ID FES_FSVGA Reviewed; 609 AA. AC P00542; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=Tyrosine-protein kinase transforming protein Fes; DE EC=2.7.10.2; GN Name=V-FES; OS Feline sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein OS feline leukemia oncovirus B). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus. OX NCBI_TaxID=11774; 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 -!- DOMAIN: The F-BAR domain is truncated and contains only the FCH region CC (the coiled-coil region is missing). {ECO:0000305}. 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=AAA43041.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02087; AAA43041.1; ALT_INIT; Genomic_RNA. DR PIR; A00651; TVMVGC. DR SMR; P00542; -. 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd10361; SH2_Fps_family; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR031160; F_BAR. DR InterPro; IPR001060; FCH_dom. 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 PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24418:SF197; TYROSINE-PROTEIN KINASE FES_FPS; 1. DR Pfam; PF00611; FCH; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF00017; SH2; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00055; FCH; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR PROSITE; PS51741; F_BAR; 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..609 FT /note="Tyrosine-protein kinase transforming protein Fes" FT /id="PRO_0000088087" FT DOMAIN 8..174 FT /note="F-BAR; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077" FT DOMAIN 247..336 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 348..609 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 152..208 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 152..177 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 470 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 354..362 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 377 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 500 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" SQ SEQUENCE 609 AA; 68769 MW; 53D4919757CF73A3 CRC64; AARADGTMGF SSELCSPQGH GAEQQMQEAE LRLLEGMRKW MAQRVKSDRE YAGLLHHMSL QDGGGRGTGP YSPISQSWAE ITSQTEGLSR LLRQHAEDLN SGPLSKLGLL IRERQQLRKT YSEQWQQLQQ ELTKTHNQDI EKLKSQYRAL ARDSAQARRK YQEASKDKDR DKAKLEQLGP GEPPPVLLLQ DDRHSTSSSE QEREGGRTPT LEILKSHISG IFRPKFSLPP PLQLVPEVQK PLHEQLWYHG ALPRAEVAEL LTHSGDFLVR ESQGKQEYVL SVLWDGQPRH FIIQSADNLY RPEGDGFASI PLLVDHLLRS QQPLTKKSGI VLNRAVPKDK WVLNHEDLVL GEQIGRGNFG EVFSGRLRAD NTLVAVKSCR ETLPPDIKAK FLQEAKILKQ YSHPNIVRLI GVCTQKQPIY IVMELVQGGD FLTFLRTEGA RLRMKTLLQM VGDAAAGMEY LESKCCIHRD LAARNCLVTE KNVLKISDFG MSREAADGIY AASGGLRQVP VKWTAPEALN YGRYSSESDV WSFGILLWET FSLGASPYPN LSNQQTREFV EKGGRLPCPE LCPDAVFRLM EQCWAYEPGQ RPSFSAIYQE LQSIRKRHR //