ID   YOO1_CAEEL              Reviewed;         331 AA.
AC   P34633;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 3.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Putative serine/threonine-protein kinase ZK507.1;
DE            EC=2.7.11.1;
GN   ORFNames=ZK507.1;
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=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
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   -!- 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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; Z29116; CAA82367.3; -; Genomic_DNA.
DR   PIR; S40735; S40735.
DR   RefSeq; NP_499015.2; NM_066614.2.
DR   AlphaFoldDB; P34633; -.
DR   SMR; P34633; -.
DR   STRING; 6239.ZK507.1; -.
DR   PaxDb; P34633; -.
DR   PeptideAtlas; P34633; -.
DR   EnsemblMetazoa; ZK507.1.1; ZK507.1.1; WBGene00013978.
DR   GeneID; 191336; -.
DR   KEGG; cel:CELE_ZK507.1; -.
DR   UCSC; ZK507.1; c. elegans.
DR   CTD; 191336; -.
DR   WormBase; ZK507.1; CE48033; WBGene00013978; -.
DR   eggNOG; KOG1164; Eukaryota.
DR   GeneTree; ENSGT00970000196451; -.
DR   HOGENOM; CLU_019279_2_5_1; -.
DR   InParanoid; P34633; -.
DR   OrthoDB; 1683154at2759; -.
DR   PhylomeDB; P34633; -.
DR   PRO; PR:P34633; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00013978; Expressed in adult organism and 2 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..331
FT                   /note="Putative serine/threonine-protein kinase ZK507.1"
FT                   /id="PRO_0000086832"
FT   DOMAIN          1..270
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          302..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        116
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
SQ   SEQUENCE   331 AA;  38116 MW;  0816A93596108326 CRC64;
     MKVNEEGFAI DDKEYAMKTE LKFASKHSSR LKIERNVMES YSKCDAQCKE HFSELIDFGQ
     SPVWKWIVMT IVGPSLEELK MKYKPSDIPP STILQCGLQT MKAIHDFHQI GFLHRDIKPA
     NYCIGYGSKS ETIYVLDFGL ARKYRLPNGQ VRPPRPKTKM IGTPRYCSRA SHRCEELGRR
     DDYESWFFMF IDLVDTTLID WKGLTRPDAY AKKQELFTKL KTYEKHPMFK VISIYLDNLV
     YDSEVKFGVL REAITDYARG CKLTLKEPLV WFNQSTCPSP STAPGTGASR MATNIDLKSI
     ASDRNEENSL DRSKTGTLSF NNSKNKKPSR Y