ID   CDC45_XENLA             Reviewed;         567 AA.
AC   Q9YHZ6; Q6GN24;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Cell division control protein 45 homolog;
GN   Name=cdc45; Synonyms=cdc45l;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=9755170; DOI=10.1093/emboj/17.19.5699;
RA   Mimura S., Takisawa H.;
RT   "Xenopus Cdc45-dependent loading of DNA polymerase alpha onto chromatin
RT   under the control of S-phase Cdk.";
RL   EMBO J. 17:5699-5707(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH TOPBP1.
RC   TISSUE=Oocyte;
RX   PubMed=12743046; DOI=10.1093/emboj/cdg238;
RA   Hashimoto Y., Takisawa H.;
RT   "Xenopus Cut5 is essential for a CDK-dependent process in the initiation of
RT   DNA replication.";
RL   EMBO J. 22:2526-2535(2003).
RN   [4]
RP   CHROMATIN BINDING.
RX   PubMed=12730133; DOI=10.1101/gad.1070003;
RA   Kubota Y., Takase Y., Komori Y., Hashimoto Y., Arata T., Kamimura Y.,
RA   Araki H., Takisawa H.;
RT   "A novel ring-like complex of Xenopus proteins essential for the initiation
RT   of DNA replication.";
RL   Genes Dev. 17:1141-1152(2003).
RN   [5]
RP   IDENTIFICATION IN THE CMG HELICASE COMPLEX.
RX   PubMed=30979826; DOI=10.26508/lsa.201900390;
RA   Priego Moreno S., Jones R.M., Poovathumkadavil D., Scaramuzza S.,
RA   Gambus A.;
RT   "Mitotic replisome disassembly depends on TRAIP ubiquitin ligase
RT   activity.";
RL   Life. Sci Alliance 2:0-0(2019).
RN   [6]
RP   IDENTIFICATION IN THE CMG HELICASE COMPLEX.
RX   PubMed=30842657; DOI=10.1038/s41586-019-1002-0;
RA   Wu R.A., Semlow D.R., Kamimae-Lanning A.N., Kochenova O.V., Chistol G.,
RA   Hodskinson M.R., Amunugama R., Sparks J.L., Wang M., Deng L., Mimoso C.A.,
RA   Low E., Patel K.J., Walter J.C.;
RT   "TRAIP is a master regulator of DNA interstrand crosslink repair.";
RL   Nature 567:267-272(2019).
CC   -!- FUNCTION: Required for initiation of chromosomal DNA replication. Binds
CC       to chromatin in a mutually dependent manner with the GINS DNA
CC       replication complex. {ECO:0000269|PubMed:9755170}.
CC   -!- SUBUNIT: Interacts with topbp1 (PubMed:12743046). Component of the CMG
CC       helicase complex, composed of the mcm2-7 complex, the GINS complex and
CC       cdc45 (PubMed:30979826, PubMed:30842657). {ECO:0000269|PubMed:12743046,
CC       ECO:0000269|PubMed:30842657, ECO:0000269|PubMed:30979826}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9755170}. Chromosome
CC       {ECO:0000269|PubMed:9755170}. Note=Associates with chromatin.
CC       {ECO:0000269|PubMed:9755170}.
CC   -!- SIMILARITY: Belongs to the CDC45 family. {ECO:0000305}.
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DR   EMBL; AF062494; AAC67520.1; -; mRNA.
DR   EMBL; BC073697; AAH73697.1; -; mRNA.
DR   RefSeq; NP_001081842.1; NM_001088373.1.
DR   AlphaFoldDB; Q9YHZ6; -.
DR   SMR; Q9YHZ6; -.
DR   MaxQB; Q9YHZ6; -.
DR   DNASU; 398081; -.
DR   GeneID; 398081; -.
DR   KEGG; xla:398081; -.
DR   CTD; 398081; -.
DR   Xenbase; XB-GENE-976062; cdc45.L.
DR   OMA; PWNLANV; -.
DR   OrthoDB; 1309031at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   GO; GO:0071162; C:CMG complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   InterPro; IPR003874; CDC45.
DR   PANTHER; PTHR10507; PTHR10507; 1.
DR   Pfam; PF02724; CDC45; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Chromosome; DNA replication; Nucleus; Reference proteome.
FT   CHAIN           1..567
FT                   /note="Cell division control protein 45 homolog"
FT                   /id="PRO_0000192817"
FT   REGION          133..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..147
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        233
FT                   /note="R -> P (in Ref. 1; AAC67520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="Q -> L (in Ref. 1; AAC67520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="R -> G (in Ref. 1; AAC67520)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   567 AA;  65618 MW;  A5DE7B8B986429F6 CRC64;
     MFVSDLRKEF FDVIVTERVL LLVAPDVDAL CACKILQALF QCDHVQYTLV PVSGWQELET
     LFLEHKEQFR YFVLINCGAN IDLLETLQPQ EEAIFYICDT HRPIDVVNIY NDSQVKLLIR
     QDDDLEIPAY DDIFNDDEED GEDSGNESDG AEPSGKRRRF DEAAVERRIE RRRQRREWEA
     RRREIIFDYE QYEYHGTSSA MMMFELAWIM SKDSNDMLWW AIVGLTDQWV QDRITQMKYV
     TDVGTLQRHV SRHNHRNEDE ENSLSIDCMR IAFEYDLRLS LYQHWSLYES ICNSCYTSAT
     LKLWSLQGQK KLQEFLADMG MPLKQVKQKF NSMDISLKEN LREMLEESAN KFGMKDVRVQ
     TFSVQFGFKN KFLASDIVFA VLSLLENTER DEKGTDNFIK ALDSLSRSNL DKLHTGLEMG
     KKLLCAIQQT VASCICTNLI LSQGPFLYCY LMEGTPDVKM FSNPISLCLL CKYLLKSFVC
     STKNKRCKLL PLVLAAPLDA EKGTVIMVGI PPEAESSDKK NFFGRAFEKA AESTSSRTLH
     NHFDMSIIEL RTEDRSKFLD ALISLLS