ID   FES_FSVST               Reviewed;         477 AA.
AC   P00543;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Tyrosine-protein kinase transforming protein Fes;
DE            EC=2.7.10.2;
GN   Name=V-FES;
OS   Feline sarcoma virus (strain Snyder-Theilen).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus.
OX   NCBI_TaxID=11780;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6183005; DOI=10.1016/0092-8674(82)90282-3;
RA   Hampe A., Laprevotte I., Galibert F., Fedele L.A., Sherr C.J.;
RT   "Nucleotide sequences of feline retroviral oncogenes (v-fes) provide
RT   evidence for a family of tyrosine-specific protein kinase genes.";
RL   Cell 30:775-785(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-Fes polyprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA43046.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; J02088; AAA43046.2; ALT_INIT; Genomic_RNA.
DR   PIR; A00652; TVMVCS.
DR   SMR; P00543; -.
DR   PRIDE; P00543; -.
DR   BRENDA; 2.7.10.2; 2234.
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   CDD; cd10361; SH2_Fps_family; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR035849; Fes/Fps/Fer_SH2.
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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Oncogene; Phosphoprotein;
KW   SH2 domain; Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..477
FT                   /note="Tyrosine-protein kinase transforming protein Fes"
FT                   /id="PRO_0000088086"
FT   DOMAIN          115..204
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          216..477
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          49..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        338
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         222..230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         368
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  53757 MW;  BB87EDB4E7A3BEB5 CRC64;
     HPREQVQLLA KKQVLQEALQ ALQVALCSQA KLQAQRELLQ AKLEQLGPGE PPPVLLLQDD
     RHSTSSSEQE REGGRTPTLE ILKSHISGIF RPKFSLPPPL QLVPEVQKPL HEQLWYHGAL
     PRAEVAELLT HSGDFLVRES QGKQEYVLSV LWDGQPRHFI IQSADNLYRP EGDGFASIPL
     LVDHLLRSQQ PLTKKSGIVL NRAVPKDKWV LNHEDLVLGE QIGRGNFGEV FSGRLRADNT
     LVAVKSCRET LPPDIKAKFL QEAKILKQYS HPNIVRLIGV CTQKQPIYIV MELVQGGDFL
     TFLRTEGARL RMKTLLQMVG DAAAGMEYLE SKCCIHRDLA ARNCLVTEKN VLKISDFGMS
     REEADGVYAA SGGLRLVPVK WTAPEALNYG RYSSESDVWS FGILLWETFS LGASPYPNLS
     NQQTREFVEK GGRLPCPELC PDAVFRLMEQ CWAYEPGQRP SFSAFYQELQ SIRKRHR