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Database: UniProt
Entry: A0A1J4K040_9EUKA
LinkDB: A0A1J4K040_9EUKA
Original site: A0A1J4K040_9EUKA 
ID   A0A1J4K040_9EUKA        Unreviewed;       618 AA.
AC   A0A1J4K040;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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   ORFNames=TRFO_06384 {ECO:0000313|EMBL:OHT04096.1};
OS   Tritrichomonas foetus.
OC   Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC   Tritrichomonas.
OX   NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT04096.1, ECO:0000313|Proteomes:UP000179807};
RN   [1] {ECO:0000313|Proteomes:UP000179807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA   Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA   Tasca T., Bogo M.R., de Souza W.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OHT04096.1}.
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DR   EMBL; MLAK01000804; OHT04096.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4K040; -.
DR   VEuPathDB; TrichDB:TRFO_06384; -.
DR   OrthoDB; 5471704at2759; -.
DR   Proteomes; UP000179807; Unassembled WGS sequence.
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   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}; Reference proteome {ECO:0000313|Proteomes:UP000179807};
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          53..309
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          444..480
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   DOMAIN          540..609
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          368..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   618 AA;  71269 MW;  FD3789784D29F122 CRC64;
     MRIQFLWTFR FEIFFSEKLL KFNKFGRKKK MLRVVTVPLT ISRKREFGST IIYKRHEELG
     RGGFAAVYRV TNQATGEEYA LKAVPKERVE KPKSLEKLKC EIAIQRSLNH QNVLKSYDNF
     EDFQNYYILL EYAPNGSVKD MVKKAGHLSE YETARILREV MSGLCYLHDN RIIHRDLKLE
     NFLIGKDGKV KIADFGLSTR LDFDDERKYT VCGTPNYLSP ELLTNSSKGH SYEVDIWTIG
     VCAFAMLTGK PPFETPRRKL TYEHIKNCKY SFPPDIPLSA VARDFVKVIL QIKPEKRPNA
     QDVALHPLLT QLPNKYKRIN HIPLETKPTY ETKKITPAID SKKPLLDEKK DFKKPITDLK
     KPIIRTNDLA RKNPSPTPIN NNNFNNNNIK NSNNNGNNNI HINNAHNENG AGNGTPGGGL
     ESPIQNGEPM VTMPKNCVSR FCDHSDKYGL GYMLIDGTIG ACFNDWSRMV MDPFETFVQY
     WESYQTVTPE IMDPKTGAQT KKLALIRRFA ESLKKTKSMY ELPAKHFSSA TPMKHVKYWM
     RNDDATLFRM DDRNIQVNFN DRTKLVIFWN NKKMMMVHSI KEAGKLVALT HVNSQQPNSE
     ERKRYNVARS MLAAMSVR
//
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