblasts. Overexpression of M-Ras is observed in carcinomas from breast, uterus, thyroid, stomach, colon, kidney, lung, and rectum. In addition, expression of a constitutively active M-Ras mutant in murine bone marrow induces a malignant mast cell leukemia that is distinct from the monocytic leukemia induced by H-Ras. TC21, along with H-Ras, has been shown to regulate the branching morphogenesis of ureteric bud cell branching in mice. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an ali Probab=99.28 E-value=1.7e-11 Score=90.97 Aligned_columns=154 Identities=17% Q ss_pred EEEEECCCCCHHHHHHHHCCCC--CCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 8998659886377777552766--78887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDRD--EPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r~--e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.|||||++||+... +.+.||++-.|+---.-+++.. ...+|..+|--.+..+...-+..-+. + T Consensus 5 iv~iGd~~VGKTsll~r~~~~~f~~~~~pt~~~~~~k~~~v~~~~~---~l~i~Dt~g~e~~~~~~~~~~~~a~~----~ 77 (164) T cd04145 5 LVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCEIDGQWA---ILDILDTAGQEEFSAMREQYMRTGEG----F 77 (164) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEECCEEE---EEEEEECCCCCHHHHHHHHHHCCCCE----E T ss_conf 9998079954899999987170177657530212788898889489---99885068760012454887238966----8 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=. ++.|++.+.+..+. -.+|+++||+|.|+ T Consensus 78 iivydi~~~~Sf~~-i~~w~~~i~~~~~~------------------------------------~~~piilvGNK~DL- 119 (164) T cd04145 78 LLVFSVTDRGSFEE-VDKFHTQILRVKDR------------------------------------DEFPMILVGNKADL- 119 (164) T ss_pred EEEEECCCHHHHHH-HHHHHHHHHHHCCC------------------------------------CCCEEEEEECCCCC- T ss_conf 99987699657899-99998877753489------------------------------------98479998002580- Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) .++|++.-.-.+.+|..+|+..+.+|-+.. ..+..+..+++ T Consensus 120 ----~~~r~V~~~e~~~~a~~~~~~~~E~SAk~~--~nV~e~F~~i~ 160 (164) T cd04145 120 ----EHQRKVSREEGQELARKLKIPYIETSAKDR--LNVDKAFHDLV 160 (164) T ss_pred ----CCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf ----012205988999999965996999971589--88789999999 No 75 >cd04151 Arl1 Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability. Probab=99.27 E-value=1e-10 Score=86.10 Aligned_columns=153 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHH-CCCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEE Q ss_conf 899865988637777755-2766788875310002211101578711178889715785420211000042351206778 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRC-LDRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLV 112 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rf-l~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~vi 112 (351) |+++|..|+||||||+|+ .++.....||.+..+ .....++. -.++|++||.-.+-.+-+.-... .-.+| T Consensus 2 ililG~~~~GKTsii~r~~~~~~~~~~pT~g~~~---~~i~~~~~---~~~iwD~~Gqe~~r~~~~~y~~~----a~~iI 71 (158) T cd04151 2 ILILGLDNAGKTTILYRLQLGEVVTTIPTIGFNV---ETVTYKNL---KFQVWDLGGQTSIRPYWRCYYSN----TDAII 71 (158) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEE---EEEEECCE---EEEEEECCCCCCCCHHHHHHCCC----CCEEE T ss_conf 7889508986888777664386212003200158---89861781---89997548874342135644037----78799 Q ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCC Q ss_conf 88736984689999999999999999999999852695378999999998414667760011106887799712100015 Q Ver_Hs_NP_0570 113 LVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQ 192 (351) Q Consensus 113 ivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~ 192 (351) +|+|.|...++=+..++| .++++.-.-.+ +|++|+|+|.|.=. T Consensus 72 ~V~D~sd~~~~~~~~~~l--------~~~l~~~~~~~-----------------------------~pilIl~NK~Dl~~ 114 (158) T cd04151 72 YVVDSTDRDRLGTAKEEL--------HAMLEEEELKG-----------------------------AVLLVFANKQDMPG 114 (158) T ss_pred EEEECCCHHHHHHHHHHH--------HHHHHCCCCCC-----------------------------CEEEEEEECCCCCC T ss_conf 998458834689999999--------99972004479-----------------------------88999950678621 Q ss_pred CCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 887667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 193 DFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 193 ~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) ..+.+. |...+..-.....-.-+| +|-... .-+...++.|. T Consensus 115 ~~~~~~---i~~~~~l~~~~~~~~~~~~~SA~tg--~Gi~e~f~wL~ 156 (158) T cd04151 115 ALSEAE---ISEKLGLSELKDRTWSIFKTSAIKG--EGLDEGMDWLV 156 (158) T ss_pred CCCHHH---HHHHHHHHHHHCCCEEEEEEECCCC--CCHHHHHHHHH T ss_conf 379889---9999867887138828998741369--88899999862 No 76 >cd04130 Wrch_1 Wrch-1 subfamily. Wrch-1 (Wnt-1 responsive Cdc42 homolog) is a Rho family GTPase that shares significant sequence and functional similarity with Cdc42. Wrch-1 was first identified in mouse mammary epithelial cells, where its transcription is upregulated in Wnt-1 transformation. Wrch-1 contains N- and C-terminal extensions relative to cdc42, suggesting potential differences in cellular localization and function. The Wrch-1 N-terminal extension contains putative SH3 domain-binding motifs and has been shown to bind the SH3 domain-containing protein Grb2, which increases the level of active Wrch-1 in cells. Unlike Cdc42, which localizes to the cytosol and perinuclear membranes, Wrch-1 localizes extensively with the plasma membrane and endosomes. The membrane association, localization, and biological activity of Wrch-1 indicate an atypical model of regulation distinct from other Rho family GTPases. Most Rho proteins contain a lipid modification site at the C-terminus, Probab=99.27 E-value=1.4e-11 Score=91.55 Aligned_columns=157 Identities=20% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.|.|||||+.||+.. .+.+.||..-.|+.--..++... ...+|.-+|--.+..|.+...+. .-.+ T Consensus 3 ivliGd~~VGKTsLi~r~~~~~F~~~~~~T~~~~~~~~i~i~~~~i---~l~iwDtaGqe~~~~l~~~~~~~----a~~~ 75 (173) T cd04130 3 CVLVGDGAVGKTSLIVSYTTNGYPTEYVPTAFDNFSVVVLVDGKPV---RLQLCDTAGQDEFDKLRPLCYPD----TDVF 75 (173) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCEEE---EEEEEECCCCHHHHHHHHHHCCC----CCEE T ss_conf 8998079843899988876185276533114554347775688679---99984089871256787864479----7748 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=.-.++|+..++.+..+ +|+++||+|.|+- T Consensus 76 ilvydit~~~Sf~~i~~~w~~~i~~~~~~--------------------------------------~piilVGnK~DL~ 117 (173) T cd04130 76 LLCFSVVNPSSFQNISEKWIPEIRKHNPK--------------------------------------APIILVGTQADLR 117 (173) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEECCCCCCH T ss_conf 99954499768999999889999850899--------------------------------------6499971774411 Q ss_pred CCCC-------HHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHH Q ss_conf 5887-------667899999999999860946888-512034567899988875 Q Ver_Hs_NP_0570 192 QDFE-------SEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQL 237 (351) Q Consensus 192 ~~~D-------~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl 237 (351) .+.+ ...|.+-..--+.+|..+|+.-+| +|-+.. .++..+.+.+ T Consensus 118 ~~~~~~~~~~~~~~r~Vs~~e~~~~a~~~~~~~y~EtSAktg--~nV~e~F~~~ 169 (173) T cd04130 118 TDVNVLIQLARYGEKPVSQSRAKALAEKIGACEYIECSALTQ--KNLKEVFDTA 169 (173) T ss_pred HHHHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHH T ss_conf 124566544321477789899999999718950688761478--8878999998 No 77 >pfam00025 Arf ADP-ribosylation factor family. Pfam combines a number of different Prosite families together Probab=99.27 E-value=5.2e-11 Score=87.91 Aligned_columns=155 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEE Q ss_conf 8998659886377777552-766788875310002211101578711178889715785420211000042351206778 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLV 112 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~vi 112 (351) |+++|..|+|||||++|+. ++.+.+.||++..+ ..-..++- -.+||++||-..+..+.+.-....+. +| T Consensus 18 ivllG~~~vGKTsli~r~~~~~~~~~~pTig~~~---~~i~~~~~---~~~iwD~~G~e~~r~l~~~y~~~a~~----iI 87 (176) T pfam00025 18 ILMLGLDNAGKTTILYKLKLGEVVTTIPTIGFNV---ETVTYKNV---KFTVWDVGGQESLRPLWRNYFPNTDG----VI 87 (176) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCEEEEEEEEEE---EEEEECCE---EEEEEECCCCHHHHHHHHHHCCCCCE----EE T ss_conf 9998439986889888764583020220031158---89876583---89998769715689998874125227----99 Q ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCC Q ss_conf 88736984689999999999999999999999852695378999999998414667760011106887799712100015 Q Ver_Hs_NP_0570 113 LVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQ 192 (351) Q Consensus 113 ivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~ 192 (351) +|+|.|.++++=+..++| .++++.-.-.+ +|++|+|+|.|.=. T Consensus 88 ~V~D~sd~~~~~~~~~~l--------~~ll~~~~~~~-----------------------------~pilI~~NK~Dl~~ 130 (176) T pfam00025 88 FVVDSADRDRIEEAKQEL--------HALLNEEELAD-----------------------------APLLIFANKQDLPG 130 (176) T ss_pred EEEECCCCCCHHHHHHHH--------HHHHHCCCCCC-----------------------------CEEEEEEECCCCCC T ss_conf 999648865468999999--------99850014589-----------------------------78999960668877 Q ss_pred CCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 8876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 193 DFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 193 ~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) . -++..-.-.-.|..+++...-..+-+|-... ..+...+..|+ T Consensus 131 ~-~~~~ei~~~~~l~~~~~~~~~~~~~~SAktG--~GI~E~f~wL~ 173 (176) T pfam00025 131 A-MSEAEIRELLGLHELRGSRPWEIQGCSAVTG--EGLYEGLDWLS 173 (176) T ss_pred C-CCHHHHHHHHHHHHHHCCCCEEEEEEEECCC--CCHHHHHHHHH T ss_conf 8-8989999998889872389669998750248--88899999998 No 78 >cd04173 Rnd2_Rho7 Rnd2/Rho7 subfamily. Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd3/RhoE/Rho8. Rnd2/Rho7 is transiently expressed in radially migrating cells in the brain while they are within the subventricular zone of the hippocampus and cerebral cortex. These migrating cells typically develop into pyramidal neurons. Cells that exogenously expressed Rnd2/Rho7 failed to migrate to upper layers of the brain, suggesting that Rnd2/Rho7 plays a role in the radial migration and morphological changes of developing pyramidal neurons, and that Rnd2/Rho7 degradation is necessary for proper cellular migration. The Rnd2/Rho7 GEF Rapostlin is found primarily in the brain and together with Rnd2/Rho7 induces dendrite branching. Unlike Rnd1/Rho6 and Rnd3/RhoE/Rho8, which are RhoA antagonists, Rnd2/Rho7 binds the GEF Pragmin and significantly stimulates RhoA activity and Rho-A mediated cell contraction. Rnd2/Rho7 is also found to be expressed in sperma Probab=99.26 E-value=3.7e-11 Score=88.81 Aligned_columns=152 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||++||... .+.+.||..-.|+..-..++..- ..++|.-+|--.+..|...-... .-.+ T Consensus 4 iVvvGD~~VGKTsLl~~f~~~~F~~~y~PTV~~~~~~~i~vd~~~V---~L~lWDTAGQE~y~~lr~~yYr~----ad~~ 76 (222) T cd04173 4 IVVVGDAECGKTALLQVFAKDAYPGSYVPTVFENYTASFEIDKRRI---ELNMWDTSGSSYYDNVRPLAYPD----SDAV 76 (222) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCEEE---EEEEEECCCCHHHHHHHHHHHCC----CCEE T ss_conf 9997169833788888764371067524415765799999988699---99987348870123444776338----9879 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||+|++.|.++=.-.++|+..++.+.. .+|+++||+|.|+= T Consensus 77 llvFdIt~~~SF~nv~~kW~~ei~~~~p--------------------------------------~~pIILVGnK~DLR 118 (222) T cd04173 77 LICFDISRPETLDSVLKKWQGETQEFCP--------------------------------------NAKVVLVGCKLDMR 118 (222) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCC--------------------------------------CCCEEEECCCCCCC T ss_conf 9998658854789999988899997079--------------------------------------98489980366765 Q ss_pred CCCCHHHHH--------HHHHHHHHHHHHCCCEEEE-EECHHHHHHH-HHHH Q ss_conf 588766789--------9999999999860946888-5120345678-9998 Q Ver_Hs_NP_0570 192 QDFESEKRK--------VICKTLRFVAHYYGASLMF-TSKSEALLLK-IRGV 233 (351) Q Consensus 192 ~~~D~e~rK--------~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r-~r~~ 233 (351) .+ ....++ +--.-=..+|-.+||--++ +|-+.+ .+ ++.+ T Consensus 119 ~D-~~~~~~l~~~~~~pVs~eeg~~lA~~igA~~y~EcSAk~~--~n~V~ev 167 (222) T cd04173 119 TD-LATLRELSKQRLIPVTHEQGTVLAKQVGAVSYVECSSRSS--ERSVRDV 167 (222) T ss_pred CC-HHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEECCCCC--CCCHHHH T ss_conf 89-8899999856899889899999999739821365304579--9667899 No 79 >cd04126 Rab20 Rab20 subfamily. Rab20 is one of several Rab proteins that appear to be restricted in expression to the apical domain of murine polarized epithelial cells. It is expressed on the apical side of polarized kidney tubule and intestinal epithelial cells, and in non-polarized cells. It also localizes to vesico-tubular structures below the apical brush border of renal proximal tubule cells and in the apical region of duodenal epithelial cells. Rab20 has also been shown to colocalize with vacuolar H+-ATPases (V-ATPases) in mouse kidney cells, suggesting a role in the regulation of V-ATPase traffic in specific portions of the nephron. It was also shown to be one of several proteins whose expression is upregulated in human myelodysplastic syndrome (MDS) patients. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bo Probab=99.25 E-value=4.2e-11 Score=88.46 Aligned_columns=155 Identities=20% Q ss_pred EEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEE Q ss_conf 8998659886377777552-766788875310002211101578711178889715785420211000042351206778 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLV 112 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~vi 112 (351) |++||+.+.|||||++||. +......||++.+| .......--.++|-.+|--.+..|...-.+.... +| T Consensus 3 ivliGd~~VGKTsLi~r~~~~~F~~~~~Tig~~~------~~k~~~~~~l~IWDTAGqE~f~~l~~~yyr~a~~----~i 72 (220) T cd04126 3 VVLLGDMNVGKTSLLHRYMERRFKDTVSTVGGAF------YLKQWGPYNISIWDTAGREQFHGLGSMYCRGAAA----VI 72 (220) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEE------EEEEEEEEEEEEEECCCCHHHHHHHHHHCCCCCE----EE T ss_conf 8998079832899988876371057546223568------8872247999997547623545677865058978----99 Q ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCC Q ss_conf 88736984689999999999999999999999852695378999999998414667760011106887799712100015 Q Ver_Hs_NP_0570 113 LVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQ 192 (351) Q Consensus 113 ivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~ 192 (351) ||.|++.+.++ +.++.|+..++..... .+|++|||+|.|+=. T Consensus 73 lVyDit~~~SF-~~i~~~~~~~~~~~~~-------------------------------------~~~iilvGNK~DL~~ 114 (220) T cd04126 73 LTYDVSNVQSL-EELEDRFLGLTDTANE-------------------------------------DCLFAVVGNKLDLTE 114 (220) T ss_pred EEEECCCHHHH-HHHHHHHHHHHHHCCC-------------------------------------CCEEEEEECCCCCCC T ss_conf 99766997788-9999999999983499-------------------------------------958999714634222 Q ss_pred CCCHHH--------------HHHHHHHHHHHHHHCCCE--------------EEEEECHHHHHHHHHHHHHHHH Q ss_conf 887667--------------899999999999860946--------------8885120345678999888750 Q Ver_Hs_NP_0570 193 DFESEK--------------RKVICKTLRFVAHYYGAS--------------LMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 193 ~~D~e~--------------rK~i~r~LR~iAH~yGA~--------------L~FtSk~e~l~~r~r~~inhl~ 238 (351) +.++.. |.+-..-.+.+|..++.. -+.||-+.. ..+-.+..+++ T Consensus 115 ~~~~~~~~~~~~~~~~~e~~r~V~~ee~~~~a~~~~~~~~~~~~~~~~~~~~y~EtSAKtg--~nV~e~F~~l~ 186 (220) T cd04126 115 EGALAGQEKDAGDRVSPEDQRQVTLEDAKAFYKRINKYKMLDEDLSPAAEKMCFETSAKTG--YNVDELFEYLF 186 (220) T ss_pred CCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHCCCCCCCHHCCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf 2211222211111123100045678999999998522100000000103753689751578--78889999999 No 80 >cd04160 Arfrp1 Arfrp1 subfamily. Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development. Probab=99.24 E-value=1.4e-10 Score=85.15 Aligned_columns=157 Identities=25% Q ss_pred EEEEEECCCCCHHHHHHHHCCCCCCCC--------CCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCC Q ss_conf 589986598863777775527667888--------753100022111015787111788897157854202110000423 Q Ver_Hs_NP_0570 33 FVFFIGSKNGGKTTIILRCLDRDEPPK--------PTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGD 104 (351) Q Consensus 33 ~v~~vGsk~~GKTTli~Rfl~r~e~~K--------PTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~ 104 (351) +|+++|..|+|||||++|+-.+....+ ||++.++ .+...++. -.++|.+||-..+..+.+.-... T Consensus 1 ~IvliG~~~~GKTsll~rl~~~~~~~~~~~~~~~~~T~g~~~---~~i~~~~~---~l~iwD~~Gqe~~~~~~~~y~~~- 73 (167) T cd04160 1 SVLILGLDNAGKTTFLEQLKTLFSKYKGLPPSKITPTVGLNI---GTIEVGNA---RLKFWDLGGQESLRSLWDKYYAE- 73 (167) T ss_pred CEEEEECCCCCHHHHHHHHHHHCCCCCCCCCCCEEEEEEEEE---EEEEECCE---EEEEEECCCCHHHHHHHHHHCCC- T ss_conf 978995189868999999852024456754440333554589---88888788---99998468740467767641579- Q ss_pred CCCEEEEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEE Q ss_conf 51206778887369846899999999999999999999998526953789999999984146677600111068877997 Q Ver_Hs_NP_0570 105 TLRTFSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVII 184 (351) Q Consensus 105 ~l~~~~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIV 184 (351) .-.+|+|+|.|.+.++=++.++| +++++.-.-.+ +|++|+ T Consensus 74 ---a~~ii~VvD~sd~~~~~~~~~~l--------~~~l~~~~~~~-----------------------------~Pili~ 113 (167) T cd04160 74 ---CHAIIYVIDSTDRERFEESKSAL--------EKVLRNEALEG-----------------------------VPLLIL 113 (167) T ss_pred ---CCEEEEEEECCCCCCHHHHHHHH--------HHHHHCCCCCC-----------------------------CEEEEE T ss_conf ---86799997448753568899999--------99972215589-----------------------------779998 Q ss_pred CCEECCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 121000158876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 185 GSKYDVFQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 185 g~KYD~F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) |+|.|.=.....|.-+-+..-.-..++...-..+-+|-... ..+...+.-|+ T Consensus 114 ~NK~Dl~~~~~~eei~~~l~~~~~~~~~r~~~~~~~SA~tG--~Gv~e~f~wL~ 165 (167) T cd04160 114 ANKQDLPDALSVEEIKEVFQDKAEEIGRRDCLVLPVSALEG--TGVREGIEWLV 165 (167) T ss_pred ECCCCCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 34879531237889999999889987408917999851368--88899999984 No 81 >cd04174 Rnd1_Rho6 Rnd1/Rho6 subfamily. Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2/Rho7 and Rnd3/RhoE/Rho8. Rnd1/Rho6 binds GTP but does not hydrolyze it to GDP, indicating that it is constitutively active. In rat, Rnd1/Rho6 is highly expressed in the cerebral cortex and hippocampus during synapse formation, and plays a role in spine formation. Rnd1/Rho6 is also expressed in the liver and in endothelial cells, and is upregulated in uterine myometrial cells during pregnancy. Like Rnd3/RhoE/Rho8, Rnd1/Rho6 is believed to function as an antagonist to RhoA. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation. Probab=99.23 E-value=2.7e-11 Score=89.65 Aligned_columns=142 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |++||+.+.|||||+.||... .+.+.||.+-.|+-.-..+++.- -.++|.-+|.-.+..|...... .+-++ T Consensus 16 iVlVGD~~VGKTsLl~~~~~~~F~~~y~pTv~~~y~~~i~v~~~~v---~L~lWDTAGQE~y~~lrplyYr----~ad~~ 88 (232) T cd04174 16 LVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTAGLETEEQRV---ELSLWDTSGSPYYDNVRPLCYS----DSDAV 88 (232) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCEEE---EEEEEECCCCHHHHHHHHHHCC----CCCEE T ss_conf 9998359713889998874372276514427765799998879589---9988526898035678785235----64679 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||+|++.|+++=.-+.+|+..++.+... +|+++||+|.|+= T Consensus 89 llvFdit~~~Sfenv~~kW~~Ei~~~~p~--------------------------------------~pIiLVGnK~DLR 130 (232) T cd04174 89 LLCFDISRPETVDSALKKWKAEIMDYCPS--------------------------------------TRILLIGCKTDLR 130 (232) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCC T ss_conf 99975487457888898306889872789--------------------------------------7189984465554 Q ss_pred CCCCHHHHHHHHHHHH--------HHHHHCCCEEEE-EE Q ss_conf 5887667899999999--------999860946888-51 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLR--------FVAHYYGASLMF-TS 221 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR--------~iAH~yGA~L~F-tS 221 (351) .+ .....+.-.+-.| .+|-.+||..|+ +| T Consensus 131 ~d-~~~~~~L~~~~~~pVt~eeG~~~Ak~iga~~Y~EcS 168 (232) T cd04174 131 TD-LSTLMELSNQKQAPISYEQGCALAKQLGAEVYLECS 168 (232) T ss_pred CC-HHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEC T ss_conf 79-889999985689887989999999973981788730 No 82 >cd01893 Miro1 Miro1 subfamily. Miro (mitochondrial Rho) proteins have tandem GTP-binding domains separated by a linker region containing putative calcium-binding EF hand motifs. Genes encoding Miro-like proteins were found in several eukaryotic organisms. This CD represents the N-terminal GTPase domain of Miro proteins. These atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. Most Rho proteins contain a lipid modification site at the C-terminus; however, Miro is one of few Rho subfamilies that lack this feature. Probab=99.23 E-value=1e-10 Score=86.08 Aligned_columns=156 Identities=19% Q ss_pred EEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEE Q ss_conf 8998659886377777552-766788875310002211101578711178889715785420211000042351206778 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLV 112 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~vi 112 (351) |++||+.+.|||||++||. +......|++.=+|+....-.+++- ..++|-.+|.-....+....++. .-.++ T Consensus 3 ivliGd~~VGKTsL~~rf~~~~F~~~~~~t~~~~~~~~~~~~~~v---~l~iwDtagqe~~~~~~~~~~~~----a~~~i 75 (166) T cd01893 3 IVLIGDEGVGKSSLIMSLVSEEFPENVPRVLPEITIPADVTPERV---PTTIVDTSSRPQDRANLAAEIRK----ANVIC 75 (166) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCEEEEEEEEEECCCEE---EEEEEECCCCCCCHHHHHHHHCC----CCEEE T ss_conf 899807983388998887548006665651035799899718568---99998725887505667876138----98899 Q ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCC Q ss_conf 88736984689999999999999999999999852695378999999998414667760011106887799712100015 Q Ver_Hs_NP_0570 113 LVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQ 192 (351) Q Consensus 113 ivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~ 192 (351) ||.|++.++++=.-.++|++.+|...++ +|++|||+|+|+=. T Consensus 76 ivydi~~~~Sf~~i~~~W~~~i~~~~~~--------------------------------------~piilVGNK~DL~~ 117 (166) T cd01893 76 LVYSVDRPSTLERIRTKWLPLIRRLGVK--------------------------------------VPIILVGNKSDLRD 117 (166) T ss_pred EEEECCCHHHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEEECCCCCCC T ss_conf 9986488678788998879999751689--------------------------------------57999715764223 Q ss_pred CCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 887667899999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 193 DFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 193 ~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) +....... .+.+-..+-......+| +|-+.. .++..+-.+.+ T Consensus 118 ~~~~~~~e--~~~~~~~~~~~~i~~~~EtSAkt~--~nV~e~F~~a~ 160 (166) T cd01893 118 GSSQAGLE--EEMLPIMNEFREIETCVECSAKTL--INVSEVFYYAQ 160 (166) T ss_pred CCCCCHHH--HHHHHHHHHHCCCCEEEEEEECCC--CCHHHHHHHHH T ss_conf 54210147--899999997427750788750368--88789999999 No 83 >KOG0078 GTP-binding protein SEC4, small G protein superfamily, and related Ras family GTP-binding proteins [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport] Probab=99.22 E-value=3.5e-11 Score=88.95 Aligned_columns=154 Identities=25% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|..++|||+++.||.+. ...+.-|+++|| .+|....+. .+...-+|--+|..-+-.++.--.+. .+-+ T Consensus 15 illiGDs~vGKt~~l~rf~d~~f~~~~~sTiGIDF-k~kti~l~g-~~i~lQiWDtaGQerf~ti~~sYyrg----A~gi 88 (207) T KOG0078 15 LLLIGDSGVGKTCLLLRFSDDSFNTSFISTIGIDF-KIKTIELDG-KKIKLQIWDTAGQERFRTITTAYYRG----AMGI 88 (207) T ss_pred EEEEECCCCCCHHHHEEEECCCCCCCCCEEEEEEE-EEEEEEECC-EEEEEEEEECCCCHHHHHHHHHHHHH----CCEE T ss_conf 99983588660132100003667888650788656-788887288-36899997315431467788988744----0705 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) ++|.|++...+.-...- |++.++.|.+. ++|+++||+|.|.. T Consensus 89 ~LvyDitne~Sfeni~~-W~~~I~e~a~~-------------------------------------~v~~iLvGNK~D~~ 130 (207) T KOG0078 89 LLVYDITNEKSFENIRN-WIKNIDEHASD-------------------------------------DVVKILVGNKCDLE 130 (207) T ss_pred EEEEEECCHHHHHHHHH-HHHHHHHHCCC-------------------------------------CCCEEEECCCCCCC T ss_conf 89998246166654689-99999751799-------------------------------------85189861765723 Q ss_pred CCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 58876678999999999998609468885120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r~r~~inhl~ 238 (351) . +|.+-..--..+|+.||...+.+|-+.+ .++-..+.+|+ T Consensus 131 ~-----~R~V~~e~ge~lA~e~G~~F~EtSAk~~--~NI~eaF~~La 170 (207) T KOG0078 131 E-----KRQVSKERGEALAREYGIKFFETSAKTN--FNIEEAFLSLA 170 (207) T ss_pred C-----CCCCCHHHHHHHHHHHCCCEEEECCCCC--CCHHHHHHHHH T ss_conf 5-----7630679999999980994588646778--85889999999 No 84 >cd00878 Arf_Arl Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thu Probab=99.22 E-value=3e-11 Score=89.36 Aligned_columns=110 Identities=25% Q ss_pred EEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEE Q ss_conf 8998659886377777552-766788875310002211101578711178889715785420211000042351206778 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLV 112 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~vi 112 (351) |+++|..|+|||||++|+. +..+.+.||.+..| .....++. -.|||.++|...+..+.+.-....+ .+| T Consensus 2 iviiG~~~vGKTsli~~~~~~~~~~~~pTig~~~---~~i~~~~~---~~~i~D~~G~~~~~~l~~~y~~~a~----~iI 71 (158) T cd00878 2 ILILGLDGAGKTTILYKLKLGEVVTTIPTIGFNV---ETVEYKNV---SFTVWDVGGQDKIRPLWKHYYENTN----GII 71 (158) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCEEEEEEEEE---EEEECCCE---EEEEEECCCCCCCHHHHHHHCCCCC----EEE T ss_conf 7888439987899999986482331220254268---88530414---8999865898520467786614898----179 Q ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 887369846899999999999999999999998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 113 LVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 113 ivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) +|+|.|.+.++=...+++ +++++....++ +|++|+|+|+|. T Consensus 72 ~V~D~sd~~s~~~~~~~~--------~~~~~~~~~~~-----------------------------~pili~~NK~Dl 112 (158) T cd00878 72 FVVDSSDRERIEEAKEEL--------HKLLNEEELKG-----------------------------VPLLIFANKQDL 112 (158) T ss_pred EEEECCCCCCHHHHHHHH--------HHHHHHCCCCC-----------------------------CEEEEEEECCCC T ss_conf 998437765578999999--------99852114489-----------------------------436755401165 No 85 >cd04154 Arl2 Arl2 subfamily. Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis. Probab=99.22 E-value=5.9e-11 Score=87.54 Aligned_columns=136 Identities=22% Q ss_pred CCEEEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 7458998659886377777552-766788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 31 EKFVFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 31 ek~v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) |-.|+++|..|+|||||++|+. +..+...||++..+ ..-..++. ..++|++||-..+-.+.+.-....+ T Consensus 14 ~~kIliiG~~~~GKTsil~~l~~~~~~~~~pT~G~~~---~~i~~~~~---~l~iwD~~Gqe~~r~~~~~y~~~a~---- 83 (173) T cd04154 14 EMRILILGLDNAGKTTILKKLLGEDIDTISPTLGFQI---KTLEYEGY---KLNIWDVGGQKTLRPYWRNYFESTD---- 83 (173) T ss_pred CEEEEEEECCCCCHHHHHHHHHCCCCCCEEEEEEEEE---EEEEECCE---EEEEEECCCCHHHHHHHHHHCCCCC---- T ss_conf 7389999508987899888872895460342352168---88898588---9999875875036766553124677---- Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .+|+|+|.|.+.++=++..+|.+.+...... ++|++|+|+|.| T Consensus 84 ~iI~VvD~sd~~~~~~~~~~l~~ll~~~~~~-------------------------------------~~pilI~~NK~D 126 (173) T cd04154 84 ALIWVVDSSDRLRLDDCKRELKELLQEERLA-------------------------------------GATLLILANKQD 126 (173) T ss_pred EEEEEEECCCCCCHHHHHHHHHHHHCCHHHC-------------------------------------CCEEEEEEECCC T ss_conf 7999975388544688999999874023117-------------------------------------968999972558 Q ss_pred CCCCCCHHHHHHHHHHHHHHHHHC Q ss_conf 015887667899999999999860 Q Ver_Hs_NP_0570 190 VFQDFESEKRKVICKTLRFVAHYY 213 (351) Q Consensus 190 ~F~~~D~e~rK~i~r~LR~iAH~y 213 (351) .-...+.+.-.-...--+...|.+ T Consensus 127 l~~~~~~~ei~~~l~l~~~~~~~~ 150 (173) T cd04154 127 LPGALSEEEIREALELDKISSHHW 150 (173) T ss_pred CCCCCCHHHHHHHHHHHHHCCCCE T ss_conf 854579899999987786427965 No 86 >cd04142 RRP22 RRP22 subfamily. RRP22 (Ras-related protein on chromosome 22) subfamily consists of proteins that inhibit cell growth and promote caspase-independent cell death. Unlike most Ras proteins, RRP22 is down-regulated in many human tumor cells due to promoter methylation. RRP22 localizes to the nucleolus in a GTP-dependent manner, suggesting a novel function in modulating transport of nucleolar components. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Like most Ras family proteins, RRP22 is farnesylated. Probab=99.21 E-value=1.5e-10 Score=85.01 Aligned_columns=157 Identities=20% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCC-HHHHHHHCCCCCCCEEEEEEE--------ECCCCCHHHCEEEEEC Q ss_conf 899865988637777755276--67888753100-022111015787111788897--------1578542021100004 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALE-YTYGRRAKGHNTPKDIAHFWE--------LGGGTSLLDLISIPIT 102 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALe-YtygRra~~~~~~KdvaH~WE--------LGgg~~ls~Li~ipit 102 (351) |+++|+.|.|||+|++||+.. .+.+.||.+-+ |+..-..+++.. -.++|- ...|.+..++..-.+ T Consensus 3 VvilGd~gVGKTsli~Rf~~~~F~~~y~pTig~~~~~k~i~vdg~~~---~L~IwDt~~~~~~~~tagqE~~~~r~r~l- 78 (198) T cd04142 3 VAVLGAPGVGKTAIVRQFLAQEFPEEYIPTEHRRLYRPAVVLSGRVY---DLHILDVPNMQRYPGTAGQEWMDPRFRGL- 78 (198) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEECCEEE---EEEEEECCCCCCCCCCCCHHHHHHHHHHC- T ss_conf 89981898418999988761743776356421014687898989799---99984144311145655301111222101- Q ss_pred CCCCCEEEEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEE Q ss_conf 23512067788873698468999999999999999999999985269537899999999841466776001110688779 Q Ver_Hs_NP_0570 103 GDTLRTFSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLV 182 (351) Q Consensus 103 ~~~l~~~~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlv 182 (351) -..-.++||.|.+.+.++ +.++.|.+.+.+.. ....--+|++ T Consensus 79 ---r~ad~~ilVydIt~~~SF-~~v~~~~~~i~~~~----------------------------------~~~~~~~piv 120 (198) T cd04142 79 ---RNSRAFILVYDICSPDSF-HYVKLLRQQILETR----------------------------------PAGNKEPPIV 120 (198) T ss_pred ---CCCCEEEEEEECCCHHHH-HHHHHHHHHHHHHC----------------------------------CCCCCCCEEE T ss_conf ---278679999867996688-99999999999851----------------------------------3589996799 Q ss_pred EECCEECCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE-EECHHHHHHH--HHHHHHHH Q ss_conf 9712100015887667899999999999860946888-5120345678--99988875 Q Ver_Hs_NP_0570 183 IIGSKYDVFQDFESEKRKVICKTLRFVAHYYGASLMF-TSKSEALLLK--IRGVINQL 237 (351) Q Consensus 183 IVg~KYD~F~~~D~e~rK~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r--~r~~inhl 237 (351) |||+|.|+ .+.|.+-......+|...++..+| ||-+++.... |..++... T Consensus 121 LVGNK~DL-----~~~R~v~~e~~~~~a~~~~~~~f~EtSAK~~~NV~elF~~lvr~~ 173 (198) T cd04142 121 VVGNKRDQ-----QRHRFAPRHVLSVLVRKSWKCGYLECSAKYNWHILLLFKELLISA 173 (198) T ss_pred EEECCCCC-----CCCCCCCHHHHHHHHHHHCCCCEEEEECCCCCCHHHHHHHHHHHH T ss_conf 98247652-----115526789999999982797379986137988889999999998 No 87 >cd01871 Rac1_like Rac1-like subfamily. The Rac1-like subfamily consists of Rac1, Rac2, and Rac3 proteins, plus the splice variant Rac1b that contains a 19-residue insertion near switch II relative to Rac1. While Rac1 is ubiquitously expressed, Rac2 and Rac3 are largely restricted to hematopoietic and neural tissues respectively. Rac1 stimulates the formation of actin lamellipodia and membrane ruffles. It also plays a role in cell-matrix adhesion and cell anoikis. In intestinal epithelial cells, Rac1 is an important regulator of migration and mediates apoptosis. Rac1 is also essential for RhoA-regulated actin stress fiber and focal adhesion complex formation. In leukocytes, Rac1 and Rac2 have distinct roles in regulating cell morphology, migration, and invasion, but are not essential for macrophage migration or chemotaxis. Rac3 has biochemical properties that are closely related to Rac1, such as effector interaction, nucleotide binding, and hydrolysis; Rac2 has a slower nucleoti Probab=99.17 E-value=1.4e-10 Score=85.21 Aligned_columns=158 Identities=20% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |.++|+.+.|||||++||+.. .+.+.||++-.|+---..++..- -.++|--+|.-.+..|-..-++.. -.+ T Consensus 4 ivliGd~~VGKTsl~~r~~~~~f~~~~~pti~~~~~~~i~vd~~~v---~l~iwDTaGqe~~~~l~~~~~~~a----~~~ 76 (174) T cd01871 4 CVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPV---NLGLWDTAGQEDYDRLRPLSYPQT----DVF 76 (174) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCCCE---EEECCCCCCHHHHHHHHHHHCCCC----CEE T ss_conf 8997279843899999876173376525213111466457748602---650267874035667766431799----779 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++=.--.+|+..++.+..+ +|+++||+|+|+- T Consensus 77 ilvydvt~~~Sf~~i~~~w~~~i~~~~~~--------------------------------------~piiLVGnK~Dl~ 118 (174) T cd01871 77 LICFSLVSPASFENVRAKWYPEVRHHCPN--------------------------------------TPIILVGTKLDLR 118 (174) T ss_pred EEEEECCCCCHHHHHHHHHHHHHHHHCCC--------------------------------------CEEEEECCCCCCH T ss_conf 99975688002789999889999961799--------------------------------------6599962431211 Q ss_pred CCCCHHHHH-------HHHHHHHHHHHHCCCEEEE-EECHHHHHHHHHHHHHHHH Q ss_conf 588766789-------9999999999860946888-5120345678999888750 Q Ver_Hs_NP_0570 192 QDFESEKRK-------VICKTLRFVAHYYGASLMF-TSKSEALLLKIRGVINQLA 238 (351) Q Consensus 192 ~~~D~e~rK-------~i~r~LR~iAH~yGA~L~F-tSk~e~l~~r~r~~inhl~ 238 (351) ++.....+- +...--+.+|..+|+--+| +|-+.. .++..+...+. T Consensus 119 ~~~~~~~~~~~~~~~~vs~~eg~~~a~~~~~~~f~E~SAkt~--~nV~e~F~~li 171 (174) T cd01871 119 DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQ--KGLKTVFDEAI 171 (174) T ss_pred HHHHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEECCCC--CCHHHHHHHHH T ss_conf 004577777641466457889999999728950688641578--77789999998 No 88 >cd04147 Ras_dva Ras-dva subfamily. Ras-dva (Ras - dorsal-ventral anterior localization) subfamily consists of a set of proteins characterized only in Xenopus leavis, to date. In Xenopus Ras-dva expression is activated by the transcription factor Otx2 and begins during gastrulation throughout the anterior ectoderm. Ras-dva expression is inhibited in the anterior neural plate by factor Xanf1. Downregulation of Ras-dva results in head development abnormalities through the inhibition of several regulators of the anterior neural plate and folds patterning, including Otx2, BF-1, Xag2, Pax6, Slug, and Sox9. Downregulation of Ras-dva also interferes with the FGF-8a signaling within the anterior ectoderm. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Probab=99.16 E-value=3.2e-10 Score=82.97 Aligned_columns=156 Identities=22% Q ss_pred EEEEECCCCCHHHHHHHHCCC--CCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 899865988637777755276--678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDR--DEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r--~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|+.+.|||||+.||+.. .+.+.||++--| ++.---+..+=..++|.-+|--.+..|...-++. .-.+ T Consensus 2 IvllGd~~VGKTsLi~rf~~~~F~~~y~~Ti~~~~---~k~~~v~~~~v~l~iwDTaGqe~f~~l~~~~~r~----a~~~ 74 (198) T cd04147 2 LVFMGAAGVGKTALIQRFLYDTFEPKYRRTVEEMH---RKEYEVGGVSLTLDILDTSGSYSFPAMRKLSIQN----SDAF 74 (198) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCCE---EEEEEECCEEEEEEEECCCCHHHHHHHHHHHHCC----CCCE T ss_conf 78881798328999988761810775232200104---6789888968999973287703323476776237----8807 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCC Q ss_conf 88873698468999999999999999999999985269537899999999841466776001110688779971210001 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVF 191 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F 191 (351) +||.|++.+.++ +.++.|+..+.+.-. +-.+|++|||+|+|.- T Consensus 75 ilVyDit~~~SF-~~v~~w~~~i~~~~~------------------------------------~~~~pivLVGNK~Dll 117 (198) T cd04147 75 ALVYAVDDPESF-EEVERLREEILEVKE------------------------------------DKFVPIVVVGNKADSL 117 (198) T ss_pred EEEEECCCHHHH-HHHHHHHHHHHHHCC------------------------------------CCCCEEEEEECCCCCC T ss_conf 999864797789-999999999998518------------------------------------9998899972267662 Q ss_pred CCCCHHHHHHHHHHHHHHHH-HCCCEEEEEECHHHHHHH--HHHHHHHH Q ss_conf 58876678999999999998-609468885120345678--99988875 Q Ver_Hs_NP_0570 192 QDFESEKRKVICKTLRFVAH-YYGASLMFTSKSEALLLK--IRGVINQL 237 (351) Q Consensus 192 ~~~D~e~rK~i~r~LR~iAH-~yGA~L~FtSk~e~l~~r--~r~~inhl 237 (351) .+ .|.+-..--+..|. .||+.-+-+|-++..... |..++.+. T Consensus 118 ~~----~R~V~~~e~~~~a~~~~~~~f~EtSAk~g~nV~e~F~~l~rei 162 (198) T cd04147 118 EE----ERQVPAKDALSTVELDWNCGFVETSAKDNENVLEVFKELLRQA 162 (198) T ss_pred CC----CCCCCHHHHHHHHHHHCCCCEEEEECCCCCCHHHHHHHHHHHH T ss_conf 21----6746789999999984799389985147888789999999974 No 89 >smart00177 ARF ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop). Probab=99.13 E-value=2.5e-10 Score=83.56 Aligned_columns=121 Identities=21% Q ss_pred CCEEEEEECCCCCHHHHHHHH-CCCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 745899865988637777755-2766788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 31 EKFVFFIGSKNGGKTTIILRC-LDRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 31 ek~v~~vGsk~~GKTTli~Rf-l~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) |-.|+++|..++|||||++|+ .+......||.+..+ .....++. ..++|.+||-..+-.+.+.-.+... T Consensus 17 ~~kiviiG~~~~GKTtil~~l~~~~~~~~~pTvg~~~---~~i~~~~~---~l~iwD~~Gqe~~r~lw~~Yy~~a~---- 86 (181) T smart00177 17 EMRILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNV---ETVTYKNI---SFTVWDVGGQDKIRPLWRHYYTNTQ---- 86 (181) T ss_pred CEEEEEEEECCCCHHHHHHHHHCCCCCEEEEEECCCE---EEEEECCE---EEEEEECCCCHHHHHHHHHHCCCCC---- T ss_conf 0689998518987899999875287330220000103---56641435---9999874873457888887606896---- Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .+|+|+|.|...++=+..++|...+... +...+|++|+|+|.| T Consensus 87 ~iI~VvD~sd~~~~~~~~~~l~~~l~~~-------------------------------------~~~~~pilIl~NK~D 129 (181) T smart00177 87 GLIFVVDSNDRDRIDEAREELHRMLNED-------------------------------------ELRDAVILVFANKQD 129 (181) T ss_pred EEEEEEECCCHHHHHHHHHHHHHHHCCC-------------------------------------CCCCCEEEEEECCCC T ss_conf 8999986588334899999999985020-------------------------------------227978999950558 Q ss_pred CCCCCCHHH Q ss_conf 015887667 Q Ver_Hs_NP_0570 190 VFQDFESEK 198 (351) Q Consensus 190 ~F~~~D~e~ 198 (351) .=.....+. T Consensus 130 l~~~~~~~e 138 (181) T smart00177 130 LPDAMKAAE 138 (181) T ss_pred CCCCCCHHH T ss_conf 302179999 No 90 >cd04149 Arf6 Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed t Probab=99.12 E-value=1.4e-10 Score=85.22 Aligned_columns=113 Identities=26% Q ss_pred CCEEEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 7458998659886377777552-766788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 31 EKFVFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 31 ek~v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) |-.|+++|..|+||||||+|+. +......||.+..+ .....++. -.++|++||...+-.+.+.-.+.... T Consensus 9 ~~kililGl~~sGKTtil~~l~~~~~~~~~pTvg~~~---~~~~~~~~---~l~iwD~~Gqe~~r~lw~~Yy~~a~~--- 79 (168) T cd04149 9 EMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNV---ETVTYKNV---KFNVWDVGGQDKIRPLWRHYYTGTQG--- 79 (168) T ss_pred CEEEEEEEECCCCHHHHHHHHHCCCCCEEEEEEEEEE---EEEEECCE---EEEEEECCCCHHHHHHHHHHCCCCCE--- T ss_conf 0589998508987889887764386102430012478---89874472---89998728713567765865068877--- Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) +|.|+|.|...++=++.++| .++++.-.-.+ +|++|+|+|.| T Consensus 80 -iifVvD~sd~~~l~~~~~~l--------~~~l~~~~~~~-----------------------------~pili~~NK~D 121 (168) T cd04149 80 -LIFVVDSADRDRIDEARQEL--------HRIINDREMRD-----------------------------ALLLVFANKQD 121 (168) T ss_pred -EEEEEECCCCCCHHHHHHHH--------HHHHCCCCCCC-----------------------------CEEEEEEECCC T ss_conf -99998257732278899999--------99851313279-----------------------------78999961568 Q ss_pred C Q ss_conf 0 Q Ver_Hs_NP_0570 190 V 190 (351) Q Consensus 190 ~ 190 (351) . T Consensus 122 l 122 (168) T cd04149 122 L 122 (168) T ss_pred C T ss_conf 8 No 91 >cd04157 Arl6 Arl6 subfamily. Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that A Probab=99.12 E-value=1.6e-10 Score=84.81 Aligned_columns=113 Identities=21% Q ss_pred EEEEEECCCCCHHHHHHHH---CCCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 5899865988637777755---2766788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 33 FVFFIGSKNGGKTTIILRC---LDRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 33 ~v~~vGsk~~GKTTli~Rf---l~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) ||+++|..|+|||||++|+ -.+.+...||.+..+ .+...++. -.+||++||-..+-.|.+.-..... T Consensus 1 ~ivilGl~~aGKTtil~~l~~~~~~~~~~~pTig~~~---~~~~~~~~---~~~iwD~~G~~~~r~l~~~y~~~a~---- 70 (162) T cd04157 1 NILVVGLDNSGKTTIINQLKPENAQSQIIVPTVGFNV---ESFEKGNL---SFTAFDMSGQGKYRGLWEHYYKNIQ---- 70 (162) T ss_pred CEEEEEECCCCHHHHHHHHHCCCCCCCEEEEEEEEEE---EEEEECCE---EEEEEEECCCCCHHHHHHHHCCCCC---- T ss_conf 9788950898688888766157730114765552026---88860868---9999870687201467787515655---- Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .+|.|+|.|.+.++=..-+++ +++++.-.-++. -+|++|+|+|.| T Consensus 71 ~iI~VvDssd~~~~~~~~~~l--------~~ll~~~~~~~~---------------------------~~PiLI~~NK~D 115 (162) T cd04157 71 GIIFVIDSSDRLRLVVVKDEL--------ELLLNHPDIKHR---------------------------RVPILFFANKMD 115 (162) T ss_pred EEEEEEECCCHHHHHHHHHHH--------HHHHCCCCCCCC---------------------------CCEEEEEECCCC T ss_conf 899998568844689999999--------998503232689---------------------------826999972679 Q ss_pred C Q ss_conf 0 Q Ver_Hs_NP_0570 190 V 190 (351) Q Consensus 190 ~ 190 (351) . T Consensus 116 l 116 (162) T cd04157 116 L 116 (162) T ss_pred C T ss_conf 8 No 92 >cd04150 Arf1_5_like Arf1-Arf5-like subfamily. This subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents Probab=99.11 E-value=2.6e-10 Score=83.47 Aligned_columns=118 Identities=23% Q ss_pred EEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEE Q ss_conf 8998659886377777552-766788875310002211101578711178889715785420211000042351206778 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLV 112 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~vi 112 (351) |+++|..++|||||++|+. +......||.+... .....++. ..++|++||...+-.+.+.-... .-.+| T Consensus 3 iv~lG~~~~GKTtii~~~~~~~~~~~~pTvg~~~---~~i~~~~~---~l~iwD~~Gqe~~r~~w~~y~~~----~~~iI 72 (159) T cd04150 3 ILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNV---ETVEYKNI---SFTVWDVGGQDKIRPLWRHYFQN----TQGLI 72 (159) T ss_pred EEEEEECCCCHHHHHHHHHCCCEEEEECCEEEEE---EEEEECCE---EEEEEECCCCHHHHHHHHHHCCC----CCEEE T ss_conf 8999408986888777653376001102200158---88750671---89998758723567888986279----97799 Q ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCC Q ss_conf 88736984689999999999999999999999852695378999999998414667760011106887799712100015 Q Ver_Hs_NP_0570 113 LVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQ 192 (351) Q Consensus 113 ivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~ 192 (351) +|+|.|...++=++.+.| +++++.-.-.+ +|++|+|+|.|.=. T Consensus 73 ~VvD~sd~~~~~~~~~~l--------~~~l~~~~~~~-----------------------------~pili~~NK~Dl~~ 115 (159) T cd04150 73 FVVDSNDRERIGEAREEL--------QRMLNEDELRD-----------------------------AVLLVFANKQDLPN 115 (159) T ss_pred EEEECCCHHHHHHHHHHH--------HHHHCCCCCCC-----------------------------CEEEEEECCCCCCC T ss_conf 998548834689999999--------99842302169-----------------------------78999960568642 Q ss_pred CCCHHH Q ss_conf 887667 Q Ver_Hs_NP_0570 193 DFESEK 198 (351) Q Consensus 193 ~~D~e~ 198 (351) ....+. T Consensus 116 ~~~~~e 121 (159) T cd04150 116 AMSAAE 121 (159) T ss_pred CCCHHH T ss_conf 579899 No 93 >cd04158 ARD1 ARD1 subfamily. ARD1 (ADP-ribosylation factor domain protein 1) is an unusual member of the Arf family. In addition to the C-terminal Arf domain, ARD1 has an additional 46-kDa N-terminal domain that contains a RING finger domain, two predicted B-Boxes, and a coiled-coil protein interaction motif. This domain belongs to the TRIM (tripartite motif) or RBCC (RING, B-Box, coiled-coil) family. Like most Arfs, the ARD1 Arf domain lacks detectable GTPase activity. However, unlike most Arfs, the full-length ARD1 protein has significant GTPase activity due to the GAP (GTPase-activating protein) activity exhibited by the 46-kDa N-terminal domain. The GAP domain of ARD1 is specific for its own Arf domain and does not bind other Arfs. The rate of GDP dissociation from the ARD1 Arf domain is slowed by the adjacent 15 amino acids, which act as a GDI (GDP-dissociation inhibitor) domain. ARD1 is ubiquitously expressed in cells and localizes to the Golgi and to the lysosomal membra Probab=99.09 E-value=1.1e-09 Score=79.69 Aligned_columns=140 Identities=24% Q ss_pred EEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEE Q ss_conf 8998659886377777552-766788875310002211101578711178889715785420211000042351206778 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLV 112 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~vi 112 (351) |+++|-.|+|||||++|+. +....+.||++... .....++. ..++|++||...+-.+-+--.....- +| T Consensus 2 IliiGl~~aGKTtil~~l~~~~~~~~~pTvG~~~---~~i~~~~~---~l~iwD~gG~~~~r~~w~~Yy~~~~g----iI 71 (169) T cd04158 2 VVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNV---ETVEYKNL---KFTIWDVGGKHKLRPLWKHYYLNTQA----VV 71 (169) T ss_pred EEEEEECCCCHHHHHHHHHCCCCCCEEEEECEEE---EEEEECCE---EEEEEECCCCCHHHHHHHHHHCCCCE----EE T ss_conf 8899627986899888885583143121012068---88874574---99998738874025778875047668----99 Q ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCC Q ss_conf 88736984689999999999999999999999852695378999999998414667760011106887799712100015 Q Ver_Hs_NP_0570 113 LVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQ 192 (351) Q Consensus 113 ivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~ 192 (351) .|+|.|...++=++.++| .++++.-.-.+ +|++|+|+|.|.=. T Consensus 72 fVvDssd~~~~~e~~~~l--------~~ll~~~~~~~-----------------------------~piLi~aNK~Dl~~ 114 (169) T cd04158 72 FVVDSSHRDRVSEAHSEL--------AKLLTEKELRD-----------------------------ALLLIFANKQDVAG 114 (169) T ss_pred EEEECCCHHHHHHHHHHH--------HHHHCCCCCCC-----------------------------CEEEEEECCCCCCC T ss_conf 999655633589999999--------99844510169-----------------------------56999851558876 Q ss_pred CCCHHHHHHHHHHHHHHHHHCCCEEEEEE Q ss_conf 88766789999999999986094688851 Q Ver_Hs_NP_0570 193 DFESEKRKVICKTLRFVAHYYGASLMFTS 221 (351) Q Consensus 193 ~~D~e~rK~i~r~LR~iAH~yGA~L~FtS 221 (351) ....+.-+-.-. |..+++..--++..+| T Consensus 115 ~~~~~ei~~~l~-l~~~~~~r~~~i~~~S 142 (169) T cd04158 115 ALSVEEMTELLS-LHKLCCGRSWYIQGCD 142 (169) T ss_pred CCCHHHHHHHHH-HHHHHCCCCEEEEEEE T ss_conf 889899998963-6877338956999752 No 94 >cd04155 Arl3 Arl3 subfamily. Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation. Probab=99.08 E-value=5.4e-10 Score=81.53 Aligned_columns=121 Identities=21% Q ss_pred CCEEEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 7458998659886377777552-766788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 31 EKFVFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 31 ek~v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) |.-|+++|..|+|||||++|+. ++....-||.+..+ .....++. ..++|++||--.+..+.+.-.... - T Consensus 14 e~kiliiG~~~~GKTsll~~l~~~~~~~~~pT~g~~~---~~i~~~~~---~l~~wD~~G~~~~r~~~~~y~~~a----~ 83 (173) T cd04155 14 EPRILILGLDNAGKTTILKQLASEDISHITPTQGFNI---KTVQSDGF---KLNVWDIGGQRAIRPYWRNYFENT----D 83 (173) T ss_pred CCEEEEEEECCCCHHHHHHHHHCCCCCEEEEEEEEEE---EEEEECCE---EEEEEECCCHHHHHHHHHHHCCCC----C T ss_conf 8369998408986899888884695221441123588---99871888---999986687256799999860667----4 Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .+|.|+|.|.+.++=++.+++ +++++.-+..+ +|++|+|+|.| T Consensus 84 ~iI~VvD~sd~~~~~~~~~~l--------~~~L~~~~~~~-----------------------------~PiLi~~NK~D 126 (173) T cd04155 84 CLIYVIDSADKKRLEEAGAEL--------VELLEEEKLAG-----------------------------VPVLVFANKQD 126 (173) T ss_pred EEEEEEECCCHHHHHHHHHHH--------HHHHHHHCCCC-----------------------------CEEEEEEECCC T ss_conf 689998657844589999999--------99873003389-----------------------------47999970578 Q ss_pred CCCCCCHHH Q ss_conf 015887667 Q Ver_Hs_NP_0570 190 VFQDFESEK 198 (351) Q Consensus 190 ~F~~~D~e~ 198 (351) .=...+.+. T Consensus 127 l~~~~~~~e 135 (173) T cd04155 127 LATAAPAEE 135 (173) T ss_pred CCCCCCHHH T ss_conf 543689899 No 95 >cd04153 Arl5_Arl8 Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date. Probab=99.07 E-value=3.4e-10 Score=82.78 Aligned_columns=113 Identities=32% Q ss_pred CCEEEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEE Q ss_conf 7458998659886377777552-766788875310002211101578711178889715785420211000042351206 Q Ver_Hs_NP_0570 31 EKFVFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTF 109 (351) Q Consensus 31 ek~v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~ 109 (351) |-.|+++|..|+|||||++|+. +......||++..+ ..-..++. ..++|++||-..+-.+-+.-.+. .- T Consensus 15 ~~kililG~~~sGKTtil~~~~~~~~~~~~pTvg~~~---~~i~~~~~---~~~iwD~~Gqe~~r~~w~~y~~~----~~ 84 (174) T cd04153 15 EYKVIIVGLDNAGKTTILYQFLLGEVVHTSPTIGSNV---EEIVYKNI---RFLMWDIGGQESLRSSWNTYYTN----TD 84 (174) T ss_pred EEEEEEEEECCCCHHHHHHHHHCCCCCCEECCCCCEE---EEEEECCE---EEEEEECCCCCCCCHHHHHHCCC----CC T ss_conf 0689998508986899888875386032002100058---89872858---99998768862340466754058----88 Q ss_pred EEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEEC Q ss_conf 77888736984689999999999999999999999852695378999999998414667760011106887799712100 Q Ver_Hs_NP_0570 110 SLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYD 189 (351) Q Consensus 110 ~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD 189 (351) .+|+|+|.|.+.++=++.++| .++++.-.-.+ +|++|+|+|.| T Consensus 85 ~iI~VvD~sd~~~~~~~~~~l--------~~~l~~~~~~~-----------------------------~piLIlaNK~D 127 (174) T cd04153 85 AVILVIDSTDRERLPLTKEEL--------YKMLAHEDLRK-----------------------------AVLLVLANKQD 127 (174) T ss_pred EEEEEEECCCCCCHHHHHHHH--------HHHHCCCCCCC-----------------------------CEEEEEEECCC T ss_conf 799999668820078899999--------99852524279-----------------------------78999960668 Q ss_pred C Q ss_conf 0 Q Ver_Hs_NP_0570 190 V 190 (351) Q Consensus 190 ~ 190 (351) . T Consensus 128 l 128 (174) T cd04153 128 L 128 (174) T ss_pred C T ss_conf 8 No 96 >cd01873 RhoBTB RhoBTB subfamily. Members of the RhoBTB subfamily of Rho GTPases are present in vertebrates, Drosophila, and Dictyostelium. RhoBTB proteins are characterized by a modular organization, consisting of a GTPase domain, a proline rich region, a tandem of two BTB (Broad-Complex, Tramtrack, and Bric a brac) domains, and a C-terminal region of unknown function. RhoBTB proteins may act as docking points for multiple components participating in signal transduction cascades. RhoBTB genes appeared upregulated in some cancer cell lines, suggesting a participation of RhoBTB proteins in the pathogenesis of particular tumors. Note that the Dictyostelium RacA GTPase domain is more closely related to Rac proteins than to RhoBTB proteins, where RacA actually belongs. Thus, the Dictyostelium RacA is not included here. Most Rho proteins contain a lipid modification site at the C-terminus; however, RhoBTB is one of few Rho subfamilies that lack this feature. Probab=99.00 E-value=4.5e-09 Score=75.72 Aligned_columns=154 Identities=21% Q ss_pred EEEEECCCCCHHHHHHHHC--------CCCCCCCCCC-CCCHHHHHHHCCCCCCCEE------EEEEEECCCCCHHHCEE Q ss_conf 8998659886377777552--------7667888753-1000221110157871117------88897157854202110 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL--------DRDEPPKPTL-ALEYTYGRRAKGHNTPKDI------AHFWELGGGTSLLDLIS 98 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl--------~r~e~~KPTl-ALeYtygRra~~~~~~Kdv------aH~WELGgg~~ls~Li~ 98 (351) |++||+.+.||||||.+++ ......-||+ |++.-..-.........-+ ..+|.-+| +...+-. T Consensus 5 iVlvGDs~VGKTsLi~~~~~~~~~~~~~~~~~~~pTv~~id~~~~~~~~~~~~~~~vdg~~v~L~iWDTAG--q~~~~r~ 82 (195) T cd01873 5 CVVVGDNAVGKTRLICARACNKTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDGVSVSLRLWDTFG--DHDKDRR 82 (195) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCCCEEECCCCEEEEEEECCCEEEEECCEEEEEEEEECCC--CHHHCCC T ss_conf 99982598234665434430674445522355344110012112222101100354288579998765467--1130011 Q ss_pred EEECCCCCCEEEEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCC Q ss_conf 00042351206778887369846899999999999999999999998526953789999999984146677600111068 Q Ver_Hs_NP_0570 99 IPITGDTLRTFSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFP 178 (351) Q Consensus 99 ipit~~~l~~~~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~p 178 (351) +.-...++ ++||+|++.|.++=.-..+|+..+|++... T Consensus 83 ~~Y~~a~~----~llvfdit~~~Sf~~v~~~W~~ei~~~~~~-------------------------------------- 120 (195) T cd01873 83 FAYGRSDV----VLLCFSIASPNSLRNVKTMWYPEIRHFCPR-------------------------------------- 120 (195) T ss_pred CCCCCCCE----EEEEEECCCHHHHHHHHHHHHHHHHHHCCC-------------------------------------- T ss_conf 23468878----999974598446899998758999984589-------------------------------------- Q ss_pred CCEEEECCEECC-CCCCCHHHHHHHHHHH-------------HHHHHHCCCEEEEEECHHHHHHHHHHH Q ss_conf 877997121000-1588766789999999-------------999986094688851203456789998 Q Ver_Hs_NP_0570 179 VPLVIIGSKYDV-FQDFESEKRKVICKTL-------------RFVAHYYGASLMFTSKSEALLLKIRGV 233 (351) Q Consensus 179 iPlvIVg~KYD~-F~~~D~e~rK~i~r~L-------------R~iAH~yGA~L~FtSk~e~l~~r~r~~ 233 (351) +|+++||+|.|+ +.+.+...+.....+. +.+|..+|+..+.+|-+.. ..++.+ T Consensus 121 vpiiLVGnK~DLr~~~~~~~~~~~~~~~~~~~~~~~v~~ee~~~~A~~~g~~y~EtSAkt~--~nV~e~ 187 (195) T cd01873 121 VPVILVGCKLDLRYADLDEVNRARRPLARPIKNADILPPETGRAVAKELGIPYYETSVVTQ--FGVKDV 187 (195) T ss_pred CEEEEEECCCCCCCCCHHHHHHHHHHHHCCCCCCCCCCHHHHHHHHHHCCCCEEEEECCCC--CCHHHH T ss_conf 7199973650112244013434332210234323477889999999970995798752458--887899 No 97 >KOG0094 GTPase Rab6/YPT6/Ryh1, small G protein superfamily [Intracellular trafficking, secretion, and vesicular transport] Probab=99.00 E-value=3.7e-09 Score=76.29 Aligned_columns=174 Identities=25% Q ss_pred EEEEECCCCCHHHHHHHHC--CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 8998659886377777552--76678887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL--DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl--~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+|+|+-+.||||||+||+ .=+..+++|.|+|+---+---.++.. ...+|.-+|---+-.||.--|+. ..++ T Consensus 25 lVflGdqsVGKTslItRf~yd~fd~~YqATIGiDFlskt~~l~d~~v--rLQlWDTAGQERFrslipsY~Rd----s~va 98 (221) T KOG0094 25 LVFLGDQSVGKTSLITRFMYDKFDNTYQATIGIDFLSKTMYLEDRTV--RLQLWDTAGQERFRSLIPSYIRD----SSVA 98 (221) T ss_pred EEEEECCCCCHHHHHHHHHHCCCCCCCCCEEEEEEEEEEEEECCCEE--EEEEEECCHHHHHHHHCCCCCCC----CEEE T ss_conf 99984177641564322330032356576466667777789727168--99986241035676422200158----5279 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHH-HHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 88873698468999999999999999999-99998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDK-VIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~k-l~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) |||.|+++-+++-.|-.|+-.+.+.+-.. ++ +++||+|-|+ T Consensus 99 viVyDit~~~Sfe~t~kWi~dv~~e~gs~~vi--------------------------------------I~LVGnKtDL 140 (221) T KOG0094 99 VIVYDITDRNSFENTSKWIEDVRRERGSDDVI--------------------------------------IFLVGNKTDL 140 (221) T ss_pred EEEEECCCCCHHHHHHHHHHHHHHCCCCCCCE--------------------------------------EEEEECCHHC T ss_conf 99982246400566999999987226899708--------------------------------------9997375000 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHCCCEEEEEECHHHHHHH--HHHHHHHHHCCCCCCCEEEEECCCCEEEE Q ss_conf 158876678999999999998609468885120345678--99988875057777730575067757870 Q Ver_Hs_NP_0570 191 FQDFESEKRKVICKTLRFVAHYYGASLMFTSKSEALLLK--IRGVINQLAFGIDKSKSICVDQNKPLFIT 258 (351) Q Consensus 191 F~~~D~e~rK~i~r~LR~iAH~yGA~L~FtSk~e~l~~r--~r~~inhl~FG~~~~k~~~~D~~kPl~I~ 258 (351) +++|.+-.--=--.|-.+||--+=||-+...+.+ ||. |--++||... -+..+-.+++..|. T Consensus 141 -----~dkrqvs~eEg~~kAkel~a~f~etsak~g~NVk~lFrr-Iaa~l~~~~~-~~~~~~~~~~~~v~ 203 (221) T KOG0094 141 -----SDKRQVSIEEGERKAKELNAEFIETSAKAGENVKQLFRR-IAAALPGMEV-LEILSKQESMVDIN 203 (221) T ss_pred -----CCHHHHHHHHHHHHHHHHCEEEEEECCCCCCCHHHHHHH-HHHHCCCCHH-HHCCCCCCCCEEEE T ss_conf -----577777699999887772807999527899984899989-8874135012-21035556751788 No 98 >cd04103 Centaurin_gamma Centaurin gamma. The centaurins (alpha, beta, gamma, and delta) are large, multi-domain proteins that all contain an ArfGAP domain and ankyrin repeats, and in some cases, numerous additional domains. Centaurin gamma contains an additional GTPase domain near its N-terminus. The specific function of this GTPase domain has not been well characterized, but centaurin gamma 2 (CENTG2) may play a role in the development of autism. Centaurin gamma 1 is also called PIKE (phosphatidyl inositol (PI) 3-kinase enhancer) and centaurin gamma 2 is also known as AGAP (ArfGAP protein with a GTPase-like domain, ankyrin repeats and a Pleckstrin homology domain) or GGAP. Three isoforms of PIKE have been identified. PIKE-S (short) and PIKE-L (long) are brain-specific isoforms, with PIKE-S restricted to the nucleus and PIKE-L found in multiple cellular compartments. A third isoform, PIKE-A was identified in human glioblastoma brain cancers and has been found in various tissues. Probab=98.99 E-value=5e-09 Score=75.44 Aligned_columns=151 Identities=18% Q ss_pred EEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEEE Q ss_conf 8998659886377777552-766788875310002211101578711178889715785420211000042351206778 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSLV 112 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~vi 112 (351) |.++|+.|.|||+|++||+ ++......|++=.| .+..--....-...+|.-+|-....-+-. .-.++ T Consensus 3 vvllGd~gVGKTsL~~rf~~~~F~~~~~~~~~~~---~k~v~vdg~~~~l~IwDTaGq~~~~~~~~---------a~a~i 70 (158) T cd04103 3 LGIVGNLQSGKSALVHRYLTGSYVQLESPEGGRF---KKEVLVDGQSHLLLIRDEGGAPDAQFASW---------VDAVI 70 (158) T ss_pred EEEECCCCCCHHHHHHHHHCCEECCCCCCCCCEE---EEEEEECCEEEEEEEEECCCCCHHHHHCC---------CCEEE T ss_conf 8998289941788876654482056545543103---78899979399999863689801355306---------98699 Q ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECCCC Q ss_conf 88736984689999999999999999999999852695378999999998414667760011106887799712100015 Q Ver_Hs_NP_0570 113 LVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDVFQ 192 (351) Q Consensus 113 ivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~F~ 192 (351) ||.|++.+.++ +.+..|++.++++... ..+|+++||+|.|+=+ T Consensus 71 lVfdvt~~~SF-~~i~~w~~~i~~~~~~------------------------------------~~ipiiLVGNK~dl~~ 113 (158) T cd04103 71 FVFSLENEASF-QTVYNLYHQLSSYRNI------------------------------------SEIPLILVGTQDAISE 113 (158) T ss_pred EEEECCCHHHH-HHHHHHHHHHHHHCCC------------------------------------CCCEEEEEECCCCCCC T ss_conf 99866997678-9999999999874399------------------------------------9958999825766332 Q ss_pred CCCHHHHHHHHHHHHHHHHHCC-CEEEEEECHHHHHHHHHHHHHHHH Q ss_conf 8876678999999999998609-468885120345678999888750 Q Ver_Hs_NP_0570 193 DFESEKRKVICKTLRFVAHYYG-ASLMFTSKSEALLLKIRGVINQLA 238 (351) Q Consensus 193 ~~D~e~rK~i~r~LR~iAH~yG-A~L~FtSk~e~l~~r~r~~inhl~ 238 (351) . ..|.+-..--+.+|-.++ +..+.||-... .++..+-..++ T Consensus 114 ~---~~r~V~~~e~~~~a~~~~~~~y~EtSAk~~--~nV~~~F~~~~ 155 (158) T cd04103 114 S---NPRVIDDARARQLCADMKRCSYYETCATYG--LNVERVFQEAA 155 (158) T ss_pred C---CCCCCCHHHHHHHHHHHCCCCEEEEECCCC--CCHHHHHHHHH T ss_conf 4---574177899999999816981899851478--68789999999 No 99 >cd04162 Arl9_Arfrp2_like Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date. Probab=98.99 E-value=1.4e-09 Score=78.88 Aligned_columns=108 Identities=24% Q ss_pred EEEEECCCCCHHHHHHHHCCCC--CCCCCCCCCCHHHHHHHCCCCCCCEEEEEEEECCCCCHHHCEEEEECCCCCCEEEE Q ss_conf 8998659886377777552766--78887531000221110157871117888971578542021100004235120677 Q Ver_Hs_NP_0570 34 VFFIGSKNGGKTTIILRCLDRD--EPPKPTLALEYTYGRRAKGHNTPKDIAHFWELGGGTSLLDLISIPITGDTLRTFSL 111 (351) Q Consensus 34 v~~vGsk~~GKTTli~Rfl~r~--e~~KPTlALeYtygRra~~~~~~KdvaH~WELGgg~~ls~Li~ipit~~~l~~~~v 111 (351) |+++|-.|+|||||++|+.+.. +.+.||.+... -+-...+. -.++|++||-..+-.+-+--. -..-.+ T Consensus 2 IliLGLd~aGKTtil~~l~~~~~~~~~~PTiGfn~---~~i~~~~~---~l~~wDigGq~~~R~~W~~Yy----~~~~gi 71 (164) T cd04162 2 ILVLGLDGAGKTSLLHSLSSERSLESVVPTTGFNS---VAIPTQDA---IMELLEIGGSQNLRKYWKRYL----SGSQGL 71 (164) T ss_pred EEEEEECCCCHHHHHHHHHCCCCCCCEEEEEEEEE---EEEEECCE---EEEEEECCCCCCCHHHHHHHC----CCCCEE T ss_conf 78997479757887776727962462664451058---99871878---999987478620013467641----678789 Q ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEECC Q ss_conf 8887369846899999999999999999999998526953789999999984146677600111068877997121000 Q Ver_Hs_NP_0570 112 VLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKYDV 190 (351) Q Consensus 112 iivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KYD~ 190 (351) |.|+|.|.+.++=++-+++ +++ .-++..+|++|+|+|.|+ T Consensus 72 IfVVDssD~~rl~eak~eL--------~~l-------------------------------l~~~~~~PllvlaNKqDl 111 (164) T cd04162 72 IFVVDSADSERLPLARQEL--------HQL-------------------------------LQHPPDLPLVVLANKQDL 111 (164) T ss_pred EEEEECCCHHHHHHHHHHH--------HHH-------------------------------HHCCCCCEEEEEECCCCC T ss_conf 9998568811189999999--------999-------------------------------835799718998415487 No 100 >cd00879 Sar1 Sar1 subfamily. Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation. Probab=98.98 E-value=1.6e-09 Score=78.55 Aligned_columns=120 Identities=30% Q ss_pred CCEEEEEECCCCCHHHHHHHHC-CCCCCCCCCCCCCHHHHHHHCCCCCCCEEE-EEEEECCCCCHHHCEEEEECCCCCCE Q ss_conf 7458998659886377777552-766788875310002211101578711178-88971578542021100004235120 Q Ver_Hs_NP_0570 31 EKFVFFIGSKNGGKTTIILRCL-DRDEPPKPTLALEYTYGRRAKGHNTPKDIA-HFWELGGGTSLLDLISIPITGDTLRT 108 (351) Q Consensus 31 ek~v~~vGsk~~GKTTli~Rfl-~r~e~~KPTlALeYtygRra~~~~~~Kdva-H~WELGgg~~ls~Li~ipit~~~l~~ 108 (351) |..|+++|-.|||||||++|+. ++.....||.+.-. .....+++- ++|++||...+-.+-+--.. .. T Consensus 19 e~kIlilGLd~aGKTTil~~l~~~~~~~~~PTiG~n~-------e~i~~~~~~~~iwDigGq~~~R~~W~~Yy~----~~ 87 (190) T cd00879 19 EAKILFLGLDNAGKTTLLHMLKDDRLAQHVPTLHPTS-------EELTIGNIKFKTFDLGGHEQARRLWKDYFP----EV 87 (190) T ss_pred CEEEEEEEECCCCHHHHHHHHHCCCEEEEECCCCCEE-------EEEEECCEEEEEEECCCCCCCHHHHHHHCC----CC T ss_conf 3389999657987899888872696346520003517-------898877889999874798634246775414----63 Q ss_pred EEEEEEEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCEEEECCEE Q ss_conf 67788873698468999999999999999999999985269537899999999841466776001110688779971210 Q Ver_Hs_NP_0570 109 FSLVLVLDLSKPNDLWPTMENLLQATKSHVDKVIMKLGKTNAKAVSEMRQKIWNNMPKDHPDHELIDPFPVPLVIIGSKY 188 (351) Q Consensus 109 ~~viivlDlSkP~~lw~tle~~l~~vr~~v~kl~~~l~k~~~~~~~~l~qra~~~~~~dhpD~~~v~p~piPlvIVg~KY 188 (351) -.+|.|+|.|.+.++-++-+.+ +++++.-+-++ +|++|.++|- T Consensus 88 ~giIfVVDssD~~r~~eak~eL--------~~lL~~~~l~~-----------------------------~PiLIlaNKq 130 (190) T cd00879 88 DGIVFLVDAADPERFQESKEEL--------DSLLSDEELAN-----------------------------VPFLILGNKI 130 (190) T ss_pred CEEEEEEECCCCCCHHHHHHHH--------HHHHCCCCCCC-----------------------------CEEEEEEECC T ss_conf 1899998637865478899999--------99843301079-----------------------------7489984055 Q ss_pred CCCCCCCHHH Q ss_conf 0015887667 Q Ver_Hs_NP_0570 189 DVFQDFESEK 198 (351) Q Consensus 189 D~F~~~D~e~ 198 (351) |.=....++. T Consensus 131 Dl~~a~~~~e 140 (190) T cd00879 131 DLPGAVSEEE 140 (190) T ss_pred CCCCCCCHHH T ss_conf 8875879899 Done!