ID A0A095A3B4_SCHHA Unreviewed; 783 AA.
AC A0A095A3B4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 Flags: Fragment;
GN ORFNames=MS3_08529 {ECO:0000313|EMBL:KGB40074.1};
OS Schistosoma haematobium (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB40074.1};
RN [1] {ECO:0000313|EMBL:KGB40074.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22246508; DOI=10.1038/ng.1065;
RA Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA Wang J., Gasser R.B.;
RT "Whole-genome sequence of Schistosoma haematobium.";
RL Nat. Genet. 44:221-225(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 ---------------------------------------------------------------------------
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; KL251362; KGB40074.1; -; Genomic_DNA.
DR RefSeq; XP_012799832.1; XM_012944378.1.
DR AlphaFoldDB; A0A095A3B4; -.
DR STRING; 6185.A0A095A3B4; -.
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 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 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: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; 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:0000313|EMBL:KGB40074.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:KGB40074.1}.
FT DOMAIN 1..152
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 350..498
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000259|PROSITE:PS51984"
FT DOMAIN 499..630
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000259|PROSITE:PS51985"
FT DOMAIN 693..766
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 442..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGB40074.1"
SQ SEQUENCE 783 AA; 87776 MW; A5B40FDAC6CA402E CRC64;
ARHYLKQLIS GLLYLHSHNI LHRDLTLANL LLTKDMKVKI ADFGLATKIE PGEDHKTMCG
TPNYISPEVA SHNQQGLETD VWSLGCMFYT LIVGHPPFDT REVRSTLNRV LAVDYELPST
VSSEAADLIN SLLRREPQER LKLKAIIQHP FMLKKSRPQR HMKTSNDSGI DSIYRTPLGH
LSNSLKSHHL RKVKCNESNT HSCNTPISTA ISDTQCDTSI PYFLAPAQSH EVTSWDPAIN
VHEDVQRPTE QLNTHPNIRH TCYSDGAFEQ SRSVFSQVSD SEIKKSLLSN SNQLVNSTVN
RPYNNLSGLP LSSPSHPTAT EIITTQHADC VKGDTNISRS ELSSKSSSKP FSAHPLPLNT
FRLKPMRTYT RLAVINILQD ESACLEFLGG SAKTRQNQTS VTKSSQNLRV VEVMGINNTG
QNILIYRPNM GKGVPLNVQG LGDPSQSNLA NSETTNFGSP PPASPGDPLE FYTLNTLPQK
YWRKYQFISK FVQMVRAHTP KVTLYTNKVK CMLMENGPSG DFVTEFHNDG TRVLCTSDGS
LRITQTTEQD NSLKVKTNIT PTTITLDSNR SLSTLSPEIR KLIDYVYACR DHCRKIEQLL
ARMDSEDTSV LSCSSFPVIL GHRPNTGFNL ITSSQNYPKP TSFTNVITNE LGDQVSLSSQ
LYNLISDCLK EKYKTPLSEN QAKHDHLPTN AVFVPNVGWA SQFSDDRLQV QFNDGAKLLL
VYNRTLVYSI HYSAPPEHNQ ELPKEYVYNT SDPLPDHIYR RLEVMPTVIN QLRTVANKNK
LIS
//
