PLK_DICDI
ID PLK_DICDI Reviewed; 978 AA.
AC Q86HN7; Q555F6;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable serine/threonine-protein kinase PLK;
DE EC=2.7.11.1;
DE AltName: Full=Polo-like kinase;
GN Name=PLK; ORFNames=DDB_G0274503;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION.
RX PubMed=15548420; DOI=10.1016/s0074-7696(04)41003-1;
RA Graef R., Daunderer C., Schulz I.;
RT "Molecular and functional analysis of the dictyostelium centrosome.";
RL Int. Rev. Cytol. 241:155-202(2004).
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=2.7.11.1;
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=2.7.11.1;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AAFI02000012; EAL70144.1; -; Genomic_DNA.
DR RefSeq; XP_644113.1; XM_639021.1.
DR AlphaFoldDB; Q86HN7; -.
DR SMR; Q86HN7; -.
DR STRING; 44689.DDB0216332; -.
DR PaxDb; Q86HN7; -.
DR EnsemblProtists; EAL70144; EAL70144; DDB_G0274503.
DR GeneID; 8619543; -.
DR KEGG; ddi:DDB_G0274503; -.
DR dictyBase; DDB_G0274503; plk.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; Q86HN7; -.
DR OMA; SNEPQEP; -.
DR Reactome; R-DDI-156711; Polo-like kinase mediated events.
DR Reactome; R-DDI-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-176412; Phosphorylation of the APC/C.
DR Reactome; R-DDI-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DDI-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DDI-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DDI-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-DDI-68884; Mitotic Telophase/Cytokinesis.
DR Reactome; R-DDI-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q86HN7; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005813; C:centrosome; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:dictyBase.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR Gene3D; 3.30.1120.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50078; POLO_BOX; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..978
FT /note="Probable serine/threonine-protein kinase PLK"
FT /id="PRO_0000362029"
FT DOMAIN 163..416
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 703..772
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 831..900
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 19..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 497..555
FT /evidence="ECO:0000255"
FT COILED 592..630
FT /evidence="ECO:0000255"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 169..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 978 AA; 113599 MW; B03A677136543152 CRC64;
MVSINQNFKL PISMNSQPIQ IQQQQFKQPQ QQPQQKSNSC FSDQENYPAN IQPSSSTSSS
SSSSIHITKS MVIRPPLESN QPQPQQQQQQ QQTLQQIHHQ QVQLQQQQSL QMQQQQLQQQ
QQQQQQQQMP PPQSLPNKSN EPQEPIVVYE TIRSGDSKRL KEYRQGEFLG KGGFAKCYLM
TEVETNRIYA AKIIPKSTLQ KTRARSKLKS EIKIHSSLSH ENIVKFEHCF ENEENVYILL
ELCNQKTVMD IHKKRKYLME YETKYYVYQV IMAVQYLHNN NIIHRDLKLG NLFIDNMRIK
LGDFGLSTKV EHGERKKTIC GTPNYIAPEI LDNSNGHSYE VDVWSIGIIL YTLLIGKPPF
ETSDVKHTYQ RIKQNQYSFP DEPIISHYGK SLIISILNPV PEQRPNLTQI LEHDFFTYSP
IPKYLPVSSL TTAPSQSTIN QNMGRPLSEK TNIVNQQHLQ LAGTTSPTKN NNHHYQQYQQ
QPQQQYNNNY QQSFSPKKQI NNMNNNNNNN NNNNNNNNNN NNNNNNNLKQ YNYSNNNINY
NNNNNNINNQ FANLSPNSQQ KLSEVENDDF HYRKLRRLEK MKENDLKTQL LIKQQYTNMN
ENQQQQQQQQ QQQQQQQQQQ QRVNNNINNN GNTVTVTTGN NTVNVQIKEL ETKIANNHIS
DSPPVSSNNN YPQQIQKQQP NFNNEFYLGM PNNLVYISQY ADFTNKYGLA YVLSNSYVGA
YFNDSTKIVT LIESEIAYYM EHAKGTDGDG RRVLNVTQQH PHDTQKKVTL IKYFLNHFTN
SDTTNLLINT GATSSSINNN NNNNVENVTN NNNNNSNNSS NINPIYVKKW IKFDNGIAFR
LSDKTIQVNY LDKSRIIVSS KDMVTFVPYR GQIITGTLNY FKNGDKKISE KIKYIYGTLS
NNLYSKKPES SFQQLPQQQY QQPQHYQQQT QQPQPQPQQQ QLPQQLPQPQ QSPAKQHQYQ
PNQIQYQQSI PQPQLINQ
