ID A0A8K0P8V3_LADFU Unreviewed; 979 AA. AC A0A8K0P8V3; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 24-JUL-2024, entry version 12. 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=J437_LFUL015517 {ECO:0000313|EMBL:KAG8234949.1}; OS Ladona fulva (Scarce chaser dragonfly) (Libellula fulva). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Palaeoptera; Odonata; Epiprocta; Anisoptera; Libellulidae; Ladona. OX NCBI_TaxID=123851 {ECO:0000313|EMBL:KAG8234949.1, ECO:0000313|Proteomes:UP000792457}; RN [1] {ECO:0000313|EMBL:KAG8234949.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sampled in the wild {ECO:0000313|EMBL:KAG8234949.1}; RA Qu J., Murali S.C., Bandaranaike D., Bellair M., Blankenburg K., Chao H., RA Dinh H., Doddapaneni H., Downs B., Dugan-Rocha S., Elkadiri S., RA Gnanaolivu R.D., Hernandez B., Javaid M., Jayaseelan J.C., Lee S., Li M., RA Ming W., Munidasa M., Muniz J., Nguyen L., Ongeri F., Osuji N., Pu L.-L., RA Puazo M., Qu C., Quiroz J., Raj R., Weissenberger G., Xin Y., Zou X., RA Han Y., Richards S., Worley K., Muzny D., Gibbs R.; RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAG8234949.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sampled in the wild {ECO:0000313|EMBL:KAG8234949.1}; RA Murali S., Richards S., Bandaranaike D., Bellair M., Blankenburg K., RA Chao H., Dinh H., Doddapaneni H., Dugan-Rocha S., Elkadiri S., RA Gnanaolivu R., Hernandez B., Skinner E., Javaid M., Lee S., Li M., Ming W., RA Munidasa M., Muniz J., Nguyen L., Hughes D., Osuji N., Pu L.-L., Puazo M., RA Qu C., Quiroz J., Raj R., Weissenberger G., Xin Y., Zou X., Han Y., RA Worley K., Muzny D., Gibbs R.; RT "Ladona fulva Genome sequencing and assembly."; RL Submitted (OCT-2017) 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}. 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:KAG8234949.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KZ308860; KAG8234949.1; -; Genomic_DNA. DR Proteomes; UP000792457; Unassembled WGS sequence. DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell. DR GO; GO:0005813; C:centrosome; IEA:TreeGrafter. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0000776; C:kinetochore; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter. DR GO; GO:0000922; C:spindle pole; IEA:TreeGrafter. 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:0007052; P:mitotic spindle organization; IEA:TreeGrafter. 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; IPR000959; POLO_box_dom. 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; PS50078; POLO_BOX; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212}; KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212}; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000792457}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}. FT DOMAIN 15..268 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 601..716 FT /note="Cryptic POLO box 1 (CPB1)" FT /evidence="ECO:0000259|PROSITE:PS51984" FT DOMAIN 717..827 FT /note="Cryptic POLO box 2 (CPB2)" FT /evidence="ECO:0000259|PROSITE:PS51985" FT DOMAIN 890..967 FT /note="POLO box" FT /evidence="ECO:0000259|PROSITE:PS50078" FT BINDING 44 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 979 AA; 110413 MW; A21007C4B34DE5C0 CRC64; MATSQSSFGE SIEEYEVLNL LGKGGFASVY RAKCSKSGLE VAIKMIDKKL MKAAGMVERV RQEVAIHSRL KHPAVLELYT FFEDTNYVYL VLELCHNGEL QRFLKSNNKI LCEEDACHVF RQVVEGLIYL HSHNILHRDL TLANLLLSKD MQVKIADFGL ATQLSRPDEK HLTMCGTPNY ISPEVATRSS HGLEADVWGL GCMLYTLLIG RPPFDTDAVK STLTRVVMAD YQLPSHLSPE ARDLIDLLLK KNPKERIKLR AILDHPFMKK NQKQYEYLQK KWMTRESDSG MGTMSTDPCA GLDSLTTNGS NKERIISMYS QQSDDEFQSK LFSRADGKAT HSVLSQEKYT FPSRTEDPCN SSTSYLRCKF GNEEIKNLES RSTLYNSILK NDRDHSLERN KSCVANCCGN NRSLYSQATL SKCQCCSQSI HELGHAGDPS AKVSSFHSCK QVSDESLKEA NVCRSDAANV VKRQAMNCTR SCYSDGLLSC RMANVHLCER LGHSHCEAVE SQWKSGHAHY SCHNADVCAT DRSKRELPSE ERCHHKWPDP TGKQPDNFRT VKSSNGPMND YQDDNNVFPE KKSSIMMEQK TKPPEKAERR VLNGLTPALN TYRLQPTRHR TKNAVLSILD SGEVCIEFVK KRGGEERVID VCRISTDGMR VVLYQPNSSK GCPLENFPPE LPKQGTDAIY SYESLPQKHW KKYLYATRFI DLVKAKTPKV TYYCEKAKCL LMENSPDPDF EACFYEGGKI VKSKNEVKLI DAAGKSTVMQ MDSKDKSLNV SIMWNQFEQY YNHCIALEKS LTELADKAGV SCFPIIVGRR PPSSVKAVLQ DKENMPNNQI NISPQNAMLH SFETSSATSM HVNASYGNSA ISSSRFNIKS TNSEIKKTEP LKQVLVPSIG VASQYPSGDL KVEYLDGSQI IINSHKATTE YVSTDGKTVF YQQKDLLPFH IREKLSLMPK VLEHLMNGQE RRPQTRGLR //