ID   SRC_RSVPA               Reviewed;         523 AA.
AC   P31693;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-NOV-2023, entry version 124.
DE   RecName: Full=Tyrosine-protein kinase transforming protein Src;
DE            EC=2.7.10.2;
DE   AltName: Full=pp60v-src;
DE            Short=p60-Src;
DE            Short=v-Src;
GN   Name=V-SRC;
OS   Rous sarcoma virus (strain PA101T).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus;
OC   Rous sarcoma virus.
OX   NCBI_TaxID=31667;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1322589; DOI=10.1016/0042-6822(92)90579-e;
RA   Dezelee P., Barnier J.V., Hampe A., Laugier D., Marx M., Galibert F.,
RA   Calothy G.;
RT   "Small deletion in v-src SH3 domain of a transformation defective mutant of
RT   Rous sarcoma virus restores wild type transforming properties.";
RL   Virology 189:556-567(1992).
CC   -!- FUNCTION: This phosphoprotein, required for both the initiation and the
CC       maintenance of neoplastic transformation, is a protein kinase that
CC       catalyzes the phosphorylation of tyrosine residues in vitro.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- PTM: The phosphorylated form is termed pp60v-src.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; M84475; AAA42581.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A42994; TVFVMT.
DR   SMR; P31693; -.
DR   BRENDA; 2.7.10.2; 5464.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd10365; SH2_Src_Src; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24418:SF53; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC; 1.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Lipoprotein; Myristate; Nucleotide-binding; Oncogene;
KW   Phosphoprotein; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..523
FT                   /note="Tyrosine-protein kinase transforming protein Src"
FT                   /id="PRO_0000088151"
FT   DOMAIN          71..139
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          145..242
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          264..514
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        383
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         270..278
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         413
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   523 AA;  58778 MW;  853245739F6B90ED CRC64;
     MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATELKL
     FGDFNTSDTV TSPQRAGALA GSVTTFGTRE SRIETDLSFK KRERLQIVNN TEGTWWLAHS
     LTTGQTGYIP SNYVAPSDSI QAEEWYFGKI TRRESGRLLL NPENPRGTFL VRESETTKGA
     YCLSVSDFDN AKGLNVKHYK IRKLDSGGFY ITSRTQFSSL QQLVAYYSKH ADGLCHRLTN
     VCPTSKPQTQ GLAKDAWEIP RESLRLEVKL GQGYFGEVWM GTWNGTTRVA IKTLKPGTMS
     PEAFLQEAQV MKKLRHEKLV QLYAMVSEEP IYIVIEYMSK GSLLDFLKGE MGKYLRLPQL
     VEMAAQIASG MAYVERMNYV HRDLRAANIL VGENLVCKVA DFGLARLIED NEYTARPGAR
     FPVKWTAPEA ALYGRFTIKS DVWSFGILLT ELTTKGRVPY PGMVNGEVLD RVERGYRMPC
     PPECPESLHD LMCQCWRKDP EERPTFEYLQ AQLLPACVLK IAE
//