DKF2_CAEBR
ID DKF2_CAEBR Reviewed; 1191 AA.
AC A8XQD5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Serine/threonine-protein kinase dkf-2 {ECO:0000250|UniProtKB:O45818};
DE EC=2.7.11.13;
DE AltName: Full=D kinase family-2 {ECO:0000250|UniProtKB:O45818};
GN Name=dkf-2 {ECO:0000312|EMBL:CAP34861.2}; ORFNames=CBG17105;
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:CAP34861.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP34861.2};
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, downstream of PKC. Acts in the
CC intestine to regulate both innate immunity by promoting activation of
CC pmk-1 and also stress response and life span by acting as an upstream,
CC negative regulator of the daf-16 transcription factor (By similarity).
CC {ECO:0000250}.
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:O45818};
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:O45818};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O45818};
CC -!- ACTIVITY REGULATION: Activated by DAG and phorbol esters. Phorbol-
CC ester/DAG-type domain 1 binds phorbol ester with low affinity. Phorbol-
CC ester/DAG-type domain 2 binds phorbol ester with high affinity and
CC targets the kinase to the cell periphery, enabling phosphorylation and
CC activation by colocalized tpa-1. Both domains 1 and 2 appear to bind
CC DAG with equal affinity so may contribute equally to translocation and
CC activation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O45818}.
CC Membrane {ECO:0000250|UniProtKB:O45818}. Note=Translocation to the cell
CC membrane is required for kinase activation.
CC {ECO:0000250|UniProtKB:O45818}.
CC -!- PTM: Phosphorylation on Ser-1046 is the dominant regulator of
CC catalysis, phosphorylation on Ser-1050 has a lesser effect. Prolonged
CC phosphorylation results in ubiquitination and degradation (By
CC similarity). {ECO:0000250|UniProtKB:O45818}.
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; HE601529; CAP34861.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XQD5; -.
DR SMR; A8XQD5; -.
DR STRING; 6238.CBG17105; -.
DR PRIDE; A8XQD5; -.
DR WormBase; CBG17105a; CBP46891; WBGene00036856; Cbr-dkf-2.
DR eggNOG; KOG4236; Eukaryota.
DR HOGENOM; CLU_009772_1_0_1; -.
DR InParanoid; A8XQD5; -.
DR OMA; LHTYTRP; -.
DR OrthoDB; 367841at2759; -.
DR Proteomes; UP000008549; Chromosome V.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; IPR001849; PH_domain.
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; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
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; Immunity; Innate immunity; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1191
FT /note="Serine/threonine-protein kinase dkf-2"
FT /id="PRO_0000385353"
FT DOMAIN 632..713
FT /note="PH"
FT /evidence="ECO:0000255"
FT DOMAIN 891..1147
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 314..364
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 466..531
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 11..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1014
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 897..905
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 920
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1191 AA; 132978 MW; 3071AAB93FD8D7A9 CRC64;
MDANDFPRLF YTSMPSSSTS NHRIDRLSSS SSSTFRRDDF RRHSTTTSSE KFSTISIGES
VKLEEENGEI PEKFVQEEDT VVKTEETRVS DCDFSLTFYT AHVTSSSMLS RGDSSSINNK
TFTPDDHYSN PSDKRREVPS IRSTSSNSSS FGGHVAFVDE PSEENQRQQQ QYQQHQFQLP
TLLVTSTPST VFDQNDDDVF TSPYHPPNRQ YSSSSEMSGL SFQLQSGIHK KSIAVEGNEI
ALRDLRNEAF QFVKEIYPEK KCGSLEDYIL LYKHDLRSIN ILQLITTSSD VTDGTLVEIV
IGSCPQNERI VVHPHTLFVH SYKVPTFCDF CGELLFGLVK QGLKCFGCGL NYHKRCASKI
PNNCNGSKQR RPSAIPLSPS NSNILNLNER RQSRRDSCLE ALDAARPSST LGGAATPNIF
ITSDDCGDPV GGNFLQMPRK DRSCSWSGRP LWMEIAEATR VKIQVPHTFQ VHSYKLPTVC
QHCKKLLKGL LRQGMQCRGE NETEKLQNGA VAKYCKYNCH KKCSEHVAKD CSGNTKASQF
FLGTADDGVS EDRDDDLSLR SGSGGHKKAQ NTPSAPLQGS EGSGSPGGAV VSFAQGLSNA
PDDDVISSES ANIPLMRVVM SKKQTKRKNN KLLKEGWIVH YTDQQNMRKK HYWRLDTKGI
TMYQDENTTR YYKEIPLNEI LGVMTSSPEK SSEYLFEIRT GACVYFVYSS LTDEELYNII
HASPCIARKP STVSSTDSGY LGSSGASSSC VRSREGSTVS STITVDRTRR GGSTTSTENS
EAESESSYSS FASIASTASK YLGRAADCLV LMTKRNGWSD AGSPADEKSS GSLDAQSWTT
AIQSALMPVT PQSSVVGGKR VDKLKVPTEG ETGHLGAKIQ TEQEFSQLYQ IFAEEVLGSG
QFGTVYGGIH RRNGQHVAVK LIDKLKFPPN KEDLLRAEVQ ILEQVDHPGV VHFMQMLETT
DRIFVVMEKL KGDMLEMILS SEKGRLSERT TQFLVAQILE ALRYLHHQNI VHCDLKPENI
LLNSNSDFPQ VKLCDFGFAR IIGEKSFRRS VVGTPAYLAP EVLRNKGFNR SLDMWSVGVI
VYVSLSGTFP FNEDEDINDQ IQNAEFMYPP SPWKEISENA IEFINGLLQV KMSKRYTVAK
AQSHIWMQNY TIWSDLRVLE KAVGQRFVTH ESDDSRWHAY EKEHNVTPVY V
