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Database: UniProt
Entry: A0A401SRM0_CHIPU
LinkDB: A0A401SRM0_CHIPU
Original site: A0A401SRM0_CHIPU 
ID   A0A401SRM0_CHIPU        Unreviewed;       994 AA.
AC   A0A401SRM0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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};
DE   Flags: Fragment;
GN   ORFNames=chiPu_0011492 {ECO:0000313|EMBL:GCC33026.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC33026.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC33026.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
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:GCC33026.1}.
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DR   EMBL; BEZZ01000480; GCC33026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401SRM0; -.
DR   STRING; 137246.A0A401SRM0; -.
DR   OMA; NIVERCH; -.
DR   Proteomes; UP000287033; Unassembled WGS sequence.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; 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   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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          10..276
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          615..728
FT                   /note="Cryptic POLO box 1 (CPB1)"
FT                   /evidence="ECO:0000259|PROSITE:PS51984"
FT   DOMAIN          729..842
FT                   /note="Cryptic POLO box 2 (CPB2)"
FT                   /evidence="ECO:0000259|PROSITE:PS51985"
FT   DOMAIN          914..978
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          280..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:GCC33026.1"
SQ   SEQUENCE   994 AA;  110770 MW;  B607D4757D8C5FB3 CRC64;
     LVVGVNGGFF ENGGIVFRGG WREVARVLTS YSVPWGGAAV NGMATVCIGD TIKIDKKAMH
     KVGMVQRVRN EVEIHCQLKH PSILELYNYF EDDNYVYLVL EMCHNGEMSR YLKNRKATFS
     EDEARHFMHH IVTGMLYLHS HGILHRDLTL SNLLLTSDMN IKIADFGLAT QLKMPNEKHF
     TMCGTPNYIA PEIATHSAHG LESDVWSLGC MFYTFLVGKP PFDTDTVKHT LNKVMLADYK
     MPTFISNEAQ DLIYQLLRKN PEDRISLSSV LDHSFMLKCP SSRSKSSETV EDSMDSGHAT
     ISTGYTTGTG SSGASTMGRL QLKTKQVIGQ FLPNKMAVIT SHNRLNNSSM EGSAVFSDKS
     IQNSEIIRAD RGRIVQIAEE ERPHSRWLRR AHSTDRSGTF QSQITEKPGS TLERCHSVDA
     LTISARPRMY SPANLYGDGY IDNQQVNKDS SDIGGSHDKS TISPPVKQAA KSKVTQEAES
     NGPFLEQLSQ IGMTHRWFED GQAHNAPFKT VMDVSAESST SGSFQCGRKQ QVMKEVISAS
     TWGKHPSNQV KNDSFYQESC FKAQMGIRKY DGVLRPHSAK AGNEQADVPY NCRQVLKPQG
     FIQQERQPSE NRSKMLQELV SPLRAHRLKP IRQKTKNAVV SILDSEEVCM ELLKGSGTQE
     RVKEVLRISS DGSMIHIYYP NEGKGFPLDD RPPSPPEDVF VYRFDNLPEK YWKKYQYASK
     FVHLVRSKTP KVTLYTKYAK CMLMENSPQA DVEVCFYDGA KINKSSEFLR IIEKSGKSHT
     YKGTKINGPS EEINSYMEHA HEAHQTCLEL ESIIAVQDER KEMQVSFFPI IIGRRPSSTD
     PMLSPAPSVG SKSAVGEQPQ IQHIFSSQAT SITPSICSCE SSSLTTITVE KNKSAPSTQT
     VVSPSPGQVL KSVFVPNVGW ASQLISGEVW VQFNDGSQLL VQAGVASVIY TSPQGQAIRY
     GQNEKIPDHV KGKLQCLSSI LGLLANQTNQ HTIQ
//
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