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FPS_FUJSV
ID   FPS_FUJSV               Reviewed;         873 AA.
AC   P00530;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Tyrosine-protein kinase transforming protein Fps;
DE            EC=2.7.10.2;
GN   Name=V-FPS;
OS   Fujinami sarcoma virus.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.
OX   NCBI_TaxID=11885;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6291784; DOI=10.1016/0092-8674(82)90283-5;
RA   Shibuya M., Hanafusa H.;
RT   "Nucleotide sequence of Fujinami sarcoma virus: evolutionary relationship
RT   of its transforming gene with transforming genes of other sarcoma
RT   viruses.";
RL   Cell 30:787-795(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] (CLONE TS).
RX   PubMed=2877522; DOI=10.1016/0042-6822(86)90172-8;
RA   Chen L.H., Hatada E., Wheatley W., Lee W.H.;
RT   "Single amino acid substitution, from Glu1025 to Asp, of the fps oncogenic
RT   protein causes temperature sensitivity in transformation and kinase
RT   activity.";
RL   Virology 155:106-119(1986).
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-Fps 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=AAA42402.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; J02194; AAA42402.1; ALT_INIT; Genomic_RNA.
DR   EMBL; M14930; AAA42403.1; -; Genomic_RNA.
DR   PIR; A00636; TVFVF.
DR   PIR; A26898; TVFVFS.
DR   SMR; P00530; -.
DR   BindingDB; P00530; -.
DR   ChEMBL; CHEMBL5708; -.
DR   BRENDA; 2.7.10.2; 2335.
DR   Proteomes; UP000124870; 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   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; IPR016250; Tyr-prot_kinase_Fes/Fps.
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   PIRSF; PIRSF000632; TyrPK_fps; 1.
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; Coiled coil; Kinase; Nucleotide-binding; Oncogene;
KW   Phosphoprotein; SH2 domain; Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..873
FT                   /note="Tyrosine-protein kinase transforming protein Fps"
FT                   /id="PRO_0000088096"
FT   DOMAIN          50..313
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          511..600
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          612..865
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   REGION          445..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        734
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         618..626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         764
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   VARIANT         63
FT                   /note="T -> S (in clone TS)"
FT   VARIANT         251
FT                   /note="H -> R (in clone TS)"
FT   VARIANT         300
FT                   /note="K -> E (in clone TS)"
FT   VARIANT         343
FT                   /note="N -> S (in clone TS)"
FT   VARIANT         438
FT                   /note="A -> T (in clone TS)"
FT   VARIANT         447
FT                   /note="E -> D (in clone TS)"
FT   VARIANT         463
FT                   /note="R -> C (in clone TS)"
FT   VARIANT         716
FT                   /note="E -> D (in clone TS)"
SQ   SEQUENCE   873 AA;  99536 MW;  1D774D48B18466B6 CRC64;
     ASGQLHRPQP QEHTSTSAAA GTWRLTQASE SRHRLPHCSA APSHQDHSAM GFGPELWCPK
     GHTELLRLQD SELRLLELMK KWMSQRAKSD REYAGMLHHM FSQLEKQEGL GHLRATDHSS
     QIGESWWVLA SQTETLSQTL RRHAEELAAG PLAKLSILIR DKQQLRKVFS EQWQQLSQEY
     AWTTQQEVEK LKAQYRSLVR DSTQAKRKYQ EASKDKEREK AKEKYVRSLS KLYALHNQYV
     LAVQAAALHH HHHYQRALPT LHESLYSLQQ EMVLVLKEIL GEYCSITSLV QEDVLAIHQK
     VAHAVEMIDP ATEYSSFVQC HRYDSEVPPA VTFDESLLEE AENLEPGELQ LNELTIESVQ
     HSLTSIEEEL LASRKAVSSK EQRVWELQVE LRGEELALSP GERVHLLGKR QGLREAQQQL
     QGLVCAQAKL QAQRDMLANK LAELGSEEPP PALPLQEDRQ SARSTDQERS GVTALKTIKN
     HISGIFSPRF SLPPPVPLIP EVQKPLCQQA WYHGAIPRSE VQELLKYSGD FLVRESQGKQ
     EYVLSVLWDG QPRHFIIQAA DNLYRLEDDG LPTIPLLIDH LLQSQRPITR KSGIVLTRAV
     LKDKWVLNHE DVLLGERIGR GNFGEVFSGR LRADNTPVAV KSCRETLPPE LKAKFLQEAR
     ILKQCNHPNI VRLIGVCTQK QPIYIVMELV QGGDFLSFLR SKGPRLKMKK LIKMMENAAA
     GMEYLESKHC IHRDLAARNC LVTEKNTLKI SDFGMSRQEE DGVYASTGGM KQIPVKWTAP
     EALNYGWYSS ESDVWSFGIL LWEAFSLGAV PYANLSNQQT REAIEQGVRL EPPEQCPEDV
     YRLMQRCWEY DPHRRPSFGA VHQDLIAIRK RHR
 
 
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