ID   CDC71_ENCCU             Reviewed;         351 AA.
AC   Q8SR85;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable cell division control protein 7 homolog 1;
DE            EC=2.7.11.1;
GN   Name=CDC7-1; OrderedLocusNames=ECU08_1960;
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=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   [2]
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: Serine/threonine-protein kinase. Needed for the initiation of
CC       DNA synthesis during mitosis as well as for synaptonemal complex
CC       formation and commitment to recombination during meiosis (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=2.7.11.1;
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDC7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AL590448; CAD26498.1; -; Genomic_DNA.
DR   RefSeq; NP_597322.1; NM_001041931.1.
DR   AlphaFoldDB; Q8SR85; -.
DR   SMR; Q8SR85; -.
DR   STRING; 284813.Q8SR85; -.
DR   GeneID; 859744; -.
DR   KEGG; ecu:ECU08_1960; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_1960; -.
DR   HOGENOM; CLU_000288_118_2_1; -.
DR   InParanoid; Q8SR85; -.
DR   OMA; VELAHIF; -.
DR   OrthoDB; 1361975at2759; -.
DR   Proteomes; UP000000819; Chromosome VIII.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_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   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Kinase; Magnesium; Meiosis;
KW   Metal-binding; Mitosis; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..351
FT                   /note="Probable cell division control protein 7 homolog 1"
FT                   /id="PRO_0000384419"
FT   DOMAIN          21..341
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        137
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         27..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   351 AA;  39733 MW;  53F627A2E0F14FB2 CRC64;
     MEEEKILESD LRHISFVMPK YTPIEKIGEG SFSVVYKALD AESGRYVALK AITRTSSPAR
     VLDEMMFLKT LGGRKNCMGL LGCFRNEDQV VAVFPYFEPI DFREFISNAN LADIKRYLHN
     LLIAIEHVHS NGIMHRDLKP GNFLYNKESG RGMLIDFGLA QYEEYSEGQH AEGGAKPAGP
     LLFFNSVVSK TKPPGYYERD GRPPMKAPRA GTRGFRAPEV LFRCQRQTGA IDMWSVGVIF
     LTILTTQYPF FYSSDDIDSI VEIATIFGHA EMRKAAKFYG RVWRSNIDSI PEERIPFETI
     VESLNPWAEI GSDGYDLLYR MLDLCSSSRI TASDALSHPF FDDLKTHENC A