ID A0A151PEB0_ALLMI Unreviewed; 955 AA.
AC A0A151PEB0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 Name=PLK4 {ECO:0000313|EMBL:KYO47368.1};
GN ORFNames=Y1Q_0001183 {ECO:0000313|EMBL:KYO47368.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO47368.1};
RN [1] {ECO:0000313|EMBL:KYO47368.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO47368.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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:KYO47368.1}.
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DR EMBL; AKHW03000422; KYO47368.1; -; Genomic_DNA.
DR RefSeq; XP_006274064.1; XM_006274002.3.
DR AlphaFoldDB; A0A151PEB0; -.
DR STRING; 8496.A0A151PEB0; -.
DR GeneID; 102561880; -.
DR KEGG; amj:102561880; -.
DR CTD; 10733; -.
DR eggNOG; KOG0575; Eukaryota.
DR OrthoDB; 5471704at2759; -.
DR PhylomeDB; A0A151PEB0; -.
DR Proteomes; UP000050525; 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 CDD; cd13114; POLO_box_Plk4_1; 1.
DR CDD; cd13115; POLO_box_Plk4_2; 1.
DR CDD; cd13116; POLO_box_Plk4_3; 1.
DR CDD; cd14186; STKc_PLK4; 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:SF89; 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:0000313|EMBL:KYO47368.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:KYO47368.1}.
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 579..692
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000259|PROSITE:PS51984"
FT DOMAIN 693..805
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000259|PROSITE:PS51985"
FT DOMAIN 878..942
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 364..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 955 AA; 106355 MW; 47FF38BF48F0572A CRC64;
MAACIGEKIE DFQVGNLLGK GSFAGVYRAV SRKTGLEVAI KMIDKKAMHK VGMVQRVQNE
VKIHCQLKHP SILELYNYFE DCNYVYLILE MCHNGEMSRY LKNRQKPFSE EETRHLMHQI
ITGMLYLHSH GILHRDLTLS NLLLTSNMNI KIADFGLATQ LKMPHEKHYT MCGTPNYISP
EIATRSAHGL ESDVWSLGCM FYTLLIGKPP FDTDTVKNTL NKVVLADYET PAFLSGEAQD
LIRKLLRKNP ADRLSLSSVL DHPFMSRCNS ARSKDSGTVE DSMDSGNATI STAFTGSSSI
SISGYMKEKK RFLVGQPLPN KLTLFPKNKN SSDASSDASS SYNIWGIQGK ETGVTGRGRT
MQLAEERPHS RYLRRAHSSD RSGTSSSQTQ GVPNSVERCH SLELLSKPRT GMMEHIDSYS
STNSYGDIPS IFKEKTSSSS GIQTQSNYLC PMKSSVGLLE QKTQTETMQQ WLGGMQTNAH
LRQPADSISL GIQKFHLCDH LDVQQEMSRD LWNDIKDKKN PDVSLDSACP INQFSAKKYA
SGLPCKRSKA QPASTFVLHP TSEQKKAWGK EPLGHQKPSL RSILSPLSAH RLKPIRQKTK
NAVVSILDAG EVCMEFIKEH HSQEFVKEVL KISCDGSVIT VYHPNEGRGF LLDDRPPSPP
EDVCMYSFDN LPEKYWKKYQ YAAKFVHLVR SKTPKVTFYT RYAKCMLMEN FPTADAEVCF
YDGAKIHKTA GITRVIEKSG KSYTLKEENE SVLKNEMQIY MDHANEGHRI CLALEAAVLE
EEKRNENVPF FPIIVGRKPG NTESPKALML PSVDADSTGK ATSLERNRAV SSPSQAPNIS
PSMVSYEGSA LTTAVAETCS SNQKECNSNS AQLVKSVFVK NVGWASQLTS GAVWVQFNDG
SQLVAQAGVS SITYTSPNGQ TTRYGENEKL PEYIKEKLHC LSSILVMFTN PAGPH
//
