ID A0A151WMF3_9HYME Unreviewed; 863 AA.
AC A0A151WMF3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=polo kinase {ECO:0000256|ARBA:ARBA00012424};
DE EC=2.7.11.21 {ECO:0000256|ARBA:ARBA00012424};
GN ORFNames=ALC60_12054 {ECO:0000313|EMBL:KYQ48998.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ48998.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ48998.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ48998.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ48998.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; KQ982944; KYQ48998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151WMF3; -.
DR STRING; 64791.A0A151WMF3; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24345:SF92; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KYQ48998.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 275..527
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 672..736
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 774..848
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 61..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 97641 MW; 58477AB300FB1D74 CRC64;
MLPPSIIDVQ GAIPRDITIN SRGLLSETMC GTELRSTEVA ATCHVARYRE EFDETIRTVS
EPECSKRKID SAGTGSTRSV PDGRSRQFGF SKGSASLQSL VRRRSRRHGT SLPSEVELSS
RQVIYPAVPS DLLKDIGGGT AMFRNEEEAR TATPTSTLIY ATSSAQPSTS RTDNNLAQDV
STSASNVATT TGSNITSTTN GGRFGNVPVS LARTTSVAKA PGPSMPSSWN NSAEQESDYV
VDPVQGNAYY KGQFLGKPTH PGHTSRRTRY IDLVASRTLP VLGGGFARVY LMTDVSNGNQ
YACKIIPKNR MQRIHMQKIA REIMIHKELN HVNVVQMHHY FEDNLNVYML LEACPRKSLM
HVLKYRGKVT EPEARYYMKQ MVTGVAYIHS QKVVHRDLKP GNMFLSDRMI VKIGDFGLAT
RPDGQRRRVT ICGTPNYIAP EVLYKQAYSY EADVWALGCI LYALLVGQPP FDTATLKETY
ARICNNHYRE VDDSIASRSG QDLIRWLLQS NPELRPSLER VKEHVYLTKE YVPASLPHTC
CYQMPPASII EPPSSPSSVS TVARNPEIKA QLWQQSLVYP DSLRYQQTIK SLQKESKVSS
WLVRKLPKLP RFRQRLSSVL CPDHKKTGLV AQSMQMHRAL EACVPEMKRN NACNPPTVED
IVPLFVTKWI DYSNKYGLGF QLSDRSVGVL FNDNTKISYT HDRRRVEYMT TDDEMTRYHR
ERDVPAPLQK KLELLRHFTE YMDDFLTEGG ELKKYRAPPR QSKNACVPRM RRWLRTDKAI
VMELTVPLLQ VNFFVDHTKM VVSQESAGGR GYLITYIDTG RHASSYWLND LRDLGCTPDL
YERLYYVCKV TREFAELDNN TTA
//
