ID T2MFR1_HYDVU Unreviewed; 619 AA.
AC T2MFR1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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};
GN Name=PLK1 {ECO:0000313|EMBL:CDG70750.1};
GN Synonyms=LOC100205568 {ECO:0000313|RefSeq:XP_002162247.3};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG70750.1};
RN [1] {ECO:0000313|EMBL:CDG70750.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG70750.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(2013).
RN [2] {ECO:0000313|RefSeq:XP_002162247.3}
RP IDENTIFICATION.
RC STRAIN=105 {ECO:0000313|RefSeq:XP_002162247.3};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|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 EMBL; HAAD01004518; CDG70750.1; -; mRNA.
DR RefSeq; XP_002162247.3; XM_002162211.3.
DR EnsemblMetazoa; XM_002162211.3; XP_002162247.3; LOC100205568.
DR EnsemblMetazoa; XM_047268488.1; XP_047124444.1; LOC100205568.
DR OMA; IQIHKSM; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000694840; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
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}; Reference proteome {ECO:0000313|Proteomes:UP000694840};
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 47..299
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 432..495
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 529..598
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT BINDING 76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 619 AA; 71285 MW; 455F7B64ED1BACF5 CRC64;
MNKISNTEKY RQKMAEKPKI TTLPVDKITP APELAEEIVN PDTGVVYIRG KFLGKGGFAK
CYEMTDKVTN SVFAGKIVPK SLLTKSHQRD KMAQEIQIHR ELSYKHIVGF HSYFEDAHYV
YIILELCNKR SMMELYKRRK AVTEPEVRFY MKQIVDAVCF LHSKHIIHRD LKLGNLFLND
DFQVKIGDFG LATRVEFDGE RKKTLCGTPN YIAPEVLCKK GHSYEVDVWS VGCILYTLLV
GKPPFETMSL KETYHRIKKN EYYIPAKVPH SAQMLIIKML RPEPETRPTM KECQEDRFFT
DGFTPISLPN SSLTMAPRFA SAQYYSDRRP LSDANRDLGK AVLSNIPESS TTVDKNNVSR
AVFVKDGLGH EIDEDPAEET DGEPDDHYLG HLQKLLDRVL ESRPADRDSI NMDEAEDPAL
TPVSWVSKWV DYSDKYGLGY QLSDGSVGVL FNDATRLLMH EDEKSLQYID KLNKETFFTI
DNAPPNMQKK KTLLEYFHDY MNEHLLKTGS GVATKGMESA RLPYLRSWFR TRSGIILHLN
IGILQINFFQ DHTKVIICPK MDAFSYIDEN RNFRTYKLSG IEKHGCTREI FVRLRYAKTM
VERLSKKLAE EKKEKLSAI
//
