ID   SRC_AVIS2      STANDARD;      PRT;   587 AA.
AC   P15054;
DT   01-APR-1990 (Rel. 14, Created)
DT   01-APR-1990 (Rel. 14, Last sequence update)
DT   01-NOV-1997 (Rel. 35, Last annotation update)
DE   TYROSINE-PROTEIN KINASE TRANSFORMING PROTEIN SRC (EC 2.7.1.112) (P60-
DE   SRC).
GN   V-SRC.
OS   Avian sarcoma virus (strain PR2257).
OC   Viruses; Retroid viruses; Retroviridae; Avian type C retroviruses.
OX   NCBI_TaxID=11879;
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=89094972; PubMed=2463376;
RA   Geryk J., Dezelee P., Barnier J.V., Svoboda J., Nehyba J., Karakoz I.,
RA   Rynditch A.V., Yatsula B.A., Calothy G.;
RT   "Transduction of the cellular src gene and 3' adjacent sequences in
RT   avian sarcoma virus PR2257.";
RL   J. Virol. 63:481-492(1989).
RN   [2]
RP   SEQUENCE FROM N.A.
RA   Yatsula B.A., Geryk J., Svoboda J., Rynditch A.V., Calothy G.,
RA   Dezelee P.;
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 146-249.
RA   Holland D.R., Lunney E.A., Plummer M.S., Mueller W.T., McConnell P.,
RA   Pavlovsky A., Para K.S., Shahripour A., Humblet C., Sawyer T.K.,
RA   Rubin J.R.;
RL   Submitted (MAY-1997) to the PDB data bank.
CC   -!- FUNCTION: THIS PHOSPHOPROTEIN, REQUIRED FOR BOTH THE INITIATION
CC       AND THE MAINTENANCE OF NEOPLASTIC TRANSFORMATION, IS A PROTEIN
CC       KINASE THAT CATALYZES THE PHOSPHORYLATION OF TYROSINE RESIDUES
CC       IN VITRO.
CC   -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP +
CC       PROTEIN 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.
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DR   EMBL; M21526; AAA42583.1; -.
DR   EMBL; X51863; CAA36156.1; -.
DR   PIR; A30174; TVFVPR.
DR   PDB; 1BKL; 23-JUL-97.
DR   PDB; 1BKM; 07-JUL-97.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
KW   Tyrosine-protein kinase; Transforming protein; Oncogene;
KW   Transferase; Phosphorylation; ATP-binding; Myristate;
KW   SH3 domain; SH2 domain; 3D-structure.
FT   LIPID         2      2       MYRISTATE.
FT   DOMAIN       81    142       SH3.
FT   DOMAIN      148    245       SH2.
FT   DOMAIN      267    520       PROTEIN KINASE.
FT   NP_BIND     273    281       ATP (BY SIMILARITY).
FT   BINDING     295    295       ATP (BY SIMILARITY).
FT   ACT_SITE    386    386       BY SIMILARITY.
FT   MOD_RES     416    416       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
SQ   SEQUENCE   587 AA;  65800 MW;  0A6925315EF251D9 CRC64;
     MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL
     FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL
     AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT
     KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR
     LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
     TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KGEMGKYLRL
     PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ
     GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR
     MPCPPECPES LHDLMCQCWR KDPEERPTFE YLQAFLEDYF TSTEPPVPAW REPIGLELLL
     APEASLWGTG AWLRAEGPRF GEQPQSRMWH GEVSGAPSLI KTVLGHP
//