ID NEKL4_CAEEL Reviewed; 981 AA.
AC P84199;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Serine/threonine-protein kinase D1044.8;
DE EC=2.7.11.1;
DE AltName: Full=Never in mitosis kinase like 4;
GN Name=nekl-4; ORFNames=D1044.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:0000303|PubMed:9851916};
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:0000303|PubMed:9851916};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000305}.
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DR EMBL; FO081000; CCD68375.1; -; Genomic_DNA.
DR RefSeq; NP_498178.3; NM_065777.5.
DR AlphaFoldDB; P84199; -.
DR SMR; P84199; -.
DR BioGRID; 40989; 4.
DR STRING; 6239.D1044.8.1; -.
DR PaxDb; 6239-D1044-8; -.
DR EnsemblMetazoa; D1044.8.1; D1044.8.1; WBGene00017033.
DR GeneID; 175760; -.
DR KEGG; cel:CELE_D1044.8; -.
DR AGR; WB:WBGene00017033; -.
DR WormBase; D1044.8; CE39141; WBGene00017033; nekl-4.
DR eggNOG; KOG0589; Eukaryota.
DR GeneTree; ENSGT00940000167597; -.
DR HOGENOM; CLU_011739_0_0_1; -.
DR InParanoid; P84199; -.
DR OMA; VCLQLIP; -.
DR OrthoDB; 315364at2759; -.
DR PhylomeDB; P84199; -.
DR PRO; PR:P84199; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00017033; Expressed in larva and 1 other cell type or tissue.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IBA:GO_Central.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR43671; SERINE/THREONINE-PROTEIN KINASE NEK; 1.
DR PANTHER; PTHR43671:SF92; SERINE_THREONINE-PROTEIN KINASE NEK10; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00185; ARM; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; ARM repeat; 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; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..981
FT /note="Serine/threonine-protein kinase D1044.8"
FT /id="PRO_0000086420"
FT DOMAIN 453..725
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 735..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 591
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 459..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 981 AA; 111652 MW; 8E5E38E5A67BAA29 CRC64;
MTEEVGQKLL ESLSLFKLGD IGYARIECEL LTTFLEEQLE NNLDSLSIHE LSTNLIRNRI
CCREFIESRP AKKWVFLIFR LARTLFRDKT RIATFHSVNL HSEFVQVFWR NLTYQTKSYR
NCKFQTFQFI ASRFLRSEHD WNVTVVNCLN VTQKLIDNGE NARKFVDCNL EDAVLVLLAT
RQMTVLQHSL EILGRLSDWS TTCRENLCES NTIDVCLQLI PDGDILTQKL CISLLRILSC
EEQAREQIRI YDGVPTLLGL LSIKNSRLQW HVAWTLAQLA EQHETSLEIA QLGGISLIFA
AISNPKPPGK AVGDWVAMLT GLTALLAQLA QASSNQQLMS NANGVYILGK LLAIKKNVTT
DETIDSWDLL QCSIFRVLRL MYTFERSRQL LKKVLPTEIF EKFVDVGNYN SVLTDYDQIA
KMYDNLIEEN IEIMKDWETV NERRQAVGEV GEYELLDQLG AGAFGCVYTV RKKAQSHSEN
PAKLLALKEI FMTNLNDRES DKSFGDMISE VKIIKQQLRH PNIVRYRRIF VENHRLYIVM
DLIQGCSLRD LIITMKEKKG NFEEKKIWAM VVQMMLALRY LHKEKQIVHR DLKPNNIMMT
TDERVVITDF GLAKQKGPEY LKSAAGTIIY SCPEIVQNLP YGEKADIWSF GCCIYEMCQL
QPVFHSTNML TLAMQIVEAK YDPLNEMWSD DLRFLITSCL APDPSARPDI LKVSGMCGVR
LLEYLDDVAR QQASTSDMTA SQSSYNIKID ESPSSLNSST SSYKRPGRSS KTSGSGKLPP
INPAPRRNHS MSAGETPRPS SIVCLPRITD KYSVMFPSAP SAIPSRRRVQ TCSTEHPARS
SSSTELKVSK QSDGLTVSSN VLRQIQDPVL TILNQIHRIL VVTDKETIST SMNHQRRLVE
MFRKNLLGRE NDAVQMKTHL RKLAAESPEE IQMNLGFSDF RPVLVQSHIN GYQKDQKVTK
ITYEQLSACI ECLIAENPAA K
//
