Query Fun_Sc_NP_014028.1_Dyn3p Command /cluster/toolkit/production/bioprogs/hhpred/hhsearch -cpu 4 -v 1 -i /cluster/toolkit/production/tmp/production/96190/c_Sc_Dyn3.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/96190/c_Sc_Dyn3.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 pfam05783 DLIC Dynein light in 100.0 0 0 669.0 17.1 276 2-301 24-365 (475) 2 KOG3905 Dynein light intermedi 100.0 0 0 635.9 18.7 276 2-301 29-370 (473) 3 KOG3929 Uncharacterized conser 99.4 1.1E-13 5E-18 101.5 3.2 255 12-288 31-324 (363) 4 cd04101 RabL4 RabL4 (Rab-like4 98.1 0.00032 1.5E-08 44.2 15.4 159 28-208 3-164 (164) 5 cd04128 Spg1 Spg1p. Spg1p (se 97.9 0.00092 4.4E-08 41.4 15.3 170 28-218 3-173 (182) 6 cd00154 Rab Rab family. Rab G 97.9 0.0011 5.3E-08 40.9 15.0 151 28-201 3-155 (159) 7 cd00877 Ran Ran (Ras-related n 97.8 0.00058 2.7E-08 42.6 13.2 157 28-214 3-162 (166) 8 cd04122 Rab14 Rab14 subfamily. 97.6 0.003 1.4E-07 38.3 13.7 157 28-211 5-164 (166) 9 cd01866 Rab2 Rab2 subfamily. 97.6 0.0036 1.7E-07 37.8 14.1 158 28-213 7-168 (168) 10 cd04106 Rab23_lke Rab23-like s 97.6 0.0041 1.9E-07 37.5 14.1 159 28-210 3-162 (162) 11 cd04110 Rab35 Rab35 subfamily. 97.5 0.0051 2.4E-07 36.9 13.8 150 28-202 9-161 (199) 12 cd04113 Rab4 Rab4 subfamily. 97.5 0.0099 4.7E-07 35.2 15.3 154 28-204 3-158 (161) 13 cd04124 RabL2 RabL2 subfamily. 97.4 0.0057 2.7E-07 36.6 13.4 146 28-201 3-151 (161) 14 cd01868 Rab11_like Rab11-like. 97.4 0.018 8.5E-07 33.6 15.1 158 28-211 6-165 (165) 15 cd00876 Ras Ras family. The R 97.4 0.013 6.2E-07 34.5 14.4 151 28-202 2-155 (160) 16 cd04109 Rab28 Rab28 subfamily. 97.3 0.026 1.2E-06 32.7 15.5 194 28-244 3-198 (215) 17 cd01865 Rab3 Rab3 subfamily. 97.3 0.012 5.8E-07 34.6 13.8 158 28-213 4-165 (165) 18 cd04132 Rho4_like Rho4-like su 97.3 0.021 9.8E-07 33.3 14.9 173 26-218 1-174 (187) 19 cd01861 Rab6 Rab6 subfamily. 97.3 0.017 8.1E-07 33.8 14.4 157 28-210 3-161 (161) 20 cd01860 Rab5_related Rab5-rela 97.3 0.022 1.1E-06 33.1 14.7 158 28-211 4-163 (163) 21 cd01864 Rab19 Rab19 subfamily. 97.2 0.024 1.2E-06 32.8 14.8 157 28-210 6-165 (165) 22 cd00157 Rho Rho (Ras homology) 97.2 0.011 5.1E-07 35.0 12.9 163 28-200 3-165 (171) 23 cd04119 RJL RJL (RabJ-Like) su 97.2 0.021 9.9E-07 33.2 14.3 159 28-212 3-168 (168) 24 cd04112 Rab26 Rab26 subfamily. 97.2 0.026 1.2E-06 32.7 14.6 167 28-220 3-172 (191) 25 cd04123 Rab21 Rab21 subfamily. 97.2 0.028 1.3E-06 32.4 14.7 158 28-211 3-162 (162) 26 pfam00071 Ras Ras family. Incl 97.2 0.026 1.2E-06 32.6 14.5 160 28-212 2-162 (162) 27 cd01869 Rab1_Ypt1 Rab1/Ypt1 su 97.1 0.027 1.3E-06 32.5 14.0 160 28-213 5-166 (166) 28 cd04117 Rab15 Rab15 subfamily. 97.1 0.081 3.8E-06 29.7 16.4 157 28-207 3-161 (161) 29 cd01863 Rab18 Rab18 subfamily. 97.1 0.043 2E-06 31.3 15.0 156 28-210 3-161 (161) 30 cd04115 Rab33B_Rab33A Rab33B/R 97.1 0.034 1.6E-06 32.0 14.3 158 28-210 5-168 (170) 31 cd04125 RabA_like RabA-like su 97.1 0.046 2.2E-06 31.2 14.8 168 28-218 3-172 (188) 32 smart00174 RHO Rho (Ras homolo 97.1 0.026 1.2E-06 32.7 13.5 173 28-212 1-174 (174) 33 cd04127 Rab27A Rab27a subfamil 97.1 0.036 1.7E-06 31.8 14.1 161 28-213 7-179 (180) 34 cd01867 Rab8_Rab10_Rab13_like 97.1 0.036 1.7E-06 31.8 14.1 160 28-213 6-167 (167) 35 cd04174 Rnd1_Rho6 Rnd1/Rho6 su 97.0 0.031 1.5E-06 32.2 13.6 196 28-236 16-217 (232) 36 cd04175 Rap1 Rap1 subgroup. T 97.0 0.04 1.9E-06 31.5 13.7 158 28-212 4-164 (164) 37 cd04121 Rab40 Rab40 subfamily. 96.9 0.045 2.2E-06 31.2 13.7 162 28-212 9-171 (235) 38 cd04114 Rab30 Rab30 subfamily. 96.9 0.085 4E-06 29.5 14.6 157 28-210 10-168 (169) 39 smart00176 RAN Ran (Ras-relate 96.8 0.031 1.5E-06 32.2 12.1 166 31-226 1-169 (200) 40 cd04120 Rab12 Rab12 subfamily. 96.8 0.22 1E-05 27.1 16.1 173 28-220 3-177 (202) 41 cd04118 Rab24 Rab24 subfamily. 96.8 0.14 6.9E-06 28.1 15.1 158 28-204 3-162 (193) 42 cd01893 Miro1 Miro1 subfamily. 96.8 0.11 5.1E-06 28.9 14.4 157 28-204 3-160 (166) 43 cd04166 CysN_ATPS CysN_ATPS su 96.8 0.041 1.9E-06 31.5 12.3 139 27-179 1-165 (208) 44 cd01892 Miro2 Miro2 subfamily. 96.7 0.094 4.5E-06 29.3 14.0 160 28-211 7-169 (169) 45 cd04107 Rab32_Rab38 Rab38/Rab3 96.7 0.13 6.3E-06 28.4 14.7 181 28-232 3-190 (201) 46 cd04146 RERG_RasL11_like RERG/ 96.7 0.048 2.3E-06 31.1 12.3 148 28-195 2-150 (165) 47 cd04131 Rnd Rnd subfamily. Th 96.7 0.1 4.9E-06 29.0 13.9 172 28-206 4-176 (178) 48 cd04139 RalA_RalB RalA/RalB su 96.7 0.17 7.9E-06 27.8 14.9 160 28-213 3-164 (164) 49 cd04136 Rap_like Rap-like subf 96.6 0.13 6E-06 28.5 14.2 150 28-201 4-156 (163) 50 cd04133 Rop_like Rop subfamily 96.6 0.11 5.1E-06 28.9 13.3 152 28-202 4-167 (176) 51 cd00878 Arf_Arl Arf (ADP-ribos 96.5 0.034 1.6E-06 31.9 10.7 108 28-147 2-111 (158) 52 cd04138 H_N_K_Ras_like H-Ras/N 96.5 0.2 9.3E-06 27.4 14.5 149 28-201 4-155 (162) 53 cd04140 ARHI_like ARHI subfami 96.5 0.14 6.5E-06 28.3 13.5 151 28-202 4-159 (165) 54 cd04134 Rho3 Rho3 subfamily. 96.5 0.22 1E-05 27.1 14.4 181 26-218 1-181 (189) 55 smart00177 ARF ARF-like small 96.4 0.053 2.5E-06 30.8 11.2 121 4-147 6-129 (181) 56 cd04137 RheB Rheb (Ras Homolog 96.4 0.15 7.1E-06 28.1 13.4 168 26-218 2-170 (180) 57 cd04145 M_R_Ras_like M-Ras/R-R 96.4 0.21 1E-05 27.1 14.1 155 24-202 1-158 (164) 58 smart00175 RAB Rab subfamily o 96.4 0.2 9.5E-06 27.3 13.8 158 28-213 3-164 (164) 59 cd04152 Arl4_Arl7 Arl4/Arl7 su 96.4 0.061 2.9E-06 30.4 11.1 113 27-147 5-120 (183) 60 pfam00025 Arf ADP-ribosylation 96.4 0.05 2.4E-06 30.9 10.7 108 28-147 18-127 (176) 61 cd04141 Rit_Rin_Ric Rit/Rin/Ri 96.4 0.35 1.7E-05 25.8 15.0 162 28-214 5-167 (172) 62 cd04111 Rab39 Rab39 subfamily. 96.3 0.27 1.3E-05 26.5 14.4 159 28-211 5-166 (211) 63 cd04172 Rnd3_RhoE_Rho8 Rnd3/Rh 96.3 0.1 4.9E-06 29.0 12.0 113 28-147 8-120 (182) 64 cd04108 Rab36_Rab34 Rab34/Rab3 96.3 0.35 1.7E-05 25.8 14.6 162 28-210 3-167 (170) 65 cd04151 Arl1 Arl1 subfamily. 96.3 0.062 2.9E-06 30.4 10.7 108 28-147 2-111 (158) 66 cd04156 ARLTS1 ARLTS1 subfamil 96.2 0.27 1.3E-05 26.6 13.8 156 28-204 2-158 (160) 67 pfam00009 GTP_EFTU Elongation 96.2 0.043 2E-06 31.3 9.5 141 27-179 5-161 (209) 68 cd04176 Rap2 Rap2 subgroup. T 96.1 0.39 1.9E-05 25.5 14.3 151 28-202 4-157 (163) 69 cd00881 GTP_translation_factor 96.1 0.092 4.4E-06 29.3 11.0 165 27-211 1-187 (189) 70 cd04135 Tc10 TC10 subfamily. 96.1 0.28 1.3E-05 26.4 13.4 166 28-202 3-168 (174) 71 cd04154 Arl2 Arl2 subfamily. 96.1 0.094 4.5E-06 29.3 11.0 109 27-147 16-126 (173) 72 smart00173 RAS Ras subfamily o 96.1 0.35 1.7E-05 25.8 13.8 158 28-212 5-165 (166) 73 cd04153 Arl5_Arl8 Arl5/Arl8 su 96.1 0.073 3.5E-06 29.9 10.3 107 28-147 18-127 (174) 74 cd04162 Arl9_Arfrp2_like Arl9/ 96.0 0.12 5.7E-06 28.6 11.0 108 28-147 2-110 (164) 75 cd01883 EF1_alpha Eukaryotic e 96.0 0.083 3.9E-06 29.6 10.1 140 27-179 1-174 (219) 76 cd01875 RhoG RhoG subfamily. 95.9 0.62 2.9E-05 24.3 14.6 185 28-221 6-191 (191) 77 cd04116 Rab9 Rab9 subfamily. 95.9 0.19 8.9E-06 27.5 11.7 153 28-200 8-163 (170) 78 cd01870 RhoA_like RhoA-like su 95.8 0.52 2.5E-05 24.8 13.8 172 28-206 4-175 (175) 79 cd04159 Arl10_like Arl10-like 95.8 0.59 2.8E-05 24.5 14.0 151 28-202 2-155 (159) 80 cd04160 Arfrp1 Arfrp1 subfamil 95.8 0.11 5.2E-06 28.9 10.2 110 27-147 1-118 (167) 81 cd04158 ARD1 ARD1 subfamily. 95.8 0.17 8E-06 27.8 11.0 108 28-147 2-111 (169) 82 cd04129 Rho2 Rho2 subfamily. 95.7 0.25 1.2E-05 26.7 11.8 113 28-147 4-116 (187) 83 cd04173 Rnd2_Rho7 Rnd2/Rho7 su 95.7 0.26 1.2E-05 26.6 11.8 113 28-147 4-116 (222) 84 cd04126 Rab20 Rab20 subfamily. 95.7 0.54 2.6E-05 24.7 13.4 158 28-202 3-184 (220) 85 cd04177 RSR1 RSR1 subgroup. R 95.6 1.2 5.7E-05 22.6 14.8 160 28-206 4-164 (168) 86 cd04157 Arl6 Arl6 subfamily. 95.5 0.24 1.1E-05 26.8 11.1 111 27-147 1-115 (162) 87 cd04130 Wrch_1 Wrch-1 subfamil 95.3 0.37 1.8E-05 25.7 11.5 113 28-147 3-115 (173) 88 KOG0458 Elongation factor 1 al 95.3 0.096 4.6E-06 29.2 8.4 147 13-175 167-346 (603) 89 cd01862 Rab7 Rab7 subfamily. 95.2 2.5 0.00012 20.7 15.5 162 28-209 3-170 (172) 90 cd04149 Arf6 Arf6 subfamily. 95.1 0.26 1.2E-05 26.6 10.1 109 27-147 11-121 (168) 91 COG1084 Predicted GTPase [Gene 95.1 0.11 5.2E-06 28.9 8.2 133 16-154 159-300 (346) 92 cd04144 Ras2 Ras2 subfamily. 95.0 1.5 7.2E-05 22.0 14.0 156 28-210 2-162 (190) 93 cd01874 Cdc42 Cdc42 subfamily. 95.0 1.1 5.4E-05 22.7 13.2 163 25-200 1-167 (175) 94 cd04155 Arl3 Arl3 subfamily. 95.0 0.43 2.1E-05 25.3 11.0 129 27-168 16-146 (173) 95 cd04142 RRP22 RRP22 subfamily. 94.9 2.6 0.00013 20.5 15.0 169 28-219 3-183 (198) 96 cd04150 Arf1_5_like Arf1-Arf5- 94.8 0.32 1.5E-05 26.1 10.0 107 28-147 3-112 (159) 97 KOG1673 Ras GTPases [General f 94.4 0.25 1.2E-05 26.7 8.6 194 15-229 5-204 (205) 98 cd04171 SelB SelB subfamily. 94.4 0.53 2.5E-05 24.7 10.3 152 28-202 3-160 (164) 99 cd01889 SelB_euk SelB subfamil 94.1 0.5 2.4E-05 24.9 9.7 168 27-207 2-185 (192) 100 cd01850 CDC_Septin CDC/Septin. 94.0 0.57 2.7E-05 24.6 9.9 143 27-183 6-180 (276) No 1 >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=0 Score=668.97 Aligned_columns=276 Identities=24% Q ss_pred CCCHHHHHHHHHHCCCCCCCCCCCCEEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCE-EEEEEE Q ss_conf 8613889988641011465536644389975983317999998514778655665575025633562121332-688998 Q Fun_Sc_NP_0140 2 DNCNAWDKLLSQNESTINSTETATITAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENY-SVDVYT 80 (312) Q Consensus 2 ~~~NlWs~iLse~~~~~~~k~~~~k~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~-R~~vy~ 80 (312) .++|||||||++|++++++|+|++||+||||+++.||++|+++| ||+++.++|+||||+|++|.|||+|++ ||+||+ T Consensus 24 ~k~nLWsSIL~~V~t~~r~Klp~~KniLVLG~~~~GKttLl~~L--qg~~~~kkg~aL~Y~YldV~DeD~Dd~~R~~vwi 101 (475) T pfam05783 24 EGQNLWSEILSEVSTRTRSKLPSGKNVLVLGDNGSGKTSLISRL--QGSERTKKGRGLEYLYLHVHDEDRDDLTRCNVWI 101 (475) T ss_pred HHHHHHHHHHHHHHCCCCCCCCCCCEEEEEECCCCCHHHHHHHH--HCCCCCCCCCCCCEEEECCCCCCHHHHCCCCEEE T ss_conf 12247898886530253334777664788508997557899975--0577667863101346323220303221542476 Q ss_pred EECCCHHHHHHHHHHHCCCC-CCCEEEEEECCCCCCHHHHHHHHHHHHHHHH---------------------------- Q ss_conf 60785435887887718778-7827999851666344689999999999864---------------------------- Q Fun_Sc_NP_0140 81 LIRNTDDALDLLKPFLQEHS-SKVRWLILLDWTLNDQKLWLNELSYAFNKIK---------------------------- 131 (312) Q Consensus 81 L~~~~~~~~~LLkp~L~~~s-~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~---------------------------- 131 (312) |+++.+| .+||||+|++++ ++|++||+|||++ ||+|+++|+.|+..|+ T Consensus 102 Ld~~~~~-~~LLK~aL~~~si~~TlViI~lDms~--PW~~i~qL~~Wi~VLrehi~~L~i~~ee~~el~e~l~~~wqeY~ 178 (475) T pfam05783 102 LDGDLYH-KGLLKFALPATSLAETLVILTASMSN--PWTLLESLQKWASVLREHIDKLKIPPEEMKAGRQKLEKDWQEYV 178 (475) T ss_pred CCCCCCC-CCCCCCCCCCCCHHHHHEHHHHHHHH--HHHHHHHHHHHHHHHHHHHHHCCCCHHHHHHHHHHHHHHHHHHH T ss_conf 0875152-22321257723142201200121201--34899999999999999997138998899999999999999860 Q ss_pred ---------------------------CCCCCC-------CEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHH Q ss_conf ---------------------------068998-------7389984773456655324541157889999999999988 Q Fun_Sc_NP_0140 132 ---------------------------QLNDDN-------EFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYF 177 (312) Q Consensus 132 ---------------------------~l~~Dt-------~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~ 177 (312) .+++.+ +|+|||||||+|++|||+| +|+||||||||||||+|||+ T Consensus 179 epg~~~d~s~~r~t~~~~~~~~~~v~lPLgeg~Lt~NLGiPiiVVctKsD~ie~LEKe~-~ykeE~fDfIqq~LR~~cLq 257 (475) T pfam05783 179 EPGEDLDGSPQRRTSVVGSFDEEHVLLPLGQDTLTHNLGLPVLVVCTKCDAMSVLEKEH-DYRDEHFDFIQSHLRKFCLQ 257 (475) T ss_pred CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEECCCCEEEEEEEECCCHHHHHHCCC-CCCHHHHHHHHHHHHHHHHH T ss_conf 55346787763245665653444565778876341278826999861762133332015-66436799999999999987 Q ss_pred CCCEEEEECCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCEECCCCEEECCCCCHHHHHHHHCCCCCCCCCCCCCCC Q ss_conf 29415885256531355566778888753001247787752240115630206688814624200478874400643467 Q Fun_Sc_NP_0140 178 NDSSLFYICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEMVTRSEILIPKGCDSIGLIKTVDERFEPTEVKEQHFL 257 (312) Q Consensus 178 yGASLiYts~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~vverd~vfIP~GwDS~~KI~ii~E~F~~~~V~~~d~~ 257 (312) |||||||| ++++.+|+.++|+| ++|++|||||+.+|.|+|||+||||+|||||+||+||||||+ +|+++| T Consensus 258 YGAsLiYT---S~ke~kNldlLykY---l~HrlYgfpf~~~a~VvekDaIfIPsGWDn~kKI~Il~Enf~--~~k~~~-- 327 (475) T pfam05783 258 YGAALIYT---SVKETKNIDLLYKY---IVHRSYGFPFTTPALVVEKDAVFIPAGWDNEKKIDILHENFP--TVKAED-- 327 (475) T ss_pred CCCEEEEE---CCCCCCCHHHHHHH---HHHHHHCCCCCCCCCEEEHHEEEECCCCCCHHHHHHHHCCCC--CCCCCC-- T ss_conf 09758985---47764238999999---998860765456220010000340588881455675433654--357876-- Q ss_pred CCCCCCC--CCCCCCCCCCCCCHHHHHHHCCCHHEECCCHHHHHHH Q ss_conf 5522357--8622330310022022032013201001001789999 Q Fun_Sc_NP_0140 258 ARYMDFI--PTIDKIREDRKTTSGIDLDKLYPLEVFKVNIQEELGK 301 (312) Q Consensus 258 ~~~ed~i--p~i~k~~~~~~~~~~~d~~~l~~~q~~~~~~q~~l~~ 301 (312) +||||| |+|||.+|++++.||+| |+|++|+|++|++ T Consensus 328 -~~ed~i~kp~~rk~~~~~ei~aedd-------Q~Fl~k~q~~l~~ 365 (475) T pfam05783 328 -AYEDIITKPPVRKVVHEKEIEAEDD-------QAFLMKLQSILAK 365 (475) T ss_pred -CCCCCCCCCCCHHHHHHHHHCCCHH-------HHHHHHHHHHHCC T ss_conf -4223447884023333332000127-------8999999999716 No 2 >KOG3905 Dynein light intermediate chain [Cell motility] Probab=100.00 E-value=0 Score=635.93 Aligned_columns=276 Identities=24% Q ss_pred CCCHHHHHHHHHHCCCCCCCCCCCCEEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCE-EEEEEE Q ss_conf 8613889988641011465536644389975983317999998514778655665575025633562121332-688998 Q Fun_Sc_NP_0140 2 DNCNAWDKLLSQNESTINSTETATITAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENY-SVDVYT 80 (312) Q Consensus 2 ~~~NlWs~iLse~~~~~~~k~~~~k~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~-R~~vy~ 80 (312) +||||||+||+||+++.++|+|++||+||+|+|++||+++|.++ ||+|.+|+|+||||+|++|+||+||++ ||+||+ T Consensus 29 egqnlWs~iLsev~T~~~sklpsgk~VlvlGdn~sGKtsLi~kl--qg~e~~KkgsgLeY~yl~V~de~RDd~tr~~VWi 106 (473) T KOG3905 29 EGQNLWSEILSEVSTRTRSKLPSGKNVLVLGDNGSGKTSLISKL--QGSETVKKGSGLEYLYLHVHDEDRDDLTRCNVWI 106 (473) T ss_pred HHHHHHHHHHHHHHHCCCCCCCCCCEEEEEECCCCCHHHHHHHH--HCCCCCCCCCCCEEEEEEECCCCHHHHHHCCCEE T ss_conf 77899999986542012344778865799705887457898876--3024567765312678862131004465487148 Q ss_pred EECCCHHHHHHHHHHHCCCC-CCCEEEEEECCCCCCHHHHHHHHHHHHHHHH---------------------------- Q ss_conf 60785435887887718778-7827999851666344689999999999864---------------------------- Q Fun_Sc_NP_0140 81 LIRNTDDALDLLKPFLQEHS-SKVRWLILLDWTLNDQKLWLNELSYAFNKIK---------------------------- 131 (312) Q Consensus 81 L~~~~~~~~~LLkp~L~~~s-~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~---------------------------- 131 (312) |+|+.+|+. |||++|.+.+ .++++++..|+++ ||+|+..|..|...++ T Consensus 107 LDGd~~h~~-LLk~al~ats~aetlviltasms~--Pw~~lesLqkWa~Vl~ehidkl~i~~ee~ka~rqk~~k~wQeYv 183 (473) T KOG3905 107 LDGDLYHKG-LLKFALPATSLAETLVILTASMSN--PWTLLESLQKWASVLREHIDKLKIPPEEMKAGRQKLEKDWQEYV 183 (473) T ss_pred ECCCHHHHH-HHHHCCCCCCCCCEEEEEEEECCC--CHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHHHHC T ss_conf 718755521-243204655615458989986575--03589999999999999898625898999999999888889760 Q ss_pred ---------------------------CCCCCC-------CEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHH Q ss_conf ---------------------------068998-------7389984773456655324541157889999999999988 Q Fun_Sc_NP_0140 132 ---------------------------QLNDDN-------EFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYF 177 (312) Q Consensus 132 ---------------------------~l~~Dt-------~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~ 177 (312) .++.|+ +++|||+|||+|++|||+| +|+|||||||||+||+|||+ T Consensus 184 ep~e~~pgsp~~r~t~~~~~~de~~llPL~~dtLt~NlGi~vlVV~TK~D~~s~leke~-eyrDehfdfiq~~lRkFCLr 262 (473) T KOG3905 184 EPGEDQPGSPQRRTTVVGSSADEHVLLPLGQDTLTHNLGIPVLVVCTKCDAVSVLEKEH-EYRDEHFDFIQSHLRKFCLR 262 (473) T ss_pred CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHCCCCCEEEEEECCCHHHHHHHCC-CCCHHHHHHHHHHHHHHHHH T ss_conf 51247888862034333565531111226776200006874799984243033455201-00167899999999999986 Q ss_pred CCCEEEEECCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCEECCCCEEECCCCCHHHHHHHHCCCCCCCCCCCCCCC Q ss_conf 29415885256531355566778888753001247787752240115630206688814624200478874400643467 Q Fun_Sc_NP_0140 178 NDSSLFYICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEMVTRSEILIPKGCDSIGLIKTVDERFEPTEVKEQHFL 257 (312) Q Consensus 178 yGASLiYts~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~vverd~vfIP~GwDS~~KI~ii~E~F~~~~V~~~d~~ 257 (312) |||+|||| ||+|.||+++++|| ++|+.||++|+++|.|||||+||||+||||++||.||||||+ +|+.+| T Consensus 263 ~GaaLiyT---SvKE~KNidllyKY---ivhr~yG~~fttpAlVVEkdaVfIPAGWD~eKKI~Il~En~~--~vkaed-- 332 (473) T KOG3905 263 YGAALIYT---SVKETKNIDLLYKY---IVHRSYGFPFTTPALVVEKDAVFIPAGWDNEKKIDILHENFP--TVKAED-- 332 (473) T ss_pred CCCEEEEE---ECCCCCCHHHHHHH---HHHHHCCCCCCCHHHEEECCEEEECCCCCCCCHHHHHHCCCC--CCCCCC-- T ss_conf 06302554---11124556888888---887641553135001232031463046686300221000356--778776-- Q ss_pred CCCCCCC--CCCCCCCCCCCCCHHHHHHHCCCHHEECCCHHHHHHH Q ss_conf 5522357--8622330310022022032013201001001789999 Q Fun_Sc_NP_0140 258 ARYMDFI--PTIDKIREDRKTTSGIDLDKLYPLEVFKVNIQEELGK 301 (312) Q Consensus 258 ~~~ed~i--p~i~k~~~~~~~~~~~d~~~l~~~q~~~~~~q~~l~~ 301 (312) +|+||| ||+||+||++++.||+| |+|+||+|+.|++ T Consensus 333 -~y~d~itkpp~Rk~v~ekei~aEdd-------QaFL~k~q~iLak 370 (473) T KOG3905 333 -NYEDIITKPPVRKVVHEKEIEAEDD-------QAFLMKLQSILAK 370 (473) T ss_pred -CCCCCCCCCCCHHHHHHHHHHHHHH-------HHHHHHHHHHHHC T ss_conf -5332436884015666665410137-------8999999998605 No 3 >KOG3929 Uncharacterized conserved protein [Function unknown] Probab=99.38 E-value=1.1e-13 Score=101.50 Aligned_columns=255 Identities=19% Q ss_pred HHHCCCCCCCCCCCCEEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHH Q ss_conf 64101146553664438997598331799999851477865566557502563356212133268899860785435887 Q Fun_Sc_NP_0140 12 SQNESTINSTETATITAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDL 91 (312) Q Consensus 12 se~~~~~~~k~~~~k~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~L 91 (312) ++-+.+......+-...++.-+|..- ++.|.+||.-.-...-....|||+|---..--.--.-.++|-|-|-... .+| T Consensus 31 ~~~deqL~e~~~~~E~~I~~~Gn~~~-tt~I~~~FdR~e~~~~ptlaLEYtygRR~~g~~~kdiaN~WELGgg~~~-~~L 108 (363) T KOG3929 31 SEGDEQLAEIAEKFEFFIGSKGNGGK-TTIILRCFDRDEPPKPPTLALEYTYGRRAKGHNPKDIANFWELGGGTSL-LDL 108 (363) T ss_pred CHHHHHHHHHHCCHHCEEEEECCCCE-EEEEEECCCCCCCCCCCCEEEEEHHHHHHCCCCCHHHHHHHHCCCCCCH-HHH T ss_conf 21378999850300205677338850-6653300576567899721221012344147885145655532673246-888 Q ss_pred HHHHHCCCC-CCCEEEEEECCCCCCH-HHH------HHHHHHHHHHHH-----------------------------CCC Q ss_conf 887718778-7827999851666344-689------999999999864-----------------------------068 Q Fun_Sc_NP_0140 92 LKPFLQEHS-SKVRWLILLDWTLNDQ-KLW------LNELSYAFNKIK-----------------------------QLN 134 (312) Q Consensus 92 Lkp~L~~~s-~~~l~ViLLDWs~~Dp-~~W------lr~Lr~~~~~L~-----------------------------~l~ 134 (312) |..-++.++ ..-.++++||.|+ | ..| +.-+|.+++.+. +.- T Consensus 109 LsVPit~~~l~~~slIL~LDls~--p~~~W~t~E~~~~~~R~~vd~~~~~~~k~~~~L~E~mrqR~~~rvgqd~~d~e~~ 186 (363) T KOG3929 109 LSVPITGDTLRTFSLILVLDLSK--PNDLWPTMENLLQATRSHVDKVIMKLGKTNAKLVEEMRQRIWNRVGQDHPDHELI 186 (363) T ss_pred HHCCCCCCCHHHHHHHHHHHCCC--HHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHHHCCCCCCCCCC T ss_conf 60554556287756667651156--2443257999999999899999998741488999999999998621468740002 Q ss_pred CCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEECCCCCHHHHHHHHHHHHHHHHHHCCCCCC Q ss_conf 99873899847734566553245411578899999999999882941588525653135556677888875300124778 Q Fun_Sc_NP_0140 135 DDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYICEDHTEEKREEAQRLKYQELLKHFCEDRD 214 (312) Q Consensus 135 ~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts~ts~~~~kn~~~~l~y~~L~~h~l~~~~ 214 (312) ++.++-|+.-.+-|=.- .++.++-=--++|+||++++.|||+|.+-|. |-..+.-+-+..+.|..+|-+ T Consensus 187 dP~P~PV~IVgsKYDvF-----q~FesekRkH~C~~LRf~Ah~yGaaLlmfSs------kMe~l~K~ir~~i~HlaFG~~ 255 (363) T KOG3929 187 DPFPVPVVIVGSKYDVF-----QDFESEKRKHICKTLRFVAHYYGAALLMFSS------KMEALLKKIRGVINHLAFGID 255 (363) T ss_pred CCCCCCEEEECCCCHHH-----CCCCHHHHHHHHHHHHHHHHHHHHHHHHHHH------HHHHHHHHHHHHHHHHHCCCC T ss_conf 77885347853520001-----2663678999999999999997789999888------789999998777775404765 Q ss_pred CCCCCCEECCCCEEECCCCCHHHHHHHHCCCCCCCCCCCCCCC--CCCCCCCCCCCCCCCCCCCCHHHHHHHCCCH Q ss_conf 7752240115630206688814624200478874400643467--5522357862233031002202203201320 Q Fun_Sc_NP_0140 215 MKDHIEMVTRSEILIPKGCDSIGLIKTVDERFEPTEVKEQHFL--ARYMDFIPTIDKIREDRKTTSGIDLDKLYPL 288 (312) Q Consensus 215 ~~~~a~vverd~vfIP~GwDS~~KI~ii~E~F~~~~V~~~d~~--~~~ed~ip~i~k~~~~~~~~~~~d~~~l~~~ 288 (312) -.+...|....++||-+|-|||++|++ --|.++|.+ -++|-.--+..+.++++.+.-.-|.+.--|+ T Consensus 256 ~~~s~~vD~NkPlfi~~G~DS~~~IG~-------pp~~~nd~Ga~sp~elw~~~F~~l~PQk~~~~~kd~kttDPa 324 (363) T KOG3929 256 KSKSICVDQNKPLFITAGLDSFGQIGS-------PPVPENDIGAHSPMELWKKVFEKLFPQKSINTLKDIKTTDPA 324 (363) T ss_pred CCCCEEEECCCCEEEEECCCCHHHCCC-------CCCCCCCCCCCCHHHHHHHHHHHHCCCHHHHHHHHHHHCCCC T ss_conf 766545307874589855532233378-------888743345433378999999863341234555554301533 No 4 >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=98.08 E-value=0.00032 Score=44.17 Aligned_columns=159 Identities=13% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCC---CCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCE Q ss_conf 8997598331799999851477865566---5575025633562121332688998607854358878877187787827 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILD---TTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVR 104 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~---~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l 104 (312) ++++|+.+-|||+|+.+...+|.+++.+ +.+.+|....+.-+..+...+..|=..| ...+..+.+..+. .-.- T Consensus 3 vv~iGd~~VGKTsli~~~~~~~~~f~~~y~~T~~~~~~~~~~~i~~~~~~~l~i~DtaG-qe~~~~~~~~~~~---~a~~ 78 (164) T cd04101 3 CAVVGDPAVGKTAFVQMFHSNGAVFPKNYLMTTGCDFVVKEVPVDTDNTVELFIFDSAG-QELYSDMVSNYWE---SPSV 78 (164) T ss_pred EEEEECCCCCHHHHHHHHHHCCCEECCCCCCCEEEEEEEEEEEECCCCEEEEEEEECCC-CHHHHHHHHHHCC---CCCE T ss_conf 89980798218988887761684416665431124567999997799679999960387-2246788787424---9976 Q ss_pred EEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 99985166634468999999999986406899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 105 WLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 105 ~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +++.-|-+. +...-+. ..|+..++....+.++++|..|+| |+..+ .-.+++ .|.+|-.+|+..|. T Consensus 79 ~ilvydit~--~~Sf~~i-~~w~~~i~~~~~~~p~ilVGNK~D----L~~~r-~V~~~~-------~~~~a~~~~~~~~e 143 (164) T cd04101 79 FILVYDVSN--KASFENC-SRWVNKVRTASKHMPGVLVGNKMD----LADKA-EVTDAQ-------AQAFAQANQLKFFK 143 (164) T ss_pred EEEEEECCC--HHHHHHH-HHHHHHHHHHCCCCEEEEEECCCC----CCCCC-CCCHHH-------HHHHHHHCCCCEEE T ss_conf 999941799--7689999-999999998449973999821434----00116-789899-------99999963994999 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHH Q ss_conf 525653135556677888875300 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKH 208 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h 208 (312) + |+++..|-...+..-+-..| T Consensus 144 ~---SAktg~nV~e~F~~lar~~~ 164 (164) T cd04101 144 T---SALRGVGYEEPFESLARAFH 164 (164) T ss_pred E---ECCCCCCHHHHHHHHHHHHC T ss_conf 9---71689887899999999729 No 5 >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=97.93 E-value=0.00092 Score=41.41 Aligned_columns=170 Identities=12% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+++.+... +-.+.+....|++|....+.- ++..+.+-+.+...-+.-.-+.+..-.++. .++ T Consensus 3 ivliGd~~VGKTsLi~r~~~~~F~~~y~~TiG~~~~~k~i~v---~~~~v~l~iwDtaGqE~f~~~~~~y~~~a~--~~i 77 (182) T cd04128 3 IGLLGDAQIGKTSLMVKYVEGEFDEDYIQTLGVNFMEKTISI---RGTEITFSIWDLGGQREFINMLPLVCNDAV--AIL 77 (182) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEE---CCEEEEEEEEECCCCCCCHHHHHHHCCCCC--EEE T ss_conf 899816984388887776437127763550344678989998---896899887316888310127786403777--689 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 98516663446899999999998640689987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) +.-|-+. +..+ ..+.+|+..+++.+.....++|-.|+|-...+..+.. +-+..-.+.+|-.+|+..|.| T Consensus 78 lVfDit~--~~Sf-~~i~~W~~~i~~~~~~~~~ILVGNK~DL~~~~~~~~~-------~~~~~~~~~~a~~~~~~~~et- 146 (182) T cd04128 78 FMFDLTR--KSTL-NSIKEWYRQARGFNKTAIPILVGTKYDLFADLPPEEQ-------EEITKQARKYAKAMKAPLIFC- 146 (182) T ss_pred EEEECCC--HHHH-HHHHHHHHHHHHHCCCCCEEEEECCCCCCCCCCHHHH-------HHHHHHHHHHHHHCCCCEEEE- T ss_conf 9986599--7899-9999999999862799608998327431001442456-------778899999999729959999- Q ss_pred CCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCC Q ss_conf 56531355566778888753001247787752 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQELLKHFCEDRDMKDH 218 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~ 218 (312) |+++..|-..++.. ++-.+++.+.+.+ T Consensus 147 --SAktg~nV~e~Fe~---l~~ki~~~~~~~~ 173 (182) T cd04128 147 --STSHSINVQKIFKI---VLAKAFDLPLTIP 173 (182) T ss_pred --ECCCCCCHHHHHHH---HHHHHHCCCCCCC T ss_conf --72479887899999---9999853788877 No 6 >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=97.87 E-value=0.0011 Score=40.89 Aligned_columns=151 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCCCC-CCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 8997598331799999851477-865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEG-SNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~-~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|..+.|||+|+.++.... .+.+.++.|.++....+.-+ ....++.+|=..| .+.+-.+.+-++.. -.-++ T Consensus 3 i~ivG~~~vGKTsli~~~~~~~f~~~~~~Ti~~~~~~k~i~~~-~~~~~~~i~Dt~g-~e~~~~~~~~~~~~---~d~~i 77 (159) T cd00154 3 IVLIGDSGVGKTSLLLRFVDGKFDENYKSTIGVDFKSKTIEID-GKTVKLQIWDTAG-QERFRSITPSYYRG---AHGAI 77 (159) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEEC-CEEEEEEEEECCC-CHHHHHHHHHHCCC---CCEEE T ss_conf 8998269966899999986382474446531003688899888-9599999986599-71456777875148---98699 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC-CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 98516663446899999999998640-68998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ-LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~-l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) +..|-+. +..+ +.+..|+..+++ ...+.++++|++|+| |+.++-...++ .|.+|-++|+..+.+ T Consensus 78 iv~d~~~--~~Sf-~~i~~~~~~i~~~~~~~~piiivgnK~D----l~~~~~v~~~~--------~~~~~~~~~~~~~e~ 142 (159) T cd00154 78 LVYDITN--RESF-ENLDKWLKELKEYAPENIPIILVGNKID----LEDQRQVSTEE--------AQQFAKENGLLFFET 142 (159) T ss_pred EEEECCC--HHHH-HHHHHHHHHHHHHCCCCCEEEEEECCCC----HHHHCCCCHHH--------HHHHHHHCCCCEEEE T ss_conf 9986699--7899-9999999999982699978999841310----00102656889--------999999659969999 Q ss_pred CCCCCHHHHHHHHHHH Q ss_conf 2565313555667788 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLK 201 (312) Q Consensus 186 s~ts~~~~kn~~~~l~ 201 (312) |++...|-..++. T Consensus 143 ---Sa~~~~~i~~~F~ 155 (159) T cd00154 143 ---SAKTGENVEELFQ 155 (159) T ss_pred ---EECCCCCHHHHHH T ss_conf ---7047988789999 No 7 >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=97.85 E-value=0.00058 Score=42.65 Aligned_columns=157 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778-78279 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRW 105 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~ 105 (312) ++++|+.+-|||+|+.+... .=.+.+.+..|.++....+..+ ..+.++.+|=..| .+.| ..+.+.- .+.-. T Consensus 3 IvliGd~~VGKTsli~r~~~~~F~~~y~~Tig~~~~~~~~~~~-~~~i~l~iwDtaG-~e~f-----~~l~~~y~~~a~~ 75 (166) T cd00877 3 LVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLDFHTN-RGKIRFNVWDTAG-QEKF-----GGLRDGYYIGGQC 75 (166) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEEC-CCEEEEEEEECCC-CCCC-----CCCCCCCCCCCCE T ss_conf 8998269844899988876381166645346448889999987-9479999884578-5213-----5455120002675 Q ss_pred EEEE-CCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 9985-166634468999999999986406899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 106 LILL-DWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 106 ViLL-DWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +||+ |-+. +++.-. +..|.+.++......++++|..|+| |+.... .++..+|..+ +|+..|- T Consensus 76 ~ilvfDit~--~~Sf~~-i~~w~~~i~~~~~~ipivlVGNK~D----l~~~~~--~~~~~~~~~~--------~~~~~~E 138 (166) T cd00877 76 AIIMFDVTS--RVTYKN-VPNWHRDLVRVCGNIPIVLCGNKVD----IKDRKV--KAKQITFHRK--------KNLQYYE 138 (166) T ss_pred EEEEEECCC--HHHHHH-HHHHHHHHHHHCCCCCEEEEECCCC----CCCCCC--CHHHHHHHHH--------CCCCEEE T ss_conf 899986699--789898-9889999986459965899932677----320112--4899999995--------7994999 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCCCCCC Q ss_conf 525653135556677888875300124778 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFCEDRD 214 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l~~~~ 214 (312) | |+++..|-...+.+ ++-.+.+.| T Consensus 139 t---SAk~g~NV~e~F~~---la~~il~~~ 162 (166) T cd00877 139 I---SAKSNYNFEKPFLW---LARKLLGNP 162 (166) T ss_pred E---ECCCCCCHHHHHHH---HHHHHHCCC T ss_conf 9---70489898899999---999985378 No 8 >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=97.60 E-value=0.003 Score=38.31 Aligned_columns=157 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778-78279 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRW 105 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~ 105 (312) ++++|+.+-|||+|+.+... .=.+.+....+.+|....+ .-++.++.+-+.+.+.-+.. ..+.+.- .+.-. T Consensus 5 ivviGd~~VGKTsli~r~~~~~f~~~~~~Ti~~~~~~k~i---~~~~~~v~l~i~Dt~G~e~~----~~~~~~~~~~a~~ 77 (166) T cd04122 5 YIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRII---EVNGQKIKLQIWDTAGQERF----RAVTRSYYRGAAG 77 (166) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEEEEEEE---EECCEEEEEEEEECCCCHHH----HHHHHHHCCCCCE T ss_conf 9998269955899998876384364456210221467888---52890899998635886023----4553864269875 Q ss_pred EEEECCCCCCHHHHHHHHHHHHHHHHCC-CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 9985166634468999999999986406-899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 106 LILLDWTLNDQKLWLNELSYAFNKIKQL-NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 106 ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l-~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +|++ .+..++... ..+.+|+...++. +.+.++++|..|+| |+.++ .-..++ .+.+|-++|+..+- T Consensus 78 ~ilv-ydit~~~Sf-~~i~~w~~~~~~~~~~~~~iilVGNK~D----L~~~r-~v~~~e-------~~~~a~~~~~~~~E 143 (166) T cd04122 78 ALMV-YDITRRSTY-NHLSSWLTDARNLTNPNTVIFLIGNKAD----LEAQR-DVTYEE-------AKQFADENGLLFLE 143 (166) T ss_pred EEEE-EECCCHHHH-HHHHHHHHHHHHCCCCCCEEEEECCHHH----HHHHC-CCCHHH-------HHHHHHHCCCEEEE T ss_conf 9998-207998789-9999999999740489957999637254----44303-541789-------99999964991999 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCCC Q ss_conf 525653135556677888875300124 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFCE 211 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l~ 211 (312) | |+++..|-...+.+ ++-.++ T Consensus 144 ~---SAk~~~nV~e~F~~---l~~~i~ 164 (166) T cd04122 144 C---SAKTGENVEDAFLE---TAKKIY 164 (166) T ss_pred E---ECCCCCCHHHHHHH---HHHHHH T ss_conf 9---71589887899999---999985 No 9 >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=97.60 E-value=0.0036 Score=37.80 Aligned_columns=158 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778-78279 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRW 105 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~ 105 (312) ++++|..+-|||+|+.+... .-.+.+.+..|.+|....+.- ++..+.+-+.+.+.-+.- ..+.+.- .+.-. T Consensus 7 ivliGd~~VGKTsli~r~~~~~f~~~~~~Ti~~~~~~k~i~~---~~~~v~l~iwDt~G~e~~----~~l~~~~~~~a~~ 79 (168) T cd01866 7 YIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITI---DGKQIKLQIWDTAGQESF----RSITRSYYRGAAG 79 (168) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEECCC---CCCEEEEEEEECCCCCCH----HHHHHHHCCCCCE T ss_conf 999816984389999998548257544530000001232146---784289998753888411----2453653479977 Q ss_pred EEEE-CCCCCCHHHHHHHHHHHHHHHHC-CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEE Q ss_conf 9985-16663446899999999998640-689987389984773456655324541157889999999999988294158 Q Fun_Sc_NP_0140 106 LILL-DWTLNDQKLWLNELSYAFNKIKQ-LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLF 183 (312) Q Consensus 106 ViLL-DWs~~Dp~~Wlr~Lr~~~~~L~~-l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLi 183 (312) +|++ |-+. +..+ ..+..|+...++ .+...++++|-.|+| |+++. ....++ .+.++-++|+..+ T Consensus 80 ~iivfdvt~--~~Sf-~~i~~w~~~~~~~~~~~~piilVGnK~D----L~~~r-~v~~~e-------~~~~a~~~~~~~~ 144 (168) T cd01866 80 ALLVYDITR--RETF-NHLTSWLEDARQHSNSNMTIMLIGNKCD----LESRR-EVSYEE-------GEAFAKEHGLIFM 144 (168) T ss_pred EEEEEECCC--HHHH-HHHHHHHHHHHHHCCCCCEEEEEECCHH----HHHHC-CCCHHH-------HHHHHHHCCCEEE T ss_conf 999976699--7789-9999999999973699968999833201----23304-776889-------9999996598499 Q ss_pred EECCCCCHHHHHHHHHHHHHHHHHHCCCCC Q ss_conf 852565313555667788887530012477 Q Fun_Sc_NP_0140 184 YICEDHTEEKREEAQRLKYQELLKHFCEDR 213 (312) Q Consensus 184 Yts~ts~~~~kn~~~~l~y~~L~~h~l~~~ 213 (312) -+ |+++..|-...+.. ++..++.+ T Consensus 145 E~---SAkt~~nV~~~F~~---la~~i~~~ 168 (168) T cd01866 145 ET---SAKTASNVEEAFIN---TAKEIYEK 168 (168) T ss_pred EE---ECCCCCCHHHHHHH---HHHHHHHC T ss_conf 98---61579887899999---99999719 No 10 >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=97.57 E-value=0.0041 Score=37.51 Aligned_columns=159 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+... .-.+.+.+..|.+|....+.-+ ..+..+.+-+-+.+..+.-..+.+..-..+.-.++| T Consensus 3 i~~iGd~~vGKTsli~r~~~~~f~~~~~~Tig~~~~~k~v~v~-~~~~~v~l~iwDt~g~e~~~~~~~~~~~~~~~~llv 81 (162) T cd04106 3 VIVVGNGNVGKSSMIQRFVKGIFTKDYKKTIGVDFLEKQIFLR-QSDEDVRLMLWDTAGQEEFDAITKAYYRGAQACILV 81 (162) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEEE-ECCEEEEEEEECCCCCCHHHHHHHHHCCCCCEEEEE T ss_conf 8998079844899999986282275556410104677789970-088479999871888800345537641489789999 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 98516663446899999999998640689987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) + +..|+...-+ +..|...++....+.++++|-.|+|-...-+=.. +-.+.+|-.+|+..|-| T Consensus 82 y----dvt~~~Sf~~-i~~w~~~i~~~~~~~p~ilVGNK~Dl~~~~~vs~------------~~~~~~a~~~~~~~~E~- 143 (162) T cd04106 82 F----STTDRESFEA-IESWKEKVEAECGDIPMVLVQTKIDLLDQAVITN------------EEAEALAKRLQLPLFRT- 143 (162) T ss_pred E----ECCCHHHHHH-HHHHHHHHHHHCCCCEEEEEECCCCCCCCCCCCH------------HHHHHHHHHCCCCEEEE- T ss_conf 8----6699789999-9999999998549937999821423212465898------------99999999669959999- Q ss_pred CCCCHHHHHHHHHHHHHHHHHHCC Q ss_conf 565313555667788887530012 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQELLKHFC 210 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~L~~h~l 210 (312) |+++..|-...+.+ ++.++ T Consensus 144 --SAk~~~nV~e~F~~---la~k~ 162 (162) T cd04106 144 --SVKDDFNVTELFEY---LAEKC 162 (162) T ss_pred --ECCCCCCHHHHHHH---HHHHC T ss_conf --71589887899999---98509 No 11 >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=97.50 E-value=0.0051 Score=36.92 Aligned_columns=150 Identities=13% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC--CCCE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778--7827 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS--SKVR 104 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s--~~~l 104 (312) ++++|+.+-|||+++.+... .-.+.+....|.+|....+.-+ ....++.+|=-.|---- ..+++.- .-.. T Consensus 9 vv~iGd~~VGKTsli~r~~~~~F~~~y~~Tig~~~~~k~v~i~-~~~~~l~iwDtaGqe~~------~~l~~~y~~~a~~ 81 (199) T cd04110 9 LLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEIN-GERVKLQIWDTAGQERF------RTITSTYYRGTHG 81 (199) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCCCCHH------HHHHHHHCCCCCE T ss_conf 9998269843899998876180076646511223578889985-83999999866997035------6776765038987 Q ss_pred EEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 99985166634468999999999986406899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 105 WLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 105 ~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +|+.-|-+. +..+ ..+..|+..+++..++.++++|..|+| |+..+-.-.++...|-.+ +|+..|. T Consensus 82 ~ilVydit~--~~Sf-~~i~~w~~~i~~~~~~~~~iLVGNK~D----l~~~r~v~~ee~~~~a~~--------~~~~f~E 146 (199) T cd04110 82 VIVVYDVTN--GESF-VNVKRWLQEIEQNCDDVCKVLVGNKND----DPERKVVETEDAYKFAGQ--------MGISLFE 146 (199) T ss_pred EEEEEECCC--HHHH-HHHHHHHHHHHHHCCCCCEEEEEECCC----CHHHCCCCHHHHHHHHHH--------CCCCEEE T ss_conf 999987799--7799-999999999985125673699840336----311226568999999996--------6995999 Q ss_pred ECCCCCHHHHHHHHHHHH Q ss_conf 525653135556677888 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKY 202 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y 202 (312) | |+++..|-..++.. T Consensus 147 t---SAktg~nV~e~F~~ 161 (199) T cd04110 147 T---SAKENINVEEMFNC 161 (199) T ss_pred E---ECCCCCCHHHHHHH T ss_conf 9---71589888899999 No 12 >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=97.50 E-value=0.0099 Score=35.19 Aligned_columns=154 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||.++.+... .=.+.+.+..|.+|....+.- |+.++.+-+.+.+..+...-+.+.. -..-.-++ T Consensus 3 iviiGd~~VGKTsli~~~~~~~f~~~~~~Tig~~~~~~~i~~---~~~~~~l~i~Dt~G~e~~~~l~~~~--~~~a~~~i 77 (161) T cd04113 3 FIIIGSSGTGKSCLLHRFVENKFKEDSQHTIGVEFGSKIIRV---GGKRVKLQIWDTAGQERFRSVTRSY--YRGAAGAL 77 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCCEEEEEEEE---CCEEEEEEEEECCCCCHHHHHHHHH--CCCCCEEE T ss_conf 899826985589999998628106665641012013589988---8969999983258870134555864--26997799 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCC-CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 985166634468999999999986406-8998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQL-NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l-~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) +.-|-+. +..+ ..++.|+..++.. +.+.++++|+.|+| |+.+.-...++. +.+|-++|...+.+ T Consensus 78 ivydi~~--~~Sf-~~i~~w~~~~~~~~~~~~~iilvgNK~D----L~~~r~v~~~e~--------~~~a~~~~~~~~e~ 142 (161) T cd04113 78 LVYDITN--RTSF-EALPTWLSDARALASPNIVVILVGNKSD----LADQREVTFLEA--------SRFAQENGLLFLET 142 (161) T ss_pred EEEECCC--HHHH-HHHHHHHHHHHHHCCCCCEEEEEECCCC----CCCCCCCCHHHH--------HHHHHHCCCEEEEE T ss_conf 9985598--6689-9999999999872489968999832456----421334588999--------99999659909999 Q ss_pred CCCCCHHHHHHHHHHHHHH Q ss_conf 2565313555667788887 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQE 204 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~ 204 (312) |+++..|-...+...+ T Consensus 143 ---Sak~~~ni~e~F~~la 158 (161) T cd04113 143 ---SALTGENVEEAFLKCA 158 (161) T ss_pred ---ECCCCCCHHHHHHHHH T ss_conf ---7158988889999999 No 13 >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=97.44 E-value=0.0057 Score=36.64 Aligned_columns=146 Identities=12% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC--CCCE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778--7827 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS--SKVR 104 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s--~~~l 104 (312) ++++|+.+-|||+|+.+... .-.+.+....++++....+.-+ .....+.+|=..|.-.- ..+.+.- .-.- T Consensus 3 iiliGd~~VGKTsli~r~~~~~f~~~~~~t~~~~~~~k~~~~~-~~~v~l~iwDt~G~e~~------~~~~~~~~~~a~~ 75 (161) T cd04124 3 IILLGDSAVGKSKLVERFLMDGYEPQQLSTYALTLYKHNAKFE-GKTILVDFWDTAGQERF------QTMHASYYHKAHA 75 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCCCCHH------HHHHHHHCCCCCE T ss_conf 8998069944889887865386376623532567899999998-86999999745784110------3566743024785 Q ss_pred EEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 99985166634468999999999986406899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 105 WLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 105 ~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +++.-|-+ -..=...+..|+..+++..++.++++|..|+| |+.+ +.+--+.++-++++..|. T Consensus 76 ~ilvfDit---~~~Sf~~l~~W~~~i~~~~~~~p~ilVGNK~D----l~~~-----------~~~~~~~~a~~~~~~~fe 137 (161) T cd04124 76 CILVFDVT---RKITYKNLSKWYEELREYRPEIPCIVVANKID----LDPS-----------VTQKKFNFAEKHNLPLYY 137 (161) T ss_pred EEEEEECC---CHHHHHHHHHHHHHHHHHCCCCEEEEEECCCC----CCHH-----------HHHHHHHHHHHCCCCEEE T ss_conf 89998669---96688999999999998469937999823765----6435-----------689999999965991999 Q ss_pred ECCCCCHHHHHHHHHHH Q ss_conf 52565313555667788 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLK 201 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~ 201 (312) | |+++..|-...+. T Consensus 138 t---SAk~g~nV~e~F~ 151 (161) T cd04124 138 V---SAADGTNVVKLFQ 151 (161) T ss_pred E---ECCCCCCHHHHHH T ss_conf 9---7268988789999 No 14 >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=97.35 E-value=0.018 Score=33.62 Aligned_columns=158 Identities=11% Q ss_pred EEEECCCCHHHHHHHHHHCCCC-CCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 8997598331799999851477-865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEG-SNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~-~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|..+.|||+|+.+..... .+.+.+..|.++....+ ..++..+.+-+.+.+..+.-..+.+..=..+.-..+| T Consensus 6 i~~iG~~~VGKTsli~r~~~~~F~~~~~~Tig~~~~~k~v---~~~~~~~~l~iwDtaG~e~~~~~~~~~~~~a~~~iiv 82 (165) T cd01868 6 IVLIGDSGVGKSNLLSRFTRNEFNLDSKSTIGVEFATRSI---QIDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLV 82 (165) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEE---EECCEEEEEEEECCCCCHHHHHHHHHHHCCCCEEEEE T ss_conf 9998269965899999986385674556410012468898---6489089999853898612457767650488679999 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCC-CEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 9851666344689999999999864068998-738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDN-EFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt-~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) + |-+. +..+.+- ..|+..++...... ++++|..|+| |+..+-.-.++.-+|..+ +|+..+-| T Consensus 83 y--Dit~--~~Sf~~i-~~w~~~i~~~~~~~~piilVGNK~D----L~~~r~v~~~e~~~~a~~--------~~~~~~e~ 145 (165) T cd01868 83 Y--DITK--KQTFENV-ERWLKELRDHADSNIVIMLVGNKSD----LRHLRAVPTEEAKAFAEK--------NGLSFIET 145 (165) T ss_pred E--ECCC--HHHHHHH-HHHHHHHHHHCCCCCEEEEEECCCC----HHHCCCCCHHHHHHHHHH--------CCCCEEEE T ss_conf 7--4699--7789999-9999999983289937999821656----212037768899999996--------59949999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCC Q ss_conf 25653135556677888875300124 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCE 211 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~ 211 (312) |+++..|-...+.. ++-.++ T Consensus 146 ---Sak~g~ni~~~F~~---l~~~i~ 165 (165) T cd01868 146 ---SALDGTNVEEAFKQ---LLTEIY 165 (165) T ss_pred ---ECCCCCCHHHHHHH---HHHHCC T ss_conf ---71479888899999---998709 No 15 >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=97.35 E-value=0.013 Score=34.48 Aligned_columns=151 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCC-CEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 8997598331799999851477865566557-502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTL-INYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~-L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+.|||+|+.+. -+.+++.+..+ ++-+|.-...-...+.++.+|=..| ...+..+.+..+ +.-..++ T Consensus 2 i~~iGd~~vGKTsli~r~--~~~~f~~~~~~ti~~~~~k~~~~~~~~~~l~i~Dt~G-~e~~~~~~~~~~---~~a~~~i 75 (160) T cd00876 2 VVVLGAGGVGKSAITIQF--VKGTFVEEYDPTIEDSYRKTIVVDGETYTLDILDTAG-QEEFSAMRDLYI---RQGDGFI 75 (160) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCCCCCCHHHEEEEEEEECCEEEEEEEEECCC-CHHHHHHHHHHH---CCCCEEE T ss_conf 788807996689999998--7281067535420022677888848289999863588-413346888764---0461789 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC--CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 98516663446899999999998640--6899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ--LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~--l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +.-|=+. +..+ ..+..|+..+++ .....++++|..|+| |..++-...++ .+.++-++|+..+- T Consensus 76 ivfdi~~--~~Sf-~~i~~w~~~i~~~~~~~~~piilvgNK~D----l~~~r~v~~~e--------~~~~a~~~~~~~~e 140 (160) T cd00876 76 LVYSITD--RESF-EEIKGYREQILRVKDDEDIPIVLVGNKCD----LENERQVSKEE--------GKALAKEWGCPFIE 140 (160) T ss_pred EEEECCC--HHHH-HHHHHHHHHHHHHCCCCCCEEEEEECCCC----CHHHCCCCHHH--------HHHHHHHCCCCEEE T ss_conf 9986699--7799-99999999999853899967999821326----30011676889--------99999964996999 Q ss_pred ECCCCCHHHHHHHHHHHH Q ss_conf 525653135556677888 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKY 202 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y 202 (312) | |+++..|-..++.. T Consensus 141 ~---Sak~~~nV~~~F~~ 155 (160) T cd00876 141 T---SAKDNINIDEVFKL 155 (160) T ss_pred E---EECCCCCHHHHHHH T ss_conf 9---70489888899999 No 16 >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=97.31 E-value=0.026 Score=32.68 Aligned_columns=194 Identities=12% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||.++.+... .-.+.+....|++|+...+.-+...+.++.+|-..|-.-...=.-.++-.++ .++ T Consensus 3 VvliGd~~VGKTSLi~rf~~~~F~~~y~~Tig~d~~~k~i~i~~~~~v~l~iwDtaGqe~~~~~~~~y~~~a~----~~i 78 (215) T cd04109 3 IVVLGDGAVGKTSLCRRFAKEGFGKSYKQTIGLDFFSKRVTLPGNLNVTLQVWDIGGQSIGGKMLDKYIYGAH----AVF 78 (215) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEECCCCEEEEEEEECCCCCHHHHHHHHHHCCCC----EEE T ss_conf 8998269853899998877072177646514567878999975860589999864773023688998705998----489 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCC-EEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 98516663446899999999998640689987-38998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNE-FSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~-i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) +.-|=+..+.-.-+......++....-....+ |++|--|+|- +..+.+=.+++ +.+|-++|+..|.| T Consensus 79 lVYdIt~~~SF~~i~~W~~~i~~~~~~~~~~~~iiLVGNK~DL----~~~R~Vs~ee~--------~~~A~~~~~~f~Ev 146 (215) T cd04109 79 LVYDVTNSQSFENLEDWYSMVRKVLKSSETQPLVVLVGNKTDL----EHNRTVKDDKH--------ARFAQANGMESCLV 146 (215) T ss_pred EEEECCCHHHHHHHHHHHHHHHHHHHCCCCCCEEEEECCCCCH----HHCCCCCHHHH--------HHHHHHCCCCEEEE T ss_conf 9975389768999999999999873105898189996054240----12066798999--------99999649959999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCEECCCCEEECCCCCHHHHHHHHCC Q ss_conf 25653135556677888875300124778775224011563020668881462420047 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEMVTRSEILIPKGCDSIGLIKTVDE 244 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~vverd~vfIP~GwDS~~KI~ii~E 244 (312) |+++..|-..++.. ++-.+.|-..++. ++-..+.+.-...-..-+.+++.++ T Consensus 147 ---SAktg~nV~elF~~---la~~i~~~~~~~~-~~~~~~~~~~~~~~~~~~~~~~~~~ 198 (215) T cd04109 147 ---SAKTGDRVNLLFQQ---LAAELLGVDLSKA-ELEQSQRVVKAVVVNTEERVSIPHQ 198 (215) T ss_pred ---ECCCCCCHHHHHHH---HHHHHHCCCCCHH-HCCCCCCCCCCCCCCCCCCEECCCC T ss_conf ---62679888899999---9999808631101-0454432000112344431004565 No 17 >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=97.31 E-value=0.012 Score=34.64 Aligned_columns=158 Identities=12% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+++.+... +=.+.+.+..|.+|....+.-+ .....+..|=..| .+.+..+.+..+ +.-.-++ T Consensus 4 iilvGd~~VGKTsli~rf~~~~f~~~y~~Ti~~~~~~k~i~~~-~~~v~l~iwDt~G-~e~~~~~~~~~~---~~~~~~i 78 (165) T cd01865 4 LLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFRN-DKRVKLQIWDTAG-QERYRTITTAYY---RGAMGFI 78 (165) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCC-CCHHHHHHHHHC---CCCCEEE T ss_conf 9998079953899888764481066634303656789999877-9389999974588-701345656433---6998899 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCC-CCCCEEEEEECCCHHHH--HHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEE Q ss_conf 9851666344689999999999864068-99873899847734566--55324541157889999999999988294158 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLN-DDNEFSVWCLNSGEILN--LQRHTTVWQSVHIDFILQTLRSFCYFNDSSLF 183 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~-~Dt~i~VVc~~sD~i~~--LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLi 183 (312) +.-|-+. +..+ ..+.+|.+.+++.. .+.++++|-.|+|-... ...+.+ +.+|=++|...| T Consensus 79 ivfd~t~--~~Sf-~~i~~w~~~i~~~~~~~~~iilVGNK~Dl~~~r~v~~~~~--------------~~~a~~~~~~y~ 141 (165) T cd01865 79 LMYDITN--EESF-NAVQDWSTQIKTYSWDNAQVILVGNKCDMEDERVVSSERG--------------RQLADQLGFEFF 141 (165) T ss_pred EEEECCC--HHHH-HHHHHHHHHHHHHCCCCEEEEEEECCCCHHHHHHHHHHHH--------------HHHHHHCCCCEE T ss_conf 9986698--6689-9999999999860699608999721777246553138899--------------999996599499 Q ss_pred EECCCCCHHHHHHHHHHHHHHHHHHCCCCC Q ss_conf 852565313555667788887530012477 Q Fun_Sc_NP_0140 184 YICEDHTEEKREEAQRLKYQELLKHFCEDR 213 (312) Q Consensus 184 Yts~ts~~~~kn~~~~l~y~~L~~h~l~~~ 213 (312) .| |+++..|-...+.. ++..+..+ T Consensus 142 Et---SAk~~~nV~e~F~~---l~~~i~~k 165 (165) T cd01865 142 EA---SAKENINVKQVFER---LVDIICDK 165 (165) T ss_pred EE---ECCCCCCHHHHHHH---HHHHHHCC T ss_conf 99---71589887899999---99998429 No 18 >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=97.30 E-value=0.021 Score=33.27 Aligned_columns=173 Identities=9% Q ss_pred CEEEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCE Q ss_conf 4389975983317999998514-778655665575025633562121332688998607854358878877187787827 Q Fun_Sc_NP_0140 26 ITAIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVR 104 (312) Q Consensus 26 k~~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l 104 (312) |-++++|+++-|||+++.+... .-.+.+.+..+..|.......+ .....+.+|=-.|. ..|-.+-+.....-. - T Consensus 1 ~KVvliGd~~VGKTsli~r~~~~~F~~~~~~Ti~~~~~~~~~~~~-~~~v~l~iwDtaGq-e~f~~l~~~~~~~a~---~ 75 (187) T cd04132 1 KKIVVVGDGGCGKTCLLIVYSQGKFPEEYVPTVFENYVTNIQGPN-GKIIELALWDTAGQ-EEYDRLRPLSYPDVD---V 75 (187) T ss_pred CEEEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECC-CEEEEEEEECCCCC-HHHHHHHHHHHCCCC---E T ss_conf 968998179832899998876182267646515767899999738-81899986148775-245778887724897---5 Q ss_pred EEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 99985166634468999999999986406899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 105 WLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 105 ~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +++.-|-+. +..+-+....|+..+++...+.++++|..|+|-.+.-+...-+-.++. +.++-..|+..++ T Consensus 76 ~ilvyDit~--~~Sf~~~~~~W~~~i~~~~~~~piilVGNK~DL~~~~~~~r~V~~~e~--------~~~a~~~~~~~y~ 145 (187) T cd04132 76 LLICYAVDN--PTSLDNVEDKWFPEVNHFCPGTPIMLVGLKTDLRKDKNLDRKVTPAQA--------ESVAKKQGAFAYL 145 (187) T ss_pred EEEEEECCC--HHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCHHHHCCCCCCCHHHH--------HHHHHHCCCCEEE T ss_conf 899986599--789999998778999984589779998416751223111367898899--------9999973893268 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCC Q ss_conf 5256531355566778888753001247787752 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDH 218 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~ 218 (312) - +|++...|-..++.. ++-..+.++.+.. T Consensus 146 E--tSAk~g~nV~e~F~~---l~~~~l~~~~~~~ 174 (187) T cd04132 146 E--CSAKTMENVEEVFDT---AIEEALKKEGKAI 174 (187) T ss_pred E--EEECCCCCHHHHHHH---HHHHHHHCCCCCC T ss_conf 9--861278887899999---9999986047776 No 19 >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=97.29 E-value=0.017 Score=33.77 Aligned_columns=157 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+.|||+|+.+... .-.+.+.+..|.+|....+.-+ ..+.++.+|=..| ...+..+.+.++ +.-..++ T Consensus 3 I~~iG~~~vGKTsli~r~~~~~f~~~~~~Tig~~~~~k~i~~~-~~~v~l~i~Dt~G-~e~~~~l~~~~~---~~~~~~i 77 (161) T cd01861 3 LVFLGDQSVGKTSIITRFMYDTFDNQYQATIGIDFLSKTMYLE-DKTVRLQLWDTAG-QERFRSLIPSYI---RDSSVAV 77 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEEC-CEEEEEEEECCCC-CHHHHHHHHHHC---CCCCCEE T ss_conf 8998179855899999886381266557434336888899887-9399999851788-425778889860---3888179 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHH-CCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 9851666344689999999999864-068998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIK-QLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~-~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) +.-|-+. +-.+-+ +..|+..++ ..+.+.++++|..|+|-...-+-.. +-.+.++-++|+..|-+ T Consensus 78 lvyd~t~--~~Sf~~-~~~w~~~i~~~~~~~~~iilVgNK~Dl~~~~~v~~------------~~~~~~a~~~~~~~~E~ 142 (161) T cd01861 78 VVYDITN--RQSFDN-TDKWIDDVRDERGNDVIIVLVGNKTDLSDKRQVST------------EEGEKKAKELNAMFIET 142 (161) T ss_pred EEEECCC--HHHHHH-HHHHHHHHHHHCCCCCEEEEEECCCCHHHCCCCCH------------HHHHHHHHHCCCCEEEE T ss_conf 9985398--768999-99999888862399978999715533212136768------------89999999659939999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCC Q ss_conf 2565313555667788887530012 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFC 210 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l 210 (312) |++...|-...+.. ++..+ T Consensus 143 ---Sak~~~nV~e~F~~---ia~~l 161 (161) T cd01861 143 ---SAKAGHNVKELFRK---IASAL 161 (161) T ss_pred ---ECCCCCCHHHHHHH---HHHHC T ss_conf ---71489787899999---99839 No 20 >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=97.26 E-value=0.022 Score=33.07 Aligned_columns=158 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|..+.|||+|+.+... +=.+.+.+..|..|....+.-| .....++.|=..| ...+.++.+..... -.-++ T Consensus 4 i~iiG~~gvGKTsli~r~~~~~f~~~~~pTig~~~~~k~i~~~-~~~v~l~i~Dt~G-~e~~~~l~~~~~~~---a~~~i 78 (163) T cd01860 4 LVLLGDSSVGKSSLVLRFVKNEFSENQESTIGAAFLTQTVNLD-DTTVKFEIWDTAG-QERYRSLAPMYYRG---AAAAI 78 (163) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEEEEEEEEEC-CEEEEEEEECCCC-CHHHHHHHHHHHCC---CCEEE T ss_conf 9998169965899999886283375535101322568899888-8799999704898-31245666765138---88499 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC-CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 98516663446899999999998640-68998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ-LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~-l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) +.-|-+ ..-=...+..|+..+++ ...+.++++|..|+| |+.++..-.++ .+.+|-++|+..+.+ T Consensus 79 lvydit---~~~Sf~~i~~w~~~i~~~~~~~~~iilVgNK~D----l~~~r~v~~~e--------~~~~a~~~~~~~~e~ 143 (163) T cd01860 79 VVYDIT---SEESFEKAKSWVKELQRNASPNIIIALVGNKAD----LESKRQVSTEE--------AQEYADENGLLFFET 143 (163) T ss_pred EEEECC---CHHHHHHHHHHHHHHHHHCCCCCEEEEEECCHH----HHHCCCCCHHH--------HHHHHHHCCCEEEEE T ss_conf 998659---978999999988765530699958999832210----54305887899--------999999659929999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCC Q ss_conf 25653135556677888875300124 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCE 211 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~ 211 (312) |+++..|-...+.. ++..+. T Consensus 144 ---SAk~~~nI~~~F~~---l~~~i~ 163 (163) T cd01860 144 ---SAKTGENVNELFTE---IAKKLP 163 (163) T ss_pred ---ECCCCCCHHHHHHH---HHHHCC T ss_conf ---71489888899999---998579 No 21 >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=97.25 E-value=0.024 Score=32.83 Aligned_columns=157 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+... .-.+.+.+..|.++....+.- ++.++.+.+.+.+.-+-...+.+..-..+.-..+| T Consensus 6 ivivGd~~vGKTsli~rf~~~~F~~~~~~tig~~~~~k~i~~---~~~~v~l~iwDt~G~e~~~~l~~~~~~~~~~~ilv 82 (165) T cd01864 6 IILIGDSNVGKTCVVQRFKSGTFSERQGNTIGVDFTMKTLEI---EGKRVKLQIWDTAGQERFRTITQSYYRSANGAIIA 82 (165) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEE---CCEEEEEEEEECCCCCHHHHHHHHHCCCCCEEEEE T ss_conf 999807994489999987628207766771125778999998---89589999975488701357768642699879999 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCC-CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEE-EE Q ss_conf 985166634468999999999986406-8998738998477345665532454115788999999999998829415-88 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQL-NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSL-FY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l-~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASL-iY 184 (312) + +..++..+-+ +..|+..+++. +.+.++++|..|+| |+.++.. -..-.+.+|-++|+-- |- T Consensus 83 y----dit~~~Sf~~-l~~w~~~i~~~~~~~~~ivlVGNK~D----l~~~r~V--------~~~~~~~~a~~~~~~~~~E 145 (165) T cd01864 83 Y----DITRRSSFES-VPHWIEEVEKYGASNVVLLLIGNKCD----LEEQREV--------LFEEACTLAEKNGMLAVLE 145 (165) T ss_pred E----ECCCHHHHHH-HHHHHHHHHHCCCCCCEEEEEECCCC----CCCCCCC--------CHHHHHHHHHHCCCCEEEE T ss_conf 8----7599779999-99988889851698957999724211----0003554--------5789999999649948999 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCC Q ss_conf 52565313555667788887530012 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFC 210 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l 210 (312) | |+++..|-...+.+ ++..+ T Consensus 146 ~---SAk~~~nv~e~F~~---la~~i 165 (165) T cd01864 146 T---SAKESQNVEEAFLL---MATEL 165 (165) T ss_pred E---EECCCCCHHHHHHH---HHHHC T ss_conf 7---40489898899999---99829 No 22 >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=97.24 E-value=0.011 Score=34.99 Aligned_columns=163 Identities=6% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+.+-|||+|+.+.....-.+-...+....+...+.-+ .....+.+|=..| ...+-.+.+.+. +.-.-+++ T Consensus 3 i~liGd~~VGKTsli~r~~~~~f~~~~~~Ti~~~~~~~i~~~-~~~~~l~iwDt~G-~e~~~~l~~~~~---~~a~~~il 77 (171) T cd00157 3 IVVVGDGAVGKTCLLISYTTGKFPTEYVPTVFDNYSATVTVD-GKQVNLGLWDTAG-QEEYDRLRPLSY---PNTDVFLI 77 (171) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCC-CHHHHHHHHHHH---CCCCEEEE T ss_conf 899807995489999998638316653432652145578755-6799999960677-434678989873---28985899 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEECC Q ss_conf 85166634468999999999986406899873899847734566553245411578899999999999882941588525 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYICE 187 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts~ 187 (312) .-|-+. +...-+.+..|+..++....+.++++|..|+|-.+.=+..- ...+.+=-.-.+-.+.+|-.+|+..+|- T Consensus 78 vydit~--~~Sf~~~~~~w~~~i~~~~~~~piilVgnK~DL~~~~~~~~-~~~~~~r~Vs~~e~~~~a~~~~~~~f~E-- 152 (171) T cd00157 78 CFSVDS--PSSFENVKTKWIPEIRHYCPNVPIILVGTKIDLRDDENTLK-KLEKGKEPITPEEGEKLAKEIGAIGYME-- 152 (171) T ss_pred EEECCC--HHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCCCCHHHHH-HHHCCCCCCCHHHHHHHHHHCCCCEEEE-- T ss_conf 971688--65899999998999998468956999853744212112232-2101357789899999999739952788-- Q ss_pred CCCHHHHHHHHHH Q ss_conf 6531355566778 Q Fun_Sc_NP_0140 188 DHTEEKREEAQRL 200 (312) Q Consensus 188 ts~~~~kn~~~~l 200 (312) +|+++..|-..++ T Consensus 153 tSAktg~nV~e~F 165 (171) T cd00157 153 CSALTQEGVKEVF 165 (171) T ss_pred EECCCCCCHHHHH T ss_conf 7504898878999 No 23 >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=97.23 E-value=0.021 Score=33.24 Aligned_columns=159 Identities=14% Q ss_pred EEEECCCCHHHHHHHHHHCCCC-CCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 8997598331799999851477-865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEG-SNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~-~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-||++++.+..... .+.+.+..|.+|....+.-+ ....++.+|=..|.... ..+.+.+. +.-.-++ T Consensus 3 ivivGd~~vGKTsli~r~~~~~f~~~y~~Tig~~~~~k~i~~~-~~~~~l~iwDtaG~e~~-~~~~~~~~---~~a~~~i 77 (168) T cd04119 3 VISMGNSGVGKSCIIKRYCEGRFVSKYLPTIGIDYGVKKVSVR-NKEVRVNFFDLSGHPEY-LEVRNEFY---KDTQGVL 77 (168) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCCCHHH-HHHHHHHH---CCCCEEE T ss_conf 8998079854899998877180166536503555556788887-94899998606898125-78878872---3999389 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC------CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCC Q ss_conf 98516663446899999999998640------689987389984773456655324541157889999999999988294 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ------LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDS 180 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~------l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGA 180 (312) +.-|=+. +...-+ +..|+..+++ .....++++|-.|+|-...-+-.. +-.+.+|-.+|+ T Consensus 78 lvydit~--~~Sf~~-i~~w~~~~~~~~~~~~~~~~~~iilvGNK~Dl~~~r~V~~------------~~~~~~a~~~~~ 142 (168) T cd04119 78 LVYDVTD--RQSFEA-LDSWLKEMKQEGGPHGNMENIVVVVCANKIDLTKHRAVSE------------DEGRLWAESKGF 142 (168) T ss_pred EEEECCC--HHHHHH-HHHHHHHHHHHCCCCCCCCCCEEEEEECCCCCCCCCCCCH------------HHHHHHHHHCCC T ss_conf 9985699--778999-9999999998605556668747999705323323576798------------999999996499 Q ss_pred EEEEECCCCCHHHHHHHHHHHHHHHHHHCCCC Q ss_conf 15885256531355566778888753001247 Q Fun_Sc_NP_0140 181 SLFYICEDHTEEKREEAQRLKYQELLKHFCED 212 (312) Q Consensus 181 SLiYts~ts~~~~kn~~~~l~y~~L~~h~l~~ 212 (312) ..|-| |+++..|-...+.. ++..+.+ T Consensus 143 ~~~E~---SAk~~~nV~e~F~~---l~~~i~d 168 (168) T cd04119 143 KYFET---SACTGEGVNEMFQT---LFSSIVD 168 (168) T ss_pred EEEEE---ECCCCCCHHHHHHH---HHHHHCC T ss_conf 19999---71589787899999---9998559 No 24 >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=97.21 E-value=0.026 Score=32.66 Aligned_columns=167 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCCCCC--CCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEE Q ss_conf 89975983317999998514778--6556655750256335621213326889986078543588788771877878279 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGS--NSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRW 105 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~--e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~ 105 (312) ++++|+.+-|||+|+.+.....- +.+....|..|....+.-+ ....++.+|=-.|- +.+..+.+.....-.- + T Consensus 3 Iv~iGd~~VGKTsli~r~~~~~f~~~~~~~Tig~~~~~k~i~~~-~~~i~l~iwDtaGq-e~~~~l~~~yy~~a~~---~ 77 (191) T cd04112 3 VMLLGDSGVGKTCLLVRFKDGAFLNGNFIATVGIDFRNKVVTVD-GVKVKLQIWDTAGQ-ERFRSVTHAYYRDAHA---L 77 (191) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEEC-CEEEEEEEEECCCC-HHHHHHHHHHHCCCCE---E T ss_conf 89982699548999988762822587634211100367789887-93899998755887-0124553666138977---9 Q ss_pred EEEECCCCCCHHHHHHHHHHHHHHHHCC-CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 9985166634468999999999986406-899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 106 LILLDWTLNDQKLWLNELSYAFNKIKQL-NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 106 ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l-~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +|.-|-+. +..+-. +..|+..+++. ..+.++++|-.|+| |+.++ .-+.++. +.++-.+|+..|- T Consensus 78 iivyDit~--~~Sf~~-i~~w~~~i~~~~~~~~~ivlVGNK~D----L~~~r-~V~~~e~-------~~~a~~~~~~~~E 142 (191) T cd04112 78 LLLYDITN--KASFDN-IRAWLTEIKEYAQEDVVIMLLGNKAD----MSGER-VVKREDG-------ERLAKEYGVPFME 142 (191) T ss_pred EEEEECCC--HHHHHH-HHHHHHHHHHHCCCCCEEEEEEECCC----CCCCC-CCCHHHH-------HHHHHHCCCCEEE T ss_conf 99987799--789999-99999988852699948999863277----63225-5388999-------9999966995999 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCC Q ss_conf 525653135556677888875300124778775224 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIE 220 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~ 220 (312) | |+++..|-..++.. ++..+..+....+.. T Consensus 143 t---SAk~~~nI~e~F~~---l~~~i~~~~~~~~~~ 172 (191) T cd04112 143 T---SAKTGLNVELAFTA---VAKELKHRKYEQPDE 172 (191) T ss_pred E---ECCCCCCHHHHHHH---HHHHHHHHCCCCCCC T ss_conf 9---62589888899999---999999723788876 No 25 >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=97.20 E-value=0.028 Score=32.43 Aligned_columns=158 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+.|||+|+.+... .-.+.+....+.++....+.-+ +.++.+-+.+.+..+-..-+.+..-.++.-..+| T Consensus 3 i~~iGd~~vGKTsli~r~~~~~f~~~~~~ti~~~~~~k~i~~~---~~~~~l~iwDt~G~~~~~~~~~~~~~~a~~~ilv 79 (162) T cd04123 3 VVLLGEGRVGKTSLVLRYVENKFNEKHESTTQASFFQKTVNIG---GKRIDLAIWDTAGQERYHALGPIYYRDADGAILV 79 (162) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCCCEEEEEECC---CCEEEEEEEECCCCHHHHHHHHHHHCCCCEEEEE T ss_conf 8998269965899999986281177645411244135533159---9389999730787502356657661489868999 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC-CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 98516663446899999999998640-68998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ-LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~-l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) + |-+. +..+-+. +.|+..++. .+.+.++++|..|+| |++++..-.++ .+.+|-++|+..+-+ T Consensus 80 y--dit~--~~Sf~~i-~~w~~~i~~~~~~~~piilVGNK~D----l~~~r~V~~~~--------~~~~a~~~~~~~~E~ 142 (162) T cd04123 80 Y--DITD--ADSFQKV-KKWIKELKQMRGNNISLVIVGNKID----LERQRVVSKSE--------AEEYAKSVGAKHFET 142 (162) T ss_pred E--ECCC--HHHHHHH-HHHHHHHHHHCCCCCEEEEEEEHHH----HHHHCCCCHHH--------HHHHHHHCCCCEEEE T ss_conf 4--2798--7789999-9999989973189965999840023----12102547789--------999999649938999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCC Q ss_conf 25653135556677888875300124 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCE 211 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~ 211 (312) |+++..|-...+.. ++..+. T Consensus 143 ---Sak~~~nv~e~F~~---l~~~il 162 (162) T cd04123 143 ---SAKTGKGIEELFLS---LAKRMI 162 (162) T ss_pred ---ECCCCCCHHHHHHH---HHHHHC T ss_conf ---71589787899999---999829 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=97.19 E-value=0.026 Score=32.64 Aligned_columns=160 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+.|||+|+.++.. .-.+.+.+..+..+....+.-+ .....+..|-..| ...+..+.+-++.. -..++ T Consensus 2 i~viG~~~vGKTsli~r~~~~~f~~~~~~Ti~~~~~~k~v~~~-~~~~~l~i~Dt~g-~e~~~~~~~~~~~~---ad~~i 76 (162) T pfam00071 2 LVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIGVDFYTKTIEVD-GKTVKLQIWDTAG-QERFRSLRPAYYRG---AQGFL 76 (162) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEEC-CEEEEEEEEECCC-CCHHHHHHHHHCCC---CCEEE T ss_conf 7888179966899999986383276544201015789999873-6799999986699-80135675865048---98899 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 98516663446899999999998640689987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) +.-|-+..+....++.....+..-.+ .+.++++|++|+|-...-+-.. +-.+.++-++|+..|.| T Consensus 77 lvfd~~~~~Sf~~i~~w~~~i~~~~~--~~~piilvgnK~Dl~~~~~i~~------------~e~~~~~~~~~~~y~e~- 141 (162) T pfam00071 77 LVYDITSRDSFENVKKWLEEILRHAD--ENVPIVLVGNKCDLEDQRVVST------------EEGEALAKELGLPFMET- 141 (162) T ss_pred EEEECCCHHHHHHHHHHHHHHHHHCC--CCCEEEEEEECCHHHHHCCCCH------------HHHHHHHHHCCCCEEEE- T ss_conf 99877997899999999999998459--9948999850420112116768------------89999999649959999- Q ss_pred CCCCHHHHHHHHHHHHHHHHHHCCCC Q ss_conf 56531355566778888753001247 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQELLKHFCED 212 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~L~~h~l~~ 212 (312) |++...|-..++.. ++..+.. T Consensus 142 --Sak~g~gI~e~F~~---l~~~i~~ 162 (162) T pfam00071 142 --SAKTNTNVEEAFEE---LAREILK 162 (162) T ss_pred --ECCCCCCHHHHHHH---HHHHHHC T ss_conf --71479888899999---9999809 No 27 >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=97.13 E-value=0.027 Score=32.54 Aligned_columns=160 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||.|+.+... .-.+.+.+..|.+|....+.-+ ....++.+|=..| .+.+..+.......- .-++ T Consensus 5 iv~vGd~~vGKTsli~r~~~~~f~~~y~~Tig~~~~~k~i~~~-~~~v~l~iwDt~G-~e~~~~l~~~~~~~a---~~~i 79 (166) T cd01869 5 LLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELD-GKTIKLQIWDTAG-QERFRTITSSYYRGA---HGII 79 (166) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCC-CHHHHHHHHHHCCCC---CEEE T ss_conf 9998269954899999875380066657601235678899998-9589999862688-601123112122689---8899 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHH-HCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 985166634468999999999986-4068998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKI-KQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L-~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) |.-|-+ ...=...+..|+..+ +...++.++++|-.|+|-...-+-+ .+-.+.++-.+|+..+-| T Consensus 80 ivfdit---~~~Sf~~i~~w~~~i~~~~~~~~~~ilVGNK~Dl~~~r~V~------------~~~~~~~a~~~~~~~~E~ 144 (166) T cd01869 80 IVYDVT---DQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTDKRVVD------------YSEAQEFADELGIPFLET 144 (166) T ss_pred EEEECC---CHHHHHHHHHHHHHHHHHCCCCCEEEEEEECCCCCCCCCCC------------HHHHHHHHHHCCCCEEEE T ss_conf 998679---85689999999999987259982799985033333245579------------899999999659959999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCCCC Q ss_conf 2565313555667788887530012477 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCEDR 213 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~~~ 213 (312) |++...|-...+.. ++..+..+ T Consensus 145 ---Sak~g~~V~e~F~~---la~~i~~~ 166 (166) T cd01869 145 ---SAKNATNVEQAFMT---MAREIKKR 166 (166) T ss_pred ---ECCCCCCHHHHHHH---HHHHHHCC T ss_conf ---71489887899999---99999609 No 28 >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=97.12 E-value=0.081 Score=29.67 Aligned_columns=157 Identities=5% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||.|+.+... .=.+.+....|.+|....+.- ++.++.+.+.+.+..+.-..+.+..-..+. -++ T Consensus 3 IiliGd~~VGKTsli~rf~~~~F~~~~~~Tig~~~~~k~i~~---~~~~i~l~iwDtaG~e~~~~l~~~~~~~a~--~~i 77 (161) T cd04117 3 LLLIGDSGVGKTCLLCRFTDNEFHSSHISTIGVDFKMKTIEV---DGIKVRIQIWDTAGQERYQTITKQYYRRAQ--GIF 77 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEEEEEEEEE---CCEEEEEEEEECCCCHHHHHHHHHHCCCCC--EEE T ss_conf 899826984489999987548217543442211146789989---896999998746987235667686446998--899 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCC-CCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 985166634468999999999986406899-8738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDD-NEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~D-t~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) +.-|-+. +...-+... |+..+++..++ .++++|..|+| |++.+ ..-..-.+.++-.+|+..|.| T Consensus 78 lvydit~--~~Sf~~i~~-w~~~i~~~~~~~~~~ilVgnK~D----l~~~r--------~v~~~e~~~~a~~~~~~~~E~ 142 (161) T cd04117 78 LVYDISS--ERSYQHIMK-WVSDVDEYAPEGVQKILIGNKAD----EEQKR--------QVGDEQGNKLAKEYGMDFFET 142 (161) T ss_pred EEEECCC--HHHHHHHHH-HHHHHHHHCCCCCEEEEEECCCC----HHHHH--------HHHHHHHHHHHHHCCCCEEEE T ss_conf 9986599--789999999-99999972579946999811578----02311--------146899999999659969999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHH Q ss_conf 2565313555667788887530 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLK 207 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~ 207 (312) |+++..|-...+...+=++ T Consensus 143 ---SAk~~~nV~e~F~~la~li 161 (161) T cd04117 143 ---SACTNSNIKESFTRLTELV 161 (161) T ss_pred ---ECCCCCCHHHHHHHHHHHC T ss_conf ---7158988789999999829 No 29 >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=97.12 E-value=0.043 Score=31.34 Aligned_columns=156 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|..+-|||+|+.+... .-.+.+.+..|.++.-..+.-+ ....++..|=..|. ..+..+.+.....-. .++ T Consensus 3 iv~iG~~~VGKTsli~r~~~~~f~~~~~~Ti~~~~~~k~i~~~-~~~~~l~iwDt~G~-e~~~~l~~~~~~~~~---~~i 77 (161) T cd01863 3 ILLIGDSGVGKSSLLLRFTDDTFDPDLAATIGVDFKVKTLTVD-GKKVKLAIWDTAGQ-ERFRTLTSSYYRGAQ---GVI 77 (161) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCCC-CHHHHHHHHHCCCCC---EEE T ss_conf 8998079965899999986282077656510002458899898-96999999754887-101245475435998---799 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC--CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 98516663446899999999998640--6899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ--LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~--l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +.-|-+ ..-=...+..|+..+++ ...+-++++|..|+| |+..... ..-.+.++..+|+..+. T Consensus 78 ~vfd~t---~~~Sf~~i~~w~~~i~~~~~~~~~~~ilvGNK~D----l~~r~v~---------~~e~~~~a~~~~~~~~e 141 (161) T cd01863 78 LVYDVT---RRDTFTNLETWLNELETYSTNNDIVKMLVGNKID----KENREVT---------REEGLKFARKHNMLFIE 141 (161) T ss_pred EEEECC---CHHHHHHHHHHHHHHHHHCCCCCCEEEEECCCCC----CCCCCCC---------HHHHHHHHHHCCCEEEE T ss_conf 998569---8679999999999999733899938999612334----3000488---------88999999966992999 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCC Q ss_conf 52565313555667788887530012 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFC 210 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l 210 (312) + |++...|-..++.. ++..+ T Consensus 142 ~---SAk~~~nv~e~F~~---l~~~i 161 (161) T cd01863 142 T---SAKTRDGVQQAFEE---LVEKI 161 (161) T ss_pred E---ECCCCCCHHHHHHH---HHHHC T ss_conf 9---70589787899999---99849 No 30 >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=97.10 E-value=0.034 Score=31.95 Aligned_columns=158 Identities=13% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+... .=.+.+....|++|....+.-| .+..++.+|=-.|--.--..+.+.....-. -++ T Consensus 5 ivliGd~~VGKTsli~r~~~~~F~~~~~~Tig~d~~~k~i~~~-~~~v~l~iwDtaGqe~f~~~l~~~y~~~a~---~~i 80 (170) T cd04115 5 IIVIGDSNVGKTCLTYRFCAGRFPERTEATIGVDFRERTVEID-GERIKVQLWDTAGQERFRKSMVQHYYRNVH---AVV 80 (170) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEEC-CEEEEEEEECCCCCHHHHHHHHHHHCCCCC---EEE T ss_conf 9998079965899999986285575445312203578999988-958999982278733567777654304898---489 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC--CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 98516663446899999999998640--6899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ--LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~--l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +.-|-+. +...-+ +..|+..+++ .+.+.++++|+.|+|--..-+-.. +-.+.+|-.+|+..|- T Consensus 81 lvydit~--~~SF~~-i~~w~~~i~~~~~~~~~p~iLVGNK~DL~~~r~Vs~------------~e~~~~A~~~~~~~fE 145 (170) T cd04115 81 FVYDVTN--MASFHS-LPSWIEECEQHSLPNEVPRILVGNKCDLREQIQVPT------------DLAQRFADAHSMPLFE 145 (170) T ss_pred EEEECCC--HHHHHH-HHHHHHHHHHHCCCCCCEEEEEECCCCCHHHCCCCH------------HHHHHHHHHCCCCEEE T ss_conf 9987699--778899-999999999725998617999802135012136798------------9999999966995999 Q ss_pred ECCCCCH---HHHHHHHHHHHHHHHHHCC Q ss_conf 5256531---3555667788887530012 Q Fun_Sc_NP_0140 185 ICEDHTE---EKREEAQRLKYQELLKHFC 210 (312) Q Consensus 185 ts~ts~~---~~kn~~~~l~y~~L~~h~l 210 (312) | |++ +..|-...+.. ++..+ T Consensus 146 ~---SAK~~~~~~nV~~~F~~---la~~l 168 (170) T cd04115 146 T---SAKDPSENDHVEAIFMT---LAHKL 168 (170) T ss_pred E---ECCCCCCCCCHHHHHHH---HHHHH T ss_conf 8---62678888687899999---99996 No 31 >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=97.07 E-value=0.046 Score=31.15 Aligned_columns=168 Identities=14% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||.++.+... .-.+.+....|.+|....+.-+ .+...+.+| +.+.-+.-..+.+..-..+.-..+| T Consensus 3 IvviGd~~VGKTsli~r~~~~~f~~~~~~Tig~d~~~k~i~~~-~~~v~l~iw--DtaGqe~~~~l~~~~~~~a~~~ilv 79 (188) T cd04125 3 VVIIGDYGVGKSSLLKRFTEDEFSESTKSTIGVDFKIKTVYIE-NKIIKLQIW--DTNGQERFRSLNNSYYRGAHGYLLV 79 (188) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEC-CEEEEEEEE--ECCCCCHHHHHHHHHHCCCCEEEEE T ss_conf 8998269954899999876280177646730212578899986-849999987--5699820256768763089859999 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCE-EEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 985166634468999999999986406899873-8998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEF-SVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i-~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) + +..++..+-. +..|+..++....+... ++|+.|+| |+.++..-.++ .+.++-++|+..|-| T Consensus 80 y----Dit~~~Sf~~-i~~w~~~i~~~~~~~~~~ilvgNK~D----L~~~r~V~~~~--------~~~~a~~~~~~~fEt 142 (188) T cd04125 80 Y----DVTDQESFEN-LKFWINEINRYARENVIKVIVANKSD----LVNNKVVDSNI--------AKSFCDSLNIPFFET 142 (188) T ss_pred E----ECCCHHHHHH-HHHHHHHHHHHCCCCCEEEEEEECCC----CHHHCCCCHHH--------HHHHHHHCCCCEEEE T ss_conf 8----6699789999-99999999861699968999851352----30123369999--------999998569929999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCC Q ss_conf 256531355566778888753001247787752 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCEDRDMKDH 218 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~ 218 (312) |+++..|-...+.+..=.+..........+ T Consensus 143 ---SAktg~nV~e~F~~l~~~il~~~~~~~~~~ 172 (188) T cd04125 143 ---SAKQSINVEEAFILLVKLIIKRLEEQELSP 172 (188) T ss_pred ---ECCCCCCHHHHHHHHHHHHHHHHHHCCCCC T ss_conf ---625898888999999999999886026886 No 32 >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=97.07 E-value=0.026 Score=32.65 Aligned_columns=173 Identities=6% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+.+-|||.|+.+. -+.+++....+-..-.....-. .|+..+.+-+.+.+.-+.-..|.+.---.+. -+++ T Consensus 1 ivliGd~~VGKTsli~rf--~~~~f~~~~~pTi~~~~~~~i~-~~~~~v~l~iwDtaGqe~~~~l~~~~y~~a~--~~il 75 (174) T smart00174 1 LVVVGDGAVGKTCLLISY--TTNAFPEDYVPTVFENYSADVE-VDGKPVELGLWDTAGQEDYDRLRPLSYPDTD--VFLI 75 (174) T ss_pred CEEECCCCCCHHHHHHHH--HCCCCCCCCCCEEEEEEEEEEE-ECCEEEEEEECCCCCCCHHHHHHHHHHCCCC--EEEE T ss_conf 678715983389999998--6182266625515432467555-7786799986466666223566687643883--6899 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHH-HHHHHHHHHHCCCEEEEEC Q ss_conf 851666344689999999999864068998738998477345665532454115788999-9999999988294158852 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFI-LQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfI-qQ~LRtvcL~yGASLiYts 186 (312) .-|=+. +.++-+....|+..+++...+.++++|-.|+|-...-+... ..++..-..+ .+..+.+|-++|+-.++- T Consensus 76 vydit~--~~Sf~~l~~~W~~~i~~~~~~~piiLVGnK~DL~~~~~~~~-~~~~~~~~~vs~~e~~~~a~~~~~~~y~E- 151 (174) T smart00174 76 CFSVDS--PASFENVKEKWYPEVKHFCPNVPIILVGTKLDLRNDEDTLE-ELSKKKQEPVTYEQGEALAKRIGAVKYIE- 151 (174) T ss_pred EEECCC--HHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCCCHHHHHH-HHHHCCCCCCCHHHHHHHHHHCCCCEEEE- T ss_conf 986388--65789999988999998478966999715656320134555-54310135688889999999718941688- Q ss_pred CCCCHHHHHHHHHHHHHHHHHHCCCC Q ss_conf 56531355566778888753001247 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQELLKHFCED 212 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~L~~h~l~~ 212 (312) +|++...|-..++ ..++-+-+.+ T Consensus 152 -tSAktg~nV~e~F--~~l~r~~l~k 174 (174) T smart00174 152 -CSALTQEGVREVF--EEAIRAALNK 174 (174) T ss_pred -EECCCCCCHHHHH--HHHHHHHHCC T ss_conf -7504887878999--9999998529 No 33 >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=97.06 E-value=0.036 Score=31.82 Aligned_columns=161 Identities=11% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCC---------CEEEEEEEEECCCHHHHHHHHHHHC Q ss_conf 89975983317999998514-7786556655750256335621213---------3268899860785435887887718 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKE---------NYSVDVYTLIRNTDDALDLLKPFLQ 97 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d---------~~R~~vy~L~~~~~~~~~LLkp~L~ 97 (312) ++++|+.+-|||+|+.+... +-.+.+....|+++....+.-+..+ ...+.+|=..| .+.+..+.+.+.. T Consensus 7 ivviGd~~vGKTsli~r~~~~~f~~~~~~Tig~~~~~k~i~~~~~~~~~~~~~~~~v~l~iwDtaG-qe~~~~l~~~~~~ 85 (180) T cd04127 7 FLALGDSGVGKTSFLYQYTDNKFNPKFITTVGIDFREKRVVYNSSGPGGTLGRGQRIHLQLWDTAG-QERFRSLTTAFFR 85 (180) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEEECCCCCCCCCCCCEEEEEEEECCC-CCHHHHHHHHHCC T ss_conf 999806984389998887638327763540111355779997125543324577279999972477-6214567688604 Q ss_pred CCCCCCEEEEEECCCCCCHHHHHHHHHHHHHHHHC--CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHH Q ss_conf 77878279998516663446899999999998640--6899873899847734566553245411578899999999999 Q Fun_Sc_NP_0140 98 EHSSKVRWLILLDWTLNDQKLWLNELSYAFNKIKQ--LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFC 175 (312) Q Consensus 98 ~~s~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~--l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvc 175 (312) .-. -+++.-|=+. +..... +..|...++. ..+..++++|+.|+| |++....=.++. +.+| T Consensus 86 ~a~---~~ilvydit~--~~Sf~~-~~~w~~~i~~~~~~~~~~ivlVgNK~D----l~~~r~Vs~~e~--------~~~a 147 (180) T cd04127 86 DAM---GFLLIFDLTN--EQSFLN-VRNWMSQLQTHAYCENPDIVLCGNKAD----LEDQRQVSEEQA--------KALA 147 (180) T ss_pred CCC---EEEEEEECCC--HHHHHH-HHHHHHHHHHHCCCCCCEEEEEECCCC----CCCCCCCCHHHH--------HHHH T ss_conf 998---8999974689--668899-999999998613678750788720235----521122487899--------9999 Q ss_pred HHCCCEEEEECCCCCHHHHHHHHHHHHHHHHHHCCCCC Q ss_conf 88294158852565313555667788887530012477 Q Fun_Sc_NP_0140 176 YFNDSSLFYICEDHTEEKREEAQRLKYQELLKHFCEDR 213 (312) Q Consensus 176 L~yGASLiYts~ts~~~~kn~~~~l~y~~L~~h~l~~~ 213 (312) -.+|+..|.| |++...|-...+.. ++-....+ T Consensus 148 ~~~~~~~~e~---SAk~~~nV~e~F~~---l~~~i~~k 179 (180) T cd04127 148 DKYGIPYFET---SAATGTNVEKAVER---LLDLVMKR 179 (180) T ss_pred HHCCCCEEEE---ECCCCCCHHHHHHH---HHHHHHHH T ss_conf 9659959999---71479887899999---99999970 No 34 >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=97.06 E-value=0.036 Score=31.80 Aligned_columns=160 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+++.+... .=.+.+..+.|.+|....+.-+ ..+.++.+|=..| .+.+..+.+.....-. .++ T Consensus 6 i~liGd~~vGKTsli~r~~~~~f~~~~~~Tig~~~~~k~v~~~-~~~v~l~iwDt~G-~e~~~~~~~~~~~~a~---~~i 80 (167) T cd01867 6 LLLIGDSGVGKSCLLLRFSEDSFNPSFISTIGIDFKIRTIELD-GKKIKLQIWDTAG-QERFRTITTAYYRGAM---GII 80 (167) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEEC-CEEEEEEEEECCC-CCHHHHHHHHHCCCCC---EEE T ss_conf 9998269843899998876381076556412125678899988-9499999986689-8002345375436998---899 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCC-CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 985166634468999999999986406-8998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQL-NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l-~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) |.-|-+ -.-=...+..|+..+++- +.+.++++|-.|+| |+..+-.-.++...|..++ |+..|.| T Consensus 81 ivfDit---~~~Sf~~i~~w~~~i~~~~~~~~~~ilVGNK~D----L~~~r~v~~~~~~~~a~~~--------~~~~~e~ 145 (167) T cd01867 81 LVYDIT---DEKSFENIRNWMRNIEEHASEDVERMLVGNKCD----MEEKRVVSKEEGEALADEY--------GIKFLET 145 (167) T ss_pred EEEECC---CHHHHHHHHHHHHHHHHHCCCCCEEEEEEECCC----CCCCCCCCHHHHHHHHHHC--------CCCEEEE T ss_conf 998569---846789999999999852699938999940467----5222466989999999964--------9959999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCCCC Q ss_conf 2565313555667788887530012477 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCEDR 213 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~~~ 213 (312) |++...|-...+.. ++..+..+ T Consensus 146 ---SAk~~~nv~~~F~~---l~~~i~~~ 167 (167) T cd01867 146 ---SAKANINVEEAFFT---LAKDIKKK 167 (167) T ss_pred ---EECCCCCHHHHHHH---HHHHHHHC T ss_conf ---70489787899999---99999709 No 35 >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=97.03 E-value=0.031 Score=32.18 Aligned_columns=196 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCE-EEEEEEEECCCHHHHHHHHHHHCCCC-CCCEE Q ss_conf 89975983317999998514778655665575025633562121332-68899860785435887887718778-78279 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENY-SVDVYTLIRNTDDALDLLKPFLQEHS-SKVRW 105 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~-R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~ 105 (312) ++++|+.+-|||.++... -...++.+-.+--+..+...-+..+.. .+++|=-+|--.- -.|.+.. +++-. T Consensus 16 iVlVGD~~VGKTsLl~~~--~~~~F~~~y~pTv~~~y~~~i~v~~~~v~L~lWDTAGQE~y------~~lrplyYr~ad~ 87 (232) T cd04174 16 LVLVGDVQCGKTAMLQVL--AKDCYPETYVPTVFENYTAGLETEEQRVELSLWDTSGSPYY------DNVRPLCYSDSDA 87 (232) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCCCCCEEEEEEEEEEEECCEEEEEEEEECCCCHHH------HHHHHHHCCCCCE T ss_conf 999835971388999887--43722765144277657999988795899988526898035------6787852356467 Q ss_pred EEEE-CCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCC---HHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCE Q ss_conf 9985-16663446899999999998640689987389984773---4566553245411578899999999999882941 Q Fun_Sc_NP_0140 106 LILL-DWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSG---EILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSS 181 (312) Q Consensus 106 ViLL-DWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD---~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGAS 181 (312) ++++ |-+. |..+-+.+..|+..++...++.+|++|-+|+| ...++++-. ...+--.-.+--..++=+.||. T Consensus 88 ~llvFdit~--~~Sfenv~~kW~~Ei~~~~p~~pIiLVGnK~DLR~d~~~~~~L~---~~~~~pVt~eeG~~~Ak~iga~ 162 (232) T cd04174 88 VLLCFDISR--PETVDSALKKWKAEIMDYCPSTRILLIGCKTDLRTDLSTLMELS---NQKQAPISYEQGCALAKQLGAE 162 (232) T ss_pred EEEEEECCC--HHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCCCCHHHHHHHH---HCCCCCCCHHHHHHHHHHCCCC T ss_conf 999975487--45788889830688987278971899844655547988999998---5689887989999999973981 Q ss_pred EEEECCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCEECCCCEEECCCCCHH Q ss_conf 5885256531355566778888753001247787752240115630206688814 Q Fun_Sc_NP_0140 182 LFYICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEMVTRSEILIPKGCDSI 236 (312) Q Consensus 182 LiYts~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~vverd~vfIP~GwDS~ 236 (312) .+.-|..-+.++--....-...-..+.++.+...++++-.+.+..+-+|+..+.. T Consensus 163 ~Y~EcSA~tge~~V~~vF~~a~~~~l~~~~~~~~~s~~~~~~~~~~~~p~~~~~~ 217 (232) T cd04174 163 VYLECSAFTSEKSIHSIFRSASLLCLNKLSPPIKKSPVRSLSKRLLHLPSRSELI 217 (232) T ss_pred EEEEECCCCCCCCHHHHHHHHHHHHHHHCCCCCCCCCHHHCCCCCCCCCCCCCCC T ss_conf 7887300102456789999999999862012234341012044311378874311 No 36 >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=96.97 E-value=0.04 Score=31.49 Aligned_columns=158 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778-78279 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRW 105 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~ 105 (312) ++++|+.+-|||+++.+... .-.+.+.+..+ +.+...+ ..|+.++.+.+.+.+.-+-- ..+.+.- .+.-. T Consensus 4 ivlvGd~~VGKTsli~r~~~~~f~~~y~~Ti~-~~~~k~i---~~~~~~~~l~iwDtaG~e~~----~~~~~~~~~~a~~ 75 (164) T cd04175 4 LVVLGSGGVGKSALTVQFVQGIFVEKYDPTIE-DSYRKQV---EVDGQQCMLEILDTAGTEQF----TAMRDLYMKNGQG 75 (164) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCC-CEEEEEE---EECCEEEEEEEEECCCCCHH----HHHHHHHCCCCCE T ss_conf 89980798538999999862800665575312-1368999---88894899998727998202----3576755058987 Q ss_pred EEEE-CCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 9985-166634468999999999986406899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 106 LILL-DWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 106 ViLL-DWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +|++ |-+.....--++...+.+...+. ..+.++++|..|+| |+.++....++ .+.+|-.+|+..|- T Consensus 76 ~ilvydit~~~Sf~~i~~~~~~i~~~~~-~~~ip~vlvGNK~D----L~~~r~V~~~~--------~~~~a~~~~~~~~E 142 (164) T cd04175 76 FVLVYSITAQSTFNDLQDLREQILRVKD-TEDVPMILVGNKCD----LEDERVVGKEQ--------GQNLARQWGCAFLE 142 (164) T ss_pred EEEEEECCCHHHHHHHHHHHHHHHHHCC-CCCCEEEEEECCCC----CCCCCCCCHHH--------HHHHHHHCCCCEEE T ss_conf 9999866997788999999888886408-99857999812565----30003340789--------99999965993899 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCCCC Q ss_conf 5256531355566778888753001247 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFCED 212 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l~~ 212 (312) | |++...|-...+.. ++..+.+ T Consensus 143 ~---Sak~~~nV~e~F~~---l~~~i~~ 164 (164) T cd04175 143 T---SAKAKINVNEIFYD---LVRQINR 164 (164) T ss_pred E---ECCCCCCHHHHHHH---HHHHHCC T ss_conf 9---71479887899999---9999629 No 37 >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=96.93 E-value=0.045 Score=31.19 Aligned_columns=162 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||.++.+.-. .-.+++....|..|....+.-| .....+.+|=-.|--.- -.+.+... ..-.-++ T Consensus 9 IVliGd~~VGKTSLi~rf~~~~f~~~y~~TiG~d~~~k~i~vd-g~~v~L~IWDTAGqE~f-~sl~~~y~---r~A~gvI 83 (235) T cd04121 9 FLLVGDSDVGKGEILASLQDGSTESPYGYNMGIDYKTTTILLD-GRRVKLQLWDTSGQGRF-CTIFRSYS---RGAQGII 83 (235) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEEC-CCEEEEEEEECCCCCHH-HCCCHHHH---CCCCCEE T ss_conf 9998169844788877642581067634302446789999885-82899998746641001-10002332---1477179 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 98516663446899999999998640689987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) +.-|-+. ++.+-+ +..|+..+++...+.++++|.-|+|-...-+-.. +--+.+|-++|+.-|=| T Consensus 84 LVYDIT~--r~SF~~-i~~W~~ei~~~~~~ipiILVGNK~DL~~~R~Vs~------------eEg~~~A~~~~~~FfEt- 147 (235) T cd04121 84 LVYDITN--RWSFDG-IDRWIKEIDEHAPGVPKILVGNRLHLAFKRQVAT------------EQAQAYAERNGMTFFEV- 147 (235) T ss_pred EEEECCC--HHHHHH-HHHHHHHHHHHCCCCEEEEEECCCCHHHCCCCCH------------HHHHHHHHHCCCCEEEE- T ss_conf 9987699--778999-9999999986328965999703224002377798------------99999999669959998- Q ss_pred CCCCHHHHHHHHHHHHHHHHHHCCCC Q ss_conf 56531355566778888753001247 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQELLKHFCED 212 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~L~~h~l~~ 212 (312) |+++..|-...+..-+=.+-..++ T Consensus 148 --SAKtn~NV~E~F~elar~~l~~~~ 171 (235) T cd04121 148 --SPLCNFNITESFTELARIVLMRHG 171 (235) T ss_pred --ECCCCCCHHHHHHHHHHHHHHHCC T ss_conf --536899888999999999998648 No 38 >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=96.85 E-value=0.085 Score=29.55 Aligned_columns=157 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCC-CCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 8997598331799999851477865-566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNS-ILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~-~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+.....-++ ..+..+.++.-..+.-+ ....++.+|=-.|- ..+..+.+.++ +.-.-++ T Consensus 10 ivliGd~~VGKTsli~rf~~~~f~~~~~~Ti~~~~~~k~~~~~-~~~v~l~iwDtaG~-e~~~~~~~~~~---~~a~~~i 84 (169) T cd04114 10 IVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEIK-GEKIKLQIWDTAGQ-ERFRSITQSYY---RSANALI 84 (169) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEEC-CEEEEEEEEECCCC-HHHHHHHHHHH---CCCCEEE T ss_conf 9998269844899999986286785433112211478899888-95999999865898-02467768760---4888389 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC-CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 98516663446899999999998640-68998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ-LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~-l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) +.-|-+. +..+ ..+.+|+..+++ .+.+.++++|..|+|-...-+-.. +-.+.++-++|...|-| T Consensus 85 ivydit~--~~Sf-~~i~~w~~~i~~~~~~~~~iilVGNK~Dl~~~r~v~~------------~~~~~~a~~~~~~~~e~ 149 (169) T cd04114 85 LTYDITC--EESF-RCLPEWLREIEQYANNKVITILVGNKIDLAERREVSQ------------QRAEEFSDAQDMYYLET 149 (169) T ss_pred EEEECCC--HHHH-HHHHHHHHHHHHHHCCCCEEEEEECCCCCCCCCCCCH------------HHHHHHHHHCCCEEEEE T ss_conf 9965598--4688-9999999999874069941899811432110236587------------89999999649839999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCC Q ss_conf 2565313555667788887530012 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFC 210 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l 210 (312) |++...|-...+.. ++-++ T Consensus 150 ---SAktg~nV~~~F~~---la~~i 168 (169) T cd04114 150 ---SAKESDNVEKLFLD---LACRL 168 (169) T ss_pred ---EECCCCCHHHHHHH---HHHHH T ss_conf ---70379888899999---99982 No 39 >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=96.82 E-value=0.031 Score=32.16 Aligned_columns=166 Identities=8% Q ss_pred ECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEEEEE Q ss_conf 75983317999998514-77865566557502563356212133268899860785435887887718778-78279998 Q Fun_Sc_NP_0140 31 YSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRWLIL 108 (312) Q Consensus 31 lg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~ViL 108 (312) +|+++-|||+|+.+... +=.+.+....|.+|....+.-+ ....++.+|=-.|- ..| -.|++.- .+.--+|| T Consensus 1 VGDsgVGKTsli~R~~~~~F~~~y~~TIGvd~~~k~i~~~-~~~I~l~IWDTAGQ-E~f-----~sl~~~yyr~a~g~il 73 (200) T smart00176 1 VGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTN-RGPIKFNVWDTAGQ-EKF-----GGLEDGYYIQAQCAII 73 (200) T ss_pred CCCCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEEC-CCEEEEEEEECCCC-CCC-----CCCCHHHHCCCCEEEE T ss_conf 9887412788877764470067635546667889999871-85799988751565-211-----0002123058847999 Q ss_pred E-CCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEECC Q ss_conf 5-166634468999999999986406899873899847734566553245411578899999999999882941588525 Q Fun_Sc_NP_0140 109 L-DWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYICE 187 (312) Q Consensus 109 L-DWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts~ 187 (312) + |-+. +.+.-. +..|++.+++..++.+|++|.-|+ |-++... ..+-+ .|+-++|..-|=| T Consensus 74 VfDVT~--~~SF~n-i~~W~~ei~~~~~~ipivLvGNK~-----------DL~~r~v--~~e~~-~fa~~~~~~y~Et-- 134 (200) T smart00176 74 MFDVTS--RVTYKN-VPNWHRDLVRVCENIPIVLCGNKV-----------DIKDRKV--KAKSI-VFHRKKNLQYYDI-- 134 (200) T ss_pred EEECCC--HHHHHH-HHHHHHHHHHHCCCCEEEEEECCC-----------CCCCCCC--HHHHH-HHHHHCCCCEEEE-- T ss_conf 976699--778888-988999999864897799981243-----------5332435--48999-9999668958998-- Q ss_pred CCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCEECCCC Q ss_conf 653135556677888875300124778775224011563 Q Fun_Sc_NP_0140 188 DHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEMVTRSE 226 (312) Q Consensus 188 ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~vverd~ 226 (312) |+++..|-...+.+ ++.++.+-|....+.+....+ T Consensus 135 -SAKt~~NVee~F~~---Larkl~~~~~~~~~~~~~l~p 169 (200) T smart00176 135 -SAKSNYNFEKPFLW---LARKLIGDPNLEFVAMPALAP 169 (200) T ss_pred -EECCCCCHHHHHHH---HHHHHHCCCCEEEEECCCCCC T ss_conf -73478777688999---999985488605752356787 No 40 >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=96.77 E-value=0.22 Score=27.10 Aligned_columns=173 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+++-|||.++.+... .-.+.+..+.|..|....+.-+ ..+.++.+|=-.| ...|-.+....... -.-++ T Consensus 3 IvliGd~~VGKTsli~rf~~~~F~~~y~~Tig~df~~k~i~i~-g~~i~lqIwDTaG-qE~f~~l~~~y~r~---a~g~i 77 (202) T cd04120 3 VIIIGSRGVGKTSLMRRFTDDTFCEACKSGVGVDFKIKTVELR-GKKIRLQIWDTAG-QERFNSITSAYYRS---AKGII 77 (202) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCC-CCHHHHHHHHHHCC---CCEEE T ss_conf 8998079842899999976381166656512357889999987-9189999875688-60357887776328---98799 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC-CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 98516663446899999999998640-68998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ-LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~-l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) +.-|-+. +.++-. |..|+..+++ .+++.++++|..|+| ||.++-+-.++...|-++ +++..||- T Consensus 78 lVyDit~--~~SF~~-l~~W~~~i~~~~~~~~~iiLVGNK~D----L~~~R~Vs~~e~~~~A~~--------~~~~~f~E 142 (202) T cd04120 78 LVYDITK--KETFDD-LPKWMKMIDKYASEDAELLLVGNKLD----CETDREISRQQGEKFAQQ--------ITGMRFCE 142 (202) T ss_pred EEEECCC--HHHHHH-HHHHHHHHHHHCCCCEEEEEEECCCC----HHHHCCCCHHHHHHHHHH--------HCCCEEEE T ss_conf 9976698--457899-99999999972499348999712221----210202367999999997--------08970899 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCC Q ss_conf 25653135556677888875300124778775224 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIE 220 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~ 220 (312) +..-...+-+++-.......+.+.......+...+ T Consensus 143 tSAk~~~NV~e~F~~l~~~i~~~~~~~~~~~~~~~ 177 (202) T cd04120 143 ASAKDNFNVDEIFLKLVDDILKKMPLDILRNELSN 177 (202) T ss_pred EECCCCCCHHHHHHHHHHHHHHHCCCCCCCCCCCC T ss_conf 85148988889999999999973431003566687 No 41 >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=96.75 E-value=0.14 Score=28.15 Aligned_columns=158 Identities=6% Q ss_pred EEEECCCCHHHHHHHHHHCCCC--CCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEE Q ss_conf 8997598331799999851477--86556655750256335621213326889986078543588788771877878279 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEG--SNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRW 105 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~--~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~ 105 (312) ++++|+.+-|||.|+.+..... .+.+.+..|..|....+.- ++..+.+-+.+.+.-+.-..+.+..-..+.-..+ T Consensus 3 vvliGd~~VGKTsli~r~~~~~F~~~~y~~Tig~~f~~k~i~~---~~~~v~l~iwDtaGqe~~~~l~~~~yr~a~~~il 79 (193) T cd04118 3 VVMLGKESVGKTSLVERYVHHRFLVGPYQNTIGAAFVAKRMVV---GERVVTLGIWDTAGSERYEAMSRIYYRGAKAAIV 79 (193) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEC---CCEEEEEEEECCCCCHHHHHHHHHHHCCCCEEEE T ss_conf 8998079832899988875273168874661332358888643---8757999986388753578989876128873899 Q ss_pred EEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 99851666344689999999999864068998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 106 LILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 106 ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) |+ +.-|+-.. ..|..|+..+++..++.++++|-.|+|-+..=+..+ .-+.++. +.++=++|+..|.| T Consensus 80 vy----dit~~~SF-~~l~~w~~~i~~~~~~~~iilVGNK~DL~~~~~~~r-~V~~ee~-------~~~A~~~~~~~fEt 146 (193) T cd04118 80 CY----DLTDSSSF-ERAKFWVKELQNLEEHCKIYLCGTKSDLIEQDRSLR-QVDFHDV-------QDFADEIKAQHFET 146 (193) T ss_pred EE----ECCCCHHH-HHHHHHHHHHHHCCCCCEEEEEECCCCHHHCCCCCC-CCCHHHH-------HHHHHHCCCCEEEE T ss_conf 98----74881017-899999999862189978999841422112066644-4688999-------99999669959999 Q ss_pred CCCCCHHHHHHHHHHHHHH Q ss_conf 2565313555667788887 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQE 204 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~ 204 (312) |+++..|-..++...+ T Consensus 147 ---SAktg~nV~elF~~ia 162 (193) T cd04118 147 ---SSKTGQNVDELFQKVA 162 (193) T ss_pred ---ECCCCCCHHHHHHHHH T ss_conf ---6258988889999999 No 42 >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=96.75 E-value=0.11 Score=28.95 Aligned_columns=157 Identities=7% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCC-EEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514778655665575-02563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLI-NYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L-~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+++-|||+++.+. -+.+++....+. +..++.+.-+ -++..+.+|=..| .+.+..+..-.+ +.-.-++ T Consensus 3 ivliGd~~VGKTsL~~rf--~~~~F~~~~~~t~~~~~~~~~~~-~~~v~l~iwDtag-qe~~~~~~~~~~---~~a~~~i 75 (166) T cd01893 3 IVLIGDEGVGKSSLIMSL--VSEEFPENVPRVLPEITIPADVT-PERVPTTIVDTSS-RPQDRANLAAEI---RKANVIC 75 (166) T ss_pred EEEEECCCCCHHHHHHHH--HCCEECCCCCCCEEEEEEEEEEC-CCEEEEEEEECCC-CCCCHHHHHHHH---CCCCEEE T ss_conf 899807983388998887--54800666565103579989971-8568999987258-875056678761---3898899 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 98516663446899999999998640689987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) +.-|-+ |++.+-+....|+..+++..++.++++|..|+| |..+...=..+ +-+-.++-.++..-.| - T Consensus 76 ivydi~--~~~Sf~~i~~~W~~~i~~~~~~~piilVGNK~D----L~~~~~~~~~e------~~~~~~~~~~~~i~~~-~ 142 (166) T cd01893 76 LVYSVD--RPSTLERIRTKWLPLIRRLGVKVPIILVGNKSD----LRDGSSQAGLE------EEMLPIMNEFREIETC-V 142 (166) T ss_pred EEEECC--CHHHHHHHHHHHHHHHHHHCCCCEEEEEECCCC----CCCCCCCCHHH------HHHHHHHHHHCCCCEE-E T ss_conf 998648--867878899887999975168957999715764----22354210147------8999999974277507-8 Q ss_pred CCCCHHHHHHHHHHHHHH Q ss_conf 565313555667788887 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQE 204 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~ 204 (312) .+|+++..|-...+.+.. T Consensus 143 EtSAkt~~nV~e~F~~a~ 160 (166) T cd01893 143 ECSAKTLINVSEVFYYAQ 160 (166) T ss_pred EEEECCCCCHHHHHHHHH T ss_conf 875036888789999999 No 43 >cd04166 CysN_ATPS CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN. Probab=96.75 E-value=0.041 Score=31.46 Aligned_columns=139 Identities=10% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCC-------------CCCCCCCCEEEE-ECCCCCCCCCE-EEEE-----------EE Q ss_conf 3899759833179999985147786-------------556655750256-33562121332-6889-----------98 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSN-------------SILDTTLINYAT-IGWTNDLKENY-SVDV-----------YT 80 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e-------------~~~~~~~L~y~y-~~v~~d~~d~~-R~~v-----------y~ 80 (312) ..+++|--..||++++..+..+... .-.......|++ .|-..+-|+.- -+++ |. T Consensus 1 ~~vv~GHVD~GKSTL~grLL~~~g~v~~~~l~~~~~~~~~~~~~~~~~a~~lD~~~eErerGiTId~~~~~f~~~~~~~~ 80 (208) T cd04166 1 RFLTCGSVDDGKSTLIGRLLYDSKSIFEDQLAALESKSCGTGGEPLDLALLVDGLQAEREQGITIDVAYRYFSTPKRKFI 80 (208) T ss_pred CEEEEEECCCCHHHHHHHHHHHHCCCCHHHHHHHHHHHHHHCCCCEEEEEECCCCHHHHHCCCEEEEEEEEEECCCCEEE T ss_conf 97889613788578999999972886788999999877650343201232307734566569548888899834897899 Q ss_pred EECCCHHHHHHHHHHHCCCCCCCEEEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCC Q ss_conf 60785435887887718778782799985166634468999999999986406899873899847734566553245411 Q Fun_Sc_NP_0140 81 LIRNTDDALDLLKPFLQEHSSKVRWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQ 160 (312) Q Consensus 81 L~~~~~~~~~LLkp~L~~~s~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~ 160 (312) +...++| .++++-.++.-+.---.|+++|=.. .+..|-++|...++.++ =.+++|+..|.|-+ +|+ T Consensus 81 iiDtPGH-~dfi~nmi~Gas~aD~ailVVda~~----G~~~QT~eh~~l~~~lg-v~~iivavNK~D~v--------~~~ 146 (208) T cd04166 81 IADTPGH-EQYTRNMVTGASTADLAILLVDARK----GVLEQTRRHSYILSLLG-IRHVVVAVNKMDLV--------DYS 146 (208) T ss_pred EEECCCH-HHHHHHHHHHHHHHCEEEEEEECCC----CHHHHHHHHHHHHHHHC-CCCEEEEEECCCCC--------CCC T ss_conf 9846773-7889999986314054788987574----42567999999999707-99179998535666--------889 Q ss_pred HHHHHHHHHHHHHHHHHCC Q ss_conf 5788999999999998829 Q Fun_Sc_NP_0140 161 SVHIDFILQTLRSFCYFND 179 (312) Q Consensus 161 de~fDfIqQ~LRtvcL~yG 179 (312) .+.|+.|.+-+..++-+.| T Consensus 147 ~~r~~~i~~~~~~~l~~~~ 165 (208) T cd04166 147 EEVFEEIVADYLAFAAKLG 165 (208) T ss_pred HHHHHHHHHHHHHHHHHCC T ss_conf 8999999999999998628 No 44 >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=96.72 E-value=0.094 Score=29.27 Aligned_columns=160 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCCCCC-CC-CCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEE Q ss_conf 89975983317999998514778-65-56655750256335621213326889986078543588788771877878279 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGS-NS-ILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRW 105 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~-e~-~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~ 105 (312) ++|+|+.+-|||.++.+.-.++- +. +.+..|..|....|.-+.++ ..+..| +....+....|.+.-- ..---+ T Consensus 7 ~~vlGd~gVGKTsll~rfv~~~F~~~~y~~Tig~~f~~k~v~v~g~~-~~l~l~--Dtagqe~~~~l~~~~~--~~a~~~ 81 (169) T cd01892 7 CFVLGAKGSGKSALLRAFLGRSFSLNAYSPTIKPRYAVNTVEVYGQE-KYLILR--EVGEDEVAILLNDAEL--AACDVA 81 (169) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCCCCCEEEEEEEEECCEE-EEEEEE--CCCCHHHHHHHHHHHC--CCCCEE T ss_conf 99980899648999999856874666211520231679888876747-899851--1573034544313220--588789 Q ss_pred EEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEE-EE Q ss_conf 99851666344689999999999864068998738998477345665532454115788999999999998829415-88 Q Fun_Sc_NP_0140 106 LILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSL-FY 184 (312) Q Consensus 106 ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASL-iY 184 (312) ++.-|=+..+.+-|+.+++.. .....+.++++|-.|+| |+..+-++.++. +.+|-++|..- +. T Consensus 82 ilVYDit~~~SF~~i~~~~~~----~~~~~~ipiilVGNK~D----L~~~RqVs~~e~--------~~~a~~~g~~~~~e 145 (169) T cd01892 82 CLVYDSSDPKSFSYCAEVYKK----YFMLGEIPCLFVAAKAD----LDEQQQRYEVQP--------DEFCRKLGLPPPLH 145 (169) T ss_pred EEEEECCCHHHHHHHHHHHHH----CCCCCCCEEEEEECCCC----CCCCCCCCCCCH--------HHHHHHCCCCCCEE T ss_conf 999867997899999999986----04899955999830367----755563363376--------89999629996368 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCCC Q ss_conf 525653135556677888875300124 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFCE 211 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l~ 211 (312) | |++...|-...+...+-.+.... T Consensus 146 ~---SAKtg~nV~e~F~~la~~A~~~~ 169 (169) T cd01892 146 F---SSKLGDSSNELFTKLATAAQYPH 169 (169) T ss_pred E---EECCCCCHHHHHHHHHHHHCCCC T ss_conf 8---70179998999999999960689 No 45 >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=96.72 E-value=0.13 Score=28.39 Aligned_columns=181 Identities=11% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+++-|||.++.+... .=.+.+.+..|.+|....+.-|......+.+|=..| .+.|..+.+.....-. -++ T Consensus 3 IvliGd~~VGKTsli~r~~~~~F~~~~~~Tig~d~~~k~i~~~~~~~v~l~iwDtaG-qe~f~~l~~~y~r~a~---~~i 78 (201) T cd04107 3 VLVIGDLGVGKTSIIKRYVHGIFSQHYKATIGVDFALKVIEWDPNTVVRLQLWDIAG-QERFGGMTRVYYRGAV---GAI 78 (201) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEECCCEEEEEEEECCCC-CHHHHHHHHHHCCCCC---EEE T ss_conf 899816995489999997718006765650344677889987697689998622788-4245566565427987---699 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC-----CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCC-C Q ss_conf 98516663446899999999998640-----68998738998477345665532454115788999999999998829-4 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ-----LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFND-S 180 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~-----l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yG-A 180 (312) +.-|-+..+. ...+..|...+.+ .+...++++|-.|+| |+.+...-.++ ...+|-.+| . T Consensus 79 lvyDit~~~S---F~~i~~W~~~i~~~~~~~~~~~ipiilVGNK~D----L~~~~~v~~~e--------~~~~a~~~~~~ 143 (201) T cd04107 79 IVFDVTRPST---FEAVLKWKADLDSKVTLPNGEPIPCLLLANKCD----LKKRLAKDGEQ--------MDQFCKENGFI 143 (201) T ss_pred EEEECCCHHH---HHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCC----CHHHCCCCHHH--------HHHHHHHCCCC T ss_conf 9987389778---999999999999874036899728999705887----30004479899--------99999963998 Q ss_pred EEEEECCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCEECCCCEEECCC Q ss_conf 1588525653135556677888875300124778775224011563020668 Q Fun_Sc_NP_0140 181 SLFYICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEMVTRSEILIPKG 232 (312) Q Consensus 181 SLiYts~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~vverd~vfIP~G 232 (312) +.|.| |+++..|-...+ ..+.-.-+-..+....++......+..+.. T Consensus 144 ~~fEt---SAktg~nV~e~F--~~l~~~i~~~~~~~~~~~~~~~~~~~~~~~ 190 (201) T cd04107 144 GWFET---SAKEGINIEEAM--RFLVKNILANDKNLQQAETPEDGSVIDLKQ 190 (201) T ss_pred CEEEE---ECCCCCCHHHHH--HHHHHHHHHHCCCCCCCCCCCCCCCCCCCC T ss_conf 26887---504897878999--999999997411246656665672113277 No 46 >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=96.70 E-value=0.048 Score=31.06 Aligned_columns=148 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+... .-.+.+.+..+-.|. .-+.-+ .+..++.+|=-.|-.......+...+..-. -++ T Consensus 2 Iv~iGd~~vGKTsLi~r~~~~~F~~~y~~ti~~~~~-k~~~v~-~~~v~l~i~DtaG~e~~~~~~~~~~~~~ad---~~i 76 (165) T cd04146 2 IAVLGASGVGKSALVVRFLTKRFIGEYDPNLESLYS-RQVTID-GEQVSLEILDTAGQQQADTEQLERSIRWAD---GFV 76 (165) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCHHHHHE-EEEEEC-CCEEEEEEECCCCCHHHHHHCCCCCCCCCC---EEE T ss_conf 788817983289999998617447754630121110-000225-944899972277720110000013546888---799 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 98516663446899999999998640689987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) +.-|-+......-++.+.+++...+..+.+.++++|..|+| |++++ .-..++ .+.+|-++|+..+.| T Consensus 77 lvydit~~~SF~~i~~~~~~i~~~~~~~~~~piilVGNK~D----L~~~r-~V~~ee-------~~~~a~~~~~~~~E~- 143 (165) T cd04146 77 LVYSITDRSSFDEISQLKQLIREIKKRDREIPVILVGNKAD----LLHYR-QVSTEE-------GEKLASELGCLFFEV- 143 (165) T ss_pred EEEECCCHHHHHHHHHHHHHHHHHCCCCCCCEEEEECCCCC----CHHCC-CCCHHH-------HHHHHHHCCCCEEEE- T ss_conf 99766985368999999999997514799827999723336----00105-469899-------999999659958998- Q ss_pred CCCCHHHHH Q ss_conf 565313555 Q Fun_Sc_NP_0140 187 EDHTEEKRE 195 (312) Q Consensus 187 ~ts~~~~kn 195 (312) |+++..| T Consensus 144 --SAk~~~~ 150 (165) T cd04146 144 --SAAEDYD 150 (165) T ss_pred --EECCCCC T ss_conf --6045880 No 47 >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=96.68 E-value=0.1 Score=29.04 Aligned_columns=172 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+.+-|||.++.+. -..+++.+-.+--+......-+ -++..+.+-+-+...-+.-.-+.+..-..+ .-+++ T Consensus 4 ivlvGd~~VGKTsli~r~--~~~~F~~~~~~Ti~~~~~~~~~-v~~~~v~l~iWDTaGqe~f~~l~~~~y~~a--~~~il 78 (178) T cd04131 4 IVVVGDVQCGKTALLQVF--AKDCYPETYVPTVFENYTASFE-IDEQRIELSLWDTSGSPYYDNVRPLCYPDS--DAVLI 78 (178) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCCCCCEEEEEEEEEEE-ECCEEEEEEEEECCCCCHHHHHHHHHCCCC--CEEEE T ss_conf 899826984489999997--5383376624136645789998-868489999875688803355768762799--67999 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEECC Q ss_conf 85166634468999999999986406899873899847734566553245411578899999999999882941588525 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYICE 187 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts~ 187 (312) .-|.+. +.+.-..+..|...+++..++.++++|-.|+|-...+....-.=....-..-..--+.++-+.||-+++-|. T Consensus 79 vfdit~--~~Sf~~v~~~W~~ei~~~~~~~~iiLVGnK~DLr~~~~~~~~l~~~~~~~Vs~eeg~~~A~~~~a~~y~E~S 156 (178) T cd04131 79 CFDISR--PETLDSVLKKWRGEIQEFCPNTKVLLVGCKTDLRTDLSTLMELSHQRQAPVSYEQGCAIAKQLGAEIYLECS 156 (178) T ss_pred EEECCC--HHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCCCCHHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEEEE T ss_conf 975688--557789999999999984598539996042122121567888763578778989999999982992577530 Q ss_pred CCCHHH-HHHHHHHHHHHHH Q ss_conf 653135-5566778888753 Q Fun_Sc_NP_0140 188 DHTEEK-REEAQRLKYQELL 206 (312) Q Consensus 188 ts~~~~-kn~~~~l~y~~L~ 206 (312) .-+.++ -+++-.+..++.+ T Consensus 157 Aktg~ngV~evF~~a~~a~l 176 (178) T cd04131 157 AFTSEKSVRDIFHVATMACL 176 (178) T ss_pred CCCCCCCHHHHHHHHHHHHH T ss_conf 11156787899999999971 No 48 >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=96.67 E-value=0.17 Score=27.77 Aligned_columns=160 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+++-|||+|+.+... .-.+.+....+..|.-... .|+..+.+-+.+.+..+-...+.+.--..+. -++ T Consensus 3 ivliGd~~VGKTsli~r~~~~~f~~~~~~Ti~~~~~~~i~----~~~~~v~l~iwDt~Gqe~~~~l~~~~~~~a~--~~i 76 (164) T cd04139 3 VIVVGAGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVV----LDGEDVQLNILDTAGQEDYAAIRDNYHRSGE--GFL 76 (164) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCEEEEEEE----ECCCEEEEEEEECCCCHHHHHHHHHHCCCCC--EEE T ss_conf 8998179854899999987182076544322321468998----8593899998427887135788887525898--799 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCC-CCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 985166634468999999999986406899-8738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDD-NEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~D-t~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) +.-|-+. +..+-+.-.-|-...+..+.+ .++++|..|+| |+.++..-.++.-+|..++ |+..|-| T Consensus 77 lvydit~--~~Sf~~i~~~~~~~~~~~~~~~ip~ilvGNK~D----l~~~r~v~~~e~~~~a~~~--------~~~~~E~ 142 (164) T cd04139 77 LVFSITD--MESFTATAEFREQILRVKDDDNVPLLLVGNKCD----LEDKRQVSSEEAANLARQW--------GVPYVET 142 (164) T ss_pred EEEECCC--HHHHHHHHHHHHHHHHHHCCCCCEEEEECCCHH----HHHHCCCCHHHHHHHHHHC--------CCCEEEE T ss_conf 9975288--557889999999999861799727999724013----2231167489999999965--------9959999 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCCCC Q ss_conf 2565313555667788887530012477 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCEDR 213 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~~~ 213 (312) |+++..|-...+.. ++..++.+ T Consensus 143 ---SAk~g~ni~e~F~~---l~~~i~~r 164 (164) T cd04139 143 ---SAKTRQNVEKAFYD---LVREIRQR 164 (164) T ss_pred ---ECCCCCCHHHHHHH---HHHHHHCC T ss_conf ---71589887899999---99999609 No 49 >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=96.65 E-value=0.13 Score=28.52 Aligned_columns=150 Identities=6% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+... .=.+.+....+ +.....+ .-|+..+.+-+.+.+..+--..+.+..-..+.-..+| T Consensus 4 iilvGd~~VGKTsli~r~~~~~f~~~~~~ti~-~~~~k~i---~v~~~~~~l~iwDtaG~e~~~~l~~~~~~~a~~~ilv 79 (163) T cd04136 4 VVVLGSGGVGKSALTVQFVQGIFVEKYDPTIE-DSYRKQI---EVDGQQCMLEILDTAGTEQFTAMRDLYIKNGQGFVLV 79 (163) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCCC-CCEEEEE---EECCEEEEEEEEECCCCHHHHHHHHHHHCCCCEEEEE T ss_conf 89970798438999998862800676565100-0126889---8889689999884799803568888751168828999 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCC--CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 985166634468999999999986406--899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQL--NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l--~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) + +..++..+ ..+..|+..+... ....++++|..|+| |+.++....++ .+.++-.+|+..|. T Consensus 80 f----dvt~~~Sf-~~i~~~~~~i~~~~~~~~ip~ilVGNK~D----L~~~r~v~~~~--------~~~~a~~~~~~~~E 142 (163) T cd04136 80 Y----SITSQSSF-NDLQDLREQILRVKDTENVPMVLVGNKCD----LEDERVVSREE--------GQALARQWGCPFYE 142 (163) T ss_pred E----ECCCHHHH-HHHHHHHHHHHHHCCCCCCEEEEECCCCC----CCCCCCCCHHH--------HHHHHHHCCCCEEE T ss_conf 7----56997888-99999999999740899938999724467----64656379899--------99999966995999 Q ss_pred ECCCCCHHHHHHHHHHH Q ss_conf 52565313555667788 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLK 201 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~ 201 (312) | |++...|-...+. T Consensus 143 ~---Sak~~~nv~e~F~ 156 (163) T cd04136 143 T---SAKSKINVDEVFA 156 (163) T ss_pred E---ECCCCCCHHHHHH T ss_conf 9---7147978789999 No 50 >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=96.55 E-value=0.11 Score=28.91 Aligned_columns=152 Identities=5% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+++-|||.++.+. -..+++..-.+--...+...-. .|+..+.+-+.+...-+--.-|.+.-=..+.-..+|+ T Consensus 4 iv~iGd~~VGKTsLi~rf--~~~~F~~~~~pTi~~~~~~~i~-~~~~~v~l~IwDTaGqe~~~~l~~~~~r~a~~~ilvy 80 (176) T cd04133 4 CVTVGDGAVGKTCMLICY--TSNKFPTDYIPTVFDNFSANVS-VDGNTVNLGLWDTAGQEDYNRLRPLSYRGADVFVLAF 80 (176) T ss_pred EEEECCCCCCHHHHHHHH--HCCEECCCCCCEEEEEEEEEEE-ECCEEEEEEEEECCCCHHHHHHHHHHCCCCCEEEEEE T ss_conf 999717984489988887--5380168635335311136788-8894899998756887146788887411447269997 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHH------------HHHCCCCCCHHHHHHHHHHHHHHH Q ss_conf 85166634468999999999986406899873899847734566------------553245411578899999999999 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILN------------LQRHTTVWQSVHIDFILQTLRSFC 175 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~------------LEKe~~~w~de~fDfIqQ~LRtvc 175 (312) +.-|+..+-+.++.|+..++..+.+.++++|-.|+|-... ...+.+ ..++ T Consensus 81 ----dvt~~~Sf~~~~~~w~~~~~~~~~~~piiLVGNK~DL~~~r~~~~~~~~~~~v~~~e~--------------~~~a 142 (176) T cd04133 81 ----SLISRASYENVLKKWVPELRHYAPNVPIVLVGTKLDLRDDKQYLADHPGASPITTAQG--------------EELR 142 (176) T ss_pred ----ECCCCHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCHHHHHHHHHHCCCCCCCHHHH--------------HHHH T ss_conf ----4487220799999989999972799489997057551112456653013354367899--------------9999 Q ss_pred HHCCCEEEEECCCCCHHHHHHHHHHHH Q ss_conf 882941588525653135556677888 Q Fun_Sc_NP_0140 176 YFNDSSLFYICEDHTEEKREEAQRLKY 202 (312) Q Consensus 176 L~yGASLiYts~ts~~~~kn~~~~l~y 202 (312) -++|+..++- +|+++..|-..++.. T Consensus 143 ~~~~~~~y~E--tSAktg~nV~e~F~~ 167 (176) T cd04133 143 KQIGAAAYIE--CSSKTQQNVKAVFDA 167 (176) T ss_pred HHCCCCEEEE--EECCCCCCHHHHHHH T ss_conf 9639974899--751378787899999 No 51 >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=96.53 E-value=0.034 Score=31.93 Aligned_columns=108 Identities=12% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|..+.|||+++.++.....+.+.++.|..+.++.. .+.++.+|-+.| ...+.++.+.....- .-+|+ T Consensus 2 iviiG~~~vGKTsli~~~~~~~~~~~~pTig~~~~~i~~-----~~~~~~i~D~~G-~~~~~~l~~~y~~~a---~~iI~ 72 (158) T cd00878 2 ILILGLDGAGKTTILYKLKLGEVVTTIPTIGFNVETVEY-----KNVSFTVWDVGG-QDKIRPLWKHYYENT---NGIIF 72 (158) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCEEEEEEEEEEEEEC-----CCEEEEEEECCC-CCCCHHHHHHHCCCC---CEEEE T ss_conf 788843998789999998648233122025426888530-----414899986589-852046778661489---81799 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCC--CCCEEEEEECCC Q ss_conf 8516663446899999999998640689--987389984773 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLND--DNEFSVWCLNSG 147 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~--Dt~i~VVc~~sD 147 (312) ..|-+..+. +..++.|+..+.+-.. +.+++|++.|+| T Consensus 73 V~D~sd~~s---~~~~~~~~~~~~~~~~~~~~pili~~NK~D 111 (158) T cd00878 73 VVDSSDRER---IEEAKEELHKLLNEEELKGVPLLIFANKQD 111 (158) T ss_pred EEECCCCCC---HHHHHHHHHHHHHHCCCCCCEEEEEEECCC T ss_conf 984377655---789999999985211448943675540116 No 52 >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=96.52 E-value=0.2 Score=27.35 Aligned_columns=149 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+... .-.+.+.+..+-.|.-..+.++ .+.++.+|=..|. +.+..+.+.++. .-.-++ T Consensus 4 vvliGd~~VGKTSli~~~~~~~f~~~y~~Ti~~~~~k~v~i~~--~~~~l~i~Dt~G~-e~~~~~~~~~~~---~a~~~i 77 (162) T cd04138 4 LVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDG--ETCLLDILDTAGQ-EEYSAMRDQYMR---TGEGFL 77 (162) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCEEEEEEEEEECC--EEEEEEEEECCCC-HHHHHHHHHHHC---CCCEEE T ss_conf 8998179954899999986180167656510014788999989--5899998746885-013466487523---897699 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCC--CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 985166634468999999999986406--899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQL--NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l--~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +.-|-+. +....+ +..|+..+++. ....++++|..|+| |+... ...++ .+.+|-.+|+.-+- T Consensus 78 lvydv~~--~~Sf~~-i~~w~~~i~~~~~~~~~piilvgNK~D----l~~r~-v~~~e--------~~~~a~~~~~~~~E 141 (162) T cd04138 78 CVFAINS--RKSFED-IHTYREQIKRVKDSDDVPMVLVGNKCD----LAART-VSSRQ--------GQDLAKSYGIPYIE 141 (162) T ss_pred EEEECCC--HHHHHH-HHHHHHHHHHHCCCCCCEEEEEEEECC----CCCCC-CCHHH--------HHHHHHHCCCCEEE T ss_conf 9986699--789999-999999998741899948999830047----53325-89899--------99999966995999 Q ss_pred ECCCCCHHHHHHHHHHH Q ss_conf 52565313555667788 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLK 201 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~ 201 (312) | |++...|-...+. T Consensus 142 ~---SAkt~~nV~e~F~ 155 (162) T cd04138 142 T---SAKTRQGVEEAFY 155 (162) T ss_pred E---ECCCCCCHHHHHH T ss_conf 9---7048978789999 No 53 >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=96.48 E-value=0.14 Score=28.30 Aligned_columns=151 Identities=7% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCC-CEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 8997598331799999851477865566557-502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTL-INYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~-L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+. -+.+++.+-.+ ++-.|.-+-........+.+|=-.| ...+..+.+..+..-. -+| T Consensus 4 IvliGd~~VGKTsli~r~--~~~~F~~~y~~ti~~~~~~~i~~~~~~~~l~i~Dt~G-~e~~~~l~~~~~~~a~---~~i 77 (165) T cd04140 4 VVVFGAGGVGKSSLVLRF--VKGTFRESYIPTIEDTYRQVISCSKNICTLQITDTTG-SHQFPAMQRLSISKGH---AFI 77 (165) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCCCCCCEECEEEEEEEECCCEEEEEEECCCC-CCCHHHHHHHHHCCCC---EEE T ss_conf 899807996589999887--6282066545420011577886369489999703776-3102356688621898---589 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCC----CCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEE Q ss_conf 9851666344689999999999864068----998738998477345665532454115788999999999998829415 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLN----DDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSL 182 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~----~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASL 182 (312) +.-|-+. +.++ ..++.|+..+++.. ...++++|-.|+| |+.++..=.++.-.|-.+. |+.. T Consensus 78 lvydit~--~~Sf-~~i~~~~~~i~~~~~~~~~~ipiilvGNK~D----l~~~r~V~~~e~~~~a~~~--------~~~~ 142 (165) T cd04140 78 LVYSVTS--KQSL-EELKPIYELICEIKGNNIEKIPIMLVGNKCD----ESHKREVSSNEGAACATEW--------NCAF 142 (165) T ss_pred EEEECCC--HHHH-HHHHHHHHHHHHHHCCCCCCCEEEEEECCCC----CCCCCCCCHHHHHHHHHHC--------CCCE T ss_conf 9987599--7788-9999999999986224889857999503114----0104668989999999956--------9958 Q ss_pred EEECCCCCHHHHHHHHHHHH Q ss_conf 88525653135556677888 Q Fun_Sc_NP_0140 183 FYICEDHTEEKREEAQRLKY 202 (312) Q Consensus 183 iYts~ts~~~~kn~~~~l~y 202 (312) |.| |+++..|-...+.. T Consensus 143 ~E~---SAk~~~nv~~~F~~ 159 (165) T cd04140 143 MET---SAKTNHNVQELFQE 159 (165) T ss_pred EEE---ECCCCCCHHHHHHH T ss_conf 999---71489887899999 No 54 >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=96.46 E-value=0.22 Score=27.06 Aligned_columns=181 Identities=6% Q ss_pred CEEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEE Q ss_conf 43899759833179999985147786556655750256335621213326889986078543588788771877878279 Q Fun_Sc_NP_0140 26 ITAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRW 105 (312) Q Consensus 26 k~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~ 105 (312) +-++++|+++-||++++.+. -...++....+--+.-. ...-..|+..+.+.+.+...-+--..|.+..=..+. -+ T Consensus 1 ~KiiliGd~~VGKTsLi~rf--~~~~F~~~~~~Ti~~~~-~~~i~vd~~~v~l~iwDTaGqE~f~~l~~~~y~~a~--~~ 75 (189) T cd04134 1 RKVVVLGDGACGKTSLLNVF--TRGYFPQVYEPTVFENY-VHDIFVDGLHIELSLWDTAGQEEFDRLRSLSYADTD--VI 75 (189) T ss_pred CEEEEEECCCCCHHHHHHHH--HCCCCCCCCCCEEEEEE-EEEEEECCEEEEEEEECCCCCHHHHHHHHHHHCCCC--EE T ss_conf 96899826983389999887--63800675166167756-786677794899998627787145778887733898--78 Q ss_pred EEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEE Q ss_conf 99851666344689999999999864068998738998477345665532454115788999999999998829415885 Q Fun_Sc_NP_0140 106 LILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYI 185 (312) Q Consensus 106 ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYt 185 (312) ++.-|-+. +.++-+....|+..+++..++.++++|..|+|-...-+.....-+...=-.-.+--..++-..||-.++- T Consensus 76 ilvydit~--~~Sf~~i~~~W~~ei~~~~~~v~iiLVGnK~DL~~~~~~~~~~~~~~~~~vs~~e~~~~a~~~~~~~y~E 153 (189) T cd04134 76 MLCFSVDS--PDSLENVESKWLGEIREHCPGVKLVLVALKCDLREARNERDDLQRYGKHTISYEEGLAVAKRINALRYLE 153 (189) T ss_pred EEEEECCC--HHHHHHHHHHHHHHHHHHCCCCEEEEEEECCCCCCCHHHHHHHHHHHCCCCCHHHHHHHHHHCCCCEEEE T ss_conf 99986688--4466899998899999835895599985046765531345667653136779899999999808950688 Q ss_pred CCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCC Q ss_conf 256531355566778888753001247787752 Q Fun_Sc_NP_0140 186 CEDHTEEKREEAQRLKYQELLKHFCEDRDMKDH 218 (312) Q Consensus 186 s~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~ 218 (312) +|+++..|-...+.. ++.......+.+| T Consensus 154 --tSAKt~~nV~e~F~~---lar~~L~~~~~~~ 181 (189) T cd04134 154 --CSAKLNRGVNEAFTE---AARVALNVRPPHP 181 (189) T ss_pred --EECCCCCCHHHHHHH---HHHHHHCCCCCCC T ss_conf --642578787899999---9999827887788 No 55 >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=96.44 E-value=0.053 Score=30.79 Aligned_columns=121 Identities=12% Q ss_pred CHHHHHHHHHHCCCCCCCCCCCCEEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEEC Q ss_conf 13889988641011465536644389975983317999998514778655665575025633562121332688998607 Q Fun_Sc_NP_0140 4 CNAWDKLLSQNESTINSTETATITAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIR 83 (312) Q Consensus 4 ~NlWs~iLse~~~~~~~k~~~~k~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~ 83 (312) +|+|+++- --..-.++++|.++.|||+++.++-........++.|.+.-++.. .+.++.+|-+.| T Consensus 6 ~~~~~~~f----------~kk~~kiviiG~~~~GKTtil~~l~~~~~~~~~pTvg~~~~~i~~-----~~~~l~iwD~~G 70 (181) T smart00177 6 GKLFSKLF----------GNKEMRILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNVETVTY-----KNISFTVWDVGG 70 (181) T ss_pred HHHHHHHH----------CCCCEEEEEEEECCCCHHHHHHHHHCCCCCEEEEEECCCEEEEEE-----CCEEEEEEECCC T ss_conf 77777751----------677068999851898789999987528733022000010356641-----435999987487 Q ss_pred CCHHHHHHHHHHHCCCC-CCCEEEEEECCCCCCHHHHHHHHHHHHHHH--HCCCCCCCEEEEEECCC Q ss_conf 85435887887718778-782799985166634468999999999986--40689987389984773 Q Fun_Sc_NP_0140 84 NTDDALDLLKPFLQEHS-SKVRWLILLDWTLNDQKLWLNELSYAFNKI--KQLNDDNEFSVWCLNSG 147 (312) Q Consensus 84 ~~~~~~~LLkp~L~~~s-~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L--~~l~~Dt~i~VVc~~sD 147 (312) .---. ++-..-- .-.-+|+++|=| -..-+...+.|+..+ .....+.+++|++-|.| T Consensus 71 qe~~r-----~lw~~Yy~~a~~iI~VvD~s---d~~~~~~~~~~l~~~l~~~~~~~~pilIl~NK~D 129 (181) T smart00177 71 QDKIR-----PLWRHYYTNTQGLIFVVDSN---DRDRIDEAREELHRMLNEDELRDAVILVFANKQD 129 (181) T ss_pred CHHHH-----HHHHHHCCCCCEEEEEEECC---CHHHHHHHHHHHHHHHCCCCCCCCEEEEEECCCC T ss_conf 34578-----88887606896899998658---8334899999999985020227978999950558 No 56 >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=96.43 E-value=0.15 Score=28.08 Aligned_columns=168 Identities=8% Q ss_pred CEEEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCE Q ss_conf 4389975983317999998514-778655665575025633562121332688998607854358878877187787827 Q Fun_Sc_NP_0140 26 ITAIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVR 104 (312) Q Consensus 26 k~~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l 104 (312) +-++++|..+-|||.|+.+... +-.+.+.+..+-.| ...+.-+ .....+.+|=..|--.-..=--.++-.++ - T Consensus 2 ~KIvliGd~~VGKTsli~rf~~~~f~~~y~~Ti~~~~-~k~i~v~-~~~~~l~iwDtaGqe~~~~l~~~~~~~a~----~ 75 (180) T cd04137 2 RKIAVLGSRSVGKSSLTVQFVEGHFVESYYPTIENTF-SKIIRYK-GQDYHLEIVDTAGQDEYSILPQKYSIGIH----G 75 (180) T ss_pred EEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCEECCC-CCCEEEC-CEEEEEEECCCCCCCCCHHHHHHHCCCCC----E T ss_conf 0789970798438999999861800776466100031-2003566-82689987478873200023366504887----3 Q ss_pred EEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 99985166634468999999999986406899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 105 WLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 105 ~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +++.-|-+..+.--.++.++..+.... ..+..++++|..|+| |..++ .-..++ .+.+|-.+|+..|. T Consensus 76 ~ilvfdit~~~Sf~~i~~~~~~i~~~~-~~~~ipiiLvGNK~D----l~~~r-~V~~~e-------~~~~a~~~~~~~~E 142 (180) T cd04137 76 YILVYSVTSRKSFEVVKVIYDKILDML-GKESVPIVLVGNKSD----LHTQR-QVSTEE-------GKELAESWGAAFLE 142 (180) T ss_pred EEEEEECCCHHHHHHHHHHHHHHHHHH-CCCCCEEEEEEECCC----CCCCC-CCCHHH-------HHHHHHHCCCCEEE T ss_conf 899854489767899999999999861-899848999420168----51236-579899-------99999965997899 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCC Q ss_conf 5256531355566778888753001247787752 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDH 218 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~ 218 (312) | |+++..|-...+.. ++..+.+.+...+ T Consensus 143 ~---SAk~~~nV~e~F~~---l~~~I~k~~~~~~ 170 (180) T cd04137 143 S---SARENENVEEAFEL---LIEEIEKVENPLD 170 (180) T ss_pred E---ECCCCCCHHHHHHH---HHHHHHHHCCCCC T ss_conf 8---61579888899999---9999997338888 No 57 >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=96.39 E-value=0.21 Score=27.11 Aligned_columns=155 Identities=8% Q ss_pred CCCEEEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCC Q ss_conf 644389975983317999998514-7786556655750256335621213326889986078543588788771877878 Q Fun_Sc_NP_0140 24 ATITAIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSK 102 (312) Q Consensus 24 ~~k~~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~ 102 (312) |+--++++|+.+-|||+|+.+... .-.+.+.+..+-.|.-...-++ ....+.+|=..|.. .+..+.+.+...-.. T Consensus 1 p~~Kiv~iGd~~VGKTsll~r~~~~~f~~~~~pt~~~~~~k~~~v~~--~~~~l~i~Dt~g~e-~~~~~~~~~~~~a~~- 76 (164) T cd04145 1 PTYKLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCEIDG--QWAILDILDTAGQE-EFSAMREQYMRTGEG- 76 (164) T ss_pred CCEEEEEECCCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEECC--EEEEEEEEECCCCC-HHHHHHHHHHCCCCE- T ss_conf 92789998079954899999987170177657530212788898889--48999885068760-012454887238966- Q ss_pred CEEEEEECCCCCCHHHHHHHHHHHHHHHHCC--CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCC Q ss_conf 2799985166634468999999999986406--89987389984773456655324541157889999999999988294 Q Fun_Sc_NP_0140 103 VRWLILLDWTLNDQKLWLNELSYAFNKIKQL--NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDS 180 (312) Q Consensus 103 ~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l--~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGA 180 (312) +++.-|-+ -.-....++.|+..+.+. ..+.++++|..|+| |++++..=.++...|..+. |+ T Consensus 77 --~iivydi~---~~~Sf~~i~~w~~~i~~~~~~~~~piilvGNK~D----L~~~r~V~~~e~~~~a~~~--------~~ 139 (164) T cd04145 77 --FLLVFSVT---DRGSFEEVDKFHTQILRVKDRDEFPMILVGNKAD----LEHQRKVSREEGQELARKL--------KI 139 (164) T ss_pred --EEEEEECC---CHHHHHHHHHHHHHHHHHCCCCCCEEEEEECCCC----CCCCCCCCHHHHHHHHHHC--------CC T ss_conf --89998769---9657899999988777534899847999800258----0012205988999999965--------99 Q ss_pred EEEEECCCCCHHHHHHHHHHHH Q ss_conf 1588525653135556677888 Q Fun_Sc_NP_0140 181 SLFYICEDHTEEKREEAQRLKY 202 (312) Q Consensus 181 SLiYts~ts~~~~kn~~~~l~y 202 (312) ..|.+ |++...|-...+.. T Consensus 140 ~~~E~---SAk~~~nV~e~F~~ 158 (164) T cd04145 140 PYIET---SAKDRLNVDKAFHD 158 (164) T ss_pred CEEEE---ECCCCCCHHHHHHH T ss_conf 69999---71589887899999 No 58 >smart00175 RAB Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking. Probab=96.38 E-value=0.2 Score=27.31 Aligned_columns=158 Identities=13% Q ss_pred EEEECCCCHHHHHHHHHHCCCC-CCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC--CCCE Q ss_conf 8997598331799999851477-865566557502563356212133268899860785435887887718778--7827 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEG-SNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS--SKVR 104 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~-~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s--~~~l 104 (312) ++++|..+-|||.++.+..... .+.+.+..+.+|....+. -|+.++.+-+.+.+..+.. ..+.+.. .-.- T Consensus 3 iviiG~~~vGKTsii~~~~~~~f~~~~~~Ti~~~~~~k~v~---~~~~~~~l~i~Dt~g~e~~----~~~~~~~~~~~d~ 75 (164) T smart00175 3 IILIGDSGVGKSSLLSRFTDGKFSEDSKSTIGVDFKTKTIE---VDGKRVKLQIWDTAGQERF----RSITSSYYRGAVG 75 (164) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEE---ECCEEEEEEEEECCCCHHH----HHHHHHHHCCCCE T ss_conf 89982699648999999862810665565022367789999---9896999998646987146----7777875048976 Q ss_pred EEEEECCCCCCHHHHHHHHHHHHHHHHCC-CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEE Q ss_conf 99985166634468999999999986406-89987389984773456655324541157889999999999988294158 Q Fun_Sc_NP_0140 105 WLILLDWTLNDQKLWLNELSYAFNKIKQL-NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLF 183 (312) Q Consensus 105 ~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l-~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLi 183 (312) +++.-|-+. +..+-.. ..|...++.. +.+.++++|..|+|-...-+-.. +-.+.++-++|...+ T Consensus 76 ~iivfdi~~--~~Sf~~i-~~w~~~i~~~~~~~~piilvgNK~Dl~~~~~i~~------------~e~~~~a~~~~~~y~ 140 (164) T smart00175 76 ALLVYDITN--RDSFENL-ENWLKELREYADPNVVIMLVGNKSDLEEQRQVST------------EEAQKFAEEHGLLFI 140 (164) T ss_pred EEEEEECCC--HHHHHHH-HHHHHHHHHHCCCCCEEEEEEECCCCCCCCCCCH------------HHHHHHHHHCCCEEE T ss_conf 999932798--7799999-9999999972699958999851102200025898------------999999996498299 Q ss_pred EECCCCCHHHHHHHHHHHHHHHHHHCCCCC Q ss_conf 852565313555667788887530012477 Q Fun_Sc_NP_0140 184 YICEDHTEEKREEAQRLKYQELLKHFCEDR 213 (312) Q Consensus 184 Yts~ts~~~~kn~~~~l~y~~L~~h~l~~~ 213 (312) -+ |++...|-...+.. ++..+..+ T Consensus 141 E~---Sak~~~~i~e~F~~---l~~~i~~~ 164 (164) T smart00175 141 ET---SAKTNTNVEEAFEE---LAKEILKR 164 (164) T ss_pred EE---ECCCCCCHHHHHHH---HHHHHHHC T ss_conf 99---70479887899999---99999719 No 59 >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=96.36 E-value=0.061 Score=30.42 Aligned_columns=113 Identities=10% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEE Q ss_conf 38997598331799999851477865566557502563356212133268899860785435887887718778-78279 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRW 105 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~ 105 (312) .++++|.++.|||+++.++.-..--...++.|.++..+-+......+.++.+|-+.|. .-.+++-..-- --.-+ T Consensus 5 kIvilG~~~~GKTsil~r~~~~~~~~~~pT~g~~~~~~~~~~~~~~~v~l~iwD~aGq-----e~~r~l~~~yy~~a~gi 79 (183) T cd04152 5 HIVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEKIKVSLGNSKGITFHFWDVGGQ-----EKLRPLWKSYTRCTDGI 79 (183) T ss_pred EEEEEECCCCCHHHHHHHHHCCCCCCEECCEEEEEEEEEEEECCCCEEEEEEEECCCC-----HHHHHHHHHHCCCCCEE T ss_conf 9999850898689988876448211100220334788987504774279999864885-----02567553113688679 Q ss_pred EEEECCCCCCHHHHHHHHHHHHHHHHCCCC--CCCEEEEEECCC Q ss_conf 998516663446899999999998640689--987389984773 Q Fun_Sc_NP_0140 106 LILLDWTLNDQKLWLNELSYAFNKIKQLND--DNEFSVWCLNSG 147 (312) Q Consensus 106 ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~--Dt~i~VVc~~sD 147 (312) |+.+|=| -..=+...+.|+..+.+... +.+++++.-|+| T Consensus 80 I~V~D~s---d~~~~~~~~~~l~~i~~~~~~~~~piLi~~NK~D 120 (183) T cd04152 80 VFVVDSV---DVERMEEAKTELHKITRFSENQGVPVLVLANKQD 120 (183) T ss_pred EEEEECC---CHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCC T ss_conf 9998537---8346899999999997112678978999961678 No 60 >pfam00025 Arf ADP-ribosylation factor family. Pfam combines a number of different Prosite families together Probab=96.36 E-value=0.05 Score=30.93 Aligned_columns=108 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|..+.|||+++.++-.+....+.++.|..+..+...+ ..+.+|-+.| .+.+-++-+.....-.. +|+ T Consensus 18 ivllG~~~vGKTsli~r~~~~~~~~~~pTig~~~~~i~~~~-----~~~~iwD~~G-~e~~r~l~~~y~~~a~~---iI~ 88 (176) T pfam00025 18 ILMLGLDNAGKTTILYKLKLGEVVTTIPTIGFNVETVTYKN-----VKFTVWDVGG-QESLRPLWRNYFPNTDG---VIF 88 (176) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCEEEEEEEEEEEEEEECC-----EEEEEEECCC-CHHHHHHHHHHCCCCCE---EEE T ss_conf 99984399868898887645830202200311588987658-----3899987697-15689998874125227---999 Q ss_pred EECCCCCCHHHHHHHHHHHHHHH--HCCCCCCCEEEEEECCC Q ss_conf 85166634468999999999986--40689987389984773 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKI--KQLNDDNEFSVWCLNSG 147 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L--~~l~~Dt~i~VVc~~sD 147 (312) .+|=+ |+.. +...+.++..+ +....+.+++|++.|+| T Consensus 89 V~D~s--d~~~-~~~~~~~l~~ll~~~~~~~~pilI~~NK~D 127 (176) T pfam00025 89 VVDSA--DRDR-IEEAKQELHALLNEEELADAPLLIFANKQD 127 (176) T ss_pred EEECC--CCCC-HHHHHHHHHHHHHCCCCCCCEEEEEEECCC T ss_conf 99648--8654-689999999985001458978999960668 No 61 >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=96.35 E-value=0.35 Score=25.84 Aligned_columns=162 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||.++.+... .-.+.+.+..+-.|.-...- ++..+.+-+.+.+..+.-..|.+..-..+. -++ T Consensus 5 i~liGd~~VGKTsli~rf~~~~F~~~y~pTi~~~~~~~i~~----~~~~v~l~iwDtaGqe~~~~l~~~~~~~a~--~~i 78 (172) T cd04141 5 IVMLGAGGVGKSAVTMQFISHSFPDYHDPTIEDAYKQQARI----DNEPALLDILDTAGQAEFTAMRDQYMRCGE--GFI 78 (172) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCEEEEEEEEEE----CCEEEEEEEECCCCCHHHHHHHHHHCCCCC--EEE T ss_conf 99970798438999999872822776566300004789989----795899986227762135567687514997--389 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 98516663446899999999998640689987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) +.-|=+.....--+....+.+...+ ...+.++++|..|+| |+.++..=.++ .+.+|=.+|+..|-| T Consensus 79 lVyditd~~Sf~~i~~w~~~i~~~~-~~~~~pivlvgNK~D----L~~~r~V~~~e--------~~~~a~~~~~~f~Et- 144 (172) T cd04141 79 ICYSVTDRHSFQEASEFKKLITRVR-LTEDIPLVLVGNKVD----LESQRQVTTEE--------GRNLAREFNCPFFET- 144 (172) T ss_pred EEEECCCHHHHHHHHHHHHHHHHHC-CCCCCEEEEEECCCH----HHHCCCCCHHH--------HHHHHHHCCCCEEEE- T ss_conf 9854289768999999999999740-799977999815601----65415667789--------999999659969999- Q ss_pred CCCCHHHHHHHHHHHHHHHHHHCCCCCC Q ss_conf 5653135556677888875300124778 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQELLKHFCEDRD 214 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~L~~h~l~~~~ 214 (312) |+++..|-...+.. ++.....++ T Consensus 145 --SAk~~~nV~~~F~~---l~~~i~~k~ 167 (172) T cd04141 145 --SAALRHYIDDAFHG---LVREIRRKE 167 (172) T ss_pred --ECCCCCCHHHHHHH---HHHHHHHHC T ss_conf --70589887899999---999999717 No 62 >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=96.34 E-value=0.27 Score=26.48 Aligned_columns=159 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-||+.++.+... .-.+.+....|.+|....+.-++.....+.+|=-.| -+.|-.+.+... +.-.-++ T Consensus 5 IviiGd~~VGKTsli~rf~~~~F~~~~~~Tig~df~~k~v~i~dgk~v~L~IwDTaG-qE~f~si~~~yy---r~a~g~i 80 (211) T cd04111 5 LIVIGDSTVGKSSLLKRFTEGRFAEVSDPTVGVDFFSRLIEIEPGVRIKLQLWDTAG-QERFRSITRSYY---RNSVGVL 80 (211) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCEEEEEEEEEEEECCCCEEEEEEEECCC-CHHHHHHHHHHH---CCCCEEE T ss_conf 999826985489999887708216765650246888999996178479999863699-715688888860---1898899 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCC-CCCCCE-EEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 985166634468999999999986406-899873-899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQL-NDDNEF-SVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l-~~Dt~i-~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) ++-|.+ -.-=...+..|...++.. +.+..+ ++|-.|+| |+.++- .=.+--+.+|-.+|+..|- T Consensus 81 lVyDit---~~~SFe~i~~w~~ei~~~~~~~~~~~iLVGNK~D----L~~~R~--------Vs~eea~~~A~~~~~~f~E 145 (211) T cd04111 81 LVFDIT---NRESFEHVHDWLEEARSHIQPHRPVFILVGHKCD----LESQRQ--------VTREEAEKLAKDLGMKYIE 145 (211) T ss_pred EEEECC---CHHHHHHHHHHHHHHHHHCCCCCCEEEEECCCCC----HHHHHC--------CCHHHHHHHHHHCCCCEEE T ss_conf 998669---9778999999999999851899858999716534----133301--------2489999999966996999 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCCC Q ss_conf 525653135556677888875300124 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFCE 211 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l~ 211 (312) | |+++..|-...+.. ++...+ T Consensus 146 t---SAktg~nV~e~F~~---la~~I~ 166 (211) T cd04111 146 T---SARTGDNVEEAFEL---LTQEIY 166 (211) T ss_pred E---ECCCCCCHHHHHHH---HHHHHH T ss_conf 9---63589888999999---999999 No 63 >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=96.29 E-value=0.1 Score=29.02 Aligned_columns=113 Identities=11% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+.+-|||.++.+. -..+++.+-.+--+......-+ -++-++.+-+.+...-+.-.-+.+..-..+ .-+++ T Consensus 8 ivlvGd~~VGKTsli~r~--~~~~F~~~~~~Ti~~~~~~~~~-i~~~~v~l~iwDTaGqe~~~~l~~~~y~~a--~~~il 82 (182) T cd04172 8 IVVVGDSQCGKTALLHVF--AKDCFPENYVPTVFENYTASFE-IDTQRIELSLWDTSGSPYYDNVRPLSYPDS--DAVLI 82 (182) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCCCCCEEEEEEEEEEE-ECCEEEEEEEECCCCCHHHHHHHHHHCCCC--CEEEE T ss_conf 999836985488998887--5380157612057753689998-878599999850788745666647652699--87999 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCC Q ss_conf 8516663446899999999998640689987389984773 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSG 147 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD 147 (312) .-|.+. +.++-+.+..|...+++..++.++++|-.|+| T Consensus 83 vfdit~--~~Sf~~v~~~W~~ei~~~~~~~~iiLVGnK~D 120 (182) T cd04172 83 CFDISR--PETLDSVLKKWKGEIQEFCPNTKMLLVGCKSD 120 (182) T ss_pred EEECCC--HHHHHHHHHHHHHHHHHHCCCCEEEEEECCCC T ss_conf 986588--55789999998999998468966999854876 No 64 >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=96.27 E-value=0.35 Score=25.79 Aligned_columns=162 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||.|+.+... .-.+.+....|..|....+.-+ ..+..+..|=..|. ..+..+.+.+...-.- +| T Consensus 3 ivliGd~~VGKTsli~rf~~~~f~~~y~~Tig~d~~~k~~~~~-~~~i~l~iwDtaG~-e~~~~~~~~~~~~a~~---~i 77 (170) T cd04108 3 VIVVGDLSVGKTCLINRFCKDVFDKNYKATIGVDFEMERFEIL-GVPFSLQLWDTAGQ-ERFKCIASTYYRGAQA---II 77 (170) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEEEEEEEC-CEEEEEEEEECCCC-HHHHHHHHHHCCCCCE---EE T ss_conf 8998169854899888876282278624425667889987518-83799998536886-0245666754048880---89 Q ss_pred EEECCCCCCHHHHHHHHHHHHHH-HHCCCCCCCEE-EEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 98516663446899999999998-64068998738-99847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNK-IKQLNDDNEFS-VWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~-L~~l~~Dt~i~-VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) |.-|=+. +...-. +..|+.. ++..+.+.... +|..|+|-...-+... +.+--+.++-++|+..|. T Consensus 78 lvyDit~--~~Sf~~-~~~w~~~~~~~~~~~~~~i~LVGnK~DL~~~~~~~~----------~~~~~~~~a~~~~~~~fE 144 (170) T cd04108 78 IVFDLTD--VASLEH-TRQWLEDALKENDPSSVLLFLVGTKKDLSSPAQYAL----------MEQDAIKLAAEMQAEYWS 144 (170) T ss_pred EEEECCC--HHHHHH-HHHHHHHHHHHHCCCCCEEEEEECCCCCCCCCCCEE----------CHHHHHHHHHHCCCCEEE T ss_conf 9975498--657899-999999998740799968999835601045311200----------378999999965995999 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCC Q ss_conf 52565313555667788887530012 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFC 210 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l 210 (312) | |+++..|-...+...+-++.-+ T Consensus 145 t---SAktg~nV~e~F~~ia~~~~~~ 167 (170) T cd04108 145 V---SALSGENVREFFFRVAALTFEL 167 (170) T ss_pred E---ECCCCCCHHHHHHHHHHHHHHC T ss_conf 9---7258878789999999999850 No 65 >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=96.25 E-value=0.062 Score=30.37 Aligned_columns=108 Identities=11% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) +|++|.++.|||+++.++-.+......++.|.++.++.. .+..+.+|-+.|. ..+-++-+..... -.-+++ T Consensus 2 ililG~~~~GKTsii~r~~~~~~~~~~pT~g~~~~~i~~-----~~~~~~iwD~~Gq-e~~r~~~~~y~~~---a~~iI~ 72 (158) T cd04151 2 ILILGLDNAGKTTILYRLQLGEVVTTIPTIGFNVETVTY-----KNLKFQVWDLGGQ-TSIRPYWRCYYSN---TDAIIY 72 (158) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEE-----CCEEEEEEECCCC-CCCCHHHHHHCCC---CCEEEE T ss_conf 788950898688877766438621200320015889861-----7818999754887-4342135644037---787999 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCC--CCCEEEEEECCC Q ss_conf 8516663446899999999998640689--987389984773 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLND--DNEFSVWCLNSG 147 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~--Dt~i~VVc~~sD 147 (312) .+|=+..+. +...++|+..+-+-.. +.++++++-|+| T Consensus 73 V~D~sd~~~---~~~~~~~l~~~l~~~~~~~~pilIl~NK~D 111 (158) T cd04151 73 VVDSTDRDR---LGTAKEELHAMLEEEELKGAVLLVFANKQD 111 (158) T ss_pred EEECCCHHH---HHHHHHHHHHHHHCCCCCCCEEEEEEECCC T ss_conf 984588346---899999999997200447988999950678 No 66 >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=96.22 E-value=0.27 Score=26.55 Aligned_columns=156 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|.++.|||+++.++ ...++....+.+||....+.-+ .+.++.+|-+.|.-- +-++-+.....-.- +|+ T Consensus 2 IlilG~~~sGKTsll~rl--~~~~~~~~~pTig~~~~~~~~~--~~v~l~iwD~~G~e~-~r~~~~~y~~~a~~---iI~ 73 (160) T cd04156 2 VLLLGLDSAGKSTLLYKL--KHAELVTTIPTVGFNVEMLQLE--KHLSLTVWDVGGQEK-MRTVWKCYLENTDG---LVY 73 (160) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCEEEEECEEEEEEEEC--CEEEEEEEECCCCHH-HHHHHHHHCCCCCE---EEE T ss_conf 789950898689988877--4586230220001048899876--837999874587403-46666764057637---999 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCC-CCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 851666344689999999999864068-9987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLN-DDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~-~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) .+|=| |+...-+....+-..|+.-. ...++++|+.|+|.-..+..+.. -=...+..+|-.++.-++.+ T Consensus 74 V~D~s--d~~~~~~~~~~l~~~l~~~~~~~~p~liv~NK~Dl~~~~~~~ei--------~~~l~l~~~~~~~~~~i~~~- 142 (160) T cd04156 74 VVDSS--DEARLDESQKELKHILKNEHIKGVPVVLLANKQDLPGALTAEEI--------TRRFKLKKYCSDRDWYVQPC- 142 (160) T ss_pred EEECC--CHHHHHHHHHHHHHHHHHHCCCCCEEEEEEECCCCCCCCCHHHH--------HHHHHHHHHHHCCCCEEEEE- T ss_conf 97257--83468999999998852001279759999605588545788999--------98998999986089389997- Q ss_pred CCCCHHHHHHHHHHHHHH Q ss_conf 565313555667788887 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQE 204 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~ 204 (312) |+.+..+-...+...+ T Consensus 143 --SA~tG~gi~e~F~~lA 158 (160) T cd04156 143 --SAVTGEGLAEAFRKLA 158 (160) T ss_pred --ECCCCCCHHHHHHHHH T ss_conf --3146857789999984 No 67 >pfam00009 GTP_EFTU Elongation factor Tu GTP binding domain. This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains. Probab=96.17 E-value=0.043 Score=31.33 Aligned_columns=141 Identities=7% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCC-----CCCCCCCCEEEEECCCCCCCCCEEEE-----------EEEEECCCHHHHH Q ss_conf 3899759833179999985147786-----55665575025633562121332688-----------9986078543588 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSN-----SILDTTLINYATIGWTNDLKENYSVD-----------VYTLIRNTDDALD 90 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e-----~~~~~~~L~y~y~~v~~d~~d~~R~~-----------vy~L~~~~~~~~~ 90 (312) |+.++|--..||++++..++.+... ..+.+....+..+....|.+-...++ .+.+...++|. + T Consensus 5 ni~i~GhvD~GKSTL~~~Ll~~~~~i~~~~~~~~~~~~~~~~D~~~~E~~rgiti~~~~~~~~~~~~~~~iiDtPGH~-d 83 (209) T pfam00009 5 NIGIIGHVDHGKTTLTDALLYVTGAIGERGEAKEGGKTSFVIDKLEEERERGITIKSAHVSFETEKRHINIIDTPGHV-D 83 (209) T ss_pred EEEEEEEECCCHHHHHHHHHHHHCCCCCCHHHHHHCHHHHCCCCCCHHHHCCCEEEEEEEEEECCCCEEEEEECCCCH-H T ss_conf 899985306877899999988622232001122101010002465004545861533478972278179998468705-7 Q ss_pred HHHHHHCCCCCCCEEEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHH Q ss_conf 78877187787827999851666344689999999999864068998738998477345665532454115788999999 Q Fun_Sc_NP_0140 91 LLKPFLQEHSSKVRWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQT 170 (312) Q Consensus 91 LLkp~L~~~s~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~ 170 (312) +++-....-+---..|+++|=.. -...|-++++..++.++.. .+.|++.|-|-+.- +|+++.|+.|.+. T Consensus 84 f~~~~~~g~~~~D~aiLVVda~~----G~~~qT~e~~~~~~~~~i~-~iiv~iNK~D~~~~------~~~~e~~~~i~~~ 152 (209) T pfam00009 84 FTKEMIRGAAQADGAILVVDAVE----GVMPQTREHLRLAKQLGVP-ILVVAINKIDRVDA------EPDEEVYEELKKE 152 (209) T ss_pred HHHHHHHHHHHHHHEEEEEECCC----CCCHHHHHHHHHHHHCCCC-EEEEEEECCCCCCC------CHHHHHHHHHHHH T ss_conf 89999999876504377775488----8335689999999973798-69999852579998------7558999999999 Q ss_pred HHHHHHHCC Q ss_conf 999998829 Q Fun_Sc_NP_0140 171 LRSFCYFND 179 (312) Q Consensus 171 LRtvcL~yG 179 (312) ++.++.++| T Consensus 153 i~~~l~~i~ 161 (209) T pfam00009 153 VRELLKKIG 161 (209) T ss_pred HHHHHHHHC T ss_conf 999998608 No 68 >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=96.14 E-value=0.39 Score=25.55 Aligned_columns=151 Identities=6% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+... .-.+.+.+..+ ++....+.-+ .....+.+|=-.| ...+..+.+.....- .-++ T Consensus 4 IvvvGd~~VGKTsli~rf~~~~f~~~y~~Ti~-~~~~k~i~~~-~~~~~l~i~Dt~G-~e~~~~~~~~~~~~a---~~~i 77 (163) T cd04176 4 VVVLGSGGVGKSALTVQFVSGTFIEKYDPTIE-DFYRKEIEVD-SSPSVLEILDTAG-TEQFASMRDLYIKNG---QGFI 77 (163) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCCCC-CEEEEEEEEC-CEEEEEEEEECCC-CCHHHHHHHHHCCCC---CEEE T ss_conf 89970798548999988763800776563100-0047899888-9689999874688-712456777425799---8699 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHH--CCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 9851666344689999999999864--06899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIK--QLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~--~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +.-|-+ |+..+-. +..|+..+. ......++++|-.|+| |+.++..-.++ .+.++=++|+..|. T Consensus 78 lvydi~--~~~Sf~~-i~~~~~~i~~~~~~~~~piilvGnK~D----l~~~r~V~~~e--------~~~~a~~~~~~y~E 142 (163) T cd04176 78 VVYSLV--NQQTFQD-IKPMRDQIVRVKGYEKVPIILVGNKVD----LESEREVSSAE--------GRALAEEWGCPFME 142 (163) T ss_pred EEEECC--CHHHHHH-HHHHHHHHHHHCCCCCCEEEEEECCCC----HHHHCCCCHHH--------HHHHHHHCCCCEEE T ss_conf 997669--9768899-999876567531899828999733200----11110246378--------99999963995899 Q ss_pred ECCCCCHHHHHHHHHHHH Q ss_conf 525653135556677888 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKY 202 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y 202 (312) + |++...|-...+.. T Consensus 143 ~---SAk~~~nV~e~F~~ 157 (163) T cd04176 143 T---SAKSKTMVNELFAE 157 (163) T ss_pred E---ECCCCCCHHHHHHH T ss_conf 9---70479887899999 No 69 >cd00881 GTP_translation_factor GTP translation factor family. This family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function. Probab=96.12 E-value=0.092 Score=29.33 Aligned_columns=165 Identities=8% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEE-----------EEEECCCHHHHHHHHHH Q ss_conf 3899759833179999985147786556655750256335621213326889-----------98607854358878877 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDV-----------YTLIRNTDDALDLLKPF 95 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~v-----------y~L~~~~~~~~~LLkp~ 95 (312) |+-++|--..||++|++.+....+...+.+..-..+....+.|.+-..-++. |.+...++| .++.+-. T Consensus 1 Ni~iiGhvd~GKTTL~~~ll~~~~~~~~~~~~~~~~~D~~~~E~~rgiti~~~~~~~~~~~~~~~~iDtPGH-~~f~~~~ 79 (189) T cd00881 1 NVGIAGHVDHGKTTLTERLLYVTGDIERDGTVEETFLDVLKEERERGITIKSGVATFEWPDRRVNFIDTPGH-EDFSSEV 79 (189) T ss_pred CEEEEEECCCCHHHHHHHHHHHHCCCCCCCEEEEEEECCCHHHHHHHHHHCEEEEEEECCCEEEEEEECCCC-HHHHHHH T ss_conf 958897348887899999998740233430001000055478888654310123687318818999817874-5567766 Q ss_pred HCCCCCCCEEEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHH Q ss_conf 18778782799985166634468999999999986406899873899847734566553245411578899999999999 Q Fun_Sc_NP_0140 96 LQEHSSKVRWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFC 175 (312) Q Consensus 96 L~~~s~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvc 175 (312) +..-+.--..++++|=.. ....|-++++..++..+- ++++++.|.|.+ .++.|+-+.+-++.+. T Consensus 80 ~~~~~~~D~~ilvVda~~----G~~~qt~~~~~~~~~~~~--~~iiviNKiD~~----------~~~~~~~v~~ei~~~l 143 (189) T cd00881 80 IRGLSVSDGAILVVDANE----GVQPQTREHLRIAREGGL--PIIVAINKIDRV----------GEEDLEEVLREIKELL 143 (189) T ss_pred HHHCCCCCEEEEEECCCC----CCCHHHHHHHHHHHHCCC--CEEEEEECCCCC----------CCCCHHHHHHHHHHHH T ss_conf 320000466899981777----644147999999996589--689998546888----------8303899999999998 Q ss_pred HHCC-----------CEEEEECCCCCHHHHHHHHHHHHHHHHHHCCC Q ss_conf 8829-----------41588525653135556677888875300124 Q Fun_Sc_NP_0140 176 YFND-----------SSLFYICEDHTEEKREEAQRLKYQELLKHFCE 211 (312) Q Consensus 176 L~yG-----------ASLiYts~ts~~~~kn~~~~l~y~~L~~h~l~ 211 (312) -.+| ++.+-..+.|+....+-..++.. ++..+. T Consensus 144 ~~~~~~~~~~~~~~~~~~~piv~~SA~~G~gi~~Lle~---i~~~lP 187 (189) T cd00881 144 GLIGFISTKEEGTRNGLLVPIVPGSALTGIGVEELLEA---IVEHLP 187 (189) T ss_pred HHHCCCCHHHHHHCCCCCEEEEEEECCCCCCHHHHHHH---HHHHCC T ss_conf 64133300233203677421798314468986899999---997377 No 70 >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=96.11 E-value=0.28 Score=26.42 Aligned_columns=166 Identities=5% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+++-||+.|+.+. -..+++.+-.+-..-....+-. -++..+.+-+.+...-+--.-+.+.--..+. -+++ T Consensus 3 ivliGd~~VGKTsLi~~~--~~~~F~~~~~~Ti~~~~~~~i~-i~~~~~~l~iwDtaGqe~~~~~~~~~~~~a~--~~il 77 (174) T cd04135 3 CVVVGDGAVGKTCLLMSY--ANDAFPEEYVPTVFDHYAVSVT-VGGKQYLLGLYDTAGQEDYDRLRPLSYPMTD--VFLI 77 (174) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCCCCCEEEECCCCEEE-ECCEEEEEEEECCCCCHHHHHHHHHHCCCCC--EEEE T ss_conf 899707984389999987--6183167645514403320035-6886899987168887026778897548998--7999 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEECC Q ss_conf 85166634468999999999986406899873899847734566553245411578899999999999882941588525 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYICE 187 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts~ 187 (312) .-|-+ |+.++-+.-..|+..+++..++.++++|-.|+|-.+.-+-....=...+-..-.+--+.++-++|+-.|+- T Consensus 78 vydit--~~~Sf~~i~~~w~~~~~~~~~~~piilVGnK~DL~~~~~~~~~~~~~~~r~Vs~eeg~~~a~~~~~~~f~E-- 153 (174) T cd04135 78 CFSVV--NPASFQNVKEEWVPELKEYAPNVPYLLVGTQIDLRDDPKTLARLNDMKEKPVTVEQGQKLAKEIGAHCYVE-- 153 (174) T ss_pred EEECC--CHHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCCCCHHHHHHHHHCCCCCCCHHHHHHHHHHCCCCEEEE-- T ss_conf 96558--63248999999899998617995489973563331214677665420267789899999999808924688-- Q ss_pred CCCHHHHHHHHHHHH Q ss_conf 653135556677888 Q Fun_Sc_NP_0140 188 DHTEEKREEAQRLKY 202 (312) Q Consensus 188 ts~~~~kn~~~~l~y 202 (312) +|+++..|-..++.. T Consensus 154 tSAkt~~~V~e~F~~ 168 (174) T cd04135 154 CSALTQKGLKTVFDE 168 (174) T ss_pred EECCCCCCHHHHHHH T ss_conf 741467777899999 No 71 >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=96.11 E-value=0.094 Score=29.27 Aligned_columns=109 Identities=8% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 38997598331799999851477865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) .++++|.++.|||+++.++..+....+.+..|.++-.+.+ ++.++.+|-+.| ...+-++-+.....- ..+| T Consensus 16 kIliiG~~~~GKTsil~~l~~~~~~~~~pT~G~~~~~i~~-----~~~~l~iwD~~G-qe~~r~~~~~y~~~a---~~iI 86 (173) T cd04154 16 RILILGLDNAGKTTILKKLLGEDIDTISPTLGFQIKTLEY-----EGYKLNIWDVGG-QKTLRPYWRNYFEST---DALI 86 (173) T ss_pred EEEEEECCCCCHHHHHHHHHCCCCCCEEEEEEEEEEEEEE-----CCEEEEEEECCC-CHHHHHHHHHHCCCC---CEEE T ss_conf 8999950898789988887289546034235216888898-----588999987587-503676655312467---7799 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHH--HCCCCCCCEEEEEECCC Q ss_conf 985166634468999999999986--40689987389984773 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKI--KQLNDDNEFSVWCLNSG 147 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L--~~l~~Dt~i~VVc~~sD 147 (312) +.+|=|..+. +.+.+.|+..+ .....+.+++|++.|+| T Consensus 87 ~VvD~sd~~~---~~~~~~~l~~ll~~~~~~~~pilI~~NK~D 126 (173) T cd04154 87 WVVDSSDRLR---LDDCKRELKELLQEERLAGATLLILANKQD 126 (173) T ss_pred EEEECCCCCC---HHHHHHHHHHHHCCHHHCCCEEEEEEECCC T ss_conf 9975388544---688999999874023117968999972558 No 72 >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=96.08 E-value=0.35 Score=25.81 Aligned_columns=158 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+|+.+... .-.+.+..+.+ ++....+.-+ .....+..|=..|.- .+..+.+.....-. -+| T Consensus 5 iiliGd~~vGKTsli~r~~~~~f~~~y~~ti~-~~~~k~~~i~-~~~~~l~iwDtaG~e-~~~~~~~~~~~~a~---~~i 78 (166) T smart00173 5 LVVLGSGGVGKSALTIQFVQGIFVDDYDPTIE-DSYRKQIEID-GEVCLLDILDTAGQE-EFSAMRDQYMRTGE---GFL 78 (166) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCC-CCEEEEEEEC-CEEEEEEEEECCCCC-CHHHHHHHHHCCCC---CEE T ss_conf 99980799648999999872802775455212-1225789898-979999986279985-12367788740799---359 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCC--CCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 985166634468999999999986406--899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQL--NDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l--~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +.-|-+. +..+-. +..|+..+... ....++++|..|+|-...-+=.. +-.+.+|-.+|+..|. T Consensus 79 ivydit~--~~Sf~~-~~~w~~~i~~~~~~~~ip~vlvgNK~Dl~~~r~v~~------------~~~~~~a~~~~~~~~E 143 (166) T smart00173 79 LVYSITD--RQSFEE-IKKFREQILRVKDRDDVPIVLVGNKCDLENERQVST------------EEGKELARQWNCPFLE 143 (166) T ss_pred EEEECCC--HHHHHH-HHHHHHHHHHHCCCCCCEEEEEECCCCCCCCCCCCH------------HHHHHHHHHCCCCEEE T ss_conf 9997499--789999-989989998742899957999811465100045767------------8999999966996999 Q ss_pred ECCCCCHHHHHHHHHHHHHHHHHHCCCC Q ss_conf 5256531355566778888753001247 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKYQELLKHFCED 212 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y~~L~~h~l~~ 212 (312) + |++...|-...+.. ++-.+.+ T Consensus 144 ~---SAk~~~nV~e~F~~---l~~~i~k 165 (166) T smart00173 144 T---SAKERINVDEAFYD---LVREIRK 165 (166) T ss_pred E---ECCCCCCHHHHHHH---HHHHHHC T ss_conf 9---72589888899999---9999960 No 73 >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=96.08 E-value=0.073 Score=29.93 Aligned_columns=107 Identities=13% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEEE Q ss_conf 8997598331799999851477865566557502563356212133268899860785435887887718778-782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~V 106 (312) ++++|.++.|||+++.++..+......++.|.++..+.+. +.++.+|-+.|.---- ++-..-- .-.-+| T Consensus 18 ililG~~~sGKTtil~~~~~~~~~~~~pTvg~~~~~i~~~-----~~~~~iwD~~Gqe~~r-----~~w~~y~~~~~~iI 87 (174) T cd04153 18 VIIVGLDNAGKTTILYQFLLGEVVHTSPTIGSNVEEIVYK-----NIRFLMWDIGGQESLR-----SSWNTYYTNTDAVI 87 (174) T ss_pred EEEEEECCCCHHHHHHHHHCCCCCCEECCCCCEEEEEEEC-----CEEEEEEECCCCCCCC-----HHHHHHCCCCCEEE T ss_conf 9998508986899888875386032002100058898728-----5899998768862340-----46675405888799 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCC--CCCEEEEEECCC Q ss_conf 98516663446899999999998640689--987389984773 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLND--DNEFSVWCLNSG 147 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~--Dt~i~VVc~~sD 147 (312) +.+|=| |+.. +...+.|+..+.+-.. +.+++|++-|.| T Consensus 88 ~VvD~s--d~~~-~~~~~~~l~~~l~~~~~~~~piLIlaNK~D 127 (174) T cd04153 88 LVIDST--DRER-LPLTKEELYKMLAHEDLRKAVLLVLANKQD 127 (174) T ss_pred EEEECC--CCCC-HHHHHHHHHHHHCCCCCCCCEEEEEEECCC T ss_conf 999668--8200-788999999985252427978999960668 No 74 >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=95.96 E-value=0.12 Score=28.64 Aligned_columns=108 Identities=15% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) +|++|.+++|||+++.++.. +..+.+.++.|.+.-.+.. ++.++.+|=+ +-...+-++-+... ..-.-+| T Consensus 2 IliLGLd~aGKTtil~~l~~~~~~~~~~PTiGfn~~~i~~-----~~~~l~~wDi-gGq~~~R~~W~~Yy---~~~~giI 72 (164) T cd04162 2 ILVLGLDGAGKTSLLHSLSSERSLESVVPTTGFNSVAIPT-----QDAIMELLEI-GGSQNLRKYWKRYL---SGSQGLI 72 (164) T ss_pred EEEEEECCCCHHHHHHHHHCCCCCCCEEEEEEEEEEEEEE-----CCEEEEEEEC-CCCCCCHHHHHHHC---CCCCEEE T ss_conf 7899747975788777672796246266445105899871-----8789999874-78620013467641---6787899 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCC Q ss_conf 98516663446899999999998640689987389984773 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSG 147 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD 147 (312) +++|=+ |+.. +.+.++++..+.+-..+.+++|++-|.| T Consensus 73 fVVDss--D~~r-l~eak~eL~~ll~~~~~~PllvlaNKqD 110 (164) T cd04162 73 FVVDSA--DSER-LPLARQELHQLLQHPPDLPLVVLANKQD 110 (164) T ss_pred EEEECC--CHHH-HHHHHHHHHHHHHCCCCCEEEEEECCCC T ss_conf 998568--8111-8999999999983579971899841548 No 75 >cd01883 EF1_alpha Eukaryotic elongation factor 1 (EF1) alpha subfamily. EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in Probab=95.96 E-value=0.083 Score=29.60 Aligned_columns=140 Identities=8% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCC---------------CCCCCCCCEEEEECCCCCCCCCEEE-----------EEEE Q ss_conf 3899759833179999985147786---------------5566557502563356212133268-----------8998 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSN---------------SILDTTLINYATIGWTNDLKENYSV-----------DVYT 80 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e---------------~~~~~~~L~y~y~~v~~d~~d~~R~-----------~vy~ 80 (312) |++++|--.+||+++...+.-+... .-+..+.+.|..+....|.+-..-+ --|. T Consensus 1 Ni~iiGHVD~GKSTL~g~LL~~~g~v~~~~~~~~~~~s~~~g~~s~~~a~~~D~~~~ErerGiTi~~~~~~fet~~~~~~ 80 (219) T cd01883 1 NLVVIGHVDAGKSTTTGHLLYLLGGVDKRTIEKYEKEAKEMGKGSFKYAWVLDTLKEERERGVTIDVGLAKFETEKYRFT 80 (219) T ss_pred CEEEEEECCCCHHHHHHHHHHHHCCCCHHHHHHHHHHHHHCCCCCCHHHEECCCCHHHHHCCCEEEEEEEEEEECCCEEE T ss_conf 96899723888688999999984886788999999988760775200000003661266569608888999970893899 Q ss_pred EECCCHHHHHHHHHHHCCCCCCCEEEEEECCCC--------CCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHH Q ss_conf 607854358878877187787827999851666--------344689999999999864068998738998477345665 Q Fun_Sc_NP_0140 81 LIRNTDDALDLLKPFLQEHSSKVRWLILLDWTL--------NDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNL 152 (312) Q Consensus 81 L~~~~~~~~~LLkp~L~~~s~~~l~ViLLDWs~--------~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~L 152 (312) +...++| .++++-.++.-+.--..|+++|=+. ..||| |+|...++.++...=|++| ++|+.. T Consensus 81 iiD~PGH-~dfi~nmi~Gas~aD~AiLVVdA~~g~fE~~~~~~~QT-----reH~~l~~~lGv~~iIVav----NKmD~v 150 (219) T cd01883 81 ILDAPGH-RDFVPNMITGASQADVAVLVVDARKGEFEAGFEKGGQT-----REHALLARTLGVKQLIVAV----NKMDDV 150 (219) T ss_pred EEECCCH-HHHHHHHHHHHHHCCEEEEEEECCCCCHHCCCCCCCHH-----HHHHHHHHHCCCCEEEEEE----ECCCCC T ss_conf 9708317-88999999998751668999876888200034557217-----9999999980898189998----424689 Q ss_pred HHCCCCCCHHHHHHHHHHHHHHHHHCC Q ss_conf 532454115788999999999998829 Q Fun_Sc_NP_0140 153 QRHTTVWQSVHIDFILQTLRSFCYFND 179 (312) Q Consensus 153 EKe~~~w~de~fDfIqQ~LRtvcL~yG 179 (312) +-+ |+++.|+.|.+.++.++-+.| T Consensus 151 ~~~---~~~~rf~~I~~~~~~~l~~~g 174 (219) T cd01883 151 TVN---WSEERYDEIKKELSPFLKKVG 174 (219) T ss_pred CCC---CCHHHHHHHHHHHHHHHHHHC T ss_conf 985---027899999999999999838 No 76 >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=95.95 E-value=0.62 Score=24.33 Aligned_columns=185 Identities=7% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-||++|+.+... .-.+.+.+..+-.|......++. ..++.+|=-.| .+.+..+-+.....-.- ++ T Consensus 6 vvliGd~~VGKTsli~r~~~~~F~~~~~pTi~~~~~~~~~~~~~--~v~l~iwDTaG-qe~~~~l~~~~~~~a~~---~i 79 (191) T cd01875 6 CVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQTAVDGR--TVSLNLWDTAG-QEEYDRLRTLSYPQTNV---FI 79 (191) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECCC--EEEEEEECCCC-CHHHHHHHHHHHCCCCE---EE T ss_conf 99870798428999888752842665355045546886665172--79998514888-54467787876238986---99 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 98516663446899999999998640689987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) +.-|=+ |+.++.+.-..|...++....+.++++|-.|+|-...-+-....-.+-.-..-.+--+.++-+.|+-.++-| T Consensus 80 ivydit--d~~Sf~~i~~~w~~~i~~~~~~vpiiLVGNK~DL~~~~~~~~~~~e~~~~~Vs~eeg~~~a~~~~~~~y~Et 157 (191) T cd01875 80 ICFSIA--SPSSYENVRHKWHPEVCHHCPNVPILLVGTKKDLRNDADTLKKLKEQGQAPITPQQGGALAKQIHAVKYLEC 157 (191) T ss_pred EEEECC--CHHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCCCCHHHHHHHHHHHCCCCCHHHHHHHHHHCCCCEEEEE T ss_conf 998648--867889999988999997268967999834766311268888887510246688999999998089506886 Q ss_pred CCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCE Q ss_conf 56531355566778888753001247787752240 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEM 221 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~v 221 (312) .....++-+++--...+. ++|+-.-...++-..| T Consensus 158 SAktg~nV~e~F~~l~r~-vl~~~p~~~~~~c~~~ 191 (191) T cd01875 158 SALNQDGVKEVFAEAVRA-VLNPTPIKDTKSCVLL 191 (191) T ss_pred ECCCCCCHHHHHHHHHHH-HHCCCCCCCCCCCEEC T ss_conf 404777878999999999-8478898878874349 No 77 >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=95.88 E-value=0.19 Score=27.47 Aligned_columns=153 Identities=12% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||+++.+... +-.+.+....|.+|....+.- ++.++.+-+.+.+..+....+.+..-..+.-..+| T Consensus 8 ivliGd~~vGKTsLi~rf~~~~f~~~~~~tig~~~~~k~i~~---~~~~~~l~i~Dtag~e~~~~l~~~~~~~~~~~iiv 84 (170) T cd04116 8 VILLGDGGVGKSSLMNRYVTNKFDTQLFHTIGVEFLNKDLEV---DGHFVTLQIWDTAGQERFRSLRTPFYRGSDCCLLT 84 (170) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCEEECCEEEECCC---CCCEEEEEEECCCCCCHHHHHHHHHHCCCCEEEEE T ss_conf 999807995489999887538117773473231102200004---79648999870789810123115763189848999 Q ss_pred EEEC--CCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 9851--66634468999999999986406899873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLD--WTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLD--Ws~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +=++ .|..+=..|..++..+...-. ..+.++++|+.|+| |++... -.+-.+.+|-.+|...+| T Consensus 85 ydit~~~Sf~~i~~w~~e~~~~~~~~~--~~~ipiilVGNK~D----L~~r~V---------~~~e~~~~~~~~~~~~~~ 149 (170) T cd04116 85 FAVDDSQSFQNLSNWKKEFIYYADVKE--PESFPFVVLGNKND----IPERQV---------STEEAQAWCRENGDYPYF 149 (170) T ss_pred EECCCHHHHHHHHHHHHHHHHHCCCCC--CCCCEEEEEECCCC----CHHHCC---------HHHHHHHHHHHCCCCEEE T ss_conf 854997689999999999998603577--89707999835422----011101---------178999999970797178 Q ss_pred ECCCCCHHHHHHHHHH Q ss_conf 5256531355566778 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRL 200 (312) Q Consensus 185 ts~ts~~~~kn~~~~l 200 (312) - +|+++.-|-...+ T Consensus 150 E--~SAk~g~nv~~~F 163 (170) T cd04116 150 E--TSAKDATNVAAAF 163 (170) T ss_pred E--EECCCCCCHHHHH T ss_conf 9--8604898878999 No 78 >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=95.84 E-value=0.52 Score=24.80 Aligned_columns=172 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+.+-|||+|+.+. -+..++..-.+--..-....-. -|+..+.+-+.+.+.-+--..+.+..-..+.-..+|+ T Consensus 4 iiliGd~~VGKTsli~r~--~~~~F~~~~~pTi~~~~~~~i~-i~~~~v~l~iwDtaGqe~~~~l~~~~~~~a~~~ilvy 80 (175) T cd01870 4 LVIVGDGACGKTCLLIVF--SKDQFPEVYVPTVFENYVADIE-VDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCF 80 (175) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCCCCCEEEEEEEEEEE-ECCEEEEEEEECCCCHHHHHHHHHHHHCCCCEEEEEE T ss_conf 899826984389999998--6382366525402213689998-9896999987058620246677787504898489997 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEECC Q ss_conf 85166634468999999999986406899873899847734566553245411578899999999999882941588525 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYICE 187 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts~ 187 (312) +..|+..+-+....|...+++...+.++++|-.|+|-...-.-....-...+-..-.+--+.++-++|+-.++-+. T Consensus 81 ----di~~~~Sf~~i~~~W~~~~~~~~~~~piiLvgnK~DL~~~~~~~~~~~~~~~~~v~~~eg~~~a~~~~~~~y~E~S 156 (175) T cd01870 81 ----SIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANKIGAFGYMECS 156 (175) T ss_pred ----ECCCHHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCCCCHHHHHHHHHHCCCCCCHHHHHHHHHHCCCCEEEEEE T ss_conf ----6686557899999889999972589529998515443343146776654104677989999999973997289874 Q ss_pred CCCHHHHHHHHHHHHHHHH Q ss_conf 6531355566778888753 Q Fun_Sc_NP_0140 188 DHTEEKREEAQRLKYQELL 206 (312) Q Consensus 188 ts~~~~kn~~~~l~y~~L~ 206 (312) ....+.-+++--.+.+.++ T Consensus 157 Aktg~nV~e~Fe~~~k~~l 175 (175) T cd01870 157 AKTKEGVREVFEMATRAAL 175 (175) T ss_pred CCCCCCHHHHHHHHHHHHC T ss_conf 1488887899999999839 No 79 >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=95.81 E-value=0.59 Score=24.47 Aligned_columns=151 Identities=11% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|.++.|||+++.++-. +-.+.+.++.|..+..+.+ ++.++.+|-..|.--...-.=.++-.++. +| T Consensus 2 IvivG~~~vGKTsl~~~~~~~~f~~~~~~Tig~~~~~i~~-----~~~~l~iwDtaGqe~~~~~~~~y~~~a~~----ii 72 (159) T cd04159 2 ITLVGLQNSGKTTLVNVIAGGQFSEDTIPTVGFNMRKVTK-----GNVTLKVWDLGGQPRFRSMWERYCRGVNA----IV 72 (159) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCEEEEEEEEEEEEEE-----CCEEEEEEECCCCHHHHHHHHHHHHCCCC----EE T ss_conf 7899428986899999875494165323000027999884-----77899998558731357889876310485----17 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCC--CCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEE Q ss_conf 9851666344689999999999864068--99873899847734566553245411578899999999999882941588 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLN--DDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFY 184 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~--~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiY 184 (312) +..|=| -..=+...++|+..+-... ..-++++++-|+|--.....+. +.+.+..-+++...--|| T Consensus 73 ~V~D~t---d~~s~~~~~~~l~~ll~~~~~~~ipili~gNK~Dl~~~~~~~e----------~~~~~~~~~~~~~~~~~~ 139 (159) T cd04159 73 YVVDAA---DRTALEAAKNELHDLLEKPSLEGIPLLVLGNKNDLPGALSVDE----------LIEQMNLKSITDREVSCY 139 (159) T ss_pred EEEECC---CHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCCCCCCCCHHH----------HHHHHHHHHHHCCCCEEE T ss_conf 998548---8667899999999875103779957999812468421258889----------999998999851894589 Q ss_pred ECCCCCHHHHHHHHHHHH Q ss_conf 525653135556677888 Q Fun_Sc_NP_0140 185 ICEDHTEEKREEAQRLKY 202 (312) Q Consensus 185 ts~ts~~~~kn~~~~l~y 202 (312) - +|+++..|....+.+ T Consensus 140 ~--~SAktg~gI~e~f~w 155 (159) T cd04159 140 S--ISCKEKTNIDIVLDW 155 (159) T ss_pred E--EECCCCCCHHHHHHH T ss_conf 9--861479888999999 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=95.79 E-value=0.11 Score=28.86 Aligned_columns=110 Identities=11% Q ss_pred EEEEECCCCHHHHHHHHHH----CC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC- Q ss_conf 3899759833179999985----14-77865566557502563356212133268899860785435887887718778- Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINIC----FP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS- 100 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l----~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s- 100 (312) +++++|.++.|||+|++++ .. ++.....-.+.+|+-+..+.- ++.++.+|-..|...-- ++-..-- T Consensus 1 ~IvliG~~~~GKTsll~rl~~~~~~~~~~~~~~~~~T~g~~~~~i~~---~~~~l~iwD~~Gqe~~~-----~~~~~y~~ 72 (167) T cd04160 1 SVLILGLDNAGKTTFLEQLKTLFSKYKGLPPSKITPTVGLNIGTIEV---GNARLKFWDLGGQESLR-----SLWDKYYA 72 (167) T ss_pred CEEEEECCCCCHHHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEEE---CCEEEEEEECCCCHHHH-----HHHHHHCC T ss_conf 97899518986899999985202445675444033355458988888---78899998468740467-----76764157 Q ss_pred CCCEEEEEECCCCCCHHHHHHHHHHHHHHH--HCCCCCCCEEEEEECCC Q ss_conf 782799985166634468999999999986--40689987389984773 Q Fun_Sc_NP_0140 101 SKVRWLILLDWTLNDQKLWLNELSYAFNKI--KQLNDDNEFSVWCLNSG 147 (312) Q Consensus 101 ~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L--~~l~~Dt~i~VVc~~sD 147 (312) .-.-+|+.+|=+ |+.. +.+.+.|+..+ .+...+.+++|++-|+| T Consensus 73 ~a~~ii~VvD~s--d~~~-~~~~~~~l~~~l~~~~~~~~Pili~~NK~D 118 (167) T cd04160 73 ECHAIIYVIDST--DRER-FEESKSALEKVLRNEALEGVPLLILANKQD 118 (167) T ss_pred CCCEEEEEEECC--CCCC-HHHHHHHHHHHHHCCCCCCCEEEEEECCCC T ss_conf 986799997448--7535-688999999997221558977999834879 No 81 >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=95.75 E-value=0.17 Score=27.76 Aligned_columns=108 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|.+++|||+++.++-.....++.++.|.+...+.+. +.++.+|-+.|..--..---.++-+.+. +|+ T Consensus 2 IliiGl~~aGKTtil~~l~~~~~~~~~pTvG~~~~~i~~~-----~~~l~iwD~gG~~~~r~~w~~Yy~~~~g----iIf 72 (169) T cd04158 2 VVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEYK-----NLKFTIWDVGGKHKLRPLWKHYYLNTQA----VVF 72 (169) T ss_pred EEEEEECCCCHHHHHHHHHCCCCCCEEEEECEEEEEEEEC-----CEEEEEEECCCCCHHHHHHHHHHCCCCE----EEE T ss_conf 8899627986899888885583143121012068888745-----7499998738874025778875047668----999 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCC--CCCEEEEEECCC Q ss_conf 8516663446899999999998640689--987389984773 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLND--DNEFSVWCLNSG 147 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~--Dt~i~VVc~~sD 147 (312) .+|=| |... +...++++..+-+-.. +.+++|++-|.| T Consensus 73 VvDss--d~~~-~~e~~~~l~~ll~~~~~~~~piLi~aNK~D 111 (169) T cd04158 73 VVDSS--HRDR-VSEAHSELAKLLTEKELRDALLLIFANKQD 111 (169) T ss_pred EEECC--CHHH-HHHHHHHHHHHHCCCCCCCCEEEEEECCCC T ss_conf 99655--6335-899999999984451016956999851558 No 82 >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=95.73 E-value=0.25 Score=26.72 Aligned_columns=113 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+.+-|||+++.+. -+..++.+..+--.......-. -|+..+.+-+.+...-+--.-+.++--..+. ++ T Consensus 4 ivliGd~~VGKTsL~~r~--~~~~F~~~~~pTi~~~~~~~i~-v~~~~v~l~iwDTaGqe~~~~l~~~~~~~a~----~~ 76 (187) T cd04129 4 LVIVGDGACGKTSLLSVF--TLGEFPEEYHPTVFENYVTDCR-VDGKPVQLALWDTAGQEEYERLRPLSYSKAH----VI 76 (187) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCCCCCCEEEEEEEEEE-ECCEEEEEEEEECCCCCHHHHHHHHHHCCCC----EE T ss_conf 899825984389999998--6173277636603665677446-7786899988655765215789998706997----89 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCC Q ss_conf 8516663446899999999998640689987389984773 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSG 147 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD 147 (312) ++=.+..++.++-+.-..|+..+++...+.++++|-.|+| T Consensus 77 ilvydi~~~~Sf~~i~~~w~~~~~~~~~~~piiLvGnK~D 116 (187) T cd04129 77 LIGFAVDTPDSLENVRTKWIEEVRRYCPNVPVILVGLKKD 116 (187) T ss_pred EEEEECCCHHHHHHHHHHHHHHHHHHCCCCEEEEEECCCC T ss_conf 9996338856788888988999998368944999835887 No 83 >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=95.71 E-value=0.26 Score=26.65 Aligned_columns=113 Identities=8% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+.+-|||.++... -...++.+-.+--+-.+...-+ -|+.++.+-+-+...-+.-+-|.|+--+++ .-++| T Consensus 4 iVvvGD~~VGKTsLl~~f--~~~~F~~~y~PTV~~~~~~~i~-vd~~~V~L~lWDTAGQE~y~~lr~~yYr~a--d~~ll 78 (222) T cd04173 4 IVVVGDAECGKTALLQVF--AKDAYPGSYVPTVFENYTASFE-IDKRRIELNMWDTSGSSYYDNVRPLAYPDS--DAVLI 78 (222) T ss_pred EEEEECCCCCHHHHHHHH--HCCCCCCCCCCEEEEEEEEEEE-ECCEEEEEEEEECCCCHHHHHHHHHHHCCC--CEEEE T ss_conf 999716983378888876--4371067524415765799999-988699999873488701234447763389--87999 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCC Q ss_conf 8516663446899999999998640689987389984773 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSG 147 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD 147 (312) .-|-+. |.++-+....|..-++...++.+|++|-+|+| T Consensus 79 vFdIt~--~~SF~nv~~kW~~ei~~~~p~~pIILVGnK~D 116 (222) T cd04173 79 CFDISR--PETLDSVLKKWQGETQEFCPNAKVVLVGCKLD 116 (222) T ss_pred EEECCC--HHHHHHHHHHHHHHHHHHCCCCCEEEECCCCC T ss_conf 986588--54789999988899997079984899803667 No 84 >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=95.69 E-value=0.54 Score=24.68 Aligned_columns=158 Identities=13% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEEE Q ss_conf 8997598331799999851477865566557502563356212133268899860785435887887718778-782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~V 106 (312) ++++|.++-|||.|+.+.....-.+.....|..|... +...+++-+.+...-+.- ..|.+.- .+.-.+ T Consensus 3 ivliGd~~VGKTsLi~r~~~~~F~~~~~Tig~~~~~k-------~~~~~~l~IWDTAGqE~f----~~l~~~yyr~a~~~ 71 (220) T cd04126 3 VVLLGDMNVGKTSLLHRYMERRFKDTVSTVGGAFYLK-------QWGPYNISIWDTAGREQF----HGLGSMYCRGAAAV 71 (220) T ss_pred EEEEECCCCCHHHHHHHHHCCEECCCCCCEEEEEEEE-------EEEEEEEEEEECCCCHHH----HHHHHHHCCCCCEE T ss_conf 8998079832899988876371057546223568887-------224799999754762354----56778650589789 Q ss_pred EEE-CCCCCCHHHHHHHHHHHHHHHH-CCCCCCCEEEEEECCCHHHH---------------HHHCCCCCCHHHHHHHHH Q ss_conf 985-1666344689999999999864-06899873899847734566---------------553245411578899999 Q Fun_Sc_NP_0140 107 ILL-DWTLNDQKLWLNELSYAFNKIK-QLNDDNEFSVWCLNSGEILN---------------LQRHTTVWQSVHIDFILQ 169 (312) Q Consensus 107 iLL-DWs~~Dp~~Wlr~Lr~~~~~L~-~l~~Dt~i~VVc~~sD~i~~---------------LEKe~~~w~de~fDfIqQ 169 (312) ||+ |=+. +.++ ..+..|+..++ ..+.+..+++|-.|+|-.+. .|.++-...++.-.|..+ T Consensus 72 ilVyDit~--~~SF-~~i~~~~~~~~~~~~~~~~iilvGNK~DL~~~~~~~~~~~~~~~~~~~e~~r~V~~ee~~~~a~~ 148 (220) T cd04126 72 ILTYDVSN--VQSL-EELEDRFLGLTDTANEDCLFAVVGNKLDLTEEGALAGQEKDAGDRVSPEDQRQVTLEDAKAFYKR 148 (220) T ss_pred EEEEECCC--HHHH-HHHHHHHHHHHHHCCCCCEEEEEECCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHH T ss_conf 99976699--7788-99999999999834999589997146342222211222211111123100045678999999998 Q ss_pred HHHHHHHHCCCE------EEEECCCCCHHHHHHHHHHHH Q ss_conf 999999882941------588525653135556677888 Q Fun_Sc_NP_0140 170 TLRSFCYFNDSS------LFYICEDHTEEKREEAQRLKY 202 (312) Q Consensus 170 ~LRtvcL~yGAS------LiYts~ts~~~~kn~~~~l~y 202 (312) .-....+..+++ -|.| |+++..|-..++.+ T Consensus 149 ~~~~~~~~~~~~~~~~~~y~Et---SAKtg~nV~e~F~~ 184 (220) T cd04126 149 INKYKMLDEDLSPAAEKMCFET---SAKTGYNVDELFEY 184 (220) T ss_pred HHHHCCCCCCCHHCCCCCEEEE---ECCCCCCHHHHHHH T ss_conf 5221000000001037536897---51578788899999 No 85 >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=95.59 E-value=1.2 Score=22.61 Aligned_columns=160 Identities=13% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+++-|||+++.+... .=.+.+....+-.| ...+.-+ .....+.+|=-.|- ..+..+.+.++. .-.-++ T Consensus 4 iiliGd~~VGKTsli~r~~~~~F~~~~~~Ti~~~~-~k~i~v~-~~~~~l~iwDtaG~-e~~~~l~~~~~~---~a~~~i 77 (168) T cd04177 4 IVVLGAGGVGKSALTVQFVQNVFIESYDPTIEDSY-RKQVEID-GRQCDLEILDTAGT-EQFTAMRELYIK---SGQGFL 77 (168) T ss_pred EEEECCCCCCHHHHHHHHHCCEECCCCCCCCCCCE-EEEEEEC-CEEEEEEEEECCCC-CHHHHHHHHHCC---CCCEEE T ss_conf 89980799548999998871800676454101103-5789898-96999998727987-124568787535---998589 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEEEEEC Q ss_conf 98516663446899999999998640689987389984773456655324541157889999999999988294158852 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSLFYIC 186 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASLiYts 186 (312) +.-|-+..+.--.+...+..+...+ .+...++++|..|+| |+.++..-.++...+-+++ |..-+|-+ T Consensus 78 lvydit~~~Sf~~l~~~~~~i~~~~-~~~~~piilvGNK~D----L~~~r~v~~~e~~~~a~~~--------~~~~~~E~ 144 (168) T cd04177 78 LVYSVTSEASLNELGELREQVLRIK-DSDNVPMVLVGNKAD----LEDDRQVSREDGVSLSQQW--------GNVPFYET 144 (168) T ss_pred EEEECCCHHHHHHHHHHHHHHHHHC-CCCCCEEEEECCCCC----CCCCCCCCHHHHHHHHHHH--------CCCCEEEE T ss_conf 9985699789999999999998631-899958999802478----4335768989999999981--------69835888 Q ss_pred CCCCHHHHHHHHHHHHHHHH Q ss_conf 56531355566778888753 Q Fun_Sc_NP_0140 187 EDHTEEKREEAQRLKYQELL 206 (312) Q Consensus 187 ~ts~~~~kn~~~~l~y~~L~ 206 (312) ......+-++.-....+..+ T Consensus 145 SAk~g~nV~e~F~~l~~~il 164 (168) T cd04177 145 SARKRTNVDEVFIDLVRQII 164 (168) T ss_pred EECCCCCHHHHHHHHHHHHH T ss_conf 60489887899999999999 No 86 >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=95.52 E-value=0.24 Score=26.82 Aligned_columns=111 Identities=10% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 38997598331799999851477865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) |++++|.++.|||+++.++-........-.+-+||-+-.+... +..+.+|-+.|..--. ++-+.....-. -+| T Consensus 1 ~ivilGl~~aGKTtil~~l~~~~~~~~~~~pTig~~~~~~~~~---~~~~~iwD~~G~~~~r-~l~~~y~~~a~---~iI 73 (162) T cd04157 1 NILVVGLDNSGKTTIINQLKPENAQSQIIVPTVGFNVESFEKG---NLSFTAFDMSGQGKYR-GLWEHYYKNIQ---GII 73 (162) T ss_pred CEEEEEECCCCHHHHHHHHHCCCCCCCEEEEEEEEEEEEEEEC---CEEEEEEEECCCCCHH-HHHHHHCCCCC---EEE T ss_conf 9788950898688888766157730114765552026888608---6899998706872014-67787515655---899 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHC----CCCCCCEEEEEECCC Q ss_conf 98516663446899999999998640----689987389984773 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQ----LNDDNEFSVWCLNSG 147 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~----l~~Dt~i~VVc~~sD 147 (312) +.+|=| |+.. +...++|+..+.+ .+.+.+++|++-|.| T Consensus 74 ~VvDss--d~~~-~~~~~~~l~~ll~~~~~~~~~~PiLI~~NK~D 115 (162) T cd04157 74 FVIDSS--DRLR-LVVVKDELELLLNHPDIKHRRVPILFFANKMD 115 (162) T ss_pred EEEECC--CHHH-HHHHHHHHHHHHCCCCCCCCCCEEEEEECCCC T ss_conf 998568--8446-89999999998503232689826999972679 No 87 >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=95.30 E-value=0.37 Score=25.67 Aligned_columns=113 Identities=10% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEE Q ss_conf 89975983317999998514778655665575025633562121332688998607854358878877187787827999 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLI 107 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~Vi 107 (312) ++++|+.+-|||+|+.+...+.-..--...+.+.+...+.-+ ....++.+|=-.|- ..+..+.+.+... -.-+++ T Consensus 3 ivliGd~~VGKTsLi~r~~~~~F~~~~~~T~~~~~~~~i~i~-~~~i~l~iwDtaGq-e~~~~l~~~~~~~---a~~~il 77 (173) T cd04130 3 CVLVGDGAVGKTSLIVSYTTNGYPTEYVPTAFDNFSVVVLVD-GKPVRLQLCDTAGQ-DEFDKLRPLCYPD---TDVFLL 77 (173) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCCC-HHHHHHHHHHCCC---CCEEEE T ss_conf 899807984389998887618527653311455434777568-86799998408987-1256787864479---774899 Q ss_pred EECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCC Q ss_conf 8516663446899999999998640689987389984773 Q Fun_Sc_NP_0140 108 LLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSG 147 (312) Q Consensus 108 LLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD 147 (312) .-|-+. +...-+.-..|+..++....+.++++|-.|+| T Consensus 78 vydit~--~~Sf~~i~~~w~~~i~~~~~~~piilVGnK~D 115 (173) T cd04130 78 CFSVVN--PSSFQNISEKWIPEIRKHNPKAPIILVGTQAD 115 (173) T ss_pred EEECCC--HHHHHHHHHHHHHHHHHHCCCCEEEEECCCCC T ss_conf 954499--76899999988999985089964999717744 No 88 >KOG0458 Elongation factor 1 alpha [Translation, ribosomal structure and biogenesis] Probab=95.26 E-value=0.096 Score=29.23 Aligned_columns=147 Identities=12% Q ss_pred HHCCCCCCCCCCCCEEEEECCCCHHHHHHHHHHCCCCCC-----------CCCCCCCCEEEEECCCCCCCC--------- Q ss_conf 410114655366443899759833179999985147786-----------556655750256335621213--------- Q Fun_Sc_NP_0140 13 QNESTINSTETATITAIIYSPSSKTLHQFINICFPEGSN-----------SILDTTLINYATIGWTNDLKE--------- 72 (312) Q Consensus 13 e~~~~~~~k~~~~k~~lilg~~~~~~~~fi~~l~~~~~e-----------~~~~~~~L~y~y~~v~~d~~d--------- 72 (312) ..+.|+..| +..+.+++|--.+||.+++..+.-+-.+ +.++.-.--+.|.-+=|+-++ T Consensus 167 ~~~~q~~~k--~~l~lvv~GhVdaGKSTLmG~lLydLg~i~~~~m~kl~~es~~~Gk~Sf~yawiLDeT~eERerGvTm~ 244 (603) T KOG0458 167 PIDEQSDPK--DHLNLVVLGHVDAGKSTLMGHLLYDLGEISSRSMHKLERESKNLGKSSFAYAWILDETKEERERGVTMD 244 (603) T ss_pred CCCCCCCCC--CCEEEEEEEEECCCCHHHHHHHHHHHCCCCHHHHHHHHHHHHHCCCCCCEEEEEECCCCCHHHCCEEEE T ss_conf 644357876--627899984214552123345777717887567899999998559621045666403320123051776 Q ss_pred -------CEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEEEEECCCCCCHHHH------HHHHHHHHHHHHCCCCCCCE Q ss_conf -------32688998607854358878877187787827999851666344689------99999999986406899873 Q Fun_Sc_NP_0140 73 -------NYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWLILLDWTLNDQKLW------LNELSYAFNKIKQLNDDNEF 139 (312) Q Consensus 73 -------~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~ViLLDWs~~Dp~~W------lr~Lr~~~~~L~~l~~Dt~i 139 (312) ..|-.+-+++.|. |. ++.+-.++-.+.-.--|+.+|.+ ..-| ..|.|+|-..|++++ =+.+ T Consensus 245 v~~~~fes~~~~~tliDaPG-hk-dFi~nmi~g~sqaD~avLvvd~s---~~~FE~gfd~~gQtrEha~llr~Lg-i~ql 318 (603) T KOG0458 245 VKTTWFESKSKIVTLIDAPG-HK-DFIPNMISGASQADVAVLVVDAS---TGEFESGFDPGGQTREHALLLRSLG-ISQL 318 (603) T ss_pred EEEEEEECCCEEEEEEECCC-CC-CCCHHHHHHHHHCCEEEEEEECC---CCCHHHCCCCCCCHHHHHHHHHHCC-CCEE T ss_conf 68999846800899982687-53-21112442121237489999767---5301113577874469999998719-6158 Q ss_pred EEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHH Q ss_conf 899847734566553245411578899999999999 Q Fun_Sc_NP_0140 140 SVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFC 175 (312) Q Consensus 140 ~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvc 175 (312) .|.+.|.|-| .|+.+.|+-|.+.|-.|+ T Consensus 319 ivaiNKmD~V--------~Wsq~RF~eIk~~l~~fL 346 (603) T KOG0458 319 IVAINKMDLV--------SWSQDRFEEIKNKLSSFL 346 (603) T ss_pred EEEEEECCCC--------CCCHHHHHHHHHHHHHHH T ss_conf 8887501245--------533789999987531231 No 89 >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=95.24 E-value=2.5 Score=20.67 Aligned_columns=162 Identities=15% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+.|||.|+.+... .=.+.+.+..|.+|....+.-+ .....+..|=..| ...+..+.+.+... -.-++ T Consensus 3 ivliGd~~vGKTsli~r~~~~~f~~~y~~Tig~~~~~k~i~~~-~~~~~l~i~Dt~G-~e~~~~l~~~~~~~---a~~~i 77 (172) T cd01862 3 VIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVTVD-DKLVTLQIWDTAG-QERFQSLGVAFYRG---ADCCV 77 (172) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEEEC-CEEEEEEEEECCC-CCCHHHHHHHHHCC---CCEEE T ss_conf 8998179844899999986281066535520015778899998-8799999986689-93003577887238---96799 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHH-----CCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCE Q ss_conf 9851666344689999999999864-----06899873899847734566553245411578899999999999882941 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIK-----QLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSS 181 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~-----~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGAS 181 (312) +.-|-+. +..+-+. ..|...+. ......++++|..|+| |+.++ .-..++ .+.+|-.+|.. T Consensus 78 lvydit~--~~Sf~~i-~~w~~e~~~~~~~~~~~~iP~ilVGnK~D----l~~~r-~v~~~e-------~~~~a~~~~~~ 142 (172) T cd01862 78 LVYDVTN--PKSFESL-DSWRDEFLIQASPSDPENFPFVVLGNKID----LEEKR-QVSTKK-------AQQWCQSNGNI 142 (172) T ss_pred EEEECCC--HHHHHHH-HHHHHHHHHHCCCCCCCCCEEEEECCCCC----HHHHC-CCCHHH-------HHHHHHHHCCC T ss_conf 9985698--5578999-99999999863877788607999714100----01211-531789-------99999970796 Q ss_pred EEEECCCCCHHHHHHHHHHHHHHHHHHC Q ss_conf 5885256531355566778888753001 Q Fun_Sc_NP_0140 182 LFYICEDHTEEKREEAQRLKYQELLKHF 209 (312) Q Consensus 182 LiYts~ts~~~~kn~~~~l~y~~L~~h~ 209 (312) -+|-|.+...++-+..-.-..+.++-+. T Consensus 143 ~~~e~SAk~~~nV~e~F~~l~~~~~~q~ 170 (172) T cd01862 143 PYFETSAKEAINVEQAFETIARKALEQE 170 (172) T ss_pred EEEEEEECCCCCHHHHHHHHHHHHHHHH T ss_conf 0799860489787899999999999851 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=95.06 E-value=0.26 Score=26.63 Aligned_columns=109 Identities=11% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEE Q ss_conf 38997598331799999851477865566557502563356212133268899860785435887887718778-78279 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRW 105 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~ 105 (312) .++++|.++.|||+++.++.........++.|.++-.+.. .+.++.+|-+.|.---. ++...-- .-.-+ T Consensus 11 kililGl~~sGKTtil~~l~~~~~~~~~pTvg~~~~~~~~-----~~~~l~iwD~~Gqe~~r-----~lw~~Yy~~a~~i 80 (168) T cd04149 11 RILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTY-----KNVKFNVWDVGGQDKIR-----PLWRHYYTGTQGL 80 (168) T ss_pred EEEEEEECCCCHHHHHHHHHCCCCCEEEEEEEEEEEEEEE-----CCEEEEEEECCCCHHHH-----HHHHHHCCCCCEE T ss_conf 8999850898788988776438610243001247889874-----47289998728713567-----7658650688779 Q ss_pred EEEECCCCCCHHHHHHHHHHHHHHHHCCCC-CCCEEEEEECCC Q ss_conf 998516663446899999999998640689-987389984773 Q Fun_Sc_NP_0140 106 LILLDWTLNDQKLWLNELSYAFNKIKQLND-DNEFSVWCLNSG 147 (312) Q Consensus 106 ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~-Dt~i~VVc~~sD 147 (312) |+.+|=| |+...-.--.++-..|..-.. +.+++|++-|.| T Consensus 81 ifVvD~s--d~~~l~~~~~~l~~~l~~~~~~~~pili~~NK~D 121 (168) T cd04149 81 IFVVDSA--DRDRIDEARQELHRIINDREMRDALLLVFANKQD 121 (168) T ss_pred EEEEECC--CCCCHHHHHHHHHHHHCCCCCCCCEEEEEEECCC T ss_conf 9998257--7322788999999985131327978999961568 No 91 >COG1084 Predicted GTPase [General function prediction only] Probab=95.06 E-value=0.11 Score=28.88 Aligned_columns=133 Identities=11% Q ss_pred CCCCCCCCCCCEEEEECCCCHHHHHHHHHHCCCCCC-----CCCCCCCCEEEEECCCCCCCCCE-EEEEEEEECCCHHHH Q ss_conf 114655366443899759833179999985147786-----55665575025633562121332-688998607854358 Q Fun_Sc_NP_0140 16 STINSTETATITAIIYSPSSKTLHQFINICFPEGSN-----SILDTTLINYATIGWTNDLKENY-SVDVYTLIRNTDDAL 89 (312) Q Consensus 16 ~~~~~k~~~~k~~lilg~~~~~~~~fi~~l~~~~~e-----~~~~~~~L~y~y~~v~~d~~d~~-R~~vy~L~~~~~~~~ 89 (312) ..+.+-.|-..|++|||.---||.+|+++++.--.| +.+|+..+||+-.++-.=|-=|. - +|+.|..+-- T Consensus 159 ~~LP~Idp~~pTivVaG~PNVGKSSlv~~iT~AkpEvA~YPFTTK~i~vGhfe~~~~R~QvIDTPG----lLDRPl~ErN 234 (346) T COG1084 159 KKLPAIDPDLPTIVVAGYPNVGKSSLVRKLTTAKPEVAPYPFTTKGIHVGHFERGYLRIQVIDTPG----LLDRPLEERN 234 (346) T ss_pred HHCCCCCCCCCEEEEECCCCCCHHHHHHHHHCCCCCCCCCCCCCCCEEEEEEECCCCEEEEEECCC----CCCCCHHHHC T ss_conf 547842488776888648986478998765168761147875214046756771872489872687----6468976606 Q ss_pred HHHHHHHCCCC-CCCEEEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHH--HHHHH Q ss_conf 87887718778-7827999851666344689999999999864068998738998477345--66553 Q Fun_Sc_NP_0140 90 DLLKPFLQEHS-SKVRWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEI--LNLQR 154 (312) Q Consensus 90 ~LLkp~L~~~s-~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i--~~LEK 154 (312) +-=+-+..+-. -.-.++++.|-|. +-.+=+..=-..+...+.+-. -+++||+.|.|-+ +.+++ T Consensus 235 ~IE~qAi~AL~hl~~~IlF~~D~Se-~cgy~lE~Q~~L~~eIk~~f~-~p~v~V~nK~D~~~~e~~~~ 300 (346) T COG1084 235 EIERQAILALRHLAGVILFLFDPSE-TCGYSLEEQISLLEEIKELFK-APIVVVINKIDIADEEKLEE 300 (346) T ss_pred HHHHHHHHHHHHHCCEEEEEECCCC-CCCCCHHHHHHHHHHHHHHHC-CCEEEEECCCCCCCHHHHHH T ss_conf 5999999999872686898973873-315898999999998876415-85688744314443201799 No 92 >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=95.05 E-value=1.5 Score=21.99 Aligned_columns=156 Identities=6% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 89975983317999998514-77865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) ++++|+.+-|||.++.+... .=.+.+.+..+-.|.-..+ -++..+.+-+.+....+--..+.+..-..+.-..+| T Consensus 2 ivliGd~gVGKTsLi~rf~~~~F~~~y~pTi~~~~~~~~~----i~~~~~~l~iwDTaGqe~~~~l~~~~~r~a~~~ilV 77 (190) T cd04144 2 LVVLGDGGVGKTALTIQLCLNHFVETYDPTIEDSYRKQVV----VDGQPCMLEVLDTAGQEEYTALRDQWIREGEGFILV 77 (190) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCCCCCCCEEEEEEEEE----ECCEEEEEEEEECCCCCHHHHHHHHHHCCCCEEEEE T ss_conf 7888179842899999987081077646640111478898----715479999974798602468878753056078999 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHH----CCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCEE Q ss_conf 9851666344689999999999864----068998738998477345665532454115788999999999998829415 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIK----QLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSSL 182 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~----~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGASL 182 (312) + +..|+...-+ +..|+..+. ....+.++++|..|+|-...-+=.. +--+.++-++|+.. T Consensus 78 y----ditd~~SF~~-i~~w~~~i~~~~~~~~~~~piilVGNK~DL~~~r~V~~------------ee~~~~a~~~~~~y 140 (190) T cd04144 78 Y----SITSRSTFER-VERFREQIQRVKDESAADVPIMIVGNKCDKVYEREVST------------EEGAALARRLGCEF 140 (190) T ss_pred E----ECCCHHHHHH-HHHHHHHHHHHHHHCCCCCEEEEEECCCCCCCCCCCCH------------HHHHHHHHHCCCCE T ss_conf 8----7599778999-99999999987420699978999705653334466798------------99999999669919 Q ss_pred EEECCCCCHHHHHHHHHHHHHHHHHHCC Q ss_conf 8852565313555667788887530012 Q Fun_Sc_NP_0140 183 FYICEDHTEEKREEAQRLKYQELLKHFC 210 (312) Q Consensus 183 iYts~ts~~~~kn~~~~l~y~~L~~h~l 210 (312) |.| |++...|-..++.. ++..+ T Consensus 141 ~E~---SAk~~~nV~e~F~~---l~~~i 162 (190) T cd04144 141 IEA---SAKTNVNVERAFYT---LVRAL 162 (190) T ss_pred EEE---ECCCCCCHHHHHHH---HHHHH T ss_conf 998---61589887899999---99999 No 93 >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=94.99 E-value=1.1 Score=22.75 Aligned_columns=163 Identities=10% Q ss_pred CCEEEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCC Q ss_conf 44389975983317999998514-77865566557502563356212133268899860785435887887718778782 Q Fun_Sc_NP_0140 25 TITAIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKV 103 (312) Q Consensus 25 ~k~~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~ 103 (312) +.-++++|+.+-|||.++.+... .-.+.+.+..+-.|.....-++ +..++.+|=-.|- +.+..+-+.....-.- T Consensus 1 tiKvvlvGd~~VGKTsli~r~~~~~F~~~~~~Ti~~~~~~~i~i~~--~~~~l~iwDTaGq-e~~~~l~~~~~r~a~~-- 75 (175) T cd01874 1 TIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGG--EPYTLGLFDTAGQ-EDYDRLRPLSYPQTDV-- 75 (175) T ss_pred CEEEEEECCCCCCHHHHHHHHHCCCCCCCCCCEEEEEEEEEEEECC--EEEEEEEEECCCC-CHHHHHHHHHCCCCCE-- T ss_conf 9789998179832789888865282266524235301679999989--5899998636776-0245666865059987-- Q ss_pred EEEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCH---HHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCC Q ss_conf 799985166634468999999999986406899873899847734---56655324541157889999999999988294 Q Fun_Sc_NP_0140 104 RWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGE---ILNLQRHTTVWQSVHIDFILQTLRSFCYFNDS 180 (312) Q Consensus 104 l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~---i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGA 180 (312) +++.-|-+ |+...-+....|+..+++..++.++++|-.|+|- ...+|+-- ...+=-.-..--+.++-++|+ T Consensus 76 -~iivydit--~~~SF~~i~~~w~~~~~~~~~~~p~ilVGnK~DL~~~~~~~~~~~---~~~~r~Vs~eeg~~~A~~~~~ 149 (175) T cd01874 76 -FLVCFSVV--SPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLRDDPSTIEKLA---KNKQKPITPETGEKLARDLKA 149 (175) T ss_pred -EEEEEECC--CHHHHHHHHHHHHHHHHHHCCCCEEEEEECCCCCCCCHHHHHHHH---HCCCCCCCHHHHHHHHHHCCC T ss_conf -99997578--642489999988999997258964999716756434157888765---213677688999999997289 Q ss_pred EEEEECCCCCHHHHHHHHHH Q ss_conf 15885256531355566778 Q Fun_Sc_NP_0140 181 SLFYICEDHTEEKREEAQRL 200 (312) Q Consensus 181 SLiYts~ts~~~~kn~~~~l 200 (312) -.++- +|+++..|-..++ T Consensus 150 ~~y~E--tSAktg~~V~e~F 167 (175) T cd01874 150 VKYVE--CSALTQKGLKNVF 167 (175) T ss_pred CEEEE--EECCCCCCHHHHH T ss_conf 50798--7514676678999 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=94.97 E-value=0.43 Score=25.26 Aligned_columns=129 Identities=7% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCCCCEEE Q ss_conf 38997598331799999851477865566557502563356212133268899860785435887887718778782799 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSSKVRWL 106 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~~~l~V 106 (312) .++++|.++.|||+++.++ .+.+...-.+-.|+....+... +.++.+|-+.| -..+-++.+.....- .-+| T Consensus 16 kiliiG~~~~GKTsll~~l--~~~~~~~~~pT~g~~~~~i~~~---~~~l~~wD~~G-~~~~r~~~~~y~~~a---~~iI 86 (173) T cd04155 16 RILILGLDNAGKTTILKQL--ASEDISHITPTQGFNIKTVQSD---GFKLNVWDIGG-QRAIRPYWRNYFENT---DCLI 86 (173) T ss_pred EEEEEEECCCCHHHHHHHH--HCCCCCEEEEEEEEEEEEEEEC---CEEEEEEECCC-HHHHHHHHHHHCCCC---CEEE T ss_conf 6999840898689988888--4695221441123588998718---88999986687-256799999860667---4689 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHH--HCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHH Q ss_conf 985166634468999999999986--40689987389984773456655324541157889999 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKI--KQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFIL 168 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L--~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIq 168 (312) +.+|=+ -..=+++.+.++..+ .......+++|++-|+|.-.....+.. -....++.++ T Consensus 87 ~VvD~s---d~~~~~~~~~~l~~~L~~~~~~~~PiLi~~NK~Dl~~~~~~~ei-~~~l~l~~~~ 146 (173) T cd04155 87 YVIDSA---DKKRLEEAGAELVELLEEEKLAGVPVLVFANKQDLATAAPAEEI-AEALNLHDLR 146 (173) T ss_pred EEEECC---CHHHHHHHHHHHHHHHHHHCCCCCEEEEEEECCCCCCCCCHHHH-HHHHHHHHHC T ss_conf 998657---84458999999999873003389479999705785436898999-9997578642 No 95 >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=94.94 E-value=2.6 Score=20.51 Aligned_columns=169 Identities=12% Q ss_pred EEEECCCCHHHHHHHHHHCC-CCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEE---------CCCHHHHHHHHHHHC Q ss_conf 89975983317999998514-77865566557502563356212133268899860---------785435887887718 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFP-EGSNSILDTTLINYATIGWTNDLKENYSVDVYTLI---------RNTDDALDLLKPFLQ 97 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~-~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~---------~~~~~~~~LLkp~L~ 97 (312) ++++|+.+-||+.++.+... +=.+.+.+..|-+++...+.-| +..+.+-+.+ ....++.+.---.+ T Consensus 3 VvilGd~gVGKTsli~Rf~~~~F~~~y~pTig~~~~~k~i~vd---g~~~~L~IwDt~~~~~~~~tagqE~~~~r~r~l- 78 (198) T cd04142 3 VAVLGAPGVGKTAIVRQFLAQEFPEEYIPTEHRRLYRPAVVLS---GRVYDLHILDVPNMQRYPGTAGQEWMDPRFRGL- 78 (198) T ss_pred EEEECCCCCCHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEEC---CEEEEEEEEECCCCCCCCCCCCHHHHHHHHHHC- T ss_conf 8998189841899998876174377635642101468789898---979999984144311145655301111222101- Q ss_pred CCCCCCEEEEEECCCCCCHHHHHHHHHHHHHHHHC-CCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHH Q ss_conf 77878279998516663446899999999998640-68998738998477345665532454115788999999999998 Q Fun_Sc_NP_0140 98 EHSSKVRWLILLDWTLNDQKLWLNELSYAFNKIKQ-LNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCY 176 (312) Q Consensus 98 ~~s~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~-l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL 176 (312) ..-.-+++.-|=+..+.-.=++.++.++...+. .+.+.+|++|--|+| |++++.. -.+-....+- T Consensus 79 --r~ad~~ilVydIt~~~SF~~v~~~~~~i~~~~~~~~~~~pivLVGNK~D----L~~~R~v--------~~e~~~~~a~ 144 (198) T cd04142 79 --RNSRAFILVYDICSPDSFHYVKLLRQQILETRPAGNKEPPIVVVGNKRD----QQRHRFA--------PRHVLSVLVR 144 (198) T ss_pred --CCCCEEEEEEECCCHHHHHHHHHHHHHHHHHCCCCCCCCEEEEEECCCC----CCCCCCC--------CHHHHHHHHH T ss_conf --2786799998679966889999999999985135899967999824765----2115526--------7899999999 Q ss_pred HCCCEEEEECCCCCHHHHHHHHHHHHHHHHHHCCCCCCC-CCCC Q ss_conf 829415885256531355566778888753001247787-7522 Q Fun_Sc_NP_0140 177 FNDSSLFYICEDHTEEKREEAQRLKYQELLKHFCEDRDM-KDHI 219 (312) Q Consensus 177 ~yGASLiYts~ts~~~~kn~~~~l~y~~L~~h~l~~~~~-~~~a 219 (312) +.++..||- +|+++..|-..++.- ++-....+.. .+|+ T Consensus 145 ~~~~~~f~E--tSAK~~~NV~elF~~---lvr~~~~~~~~~~~~ 183 (198) T cd04142 145 KSWKCGYLE--CSAKYNWHILLLFKE---LLISATTRGRSTHPA 183 (198) T ss_pred HHCCCCEEE--EECCCCCCHHHHHHH---HHHHHHCCCCCCCCC T ss_conf 827973799--861379888899999---999983678886630 No 96 >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=94.83 E-value=0.32 Score=26.07 Aligned_columns=107 Identities=12% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCC-CCCEEE Q ss_conf 8997598331799999851477865566557502563356212133268899860785435887887718778-782799 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHS-SKVRWL 106 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s-~~~l~V 106 (312) ++++|.++.|||+++.++.........++.|.+..++.. .+..+.+|-+.| .+-.+++-..-- .-.-++ T Consensus 3 iv~lG~~~~GKTtii~~~~~~~~~~~~pTvg~~~~~i~~-----~~~~l~iwD~~G-----qe~~r~~w~~y~~~~~~iI 72 (159) T cd04150 3 ILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEY-----KNISFTVWDVGG-----QDKIRPLWRHYFQNTQGLI 72 (159) T ss_pred EEEEEECCCCHHHHHHHHHCCCEEEEECCEEEEEEEEEE-----CCEEEEEEECCC-----CHHHHHHHHHHCCCCCEEE T ss_conf 899940898688877765337600110220015888750-----671899987587-----2356788898627997799 Q ss_pred EEECCCCCCHHHHHHHHHHHHHHHHCCCC--CCCEEEEEECCC Q ss_conf 98516663446899999999998640689--987389984773 Q Fun_Sc_NP_0140 107 ILLDWTLNDQKLWLNELSYAFNKIKQLND--DNEFSVWCLNSG 147 (312) Q Consensus 107 iLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~--Dt~i~VVc~~sD 147 (312) +.+|=| -..=+...+.++..+-+-.. +.++.|+.-|.| T Consensus 73 ~VvD~s---d~~~~~~~~~~l~~~l~~~~~~~~pili~~NK~D 112 (159) T cd04150 73 FVVDSN---DRERIGEAREELQRMLNEDELRDAVLLVFANKQD 112 (159) T ss_pred EEEECC---CHHHHHHHHHHHHHHHCCCCCCCCEEEEEECCCC T ss_conf 998548---8346899999999984230216978999960568 No 97 >KOG1673 Ras GTPases [General function prediction only] Probab=94.39 E-value=0.25 Score=26.70 Aligned_columns=194 Identities=13% Q ss_pred CCCCCCCCCCCCEEE-----EECCCCHHHHHHHHHHCCCCC-CCCCCCCCCEEEEECCCCCCCCCEEEEEEEEECCCHHH Q ss_conf 011465536644389-----975983317999998514778-65566557502563356212133268899860785435 Q Fun_Sc_NP_0140 15 ESTINSTETATITAI-----IYSPSSKTLHQFINICFPEGS-NSILDTTLINYATIGWTNDLKENYSVDVYTLIRNTDDA 88 (312) Q Consensus 15 ~~~~~~k~~~~k~~l-----ilg~~~~~~~~fi~~l~~~~~-e~~~~~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~ 88 (312) +++++..-++-.|.+ ++|+.+-|||+|+.+--++.- +.+.-..|+++.-.-+.-- --+..-|.|-|-|.- .| T Consensus 5 stv~~~~~~a~~n~Vslkv~llGD~qiGKTs~mvkYV~~~~de~~~q~~GvN~mdkt~~i~-~t~IsfSIwdlgG~~-~~ 82 (205) T KOG1673 5 STVANNSIPAVSNLVSLKVGLLGDAQIGKTSLMVKYVQNEYDEEYTQTLGVNFMDKTVSIR-GTDISFSIWDLGGQR-EF 82 (205) T ss_pred CCCCCCCCCCCCCEEEEEEEEEECCCCCCCEEEEEEHHCCCHHHHHHHHCCCEEEEEEEEE-CEEEEEEEEECCCHH-HH T ss_conf 6434567774111478998763066546110122111041045678874220000057861-107999843035303-55 Q ss_pred HHHHHHHHCCCCCCCEEEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHH Q ss_conf 88788771877878279998516663446899999999998640689987389984773456655324541157889999 Q Fun_Sc_NP_0140 89 LDLLKPFLQEHSSKVRWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFIL 168 (312) Q Consensus 89 ~~LLkp~L~~~s~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIq 168 (312) .+.|+-+ -+..+.++|+.|-+ ..-=+.-+-+|.++-|..+.-.--..|-+|-|..-.|-.|. .|. |- T Consensus 83 ~n~lPia---c~dsvaIlFmFDLt---~r~TLnSi~~WY~QAr~~NktAiPilvGTKyD~fi~lp~e~-Q~~------I~ 149 (205) T KOG1673 83 INMLPIA---CKDSVAILFMFDLT---RRSTLNSIKEWYRQARGLNKTAIPILVGTKYDLFIDLPPEL-QET------IS 149 (205) T ss_pred HHCCCEE---ECCCEEEEEEEECC---CHHHHHHHHHHHHHHCCCCCCCCEEEEECCHHHHEECCHHH-HHH------HH T ss_conf 4147612---33728798764157---80246789999998504786434057615524410078136-899------99 Q ss_pred HHHHHHHHHCCCEEEEECCCCCHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCEECCCCEEE Q ss_conf 9999999882941588525653135556677888875300124778775224011563020 Q Fun_Sc_NP_0140 169 QTLRSFCYFNDSSLFYICEDHTEEKREEAQRLKYQELLKHFCEDRDMKDHIEMVTRSEILI 229 (312) Q Consensus 169 Q~LRtvcL~yGASLiYts~ts~~~~kn~~~~l~y~~L~~h~l~~~~~~~~a~vverd~vfI 229 (312) ..-|+++---.|+|||- |++...|-.--+|. ++-+++..|.+.+-+.---|+++. T Consensus 150 ~qar~YAk~mnAsL~F~---Sts~sINv~KIFK~---vlAklFnL~~ti~~~~~iGdPild 204 (205) T KOG1673 150 RQARKYAKVMNASLFFC---STSHSINVQKIFKI---VLAKLFNLPWTIPEILTIGDPILD 204 (205) T ss_pred HHHHHHHHHHCCCEEEE---ECCCCCCHHHHHHH---HHHHHHCCCCCCHHHCCCCCCCCC T ss_conf 99998888744624674---12242229999999---988883572241322025650005 No 98 >cd04171 SelB SelB subfamily. SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryo Probab=94.38 E-value=0.53 Score=24.73 Aligned_columns=152 Identities=9% Q ss_pred EEEECCCCHHHHHHHHHHCCCCCCCCCC------CCCCEEEEECCCCCCCCCEEEEEEEEECCCHHHHHHHHHHHCCCCC Q ss_conf 8997598331799999851477865566------5575025633562121332688998607854358878877187787 Q Fun_Sc_NP_0140 28 AIIYSPSSKTLHQFINICFPEGSNSILD------TTLINYATIGWTNDLKENYSVDVYTLIRNTDDALDLLKPFLQEHSS 101 (312) Q Consensus 28 ~lilg~~~~~~~~fi~~l~~~~~e~~~~------~~~L~y~y~~v~~d~~d~~R~~vy~L~~~~~~~~~LLkp~L~~~s~ 101 (312) +-|.|--..||+++++.|.....+.... +.-++|.+...++. ..+.+...++| .++++-.+..-.. T Consensus 3 Vai~Gh~n~GKSTL~~~Ltg~~~d~~~~e~~~GiTi~~~~~~~~~~~~-------~~i~liDtPGh-~~f~~~~~~~~~~ 74 (164) T cd04171 3 IGTAGHIDHGKTTLIKALTGIETDRLPEEKKRGITIDLGFAYLDLPSG-------KRLGFIDVPGH-EKFIKNMLAGAGG 74 (164) T ss_pred EEEEECCCCCHHHHHHHHHCCCCCCHHHHHHCCCEEEEEEEEEECCCC-------CEEEEEECCCC-HHHHHHHHHHHHH T ss_conf 889831688778999887201101101354267166300268861688-------48999856873-6789999999876 Q ss_pred CCEEEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHCCCE Q ss_conf 82799985166634468999999999986406899873899847734566553245411578899999999999882941 Q Fun_Sc_NP_0140 102 KVRWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQTLRSFCYFNDSS 181 (312) Q Consensus 102 ~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~LRtvcL~yGAS 181 (312) --..++++|=+. -+..|-++++..++.++.. +++||..|.|.+ .++.+.-+.+-++.++-.+|+. T Consensus 75 aD~~llVvda~~----g~~~qt~e~~~~~~~~~~~-~iivvlNKiD~v----------~~~~~~~v~~~i~~~l~~~~~~ 139 (164) T cd04171 75 IDLVLLVVAADE----GIMPQTREHLEILELLGIK-RGLVVLTKADLV----------DEDWLELVEEEIRELLAGTFLA 139 (164) T ss_pred CCEEEEEEECCC----CCCCCHHHHHHHHHHHCCC-CEEEEEEEECCC----------CHHHHHHHHHHHHHHHHHCCCC T ss_conf 586798986378----8772048999999984377-001465651378----------9779999999999997524899 Q ss_pred EEEECCCCCHHHHHHHHHHHH Q ss_conf 588525653135556677888 Q Fun_Sc_NP_0140 182 LFYICEDHTEEKREEAQRLKY 202 (312) Q Consensus 182 LiYts~ts~~~~kn~~~~l~y 202 (312) -.-.-|.|+++-.|-+.++.+ T Consensus 140 ~~~iv~iSA~tG~gI~~L~e~ 160 (164) T cd04171 140 DAPIFPVSAVTGEGIEELKEY 160 (164) T ss_pred CCCEEEECCCCCCCHHHHHHH T ss_conf 845787127789997999999 No 99 >cd01889 SelB_euk SelB subfamily. SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and euk Probab=94.14 E-value=0.5 Score=24.90 Aligned_columns=168 Identities=13% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCC--------CCCCCCCCCE----EEEECCCCCCCCCEEEE----EEEEECCCHHHHH Q ss_conf 389975983317999998514778--------6556655750----25633562121332688----9986078543588 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGS--------NSILDTTLIN----YATIGWTNDLKENYSVD----VYTLIRNTDDALD 90 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~--------e~~~~~~~L~----y~y~~v~~d~~d~~R~~----vy~L~~~~~~~~~ 90 (312) |+-|.|--..||+++.+.+..-.+ ++-..|.-+. +++.......++....+ .+.+...++| .+ T Consensus 2 Ni~iiGHVDhGKTTL~~~L~~~~~~~~~D~~~~E~eRGITi~lg~~~f~~~~~~~~~~~~~~~~~~~~i~~IDtPGH-~d 80 (192) T cd01889 2 NVGVLGHVDSGKTSLAKALSEIASTAAFDKNPQSQERGITLDLGFSSFYVDKPKHLRELINPGEENLQITLVDCPGH-AS 80 (192) T ss_pred EEEEEEEECCCHHHHHHHHHHHHHHHHCCCCHHHHHCCCEEEECCEEEEECCHHHHCCCCCCCCCCEEEEEEECCCH-HH T ss_conf 18899863078779999987543221104534677658402421011341110100001245766427999755666-88 Q ss_pred HHHHHHCCCCCCCEEEEEECCCCCCHHHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHHCCCCCCHHHHHHHHHH Q ss_conf 78877187787827999851666344689999999999864068998738998477345665532454115788999999 Q Fun_Sc_NP_0140 91 LLKPFLQEHSSKVRWLILLDWTLNDQKLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQRHTTVWQSVHIDFILQT 170 (312) Q Consensus 91 LLkp~L~~~s~~~l~ViLLDWs~~Dp~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEKe~~~w~de~fDfIqQ~ 170 (312) +++--+..-+---..++++|=.. .+..|-++++..++.++ .+++||+.|.|.+.. .|.++.|+.|.+. T Consensus 81 F~~~m~~G~~~~D~aiLvV~a~~----Gv~~QT~eh~~~~~~~~--~~~iv~iNKiD~v~~------~~~~~~~~~ik~~ 148 (192) T cd01889 81 LIRTIIGGAQIIDLMLLVVDATK----GIQTQTAECLVIGEILC--KKLIVVLNKIDLIPE------EERERKIEKMKKK 148 (192) T ss_pred HHHHHHHHHHHHCEEEEEEECCC----CCCCCHHHHHHHHHHCC--CCEEEEEEECCCCCC------CHHHHHHHHHHHH T ss_conf 99999999876340688884578----85744689999999728--977999973278994------0457899999999 Q ss_pred HHHHHHHCCCEEEEECCCCCHHHHHHHHHHHHHHHHH Q ss_conf 9999988294158852565313555667788887530 Q Fun_Sc_NP_0140 171 LRSFCYFNDSSLFYICEDHTEEKREEAQRLKYQELLK 207 (312) Q Consensus 171 LRtvcL~yGASLiYts~ts~~~~kn~~~~l~y~~L~~ 207 (312) +..+.-+.|..=.-.-|.|..+-.|-..+...-.-++ T Consensus 149 i~~~l~~~~~~~~~iipiSA~tG~gI~eL~~~~~~~~ 185 (192) T cd01889 149 LQKTLEKTRFKNSPIIPVSAKPGGGEAELGKDLNNLI 185 (192) T ss_pred HHHHHHHCCCCCCCEEECCCCCCCCHHHHHHHHHHHC T ss_conf 9988511378871268703778998799999887534 No 100 >cd01850 CDC_Septin CDC/Septin. Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities. Probab=94.05 E-value=0.57 Score=24.55 Aligned_columns=143 Identities=15% Q ss_pred EEEEECCCCHHHHHHHHHHCCCCCCCCCCCCCCEEEEECCC-------CCCCCCE-EEEEEEEECCCH-HH---HHHHHH Q ss_conf 38997598331799999851477865566557502563356-------2121332-688998607854-35---887887 Q Fun_Sc_NP_0140 27 TAIIYSPSSKTLHQFINICFPEGSNSILDTTLINYATIGWT-------NDLKENY-SVDVYTLIRNTD-DA---LDLLKP 94 (312) Q Consensus 27 ~~lilg~~~~~~~~fi~~l~~~~~e~~~~~~~L~y~y~~v~-------~d~~d~~-R~~vy~L~~~~~-~~---~~LLkp 94 (312) |++|+|+++.||++||+.|+....-+.+.....-..-..-+ .+.+++- |+.+=+.+.|.. +. ..-.+| T Consensus 6 niMVvG~sGlGKsTfiNtLf~~~~~~~~~~~~~~~~~~~~t~~i~~~~~~iee~g~~l~LtviDTpGfGd~inn~~~~~~ 85 (276) T cd01850 6 NIMVVGESGLGKSTFINTLFNTKLIPSDYPPDPAEEHIDKTVEIKSSKAEIEENGVKLKLTVIDTPGFGDNINNSDCWKP 85 (276) T ss_pred EEEEEECCCCCHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCEEEEEEEEEEECCEEEEEEEEECCCCCCCCCCHHHHHH T ss_conf 89998448987899998875354567777777532246887328999999875576999999874776541261357999 Q ss_pred HHC-------------------CCCCCCEEEEEECCCCCCH-HHHHHHHHHHHHHHHCCCCCCCEEEEEECCCHHHHHHH Q ss_conf 718-------------------7787827999851666344-68999999999986406899873899847734566553 Q Fun_Sc_NP_0140 95 FLQ-------------------EHSSKVRWLILLDWTLNDQ-KLWLNELSYAFNKIKQLNDDNEFSVWCLNSGEILNLQR 154 (312) Q Consensus 95 ~L~-------------------~~s~~~l~ViLLDWs~~Dp-~~Wlr~Lr~~~~~L~~l~~Dt~i~VVc~~sD~i~~LEK 154 (312) ... +.-.++|+=..|=... | ...++.|. +..||.++.-..++-|.-|||-++.=|- T Consensus 86 I~~yI~~qf~~yl~eE~~i~R~~~~~D~RVH~cLYFI~--Ptgh~L~~lD--i~~mk~l~~~vNiIPVIaKaDtlT~~El 161 (276) T cd01850 86 IVDYIDDQFDQYLREESRIKRNPRIPDTRVHACLYFIE--PTGHGLKPLD--IEFMKRLSKRVNIIPVIAKADTLTPEEL 161 (276) T ss_pred HHHHHHHHHHHHHHHHHCCCCCCCCCCCEEEEEEEEEC--CCCCCCCHHH--HHHHHHHHCCCCEEEEEECCCCCCHHHH T ss_conf 99999999999999874112368987870479999766--9999888789--9999986132445677603335899999 Q ss_pred CCCCCCHHHHHHHHHHHHHHHHHCCCEEE Q ss_conf 24541157889999999999988294158 Q Fun_Sc_NP_0140 155 HTTVWQSVHIDFILQTLRSFCYFNDSSLF 183 (312) Q Consensus 155 e~~~w~de~fDfIqQ~LRtvcL~yGASLi 183 (312) .... +-+|.-+-.||..++ T Consensus 162 ~~~K----------~~I~~~l~~~~I~iy 180 (276) T cd01850 162 KEFK----------QRIMEDIEEHNIKIY 180 (276) T ss_pred HHHH----------HHHHHHHHHCCCEEC T ss_conf 9999----------999999998198006 Done!