CDT1_YEAST
ID CDT1_YEAST Reviewed; 604 AA.
AC P47112; D6VWL7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cell division cycle protein CDT1;
DE AltName: Full=SIC1 indispensable protein 2;
DE AltName: Full=Topoisomerase-A hypersensitive protein 11;
GN Name=TAH11; Synonyms=CDT1, SID2; OrderedLocusNames=YJR046W; ORFNames=J1641;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7668047; DOI=10.1002/yea.320110809;
RA Huang M.-E., Chuat J.-C., Galibert F.;
RT "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT genes and 14 new open reading frames including a gene most probably
RT belonging to the family of ubiquitin-protein ligases.";
RL Yeast 11:775-781(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11560884; DOI=10.1093/genetics/159.1.17;
RA Jacobson M.D., Munoz C.X., Knox K.S., Williams B.E., Lu L.L., Cross F.R.,
RA Vallen E.A.;
RT "Mutations in SID2, a novel gene in Saccharomyces cerevisiae, cause
RT synthetic lethality with sic1 deletion and may cause a defect during S
RT phase.";
RL Genetics 159:17-33(2001).
RN [5]
RP FUNCTION.
RX PubMed=11967159; DOI=10.1016/s0960-9822(02)00768-6;
RA Devault A., Vallen E.A., Yuan T., Green S., Bensimon A., Schwob E.;
RT "Identification of Tah11/Sid2 as the ortholog of the replication licensing
RT factor Cdt1 in Saccharomyces cerevisiae.";
RL Curr. Biol. 12:689-694(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MCM2.
RX PubMed=11836525; DOI=10.1038/ncb757;
RA Tanaka S., Diffley J.F.;
RT "Interdependent nuclear accumulation of budding yeast Cdt1 and Mcm2-7
RT during G1 phase.";
RL Nat. Cell Biol. 4:198-207(2002).
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 FUNCTION, DNA-BINDING, AND ASSOCIATION WITH THE MCM2-7 COMPLEX.
RX PubMed=16824194; DOI=10.1111/j.1365-2443.2006.00975.x;
RA Kawasaki Y., Kim H.D., Kojima A., Seki T., Sugino A.;
RT "Reconstitution of Saccharomyces cerevisiae prereplicative complex assembly
RT in vitro.";
RL Genes Cells 11:745-756(2006).
RN [9]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=16387651; DOI=10.1016/j.molcel.2005.11.023;
RA Randell J.C., Bowers J.L., Rodriguez H.K., Bell S.P.;
RT "Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7
RT helicase.";
RL Mol. Cell 21:29-39(2006).
RN [10]
RP FUNCTION, DNA-BINDING, AND INTERACTION WITH ORC1; ORC2 AND ORC6.
RX PubMed=17825064; DOI=10.1111/j.1567-1364.2007.00299.x;
RA Asano T., Makise M., Takehara M., Mizushima T.;
RT "Interaction between ORC and Cdt1p of Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 7:1256-1262(2007).
RN [11]
RP FUNCTION, AND INTERACTION WITH ORC6.
RX PubMed=18006685; DOI=10.1101/gad.1596807;
RA Chen S., de Vries M.A., Bell S.P.;
RT "Orc6 is required for dynamic recruitment of Cdt1 during repeated Mcm2-7
RT loading.";
RL Genes Dev. 21:2897-2907(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, ASSOCIATION WITH THE MCM2-7 COMPLEX,
RP AND FUNCTION.
RX PubMed=19896182; DOI=10.1016/j.cell.2009.10.015;
RA Remus D., Beuron F., Tolun G., Griffith J.D., Morris E.P., Diffley J.F.;
RT "Concerted loading of Mcm2-7 double hexamers around DNA during DNA
RT replication origin licensing.";
RL Cell 139:719-730(2009).
CC -!- FUNCTION: DNA replication licensing factor, required for pre-
CC replication complex assembly. Faithful duplication of the genetic
CC material requires 'once per cell cycle' DNA replication initiation and
CC elongation. Central to this control is the tightly regulated formation
CC of prereplicative complexes (preRCs) at future origins of DNA
CC replication. Required for the recruitment of the MCM2-7 helicase
CC complex to the replication origins. {ECO:0000269|PubMed:11560884,
CC ECO:0000269|PubMed:11967159, ECO:0000269|PubMed:16387651,
CC ECO:0000269|PubMed:16824194, ECO:0000269|PubMed:17825064,
CC ECO:0000269|PubMed:18006685, ECO:0000269|PubMed:19896182}.
CC -!- SUBUNIT: Associates with the MCM2-7 complex. Interacts with MCM2, ORC1,
CC ORC2 and ORC6. {ECO:0000269|PubMed:11836525,
CC ECO:0000269|PubMed:17825064, ECO:0000269|PubMed:18006685}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Undergoes cell cycle-
CC dependent changes in its nuclear localization. Exits the nucleus and
CC remains in the cytoplasm during S phase through early mitosis, and re-
CC accumulates in the nucleus around the end of mitosis.
CC -!- MISCELLANEOUS: Present with 2190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Cdt1 family. {ECO:0000305}.
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DR EMBL; L36344; AAA88748.1; -; Genomic_DNA.
DR EMBL; Z49546; CAA89574.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08833.1; -; Genomic_DNA.
DR PIR; S57065; S57065.
DR RefSeq; NP_012580.1; NM_001181704.1.
DR PDB; 5ME9; X-ray; 2.70 A; A/B/C=2-438.
DR PDB; 5MEA; X-ray; 2.15 A; A=1-438.
DR PDB; 5MEB; X-ray; 1.80 A; A/B=495-604.
DR PDB; 5MEC; X-ray; 2.13 A; A=272-438.
DR PDB; 5V8F; EM; 3.90 A; 8=1-604.
DR PDB; 5XF8; EM; 7.10 A; C=1-604.
DR PDB; 6WGG; EM; 8.10 A; 8=1-604.
DR PDB; 6WGI; EM; 10.00 A; L=1-604.
DR PDBsum; 5ME9; -.
DR PDBsum; 5MEA; -.
DR PDBsum; 5MEB; -.
DR PDBsum; 5MEC; -.
DR PDBsum; 5V8F; -.
DR PDBsum; 5XF8; -.
DR PDBsum; 6WGG; -.
DR PDBsum; 6WGI; -.
DR AlphaFoldDB; P47112; -.
DR SMR; P47112; -.
DR BioGRID; 33798; 187.
DR DIP; DIP-7948N; -.
DR IntAct; P47112; 17.
DR STRING; 4932.YJR046W; -.
DR iPTMnet; P47112; -.
DR MaxQB; P47112; -.
DR PaxDb; P47112; -.
DR PRIDE; P47112; -.
DR EnsemblFungi; YJR046W_mRNA; YJR046W; YJR046W.
DR GeneID; 853504; -.
DR KEGG; sce:YJR046W; -.
DR SGD; S000003807; TAH11.
DR VEuPathDB; FungiDB:YJR046W; -.
DR eggNOG; ENOG502QRI1; Eukaryota.
DR HOGENOM; CLU_492622_0_0_1; -.
DR InParanoid; P47112; -.
DR OMA; DCLLFHT; -.
DR BioCyc; YEAST:G3O-31681-MON; -.
DR PRO; PR:P47112; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47112; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IDA:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:SGD.
DR Gene3D; 1.10.10.1420; -; 1.
DR InterPro; IPR032054; Cdt1_C.
DR InterPro; IPR038090; Cdt1_C_WH_dom_sf.
DR Pfam; PF16679; CDT1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; DNA-binding; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..604
FT /note="Cell division cycle protein CDT1"
FT /id="PRO_0000203095"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5MEA"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:5MEA"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 109..133
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:5ME9"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 194..207
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:5MEA"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5ME9"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 299..328
FT /evidence="ECO:0007829|PDB:5MEC"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:5MEC"
FT HELIX 357..366
FT /evidence="ECO:0007829|PDB:5MEC"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:5MEC"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:5MEC"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:5MEA"
FT HELIX 399..416
FT /evidence="ECO:0007829|PDB:5MEC"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:5MEC"
FT HELIX 495..522
FT /evidence="ECO:0007829|PDB:5MEB"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:5MEB"
FT HELIX 531..542
FT /evidence="ECO:0007829|PDB:5MEB"
FT HELIX 551..564
FT /evidence="ECO:0007829|PDB:5MEB"
FT TURN 566..568
FT /evidence="ECO:0007829|PDB:5MEB"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:5MEB"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:5MEB"
FT HELIX 588..602
FT /evidence="ECO:0007829|PDB:5MEB"
SQ SEQUENCE 604 AA; 68405 MW; 099992C0E3CCA726 CRC64;
MSGTANSRRK EVLRVPVIDL NRVSDEEQLL PVVRAILLQH DTFLLKNYAN KAVLDALLAG
LTTKDLPDTS QGFDANFTGT LPLEDDVWLE QYIFDTDPQL RFDRKCRNES LCSIYSRLFK
LGLFFAQLCV KSVVSSAELQ DCISTSHYAT KLTRYFNDNG STHDGADAGA TVLPTGDDFQ
YLFERDYVTF LPTGVLTIFP CAKAIRYKPS TMATTDNSWV SIDEPDCLLF HTGTLLARWS
QGMHTTSPLQ IDPRANIVSL TIWPPLTTPI SSKGEGTIAN HLLEQQIKAF PKVAQQYYPR
ELSILRLQDA MKFVKELFTV CETVLSLNAL SRSTGVPPEL HVLLPQISSM MKRKIVQDDI
LKLLTIWSDA YVVELNSRGE LTMNLPKRDN LTTLTNKSRT LAFVERAESW YQQVIASKDE
IMTDVPAFKI NKRRSSSNSK TVLSSKVQTK SSNANALNNS RYLANSKENF MYKEKMPDSQ
ANLMDRLRER ERRSAALLSQ RQKRYQQFLA MKMTQVFDIL FSLTRGQPYT ETYLSSLIVD
SLQDSNNPIG TKEASEILAG LQGILPMDIS VHQVDGGLKV YRWNSLDKNR FSKLLQIHKS
KQQD
