DCC1_YEAST
ID DCC1_YEAST Reviewed; 380 AA.
AC P25559; D6VQZ8; Q8NIM7;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Sister chromatid cohesion protein DCC1;
DE AltName: Full=Defective in sister chromatid cohesion protein 1;
GN Name=DCC1; OrderedLocusNames=YCL016C; ORFNames=YCL16C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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 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 [6]
RP IDENTIFICATION IN THE CTF18-RFC COMPLEX, AND FUNCTION OF THE CTF18-RFC
RP COMPLEX.
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).
CC -!- FUNCTION: Component of the RFC-like complex CTF18-RFC which is required
CC for efficient establishment of chromosome cohesion during S-phase and
CC may load or unload POL30/PCNA. During a clamp loading circle, the
CC RFC:clamp complex binds to DNA and the recognition of the double-
CC stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The
CC complex presumably provides bipartite ATP sites in which one subunit
CC supplies a catalytic site for hydrolysis of ATP bound to the
CC neighboring subunit. Dissociation of RFC from the clamp leaves the
CC clamp encircling DNA. {ECO:0000269|PubMed:11389843,
CC ECO:0000269|PubMed:15964801}.
CC -!- SUBUNIT: Component of the CTF18-RFC complex, which consists of CTF18,
CC CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. {ECO:0000269|PubMed:11389843,
CC ECO:0000269|PubMed:15964801}.
CC -!- INTERACTION:
CC P25559; P38877: CTF8; NbExp=2; IntAct=EBI-5661, EBI-5216;
CC -!- MISCELLANEOUS: Present with 1660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DCC1 family. {ECO:0000305}.
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DR EMBL; X59720; CAC42963.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07467.1; -; Genomic_DNA.
DR PIR; S19342; S19342.
DR RefSeq; NP_009913.2; NM_001178663.1.
DR PDB; 5MSM; X-ray; 2.29 A; A/D=1-380.
DR PDB; 5MSN; X-ray; 2.00 A; A/B/C/D=90-380.
DR PDB; 5OKC; X-ray; 2.30 A; A/B=1-380.
DR PDB; 5OKI; X-ray; 4.50 A; C/G=1-380.
DR PDB; 6S1C; X-ray; 6.10 A; B/F=1-380.
DR PDB; 6S2E; EM; 4.20 A; B=1-380.
DR PDB; 6S2F; EM; 5.80 A; B=1-380.
DR PDBsum; 5MSM; -.
DR PDBsum; 5MSN; -.
DR PDBsum; 5OKC; -.
DR PDBsum; 5OKI; -.
DR PDBsum; 6S1C; -.
DR PDBsum; 6S2E; -.
DR PDBsum; 6S2F; -.
DR AlphaFoldDB; P25559; -.
DR SMR; P25559; -.
DR BioGRID; 30968; 582.
DR ComplexPortal; CPX-1731; CTF18-RFC complex.
DR DIP; DIP-2088N; -.
DR IntAct; P25559; 7.
DR MINT; P25559; -.
DR STRING; 4932.YCL016C; -.
DR iPTMnet; P25559; -.
DR MaxQB; P25559; -.
DR PaxDb; P25559; -.
DR PRIDE; P25559; -.
DR EnsemblFungi; YCL016C_mRNA; YCL016C; YCL016C.
DR GeneID; 850344; -.
DR KEGG; sce:YCL016C; -.
DR SGD; S000000521; DCC1.
DR VEuPathDB; FungiDB:YCL016C; -.
DR eggNOG; KOG0798; Eukaryota.
DR GeneTree; ENSGT00390000017400; -.
DR HOGENOM; CLU_034504_0_0_1; -.
DR InParanoid; P25559; -.
DR OMA; YVRTPED; -.
DR BioCyc; YEAST:G3O-29282-MON; -.
DR PRO; PR:P25559; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25559; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR InterPro; IPR019128; Dcc1.
DR PANTHER; PTHR13395; PTHR13395; 1.
DR Pfam; PF09724; Dcc1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; Reference proteome.
FT CHAIN 1..380
FT /note="Sister chromatid cohesion protein DCC1"
FT /id="PRO_0000079802"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:5MSM"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:5MSM"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:5MSM"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5MSM"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5MSM"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5MSM"
FT STRAND 57..75
FT /evidence="ECO:0007829|PDB:5MSM"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:5MSM"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:5MSM"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 182..198
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5MSM"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 254..269
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 325..335
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 341..348
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:5MSN"
FT HELIX 358..365
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:5MSN"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:5MSN"
SQ SEQUENCE 380 AA; 44074 MW; DEA59A7BBB337282 CRC64;
MSINLHSAPE YDPSYKLIQL TPELLDIIQD PVQNHQLRFK SLDKDKSEVV LCSHDKTWVL
KQRKHSNTVL LMREFVPEQP ITFDETLLFG LSKPYMDVVG FAKTESEFET RETHGELNLN
SVPIYNGELD FSDKIMKRSS TKVIGTLEEL LENSPCSALE GISKWHKIGG SVKDGVLCIL
SQDFLFKALH VLLMSAMAES LDLQHLNVED THHAVGKDIE DEFNPYTREI IETVLNKFAV
QEQEAENNTW RLRIPFIAQW YGIQALRKYV SGISMPIDEF LIKWKSLFPP FFPCDIDIDM
LRGYHFKPTD KTVQYIAKST LPMDPKERFK VLFRLQSQWD LEDIKPLIEE LNSRGMKIDS
FIMKYARRKR LGKKTVVTSR
