ID   CDC7_YEAST              Reviewed;         507 AA.
AC   P06243; D6VRX3;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Cell division control protein 7;
DE            EC=2.7.11.1;
GN   Name=CDC7; Synonyms=OAF2; OrderedLocusNames=YDL017W; ORFNames=D2855;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3537706; DOI=10.1128/mcb.6.5.1590-1598.1986;
RA   Patterson M., Sclafani R.A., Fangman W.L., Rosamond J.;
RT   "Molecular characterization of cell cycle gene CDC7 from Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 6:1590-1598(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-138.
RX   PubMed=2850010; DOI=10.1016/0167-4781(88)90104-2;
RA   Bahman M., Buck V., White A., Rosamond J.;
RT   "Characterisation of the CDC7 gene product of Saccharomyces cerevisiae as a
RT   protein kinase needed for the initiation of mitotic DNA synthesis.";
RL   Biochim. Biophys. Acta 951:335-343(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=2668893; DOI=10.1093/nar/17.14.5781;
RA   Ham J., Moore D., Rosamond J., Johnston I.R.;
RT   "Transcriptional analysis of the CDC7 protein kinase gene of Saccharomyces
RT   cerevisiae.";
RL   Nucleic Acids Res. 17:5781-5792(1989).
RN   [6]
RP   FUNCTION.
RX   PubMed=1865880; DOI=10.1007/bf00273937;
RA   Buck V., Rosamond J.;
RT   "CDC7 protein kinase activity is required for mitosis and meiosis in
RT   Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 227:452-457(1991).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
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. Required for
CC       HTA1-HTB1 locus transcription repression. {ECO:0000269|PubMed:1865880}.
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   -!- SUBUNIT: Associates with DBF4 and ORC2.
CC   -!- INTERACTION:
CC       P06243; P32562: CDC5; NbExp=11; IntAct=EBI-4451, EBI-4440;
CC       P06243; P06243: CDC7; NbExp=3; IntAct=EBI-4451, EBI-4451;
CC       P06243; P32325: DBF4; NbExp=8; IntAct=EBI-4451, EBI-5575;
CC       P06243; Q04087: LRS4; NbExp=5; IntAct=EBI-4451, EBI-32189;
CC   -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDC7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA32370.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M12624; AAA34485.1; -; Genomic_DNA.
DR   EMBL; Z48432; CAA88342.1; -; Genomic_DNA.
DR   EMBL; Z74065; CAA98574.1; -; Genomic_DNA.
DR   EMBL; X14164; CAA32369.1; -; Genomic_DNA.
DR   EMBL; X14164; CAA32370.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X15362; CAA33420.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11833.1; -; Genomic_DNA.
DR   PIR; A25228; A25228.
DR   RefSeq; NP_010267.3; NM_001180076.3.
DR   PDB; 5T2S; X-ray; 2.40 A; B/D=480-491.
DR   PDB; 7P5Z; EM; 3.30 A; 1=1-507.
DR   PDB; 7PT6; EM; 3.20 A; 8/H=1-507.
DR   PDB; 7PT7; EM; 3.80 A; 8=1-507.
DR   PDB; 7V3V; EM; 2.90 A; H=1-507.
DR   PDBsum; 5T2S; -.
DR   PDBsum; 7P5Z; -.
DR   PDBsum; 7PT6; -.
DR   PDBsum; 7PT7; -.
DR   PDBsum; 7V3V; -.
DR   AlphaFoldDB; P06243; -.
DR   EMDB; EMD-13211; -.
DR   EMDB; EMD-13619; -.
DR   EMDB; EMD-13620; -.
DR   EMDB; EMD-31685; -.
DR   SMR; P06243; -.
DR   BioGRID; 32038; 479.
DR   ComplexPortal; CPX-867; DBF4-dependent CDC7 kinase complex.
DR   DIP; DIP-1235N; -.
DR   IntAct; P06243; 79.
DR   MINT; P06243; -.
DR   STRING; 4932.YDL017W; -.
DR   MoonDB; P06243; Predicted.
DR   iPTMnet; P06243; -.
DR   MaxQB; P06243; -.
DR   PaxDb; 4932-YDL017W; -.
DR   PeptideAtlas; P06243; -.
DR   EnsemblFungi; YDL017W_mRNA; YDL017W; YDL017W.
DR   GeneID; 851545; -.
DR   KEGG; sce:YDL017W; -.
DR   AGR; SGD:S000002175; -.
DR   SGD; S000002175; CDC7.
DR   VEuPathDB; FungiDB:YDL017W; -.
DR   eggNOG; KOG1167; Eukaryota.
DR   GeneTree; ENSGT00550000075011; -.
DR   HOGENOM; CLU_000288_118_2_1; -.
DR   InParanoid; P06243; -.
DR   OMA; QGFTMEK; -.
DR   OrthoDB; 12073at2759; -.
DR   BioCyc; YEAST:G3O-29446-MONOMER; -.
DR   BRENDA; 2.7.11.1; 984.
DR   Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR   BioGRID-ORCS; 851545; 3 hits in 13 CRISPR screens.
DR   PRO; PR:P06243; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P06243; Protein.
DR   GO; GO:0005813; C:centrosome; IDA:ComplexPortal.
DR   GO; GO:0000785; C:chromatin; IDA:SGD.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
DR   GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IDA:SGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IGI:SGD.
DR   GO; GO:1902977; P:mitotic DNA replication preinitiation complex assembly; IDA:SGD.
DR   GO; GO:0001100; P:negative regulation of exit from mitosis; IPI:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:1905561; P:positive regulation of kinetochore assembly; IDA:ComplexPortal.
DR   GO; GO:0060903; P:positive regulation of meiosis I; IDA:ComplexPortal.
DR   GO; GO:1903343; P:positive regulation of meiotic DNA double-strand break formation; IDA:ComplexPortal.
DR   GO; GO:1905263; P:positive regulation of meiotic DNA double-strand break formation involved in reciprocal meiotic recombination; IMP:SGD.
DR   GO; GO:1904968; P:positive regulation of spindle attachment to meiosis I kinetochore; IMP:SGD.
DR   GO; GO:0006279; P:premeiotic DNA replication; IMP:SGD.
DR   GO; GO:0031503; P:protein-containing complex localization; IMP:SGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd14019; STKc_Cdc7; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44167:SF23; CDC7 KINASE, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR44167; OVARIAN-SPECIFIC SERINE/THREONINE-PROTEIN KINASE LOK-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell cycle; Cell division; Kinase; Magnesium;
KW   Meiosis; Metal-binding; Mitosis; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..507
FT                   /note="Cell division control protein 7"
FT                   /id="PRO_0000085766"
FT   DOMAIN          33..469
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         39..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   507 AA;  58320 MW;  B74BA9144D0EC39F CRC64;
     MTSKTKNIDD IPPEIKEEMI QLYHDLPGIE NEYKLIDKIG EGTFSSVYKA KDITGKITKK
     FASHFWNYGS NYVALKKIYV TSSPQRIYNE LNLLYIMTGS SRVAPLCDAK RVRDQVIAVL
     PYYPHEEFRT FYRDLPIKGI KKYIWELLRA LKFVHSKGII HRDIKPTNFL FNLELGRGVL
     VDFGLAEAQM DYKSMISSQN DYDNYANTNH DGGYSMRNHE QFCPCIMRNQ YSPNSHNQTP
     PMVTIQNGKV VHLNNVNGVD LTKGYPKNET RRIKRANRAG TRGFRAPEVL MKCGAQSTKI
     DIWSVGVILL SLLGRRFPMF QSLDDADSLL ELCTIFGWKE LRKCAALHGL GFEASGLIWD
     KPNGYSNGLK EFVYDLLNKE CTIGTFPEYS VAFETFGFLQ QELHDRMSIE PQLPDPKTNM
     DAVDAYELKK YQEEIWSDHY WCFQVLEQCF EMDPQKRSSA EDLLKTPFFN ELNENTYLLD
     GESTDEDDVV SSSEADLLDK DVLLISE
//