ID A0A1U8D3E9_ALLSI Unreviewed; 968 AA.
AC A0A1U8D3E9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, 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 Name=PLK4 {ECO:0000313|RefSeq:XP_014375802.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014375802.1};
RN [1] {ECO:0000313|RefSeq:XP_014375802.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_014375802.1; XM_014520316.2.
DR AlphaFoldDB; A0A1U8D3E9; -.
DR STRING; 38654.A0A1U8D3E9; -.
DR GeneID; 102387484; -.
DR KEGG; asn:102387484; -.
DR CTD; 10733; -.
DR eggNOG; KOG0575; Eukaryota.
DR InParanoid; A0A1U8D3E9; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000189705; Unplaced.
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|RefSeq:XP_014375802.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|RefSeq:XP_014375802.1}.
FT DOMAIN 24..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 591..704
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000259|PROSITE:PS51984"
FT DOMAIN 705..817
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000259|PROSITE:PS51985"
FT DOMAIN 891..955
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 374..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 968 AA; 107821 MW; 381565F498F4CABE CRC64;
MPRRRRSTPG SARGRAGDSS IQDFQVGNLL GKGSFAGVYR AVSCKTGLEV AIKMIDKKAM
HKVGMVQRVQ NEVKIHCQLK HPSILELFNY FEDCNYVYLI LEMCHNGEMS RYLKNRQKPF
SEEETRHFMH QIITGMLYLH SHGILHRDLT LSNLLLTSNM NIKIADFGLA TQLKMPHEKH
YTMCGTPNYI SPEIATRSAH GLESDVWSLG CMFYTLLIGK PPFDTDTVKN TLNKVVLADY
ETPAFLSGEA QDLIRKLLRK NPADRLSLSS VLDHPFMSRC NSARSKDSGT VEDSMDSGNA
TISTAFTGSS SISISGYMKE KKRFLVGQPL PNKLTLFPKN KNSSDASSDA SSSYNIWGIQ
GKETGVTGRG RTMQLTEERP HSRYLRRAHS SDRSGTSSSQ TQGVPDSVER CHSLELLSKP
RTGMMEHIDS YSSTNSYGDI PSIFKEKTSS SSGIQTQSNY LCPMKSSVGL LEQKTQTETM
QQWLGGMQTN AHLRQPADSI SLGIQNLHLC DHLDVQQEMS RDLWNDIKDK KNPDVSLDSA
CPINQFSVKK YASGLPCKQS KAQPASTFVL HPTSEQKKAW GKEPLGHQKP SLRSIVSPLS
AHRLKPIRQK TKNAVVSILD AGEVCMEFIK EQHSQEFVKE VLKISCDGSV ITVYHPNEGR
GFLLDDRPPS PPEDVCMYSF DSLPEKYWKK YQYAAKFVHL VRSKTPKVTF YTRYAKCMLM
ENFPTADVEV CFYDGAKIHK TAGITRVIEK SGKSYTLKEE NESVLKNEMQ IYMYHANEGH
RICLALEAAV LEEEKRNENV PFFPIIVGRK PGNTESPKAL MLPSVDADST GKATSLERNR
AVSSPSQAPN ISPSMVSYEG SALRTAVAET TCSSNQKECN SNSAQLVKSV FVKNVGWASQ
LTSGAVWVQF NDGSQLVAQA GVSSITYTSP NGQTTRYGEN EKLPEYIKEK LHCLSSILVM
FTNPAGPH
//
