RAF_MSV36
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 03-AUG-2022, entry version 103.
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.
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 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:0006468; P:protein phosphorylation; IEA:InterPro.
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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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