ID   Q07461      PRELIMINARY;      PRT;   526 AA.
AC   Q07461;
DT   01-NOV-1996 (TrEMBLrel. 01, Created)
DT   01-NOV-1996 (TrEMBLrel. 01, Last sequence update)
DT   01-OCT-2000 (TrEMBLrel. 15, Last annotation update)
DE   TYROSINE-PROTEIN KINASE TRANSFORMING PROTEIN SRC (EC 2.7.1.112) (P60-
DE   SRC).
GN   SRC.
OS   Rous sarcoma virus.
OC   Viruses; Retroid viruses; Retroviridae; Avian type C retroviruses.
OX   NCBI_TaxID=11886;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=PR-RSV-C;
RX   MEDLINE=93254440; PubMed=8387633;
RA   Kashuba V.I., Kavsan V.M., Ryndich A.V., Lazurkevich Z.V., Zubak S.V.,
RA   Popov S.V., Dostalova V., Hlozanek I.;
RT   "Complete nucleotide sequence of Rous sarcoma virus variants adapted
RT   to duck cells.";
RL   Mol. Biol. (Mosk) 27:269-278(1993).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=PR-RSV-C;
RA   Zubak S.V.;
RL   Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=PR-RSV-C;
RA   Kashuba V.I., Serge Z.V., Rynditch A.V., Kavsan V.M., Hlozanek I.;
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + PROTEIN
CC       TYROSINE PHOSPHATE.
CC   -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN.
CC   -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN.
CC   -!- SIMILARITY: TO OTHER PROTEIN-TYROSINE KINASES IN THE CATALYTIC
CC       DOMAIN. BELONGS TO THE SRC SUBFAMILY.
DR   EMBL; X51861; CAA36154.1; -.
DR   EMBL; X68524; CAA48537.1; -.
DR   HSSP; P12931; 1FMK.
DR   INTERPRO; IPR000719; -.
DR   INTERPRO; IPR000980; -.
DR   INTERPRO; IPR001245; -.
DR   INTERPRO; IPR001452; -.
DR   PFAM; PF00017; SH2; 1.
DR   PFAM; PF00018; SH3; 1.
DR   PFAM; PF00069; pkinase; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
KW   Tyrosine-protein kinase; Transforming protein; Oncogene; Transferase;
KW   Phosphorylation; ATP-binding; Myristylation; SH3 domain; SH2 domain.
FT   DOMAIN       81    142       SH3.
FT   DOMAIN      148    245       SH2.
FT   NP_BIND     273    281       ATP (BY SIMILARITY).
FT   ACT_SITE    386    386       BY SIMILARITY.
FT   BINDING     295    295       ATP (BY SIMILARITY).
FT   LIPID         2      2       MYRISTATE (BY SIMILARITY).
FT   MOD_RES     416    416       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
SQ   SEQUENCE   526 AA;  59212 MW;  5BE1DA69E0FFEA82 CRC64;
     MGSSKSKPRD PSQRRHSLEP PDSTHHGGFP ASQTPDETAA PDAHRNPSRS FGTVATEPKL
     FWGFNTSDTV TSPQRAGALA GGVTTFVALY DYESWTETDL SFKKGERLQI VNNTEGYWWL
     AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRKSETA
     KGAYCLSVSD FDNAKGPNVK HYKIYKLYSG GFYITLRTQF GSLQQLVAHY SKHADGLCHR
     LTNVCPTSKP QTQGLAKDAW EIPRESLRLE AKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
     TMSPEAFLQE AQVMKKFRHE KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL
     PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ
     GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR
     MPCPPECPES LHDLMCQCWR KDPEERPTFK YLQAQLLPAC VLEVAE
//