ZYG1_CAEBR
ID ZYG1_CAEBR Reviewed; 709 AA.
AC Q621J7; A8WU96;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable serine/threonine-protein kinase zyg-1;
DE EC=2.7.11.1;
DE AltName: Full=Zygote defective protein 1;
GN Name=zyg-1; ORFNames=CBG02462;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
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: Protein kinase that plays a central role in centrosome
CC duplication. Paternal copy is required to regulate synthesis of
CC daughter centrioles prior to fertilization. Maternal copy regulates
CC centrosome duplication during later cell cycles. Functions upstream of
CC sas-5 and sas-6, and is required for their localization to the
CC centrosome (By similarity). {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=2.7.11.1;
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}. Note=Component of the
CC centrosome. Present at centrioles only immediately before their
CC duplication (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Although it is unknown whether it is a serine/threonine or a
CC tyrosine protein kinase, it is strongly related to serine/threonine-
CC protein kinase family. {ECO:0000305}.
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DR EMBL; HE601438; CAP24058.1; -; Genomic_DNA.
DR RefSeq; XP_002630767.1; XM_002630721.1.
DR AlphaFoldDB; Q621J7; -.
DR SMR; Q621J7; -.
DR STRING; 6238.CBG02462; -.
DR PRIDE; Q621J7; -.
DR EnsemblMetazoa; CBG02462.1; CBG02462.1; WBGene00025510.
DR GeneID; 8572283; -.
DR KEGG; cbr:CBG_02462; -.
DR CTD; 8572283; -.
DR WormBase; CBG02462; CBP14405; WBGene00025510; Cbr-zyg-1.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_390907_0_0_1; -.
DR InParanoid; Q621J7; -.
DR OMA; WPIRMER; -.
DR OrthoDB; 1399796at2759; -.
DR Proteomes; UP000008549; Chromosome II.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; 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:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR040733; Zyg-1_PB1.
DR InterPro; IPR040734; Zyg-1_PB2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18531; Polo_box_2; 1.
DR Pfam; PF18544; Polo_box_3; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cytoplasm; Cytoskeleton; Developmental protein;
KW Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..709
FT /note="Probable serine/threonine-protein kinase zyg-1"
FT /id="PRO_0000086845"
FT DOMAIN 13..251
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 254..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 709 AA; 79640 MW; CDB3D321B83B050A CRC64;
MSGGKSGTKL SSFQNLQQIG QGGFGVVYSA QRENGEKVAI KKIGNAASQT RIKEEIKTMK
LLRHRNIVQF YETFFENGET YLVMELCEGG SLMDYVKQKG PLDDSTAVHI LRQLIAAVKY
IHDENILHRD LSAGNVFIKD ATKSTITVKL GDFGLATNLG QHGTACTIVG TPGFIAPQVF
GQNYDQAADV YSLGAVLYTM LTKHTPPTKG PPNLESLKKR NPSAADLVER MMHTDARRRI
QLKEIVMTDY VKAKMGEATP GSREHSRDSR SQRSREPFRS SRDGISLERR PPARSSSQPV
NSRRDPDGYR AAHEMPTTSR TSVEPDRARV RHRLSARGIG SSQEDDLRQQ IWPIRMERLV
GQRVRTPGGR YIVEMNTRCR FEVVSKGNIV LRILVVEYDP HLLIQTVYVH KMSNRVEHAR
NETDDLIELT RSPISYTSLS QLPKEVMNDY MRLEKMMVST IASRVAKITH RRPSQFPDAS
AQLMENGDLR IRFPNSLIVR RKSNGEVHNY IDGFANNKEE VRGLQLSKVR EVYACLTQLE
QCLSRMNPTM KILPMVFSAG PDIVATYNNS PSSILPSTSS QASRFPFSEI SSSQQLVPHS
APIPNKPLSS RTTSSLNVRN GVSSDENTAP AATRQKYKAR LDPVTGRIVS VQAEDNRKLR
CSTSKPDQFI FTDPSISSSE QRFMRNGRVP ERASEMLHAL LVYMKKKQN
