ID CDC45_YEAST Reviewed; 650 AA.
AC Q08032; D6VYA3; Q05908;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 187.
DE RecName: Full=Cell division control protein 45;
GN Name=CDC45; Synonyms=SLD4; OrderedLocusNames=YLR103C; ORFNames=L8004.11;
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], AND FUNCTION.
RX PubMed=9001208; DOI=10.1128/mcb.17.2.553;
RA Zou L., Mitchell J., Stillman B.;
RT "CDC45, a novel yeast gene that functions with the origin recognition
RT complex and Mcm proteins in initiation of DNA replication.";
RL Mol. Cell. Biol. 17:553-563(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8901577; DOI=10.1073/pnas.93.22.12309;
RA Hopwood B., Dalton S.;
RT "Cdc45p assembles into a complex with Cdc46p/Mcm5p, is required for
RT minichromosome maintenance, and is essential for chromosomal DNA
RT replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12309-12314(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Messenguy F., Dubois E., Vierendeels F., Scherens B.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH MCM10.
RX PubMed=15201046; DOI=10.1016/j.jmb.2004.04.066;
RA Sawyer S.L., Cheng I.H., Chai W., Tye B.K.;
RT "Mcm10 and Cdc45 cooperate in origin activation in Saccharomyces
RT cerevisiae.";
RL J. Mol. Biol. 340:195-202(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-453, AND IDENTIFICATION BY
RP 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: Required for initiation of chromosomal DNA replication. Acts
CC at the origin of replication. Also has a role in minichromosome
CC maintenance. {ECO:0000269|PubMed:8901577, ECO:0000269|PubMed:9001208}.
CC -!- SUBUNIT: Assembles into a complex with MCM5/CDC46. Interacts with
CC MCM10. {ECO:0000269|PubMed:15201046}.
CC -!- INTERACTION:
CC Q08032; P25588: MRC1; NbExp=4; IntAct=EBI-4292, EBI-412442;
CC Q08032; P53135: SLD3; NbExp=13; IntAct=EBI-4292, EBI-23925;
CC Q08032; P53840: TOF1; NbExp=3; IntAct=EBI-4292, EBI-28257;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8901577}.
CC -!- MISCELLANEOUS: Present with 1730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CDC45 family. {ECO:0000305}.
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DR EMBL; U65790; AAC49620.1; -; Genomic_DNA.
DR EMBL; U56821; AAB09053.1; -; Genomic_DNA.
DR EMBL; Z73275; CAA97668.1; -; Genomic_DNA.
DR EMBL; U53876; AAB67546.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09419.1; -; Genomic_DNA.
DR PIR; S64939; S64939.
DR RefSeq; NP_013204.1; NM_001181990.1.
DR PDB; 3JC5; EM; 4.70 A; c=1-650.
DR PDB; 3JC6; EM; 3.70 A; E=1-650.
DR PDB; 3JC7; EM; 4.80 A; c=1-650.
DR PDB; 5U8S; EM; 6.10 A; E=1-650.
DR PDB; 5U8T; EM; 4.90 A; E=1-650.
DR PDB; 6HV9; EM; 4.98 A; G=1-650.
DR PDB; 6PTJ; EM; 3.80 A; c=1-650.
DR PDB; 6PTN; EM; 5.80 A; H/h=1-650.
DR PDB; 6PTO; EM; 7.00 A; E/e/r=1-650.
DR PDB; 6SKL; EM; 3.70 A; E=1-650.
DR PDB; 6U0M; EM; 3.90 A; E=5-650.
DR PDB; 7QHS; EM; 3.30 A; E=1-650.
DR PDB; 8KG6; EM; 3.07 A; E=1-650.
DR PDB; 8KG8; EM; 4.23 A; E=1-650.
DR PDB; 8KG9; EM; 4.52 A; E=1-650.
DR PDB; 8W7M; EM; 4.12 A; E=1-650.
DR PDBsum; 3JC5; -.
DR PDBsum; 3JC6; -.
DR PDBsum; 3JC7; -.
DR PDBsum; 5U8S; -.
DR PDBsum; 5U8T; -.
DR PDBsum; 6HV9; -.
DR PDBsum; 6PTJ; -.
DR PDBsum; 6PTN; -.
DR PDBsum; 6PTO; -.
DR PDBsum; 6SKL; -.
DR PDBsum; 6U0M; -.
DR PDBsum; 7QHS; -.
DR PDBsum; 8KG6; -.
DR PDBsum; 8KG8; -.
DR PDBsum; 8KG9; -.
DR PDBsum; 8W7M; -.
DR AlphaFoldDB; Q08032; -.
DR EMDB; EMD-0288; -.
DR EMDB; EMD-10227; -.
DR EMDB; EMD-13978; -.
DR EMDB; EMD-15924; -.
DR EMDB; EMD-20471; -.
DR EMDB; EMD-20472; -.
DR EMDB; EMD-20473; -.
DR EMDB; EMD-20607; -.
DR EMDB; EMD-8518; -.
DR EMDB; EMD-8519; -.
DR SMR; Q08032; -.
DR BioGRID; 31376; 281.
DR ComplexPortal; CPX-297; CMG helicase complex.
DR DIP; DIP-2405N; -.
DR IntAct; Q08032; 38.
DR MINT; Q08032; -.
DR STRING; 4932.YLR103C; -.
DR iPTMnet; Q08032; -.
DR MaxQB; Q08032; -.
DR PaxDb; 4932-YLR103C; -.
DR PeptideAtlas; Q08032; -.
DR TopDownProteomics; Q08032; -.
DR EnsemblFungi; YLR103C_mRNA; YLR103C; YLR103C.
DR GeneID; 850793; -.
DR KEGG; sce:YLR103C; -.
DR AGR; SGD:S000004093; -.
DR SGD; S000004093; CDC45.
DR VEuPathDB; FungiDB:YLR103C; -.
DR eggNOG; KOG2475; Eukaryota.
DR GeneTree; ENSGT00390000009662; -.
DR HOGENOM; CLU_005871_3_0_1; -.
DR InParanoid; Q08032; -.
DR OMA; MYLPRQL; -.
DR OrthoDB; 1407079at2759; -.
DR BioCyc; YEAST:G3O-32251-MONOMER; -.
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; 850793; 0 hits in 10 CRISPR screens.
DR PRO; PR:Q08032; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q08032; Protein.
DR GO; GO:0071162; C:CMG complex; IDA:SGD.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:ComplexPortal.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:1902977; P:mitotic DNA replication preinitiation complex assembly; IBA:GO_Central.
DR InterPro; IPR003874; CDC45.
DR PANTHER; PTHR10507; CDC45-RELATED PROTEIN; 1.
DR PANTHER; PTHR10507:SF0; CELL DIVISION CONTROL PROTEIN 45 HOMOLOG; 1.
DR Pfam; PF02724; CDC45; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; DNA replication; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..650
FT /note="Cell division control protein 45"
FT /id="PRO_0000192819"
FT REGION 168..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..204
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 453
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 576
FT /note="T -> K (in Ref. 4; AAB67546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 74249 MW; 6500DDD62EC4E8EE CRC64;
MYYGISQFSE AYNKILRNSS SHSSCQLVIF VSCLNIDALC ATKMLSLLFK KQLVQSQIVP
IFGYSELRRH YSQLDDNINS LLLVGFGGVI DLEAFLEIDP QEYVIDTDEK SGEQSFRRDI
YVLDAHRPWN LDNIFGSQII QCFDDGTVDD TLGEQKEAYY KLLELDEESG DDELSGDEND
NNGGDDEATD ADEVTDEDEE DEDETISNKR GNSSIGPNDL SKRKQRKKQI HEYEGVLEEY
YSQGTTVVNS ISAQIYSLLS AIGETNLSNL WLNILGTTSL DIAYAQVYNR LYPLLQDEVK
RLTPSSRNSV KTPDTLTLNI QPDYYLFLLR HSSLYDSFYY SNYVNAKLSL WNENGKKRLH
KMFARMGIPL STAQETWLYM DHSIKRELGI IFDKNLDRYG LQDIIRDGFV RTLGYRGSIS
ASEFVEALTA LLEVGNSTDK DSVKINNDNN DDTDGEEEED NSAQKLTNLR KRWVSNFWLS
WDALDDRKVE LLNRGIQLAQ DLQRAIFNTG VAILEKKLIK HLRIYRLCVL QDGPDLDLYR
NPLTLLRLGN WLIECCAESE DKQLLPMVLA SIDENTDTYL VAGLTPRYPR GLDTIHTKKP
ILNNFSMAFQ QITAETDAKV RIDNFESSII EIRREDLSPF LEKLTLSGLL
//
