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
//
