ID   FPS_AVISP               Reviewed;         533 AA.
AC   P00541;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Tyrosine-protein kinase transforming protein Fps;
DE            EC=2.7.10.2;
GN   Name=V-FPS;
OS   Avian sarcoma virus (strain PRCII).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11880;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6321783; DOI=10.1128/jvi.50.1.125-131.1984;
RA   Huang C.-C., Hammond C., Bishop J.M.;
RT   "Nucleotide sequence of v-fps in the PRCII strain of avian sarcoma virus.";
RL   J. Virol. 50:125-131(1984).
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-Fps polyprotein.
CC   -!- MISCELLANEOUS: Present in the avian viruses PRCII and Fujinami sarcoma
CC       virus (FSV). PRCII is less oncogenic than FSV and has a slightly
CC       different v-Fps protein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fes/fps subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; K01690; AAA42415.1; -; Genomic_RNA.
DR   PIR; A00650; TVFVFP.
DR   SMR; P00541; -.
DR   BRENDA; 2.7.10.2; 600.
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; 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; 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..533
FT                   /note="Tyrosine-protein kinase transforming protein Fps"
FT                   /id="PRO_0000088094"
FT   DOMAIN          50..124
FT                   /note="F-BAR; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          171..260
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          272..525
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        394
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         278..286
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         301
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         424
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   533 AA;  60506 MW;  2F765877C2522D8A CRC64;
     ASGQLHRPQP QEHTSTSAAA GTWRHTQASE SRHRLPHCSA APSHQDHSAM GFGPELWCPK
     GHSELLRLQD SELRLLELMK KWMSERAKSD REYAGMLHHM FSQLGSEEPP PALPLQEDRQ
     SVCSTDQERS GVTALETIKN HISGIFSPRF SLPPPVPLIP EVQKPLCQQA WYHGAIPRSE
     VQELLKCSGD FLVRESQGKQ EYVLSVLWDG QPRHFIIQAA DNLYRLEGDG FPTIPLLIDH
     LLQSQQPITR KSGIVLTRAV LKDKWVLNHE DVLLGERIGR GNFGEVFSGR LRADNTPVAV
     KSCRETLPPE LKAKFLQEAR ILKQYNHPNI VRLIGVCTQK QPIYIVMELV QGGDFLSFLR
     SKGPHLKMKE LIKMMENAAA GMEYLESKHC IHRDLAARNC LVTEKNTLKI SDFGMSRQEE
     DGVYASTGGM KQIPVKWTAP EALNYGRYSS ESDVWSFGIL LWEAFSLGAV PYANLSNQQT
     REAIEQGVRL EPPEQCPEDV YRLMQRCWEY DPRRRPSFGA VHQDLIAIRK RHR