ID   YMX8_CAEEL              Reviewed;         346 AA.
AC   P34516;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Putative serine/threonine-protein kinase K06H7.1;
DE            EC=2.7.11.1;
GN   ORFNames=K06H7.8;
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=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; FO080533; CCD64455.1; -; Genomic_DNA.
DR   PIR; S44848; S44848.
DR   RefSeq; NP_498768.1; NM_066367.1.
DR   AlphaFoldDB; P34516; -.
DR   SMR; P34516; -.
DR   STRING; 6239.K06H7.8; -.
DR   PaxDb; P34516; -.
DR   PRIDE; P34516; -.
DR   EnsemblMetazoa; K06H7.8.1; K06H7.8.1; WBGene00019459.
DR   GeneID; 187079; -.
DR   KEGG; cel:CELE_K06H7.8; -.
DR   UCSC; K06H7.8; c. elegans.
DR   CTD; 187079; -.
DR   WormBase; K06H7.8; CE25045; WBGene00019459; -.
DR   eggNOG; KOG1164; Eukaryota.
DR   GeneTree; ENSGT00970000196431; -.
DR   HOGENOM; CLU_019279_2_5_1; -.
DR   InParanoid; P34516; -.
DR   OMA; KERYSYM; -.
DR   OrthoDB; 243860at2759; -.
DR   PhylomeDB; P34516; -.
DR   PRO; PR:P34516; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00019459; Expressed in adult organism and 1 other tissue.
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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..346
FT                   /note="Putative serine/threonine-protein kinase K06H7.1"
FT                   /id="PRO_0000086830"
FT   DOMAIN          20..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          302..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        141
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         26..34
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   346 AA;  39432 MW;  659524B1AB9F087B CRC64;
     MPGDVGEETL EIGAVVGKRY KVVQKLGEGG CGSVFKVEDT SEKGQHYALK VEFKSQDAGN
     ILKMEVQILS QLISKKHVAK CVASGKKERY SYMVMTLLGE SLDSLLKKHG PFLNVSTQVR
     IGICILFGIK QVHDIGYLHR DLKPANVAMG CKGSADERYF LVLDFGLARQ YIADEDDGLK
     MRRPREKTYF RGTARYCSVA MHDRYEQGRV DDLWALVYIL AEMRCRLAWH DVDDKVEIGE
     MKRKIHDEVL FAKSPVQMLS FVKTVRSTLF YHRPDYEKLF KLLEDVMKCA NYKWSDPYHW
     EPEKKKNPAS QGNKFGLGKK GTKESGELPE ASFFTVDDFN TNPLGF