CTF18_YEAST
ID CTF18_YEAST Reviewed; 741 AA.
AC P49956; D6VZQ2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Chromosome transmission fidelity protein 18;
GN Name=CTF18; Synonyms=CHL12; OrderedLocusNames=YMR078C; ORFNames=YM9582.03C;
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=CL10;
RX PubMed=7896091; DOI=10.1093/genetics/138.4.1067;
RA Kouprina N., Kroll E., Kirillov A., Bannikov V., Zakharyev V., Larionov V.;
RT "CHL12, a gene essential for the fidelity of chromosome transmission in the
RT yeast Saccharomyces cerevisiae.";
RL Genetics 138:1067-1079(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 FUNCTION, AND IDENTIFICATION IN THE CTF18-RFC COMPLEX.
RX PubMed=11389843; DOI=10.1016/s1097-2765(01)00254-4;
RA Mayer M.L., Gygi S.P., Aebersold R., Hieter P.;
RT "Identification of RFC(Ctf18p, Ctf8p, Dcc1p): an alternative RFC complex
RT required for sister chromatid cohesion in S. cerevisiae.";
RL Mol. Cell 7:959-970(2001).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=11287619; DOI=10.1128/mcb.21.9.3144-3158.2001;
RA Hanna J.S., Kroll E.S., Lundblad V., Spencer F.A.;
RT "Saccharomyces cerevisiae CTF18 and CTF4 are required for sister chromatid
RT cohesion.";
RL Mol. Cell. Biol. 21:3144-3158(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH RFC2; RFC3; RFC4 AND RFC5.
RX PubMed=11486023; DOI=10.1128/mcb.21.17.5838-5845.2001;
RA Naiki T., Kondo T., Nakada D., Matsumoto K., Sugimoto K.;
RT "Chl12 (Ctf18) forms a novel replication factor C-related complex and
RT functions redundantly with Rad24 in the DNA replication checkpoint
RT pathway.";
RL Mol. Cell. Biol. 21:5838-5845(2001).
RN [7]
RP INTERACTION WITH ECO1.
RX PubMed=12665596; DOI=10.1128/mcb.23.8.2999-3007.2003;
RA Kenna M.A., Skibbens R.V.;
RT "Mechanical link between cohesion establishment and DNA replication:
RT Ctf7p/Eco1p, a cohesion establishment factor, associates with three
RT different replication factor C complexes.";
RL Mol. Cell. Biol. 23:2999-3007(2003).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE CTF18-RFC COMPLEX, FUNCTION OF THE
RP CTF18-RFC COMPLEX, AND MUTAGENESIS OF LYS-189.
RX PubMed=15964801; DOI=10.1128/mcb.25.13.5445-5455.2005;
RA Bylund G.O., Burgers P.M.;
RT "Replication protein A-directed unloading of PCNA by the Ctf18 cohesion
RT establishment complex.";
RL Mol. Cell. Biol. 25:5445-5455(2005).
RN [9]
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).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Essential for the fidelity of chromosome transmission.
CC Required for the DNA replication block checkpoint. Component of the
CC RFC-like complex CTF18-RFC which is required for efficient
CC establishment of chromosome cohesion during S-phase and may load or
CC unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex
CC binds to DNA and the recognition of the double-stranded/single-stranded
CC junction stimulates ATP hydrolysis by RFC. The complex presumably
CC provides bipartite ATP sites in which one subunit supplies a catalytic
CC site for hydrolysis of ATP bound to the neighboring subunit.
CC Dissociation of RFC from the clamp leaves the clamp encircling DNA.
CC {ECO:0000269|PubMed:11287619, ECO:0000269|PubMed:11389843,
CC ECO:0000269|PubMed:11486023, ECO:0000269|PubMed:15964801}.
CC -!- SUBUNIT: Component of the CTF18-RFC complex, which consists of CTF18,
CC CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. CTF18 interacts with ECO1.
CC {ECO:0000269|PubMed:11287619, ECO:0000269|PubMed:11389843,
CC ECO:0000269|PubMed:11486023, ECO:0000269|PubMed:12665596,
CC ECO:0000269|PubMed:15964801}.
CC -!- INTERACTION:
CC P49956; P38877: CTF8; NbExp=4; IntAct=EBI-4560, EBI-5216;
CC P49956; P43605: ECO1; NbExp=2; IntAct=EBI-4560, EBI-22988;
CC P49956; P40348: RFC2; NbExp=2; IntAct=EBI-4560, EBI-14992;
CC P49956; P38629: RFC3; NbExp=3; IntAct=EBI-4560, EBI-15000;
CC P49956; P40339: RFC4; NbExp=5; IntAct=EBI-4560, EBI-15009;
CC P49956; P38251: RFC5; NbExp=4; IntAct=EBI-4560, EBI-15016;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. CTF18
CC subfamily. {ECO:0000305}.
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DR EMBL; L24514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z49259; CAA89224.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09976.1; -; Genomic_DNA.
DR PIR; S50340; S50340.
DR RefSeq; NP_013795.1; NM_001182577.1.
DR PDB; 5MSM; X-ray; 2.29 A; C/F=666-741.
DR PDB; 5OKC; X-ray; 2.30 A; G/I=715-741.
DR PDB; 5OKI; X-ray; 4.50 A; E/I=715-740.
DR PDB; 6S1C; X-ray; 6.10 A; D/H=713-741.
DR PDB; 6S2E; EM; 4.20 A; E=713-741.
DR PDB; 6S2F; EM; 5.80 A; E=713-741.
DR PDBsum; 5MSM; -.
DR PDBsum; 5OKC; -.
DR PDBsum; 5OKI; -.
DR PDBsum; 6S1C; -.
DR PDBsum; 6S2E; -.
DR PDBsum; 6S2F; -.
DR AlphaFoldDB; P49956; -.
DR SMR; P49956; -.
DR BioGRID; 35254; 534.
DR ComplexPortal; CPX-1731; CTF18-RFC complex.
DR DIP; DIP-5868N; -.
DR IntAct; P49956; 15.
DR MINT; P49956; -.
DR STRING; 4932.YMR078C; -.
DR iPTMnet; P49956; -.
DR MaxQB; P49956; -.
DR PaxDb; P49956; -.
DR PRIDE; P49956; -.
DR EnsemblFungi; YMR078C_mRNA; YMR078C; YMR078C.
DR GeneID; 855102; -.
DR KEGG; sce:YMR078C; -.
DR SGD; S000004683; CTF18.
DR VEuPathDB; FungiDB:YMR078C; -.
DR eggNOG; KOG1969; Eukaryota.
DR GeneTree; ENSGT00550000075029; -.
DR HOGENOM; CLU_004894_3_1_1; -.
DR InParanoid; P49956; -.
DR OMA; SYEDPMV; -.
DR BioCyc; YEAST:G3O-32780-MON; -.
DR PRO; PR:P49956; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P49956; protein.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IPI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD.
DR GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; DNA replication; DNA-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..741
FT /note="Chromosome transmission fidelity protein 18"
FT /id="PRO_0000089645"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 189
FT /note="K->E: Fails to unload PCNA."
FT /evidence="ECO:0000269|PubMed:15964801"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:5MSM"
FT HELIX 736..739
FT /evidence="ECO:0007829|PDB:5MSM"
SQ SEQUENCE 741 AA; 84373 MW; DC054EA712BD1BB2 CRC64;
MVDTAPYIGS LGRSSLFDTG DIEQAPGNNA IGINEEDIHA FVSSTGETVQ LKKKPAKLAT
GNISLYTNPD TVWRSDDTYG ININYLLDKI EASGDDRTNA QKTSPITGKI GSDTLWVEKW
RPKKFLDLVG NEKTNRRMLG WLRQWTPAVF KEQLPKLPTE KEVSDMELDP LKRPPKKILL
LHGPPGIGKT SVAHVIAKQS GFSVSEINAS DERAGPMVKE KIYNLLFNHT FDTNPVCLVA
DEIDGSIESG FIRILVDIMQ SDIKATNKLL YGQPDKKDKK RKKKRSKLLT RPIICICNNL
YAPSLEKLKP FCEIIAVKRP SDTTLLERLN LICHKENMNI PIKAINDLID LAQGDVRNCI
NNLQFLASNV DSRDSSASDK PACAKNTWAS SNKDSPISWF KIVNQLFRKD PHRDIKEQFY
ELLNQVELNG NSDRILQGCF NIFPYVKYSD NGIRKPANIS DWLFFHDLMY QSMYAHNGEL
LRYSALVPLV FFQTFGDIAN KDDIRMKNSE YEQRELKRAN SDIVSLIMRH ISVQSPLMAS
FTDRKSLIFE ILPYLDSMIS SDFNKIRNLK LKQAIMEELV QLLKSFQLNL IQNRSEGFDV
RGGLTIDPPI DEVVLLNPKH INEVQHKRAN NLSSLLAKIE ENRAKKRHID QVTEDRLQSQ
EMHSKKVKTG LNSSSSTIDF FKNQYGLLKQ TQELEETQKT IGSDETNQAD DCNQTVKIWV
KYNEGFSNAV RKNVTWNNLW E
