ID   YES_AVISY               Reviewed;         528 AA.
AC   P00527;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-NOV-2023, entry version 127.
DE   RecName: Full=Tyrosine-protein kinase transforming protein Yes;
DE            EC=2.7.10.2;
DE   Flags: Fragment;
GN   Name=V-YES;
OS   Y73 avian sarcoma virus (Y73SV) (Avian sarcoma virus (strain Y73)).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11884;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=6281656; DOI=10.1038/297205a0;
RA   Kitamura N., Kitamura A., Toyoshima K., Hirayama Y., Yoshida M.;
RT   "Avian sarcoma virus Y73 genome sequence and structural similarity of its
RT   transforming gene product to that of Rous sarcoma virus.";
RL   Nature 297:205-208(1982).
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 a Gag-Yes polyprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA24496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; V01170; CAA24496.1; ALT_INIT; Unassigned_RNA.
DR   PIR; A00633; TVFVG9.
DR   SMR; P00527; -.
DR   BRENDA; 2.7.10.2; 600.
DR   Proteomes; UP000164967; Genome.
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; cd09933; SH2_Src_family; 1.
DR   CDD; cd12007; SH3_Yes; 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   InterPro; IPR035751; Yes_SH3.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24418:SF90; TYROSINE-PROTEIN KINASE YES; 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; Nucleotide-binding; Oncogene; Phosphoprotein;
KW   SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
FT   CHAIN           <1..528
FT                   /note="Tyrosine-protein kinase transforming protein Yes"
FT                   /id="PRO_0000088179"
FT   DOMAIN          81..142
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          148..245
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          267..520
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         273..281
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         416
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   528 AA;  59104 MW;  98F748C8879D7709 CRC64;
     DKGPAMKYRT DNTPEPISSH VSHYGSDSSQ ATQSPAIKGS AVNFNSHSMT PFGGPSGMTP
     FGGASSSFSA VPSPYPSTLT GGGTVFVALY DYEARTTDDL SFKGGERFQI INNTEGDWWE
     ARSIATGKTG YIPSNYVAPA DSIEAEEWYF GKMGRKDAER LLLNPGNQRG IFLVRESETT
     KGAYSLSIRD WDEVRGDNVK HYKIRKLDNG GYYITTRAQF ESLQKLVKHS REHADGLCHK
     LTTVCPTVKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT KVAIKTLKLG
     TMMPEAFLQE AQIMKKLRHD KLVPLYAVVS EEPIYIVTEF MTKGSLLDFL KEGEGKFLKL
     PQLVDMAAQI ADGMAYIERM NYIHRDLRAA NILVGDNLVC KIADFGLARL IEDNEYTARQ
     GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELVTKGR VPYPGMVNRE VLEQVERGYR
     MPCPQGCPES LHELMKLCWK KDPDERPTFE YIQSFLEDYF TAAEPSGY
//