PLK3_CAEEL
ID PLK3_CAEEL Reviewed; 615 AA.
AC Q20845;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Serine/threonine-protein kinase plk-3;
DE EC=2.7.11.21;
DE AltName: Full=Polo-like kinase 3;
GN Name=plk-3; Synonyms=plc2; ORFNames=F55G1.8;
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 [MRNA].
RX PubMed=10376213; DOI=10.3109/10425179909008427;
RA Ouyang B., Wang Y., Dai W.;
RT "Caenorhabditis elegans contains structural homologs of human prk and
RT plk.";
RL DNA Seq. 10:109-113(1999).
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 -!- FUNCTION: May be required for cell division and may have a role during
CC G1 or S phase. {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=2.7.11.21;
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=2.7.11.21;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AF059024; AAC14425.1; -; mRNA.
DR EMBL; FO081135; CCD69395.1; -; Genomic_DNA.
DR PIR; T29223; T29223.
DR RefSeq; NP_501196.1; NM_068795.6.
DR AlphaFoldDB; Q20845; -.
DR SMR; Q20845; -.
DR BioGRID; 57374; 4.
DR DIP; DIP-26696N; -.
DR IntAct; Q20845; 1.
DR STRING; 6239.F55G1.8.1; -.
DR PaxDb; Q20845; -.
DR EnsemblMetazoa; F55G1.8.1; F55G1.8.1; WBGene00004044.
DR GeneID; 266900; -.
DR KEGG; cel:CELE_F55G1.8; -.
DR UCSC; F55G1.8.1; c. elegans.
DR CTD; 266900; -.
DR WormBase; F55G1.8; CE07285; WBGene00004044; plk-3.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000166918; -.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; Q20845; -.
DR OMA; RITESQC; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; Q20845; -.
DR BRENDA; 2.7.11.21; 1045.
DR SignaLink; Q20845; -.
DR PRO; PR:Q20845; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004044; Expressed in germ line (C elegans) and 4 other tissues.
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 CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR Gene3D; 3.30.1120.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50078; POLO_BOX; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..615
FT /note="Serine/threonine-protein kinase plk-3"
FT /id="PRO_0000086571"
FT DOMAIN 35..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 402..463
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 505..573
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 41..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 615 AA; 70436 MW; D510C727329C4B26 CRC64;
MQHVLRTRGN SAQDKNKKHV PNVPPIIYDD MQVPYEKGAF LGEGGFAHCF EFRKLDCNDR
LAVKVVPKVI LLKSTAREKL TREVEIHRQL SHRNIVQFHH FFEDSQNVYF TLELCSKNSL
MELNKQRGPL TEHEARFYTI QVAEGVKHLH NLQIIHRDLK LGNLFLNEHL QVKIGDFGLA
TFCEKNEKKM TRGGTPNYIA PEVLNETGHA FEVDIWAIGC ILYVLLFGSP PFESRRVQET
YVRIKNNDYV VPENASPTAN RLIRSLLDPV PDRRPTAEAV LLDQFFKTTI EPTYPPVHQQ
LHKEQDVKYF APINPVLPHV EEPISPIYQE VANEETSEIR RFVKTEQASS FGDELSQLQA
QISHILQNVV ASKNKSSTRF GLNHSPEATP IFWVSQWVHF PNHGIGYRLC ENSSGMLFND
NTQMKVNSAG NQLTFVDENN TEQFYTMNDQ VPMNLQTKIN IFSNVQSYMN THLEADTHLE
AEDQCVNKVP PLRNFARLPT IQNWFETKSA VIFHLSNGTV QINFLDHVKM VLCPLLKSVT
FIEENKRVST FTFANILTNS CPKKYLSRIE YAQAKIKLLR PTNNQEHVVY VDSPCRPTTS
NTAHGAPLAS SRYLA
