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Database: UniProt
Entry: SEA_AVIET
LinkDB: SEA_AVIET
Original site: SEA_AVIET 
ID   SEA_AVIET               Reviewed;         370 AA.
AC   P23049; Q85458; Q85459;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-NOV-2023, entry version 100.
DE   RecName: Full=Tyrosine-protein kinase transforming protein SEA;
DE            EC=2.7.10.2;
GN   Name=V-SEA;
OS   Avian erythroblastosis virus (strain S13).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus;
OC   Avian leukosis virus.
OX   NCBI_TaxID=11863;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2546151; DOI=10.1073/pnas.86.14.5291;
RA   Smith D.R., Vogt P.K., Hayman M.J.;
RT   "The v-sea oncogene of avian erythroblastosis retrovirus S13: another
RT   member of the protein-tyrosine kinase gene family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:5291-5295(1989).
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   -!- MISCELLANEOUS: This protein is synthesized as an Env-Sea polyprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA42392.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M25158; AAA42392.1; ALT_INIT; Genomic_RNA.
DR   SMR; P23049; -.
DR   BRENDA; 2.7.10.2; 589.
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   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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416:SF113; MACROPHAGE-STIMULATING PROTEIN RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Oncogene; Phosphoprotein;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..370
FT                   /note="Tyrosine-protein kinase transforming protein SEA"
FT                   /id="PRO_0000088136"
FT   DOMAIN          60..323
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          345..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         66..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         216
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   370 AA;  41701 MW;  DD02ABBD58BD190D CRC64;
     ADSPGLARPH AHFASAGADA AGGGSPVLLL RTTSCCLEDL RPELLEEVKD ILIPEERLIT
     HRSRVIGRGH FGSVYHGTYM DPLLGNLHCA VKSLHRITYL EEVEEFLREG ILMKGFHHPQ
     VLSLLGVCLP RHGLPLVVLP YMRHGDLRHF VRAQERSPTV KELIGFGLQV ALGMEYLAQK
     KFVHRDLAAR NCMLDETLTV KVADFGLARD VFGKEYYSIR QHRHAKLPVR WMALESLQTQ
     KFTTKSDVWS FGVLMWELLT RGASPYPEVD PYDMARYLLR GRRLPQPQPC PDTLYGVMLS
     CWAPTPEERP SFSGLVCELE RVLASLEGEH YINMAVTYVN LESGPPFPPA PRGQLPDSED
     EEDEEEEVAE
//
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