CDC5_ENCCU
ID CDC5_ENCCU Reviewed; 472 AA.
AC Q8SWM6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable cell cycle serine/threonine-protein kinase CDC5 homolog;
DE EC=2.7.11.21;
GN Name=CDC5; OrderedLocusNames=ECU01_0630;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11157783; DOI=10.1101/gr.164301;
RA Peyret P., Katinka M.D., Duprat S., Duffieux F., Barbe V., Barbazanges M.,
RA Weissenbach J., Saurin W., Vivares C.P.;
RT "Sequence and analysis of chromosome I of the amitochondriate intracellular
RT parasite Encephalitozoon cuniculi (Microspora).";
RL Genome Res. 11:198-207(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
RN [4]
RP PREDICTION OF FUNCTION.
RX PubMed=17784954; DOI=10.1186/1471-2164-8-309;
RA Miranda-Saavedra D., Stark M.J.R., Packer J.C., Vivares C.P., Doerig C.,
RA Barton G.J.;
RT "The complement of protein kinases of the microsporidium Encephalitozoon
RT cuniculi in relation to those of Saccharomyces cerevisiae and
RT Schizosaccharomyces pombe.";
RL BMC Genomics 8:309-309(2007).
CC -!- FUNCTION: Protein kinase required for the cell cycle where it is
CC involved in mitotic exit. Required to form a bipolar spindle, the actin
CC ring and septum. Functions upstream of the whole septum formation
CC pathway, including actin ring formation (regulated by late septation
CC genes) and septal material deposition (regulated by early septation
CC genes). Behaves as a 'septum-promoting factor', and could also be
CC involved in inducing other late events of cell division (By
CC similarity). {ECO:0000250}.
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000250}.
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; AL391737; CAD24933.2; -; Genomic_DNA.
DR RefSeq; XP_965898.1; XM_960805.1.
DR AlphaFoldDB; Q8SWM6; -.
DR SMR; Q8SWM6; -.
DR STRING; 284813.Q8SWM6; -.
DR PRIDE; Q8SWM6; -.
DR GeneID; 860238; -.
DR KEGG; ecu:ECU01_0630; -.
DR VEuPathDB; MicrosporidiaDB:ECU01_0630; -.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; Q8SWM6; -.
DR OrthoDB; 507604at2759; -.
DR Proteomes; UP000000819; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.30.1120.30; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50078; POLO_BOX; 1.
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; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Mitosis; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..472
FT /note="Probable cell cycle serine/threonine-protein kinase
FT CDC5 homolog"
FT /id="PRO_0000384418"
FT DOMAIN 24..279
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 314..384
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 472 AA; 54024 MW; 2CDFA9A519854D70 CRC64;
MSTKVELYME IGTVITDLEY HTKYMLKKLL GRGAYAQCYL AEIESGEQYA MKVVRLKDIK
SRKVHEKLES EIAIHSKLDN PNVVKMYRSF RSSEYVFMVL ELCERGALDA LLKRNGKLKE
RHVARFVKQT VEGLIYLHNS VSVVHRDLKL GNLFLDSKFN VKIGDFGLSA VIKDGEKKVT
MCGTPNYIAP EVLFGKASGH SFEADIWSLG VIIYTLLVGV PPFQKKNVED IYKMIKLNNY
IFPENCDLSS EAIDLITQIL NTNPLERPTL EHILSHKFLS KKEHFLMKIY RNLMTNRTEE
GVVDTDYVLF SIPVTKLRGV GYVLKSGVYG IYFSDHRNLM LKPNRKSVIY LNSTIESGKR
VFYKEEHLVE KIPAEIAESY KGLQYFIRTF DNGFSFLDVE PCFIVKIRKI ECGFLFVMAD
STIVFDFVDG WRVVLSRCGE RVSCYNGLGL ASFNQEIRGR CIEILRGCLG CG
