FES_FSVGA
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 03-AUG-2022, entry version 125.
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 CDD; cd10361; SH2_Fps_family; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.505.10; -; 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 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; SSF103657; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 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
