DKF1_CAEBR
ID DKF1_CAEBR Reviewed; 760 AA.
AC A8XWC4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Serine/threonine-protein kinase dkf-1 {ECO:0000250|UniProtKB:Q9XUJ7, ECO:0000312|EMBL:CAP36943.2};
DE EC=2.7.11.13;
DE AltName: Full=D kinase family-1 {ECO:0000250|UniProtKB:Q9XUJ7};
GN Name=dkf-1 {ECO:0000312|EMBL:CAP36943.2}; ORFNames=CBG19775;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP36943.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP36943.2};
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: Converts transient diacylglycerol (DAG) signals into
CC prolonged physiological effects, independently of PKC. Role in the
CC regulation of growth and neuromuscular control of movement. Involved in
CC immune response to S.aureus bacterium by activating transcription
CC factor hlh-30 downstream of phospholipase plc-1.
CC {ECO:0000250|UniProtKB:Q9XUJ7}.
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=2.7.11.13;
CC Evidence={ECO:0000250|UniProtKB:Q9XUJ7};
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=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q9XUJ7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9XUJ7};
CC -!- ACTIVITY REGULATION: Activated by DAG and phorbol esters. Phorbol-
CC ester/DAG-type domain 1 binds phorbol ester with high affinity and
CC mediates accumulation at the cell periphery. Phorbol-ester/DAG-type
CC domain 2 binds phorbol ester with low affinity but may mediate initial
CC contact, resulting in a conformational change allowing previously
CC occluded domain 1 to anchor the kinase. Phosphorylation on Thr-626 is
CC then also required for activation and may also result in a further
CC conformational change (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9XUJ7}.
CC Membrane {ECO:0000250|UniProtKB:Q9XUJ7}. Note=Translocation to the cell
CC membrane is required for kinase activation. On activation, the protein
CC may migrate back to the cytoplasm (By similarity).
CC {ECO:0000250|UniProtKB:Q9XUJ7}.
CC -!- DOMAIN: The PH domain inhibits PKD catalytic activity in the absence of
CC DAG, either by direct steric occlusion or distortion of the PKD
CC catalytic cleft. {ECO:0000250|UniProtKB:Q9XUJ7}.
CC -!- PTM: Prolonged phosphorylation at Thr-626 results in ubiquitination and
CC degradation. {ECO:0000250|UniProtKB:Q9XUJ7}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000255}.
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DR EMBL; HE601474; CAP36943.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XWC4; -.
DR SMR; A8XWC4; -.
DR STRING; 6238.CBG19775; -.
DR PRIDE; A8XWC4; -.
DR WormBase; CBG19775; CBP38325; WBGene00038940; Cbr-dkf-1.
DR eggNOG; KOG4236; Eukaryota.
DR HOGENOM; CLU_009772_1_0_1; -.
DR InParanoid; A8XWC4; -.
DR OMA; YARFIPE; -.
DR OrthoDB; 367841at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
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:0089700; P:protein kinase D signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00029; C1; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PTHR22968; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..760
FT /note="Serine/threonine-protein kinase dkf-1"
FT /id="PRO_0000385351"
FT DOMAIN 316..444
FT /note="PH"
FT /evidence="ECO:0000255"
FT DOMAIN 464..725
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 103..153
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 194..244
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ACT_SITE 589
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 470..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9XUJ7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 626
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 760 AA; 86922 MW; 4DE8E7093CEBBC17 CRC64;
MDTSGSTTDF GDHVVLRYGG TKEMVPLIRH EQMLDMLMER ARQIVQGFGS LDTRNMYLFR
HEYNSPTLLF PITSPSQIAS FSKNPGCILE IILVDRTETA VIPHVVEPES YMLPTFCDFC
GELLTGLLRQ GVKCKNCNRN FHKRVRMQQG IIVEHLDPLP QDRGLLDRPC YPHCHQRLLE
FRCPRCQRLL VSLPHTLIEH SYRQFTVCKV CDHLLVGLMK QGLKCRDCGV NVHRKCAMEL
PSNCILSENA ISRVNFADSE AEQASSSDNI PLFRLPDDIK IKKKFKKKFL HREKRIEKYV
FSRPPGQVGV RATEKKNLEG WMIHFILSDP ERRLKHYWMM QNNAIHLYNE YSEGIGVNPN
RVYRIIPLAE ITSVVQNNGK SVLAKHPPHC FEIRTTTNTV FCVGEDYHAF SGGPPKKIPR
SMSVRPTSNT TMWFQFIKES LQPPSRNNEE NAEQALEFAN LYQVLSDKTL GSGQFGTVYS
AIQRHSGKEV AVKVISKERF SKKGSGAESM RAEVAILQQT CHPGIVCLEF MCETKDKIFV
VMEKMNGDML EMILSQELGR LNSRATKFLL VQILCALKYL HDQGIAHCDL KPENVLLSDM
GSNFPQTKIC DFGYARFIPE SQFRKTVVGT PAYLPPEVLQ RKGYNKSLDM WSVGVIIYVT
LSGTFPFNEG EEVSISEQIQ NASFMFPTEP WSEVEPLAVD LIQKLLKVEI EARMSIEKCL
EHGWLKGEQL YRDLRDLEVR LNTPRYLTSP QDDVLYGPLR
