KRAF1_CAEBR
ID KRAF1_CAEBR Reviewed; 811 AA.
AC Q61UC4; A8WZR1;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Raf homolog serine/threonine-protein kinase;
DE EC=2.7.11.1;
DE AltName: Full=Abnormal cell lineage protein 45;
GN Name=lin-45 {ECO:0000250|UniProtKB:Q07292}; Synonyms=raf-1;
GN ORFNames=CBG05382;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Protein kinase that participates in the induction of vulva
CC and has a role in fertility and viability. Acts downstream of the Ras
CC protein let-60. Required for progression of developing oocytes through
CC the pachytene stage. Positively regulates lifespan upstream of mek-2
CC and mpk-1. {ECO:0000250|UniProtKB:Q07292}.
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 Evidence={ECO:0000250|UniProtKB:Q07292};
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; Evidence={ECO:0000250|UniProtKB:Q07292};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P04049};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P04049};
CC -!- SUBUNIT: Interacts with cdf-1 in a zinc-dependent manner which promotes
CC its activity. {ECO:0000250|UniProtKB:Q07292}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000305}.
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DR EMBL; HE601369; CAP25871.3; -; Genomic_DNA.
DR AlphaFoldDB; Q61UC4; -.
DR SMR; Q61UC4; -.
DR STRING; 6238.CBG05382; -.
DR WormBase; CBG05382a; CBP42271; WBGene00027841; Cbr-lin-45.
DR eggNOG; KOG0193; Eukaryota.
DR HOGENOM; CLU_023684_1_0_1; -.
DR InParanoid; Q61UC4; -.
DR OMA; MYLMEYQ; -.
DR OrthoDB; 243095at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion 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; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02196; RBD; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00455; RBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50898; RBD; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Developmental protein; Differentiation; Kinase; Meiosis;
KW Metal-binding; Nucleotide-binding; Oogenesis; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..811
FT /note="Raf homolog serine/threonine-protein kinase"
FT /id="PRO_0000294931"
FT DOMAIN 84..160
FT /note="RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 479..744
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 169..216
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 600
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P04049,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04049"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04049"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04049"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04049"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04049"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04049"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04049"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04049"
FT BINDING 485..493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04049,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P04049,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 811 AA; 89980 MW; D6A31D95B423BA1A CRC64;
MSRINLKKSS AATTPTSPHC PSPRLISLPR CASSSIDRKD QGSPMASPST PLYPKHSDSL
HSLSGHDHSG VGTSDKEPPK FKYKMIMVHL PFDQHSRVEV RPGETARDAI SKLLKKRNIT
PQLCQVNTSP DSKTEAIDLS KTMEEIALHL PDNELWVHSE YLNTVSSIKH AIVRRTFIPP
KSCDVCNNPI WMMGFRCEFC QFKFHQRCSS FAPLYCDLLQ SVPKNEDLVK QLVGIASEND
GPDRSVAEIV LAGLAPTYGQ SPAATPDSSH PDLTSIKRTG GVKRHPLAVS PQAETAQLSP
AGPYPRDRSS SAPNINAIND EATVQHNQRI LDALEAKRLE EESKDKTGSL LSTQARRPHC
YSGHILSGSR MNRLHPLVDC TPLGSNSPSS TCSSPPGGLM GPTLLGQSSS VSGSTTSSLV
AAHLHTLPLT PPQSAPPQKI SPGFFRNRSR SPGERIEAQR PRPPQKPQHE DWEILPNEFV
IHYKVGSGSF GTVYRGEFFG TVAIKKLNVV DPTPSQMAAF KNEVAVLKKT RHLNVLLFMG
WVREPEIAII TQWCEGSSLY RHIHVQEPRV EFEMSAVIDI LKQVSLGMNY LHSKNIIHRD
LKTNNIFLMD DMSTVKIGDF GLATVKTKWT VNGGQQQQQP TGSILWMAPE VIRMQDDNPY
TPQSDVYSFG VCMYEILSSH LPYSNINNRD QILFMVGRGY LKPDRSKIRT DTPKSLMKLY
DNCIMFDRNE RPVFGEVLER LRDIILPKLT RSQSAPNVLH YDSQYSVMDA VMRSQMVSSS
YIPPSTAKTP QSAAAAAAAN KKAYYNVYGL I
