ID A0A1I8CDM7_9BILA Unreviewed; 584 AA.
AC A0A1I8CDM7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Serine/threonine-protein kinase PLK {ECO:0000256|RuleBase:RU361162};
DE EC=2.7.11.21 {ECO:0000256|RuleBase:RU361162};
DE AltName: Full=Polo-like kinase {ECO:0000256|RuleBase:RU361162};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000344000.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000344000.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000344000.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00000540};
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; Evidence={ECO:0000256|ARBA:ARBA00000856,
CC ECO:0000256|RuleBase:RU361162};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000256|RuleBase:RU361162}.
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DR AlphaFoldDB; A0A1I8CDM7; -.
DR WBParaSite; RSKR_0000344000.1; RSKR_0000344000.1; RSKR_0000344000.
DR Proteomes; UP000095286; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:UniProt.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361162};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU361162};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361162}.
FT DOMAIN 24..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 379..442
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 476..545
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 584 AA; 66440 MW; 1A7812BEADB3370A CRC64;
MTDRSKAVKE VPMHIINASK HTTYQRGKFL GKGGFARCYE LISPDTKETL AGKVVAKTLL
TKRHQKDKMA QEIDIHRQLS HHNVVQMLDF FEDDDNVYIL LELCPRRSLM ELHKRRKAVT
EPEARYFTKQ VTEGCVYLHG RNIIHRDLKL GNLFLSELMD VKIGDFGLAT IVGPDGERKK
TLCGTPNYIA PEMLDKRGHS YEVDIWAIGC IVYTLLVGKP PFETMTLKDT YNRIKANNYS
LPPVVSQDAK HLIRFLLHAD PSQRPTIKQV LKFEFFLRGH LPARLPTSCL TMAPKFVNSP
SRVENPAVVT AVEVPRIPTC LPIASPAIKD KEGWYLNELY SQLSNLLKQS VPIVGVDDME
DALHPASSPV FFISKWVDYS DKYGLGYQLS DNSVGVLFND STKLVLDAAG EQIQYCERDN
AEHYFTMRDY PTSLEKKVTL LKYFRRYMRE HLVRAGATTV KEGDEIARLP VLRTWFRTKA
AIVLHLTNGT LQINFFTDHV KLIVCPHMGA VTLIDADRSL RTFKFDLLAT VGADTALVKK
LEYTQHIVDR MLNPNKNGGR FNDLTSIEAA HPPDVRHFRD SNNK
//
