ID   FGR_FSVGR               Reviewed;         545 AA.
AC   P00544;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-NOV-2023, entry version 131.
DE   RecName: Full=Tyrosine-protein kinase transforming protein Fgr;
DE            EC=2.7.10.2;
GN   Name=V-FGR; Synonyms=SRC-2;
OS   Feline sarcoma virus (strain Gardner-Rasheed).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Feline leukemia virus.
OX   NCBI_TaxID=11775;
OH   NCBI_TaxID=9681; Felidae (cat family).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6318314; DOI=10.1126/science.6318314;
RA   Naharro G., Robbins K.C., Reddy E.P.;
RT   "Gene product of v-fgr onc: hybrid protein containing a portion of actin
RT   and a tyrosine-specific protein kinase.";
RL   Science 223:63-66(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   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Fgr polyprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA25063.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X00255; CAA25063.1; ALT_INIT; Genomic_DNA.
DR   PIR; A00653; TVMVRR.
DR   SMR; P00544; -.
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; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   CDD; cd10367; SH2_Src_Fgr; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR035693; Fgr_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:SF224; TYROSINE-PROTEIN KINASE FGR; 1.
DR   Pfam; PF00022; Actin; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00190; ACTIN.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00268; ACTIN; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 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..545
FT                   /note="Tyrosine-protein kinase transforming protein Fgr"
FT                   /id="PRO_0000088090"
FT   DOMAIN          167..264
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          286..539
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          23..157
FT                   /note="Actin"
FT   ACT_SITE        405
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         292..300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         435
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  61516 MW;  7F4742EB7A7C413E CRC64;
     ARALCRPAVC RPRPLPPLPP TAMEEEVAAL VIDNGSGMCK AGFAGDDAPR AVFPSIVGRP
     RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIVTN WDDMEKIWHH TFYNELRVAP
     EEHPVLLTEA PLNPKANREK MTQIMFETFN IPSNYVAPVD SIQAEEWYFG KIGRKDAERQ
     LLSPGNARGA FLVRESETTK GAYSLSIRDW DEARGDHVKH YKIRKLDTGG YYITTRAQFN
     SVQELVQHYV EVNDGLCHLL TAACTTMKPQ TMGLAKDAWE ISRSSITLQR RLGTGCFGDV
     WLGMWNGSTK VAVKTLKPGT MSPKASLEEA QIMKLLRHDK LVQLYAVVPE EPIYIVTEFM
     CHGSLLEFLK DQEGQDLTLP QLVDMAAQVA EGMAYMERMD YIHRDLRAAN ILVGERLVCK
     IADFGLARLI EDNEYNPRQG AKFPIKWTAP EAALFGRFTI KSDVWSFGIL LTELISKGRV
     PYPGMNNREV LEQVEHGYHM PCPPGCPASL YEAMEQTWRL DPEERPTFEY LQSFLEDYFN
     GPQQN
//