ID   RAF_MSV36               Reviewed;         323 AA.
AC   P00532;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Serine/threonine-protein kinase-transforming protein raf;
DE            EC=2.7.11.1;
GN   Name=V-RAF;
OS   Murine sarcoma virus 3611.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Gammaretrovirus;
OC   Moloney murine sarcoma virus.
OX   NCBI_TaxID=11812;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6320371; DOI=10.1126/science.6320371;
RA   Kan N.C., Flordellis C.S., Mark G.E., Duesberg P.H., Papas T.S.;
RT   "A common onc gene sequence transduced by avian carcinoma virus MH2 and by
RT   murine sarcoma virus 3611.";
RL   Science 223:813-816(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6324342; DOI=10.1126/science.6324342;
RA   Mark G.E., Rapp U.R.;
RT   "Primary structure of v-raf: relatedness to the src family of oncogenes.";
RL   Science 224:285-289(1984).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- MISCELLANEOUS: This protein is synthesized as a Gag-Raf polyprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. RAF subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA46579.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; K01691; AAA46579.1; ALT_INIT; Genomic_RNA.
DR   PIR; A00638; TVMVF6.
DR   SMR; P00532; -.
DR   BindingDB; P00532; -.
DR   BRENDA; 2.7.10.2; 3471.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR23257:SF763; RAF PROTO-ONCOGENE SERINE_THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000654; Integrin-linked_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Oncogene;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..323
FT                   /note="Serine/threonine-protein kinase-transforming protein
FT                   raf"
FT                   /id="PRO_0000086601"
FT   DOMAIN          24..284
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        143
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         30..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   323 AA;  36884 MW;  52A5423A66E362F3 CRC64;
     EKNKIRPRGQ RDSSYYWKME ASEVMLSTRI GSGSFGTVYK GKWHGDVAVK ILKVVDPTPE
     QLQAFRNEVA VLRKTRHVNI LLFMGYMTKD NLAIVTQWCE GSSLYKHLHV QETKFQMFQL
     IDIARQTAQG MDYLHAKNII HRDMKSNNIF LHEGLTVKIG DFGLATVKSR WSGSQQVEQP
     TGSVLWMAPE VIRMQDDNPF SFQSDVYSYG IVLYELMAGE LPYAHINNRD QIIFMVGRGY
     ASPDLSRLYK NCPKAIKRLV ADCVKKVKEE RPLFPQILSS IELLQHSLPK INRSAPEPSL
     HRAAHTEDIN ACTLTTSPRL PVF
//