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Database: UniProt
Entry: A0A195D240_9HYME
LinkDB: A0A195D240_9HYME
Original site: A0A195D240_9HYME 
ID   A0A195D240_9HYME        Unreviewed;       754 AA.
AC   A0A195D240;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Serine/threonine-protein kinase PLK4 {ECO:0000256|ARBA:ARBA00020245};
DE            EC=2.7.11.21 {ECO:0000256|ARBA:ARBA00012424};
DE   AltName: Full=Polo-like kinase 4 {ECO:0000256|ARBA:ARBA00030332};
DE   AltName: Full=Serine/threonine-protein kinase SAK {ECO:0000256|ARBA:ARBA00030429, ECO:0000256|ARBA:ARBA00030924};
GN   ORFNames=ALC62_02146 {ECO:0000313|EMBL:KYN06911.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN06911.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYN06911.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYN06911.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN06911.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) 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};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}.
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DR   EMBL; KQ976948; KYN06911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195D240; -.
DR   STRING; 456900.A0A195D240; -.
DR   Proteomes; UP000078542; Unassembled WGS sequence.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
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   GO; GO:0051726; P:regulation of cell cycle; IEA:UniProt.
DR   CDD; cd13114; POLO_box_Plk4_1; 1.
DR   CDD; cd13115; POLO_box_Plk4_2; 1.
DR   CDD; cd13116; POLO_box_Plk4_3; 1.
DR   Gene3D; 2.40.50.930; -; 1.
DR   Gene3D; 3.30.1120.120; -; 1.
DR   Gene3D; 3.30.1120.130; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR047108; Plk4-like_POLO_box_2_sf.
DR   InterPro; IPR033699; POLO_box_Plk4_1.
DR   InterPro; IPR033698; POLO_box_Plk4_2.
DR   InterPro; IPR033696; POLO_box_Plk4_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR046437; Ser_Thr-PK_POLO_box_1_sf.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF94; SERINE_THREONINE-PROTEIN KINASE PLK4; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF18190; Plk4_PB1; 1.
DR   Pfam; PF18409; Plk4_PB2; 1.
DR   SUPFAM; SSF82615; Polo-box domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51984; CPB1; 1.
DR   PROSITE; PS51985; CPB2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KYN06911.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078542};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          33..287
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          400..513
FT                   /note="Cryptic POLO box 1 (CPB1)"
FT                   /evidence="ECO:0000259|PROSITE:PS51984"
FT   DOMAIN          514..620
FT                   /note="Cryptic POLO box 2 (CPB2)"
FT                   /evidence="ECO:0000259|PROSITE:PS51985"
FT   REGION          304..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   754 AA;  85899 MW;  F29FE5043BBE6471 CRC64;
     MVIDNRQRPF ECGAMRCLMP AISAGFGEHI EEYEVLNLLG KGGYGSVYRA RCLRSGMEVA
     IKMIDKKLMQ ANGMMDRVRQ EVEIHIRLKH PAILEAYTCF ENANYVYLVL ELCHNGELQR
     YLKAQGTKTL SEEHAAYIIK QVVQGLLYLH SYQILHRDLS LSNLLLTKDM QVKIADFGLA
     TQMSKPDEKH LTMCGTPNYI SPEVATRSSH GPEADVWSLG CMLYTLLVGK PPFETDAIKS
     TLTRVVMADY VMPLHLSDNA RDLIDKLLKK NPKDRIRLRD IHKHAFIMNI EKNKLHNERN
     NTSKNPFTDM MDSGLGKTLS SYGRSKMRSR SEERMSTLPM MPMVNDSLIS ISRGRAFLQN
     EQYGNYNVYN ESEKPRLMER HKPRKENIVE NRSVDGTEKS TKLQVSSLNS NRLEPKRHRT
     KNAILTILDN GEVCIEFIKR RNGTERINEV CRISGDGLRI VLYKLNPTVE IGMQPPPLPN
     RGADSIYSYE NLPTCHHRKY VYAFRFVKLV QAKTPKLTLY TQRSKCLFME NGPQPDCEVH
     FYNGIKVVRI DGVVKITDNN RATFVEGAFP SHLETYYEHY SESYQRCLLL ESTLASLEAA
     TGHSCFPVII GRRPNTILSD SPYLQGKENI LHTQSPVMPS FDASCSVMST GTSRSRKMNS
     IRNSNQNTKI AVPGIGFATK LLSGHIRVDY KDGSALIVSP QSHNSDIIYE SSDGIVTRYN
     RHHQQNLEIP VKEKLLQLPT IIKYFVEPMH KGIR
//
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