ID S9VSN1_9TRYP Unreviewed; 679 AA.
AC S9VSN1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=STCU_06271 {ECO:0000313|EMBL:EPY26200.1};
OS Strigomonas culicis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY26200.1, ECO:0000313|Proteomes:UP000015354};
RN [1] {ECO:0000313|EMBL:EPY26200.1, ECO:0000313|Proteomes:UP000015354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23560078;
RA Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA de Souza W., Schenkman S., de Vasconcelos A.T.;
RT "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT Family.";
RL PLoS ONE 8:E60209-E60209(2013).
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:EPY26200.1}.
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DR EMBL; ATMH01006271; EPY26200.1; -; Genomic_DNA.
DR AlphaFoldDB; S9VSN1; -.
DR EnsemblProtists; EPY26200; EPY26200; STCU_06271.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000015354; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000015354};
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 54..305
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 474..553
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 601..667
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 679 AA; 75629 MW; E35B5C7EFCD8A3F6 CRC64;
MLRMNTNIRP GVSTGANRHE RHTGLTASDL PKPTFQPGSY VYELDLATGL ANKLRVGRIL
GRGGFAKCYE VSDAHGSYAL KAINRTSLEK PKTLQKLHTE IAIHRRMKHK HIVNFIRTFK
DRYYVYILLE KCDNGTLMDL IKMRALTVPE TQYIMLQCLS AMQYMQDQYV IHRDLKPGNI
MLDSELNVKI GDFGLAAELQ YDGERKRTIC GTPNYIAPEI IDRKSHGHSY EVDAWSLGVI
LFTLLTGNPP FQMEDVESTY ARIRQCKYEF PAALSPHARD LVQHILQSSP SQRPTLLDIR
THAFFCAPPP PLLPPSSLAT FGLAVPDRQR RGTAPPESLA HAPPAREAVA PNRDAAVGPG
GAREVLRPIS TNLPGRTAKE ARPVMPPPTG GRRGTSPALL GLQPEPAPPS PAEGDAPPAR
GARAAERAED EDEKDNLAAL HEKLHQTLCG DAPEEQDDAV GPGPGVWVTE CADFSAKYGL
CYRLNTGHTG AHFNDSTKMV WEPITDRVEY YARVKVELPQ RGGETALFAR DQLEAFHMSQ
HPGTLDKKVT LIKYFKSYLG RARNTKDKVE VVSCSAYVSA QPARITDPHV GEDFVYVKRW
LRTPEAIVFR LSNKTVQVCF NDRAEVILSS EWKVVTYTDP SGKRQTLPLS SVATQSEEAA
DRLRFTKNIL YQLIKDHCL
//
