RFC4_YEAST
ID RFC4_YEAST Reviewed; 323 AA.
AC P40339; D6W1X4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Replication factor C subunit 4;
DE Short=Replication factor C4;
DE AltName: Full=Activator 1 37 kDa subunit;
GN Name=RFC4; OrderedLocusNames=YOL094C; ORFNames=O0923;
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 200060 / W303;
RX PubMed=8063832; DOI=10.1016/s0021-9258(17)31884-7;
RA Li X., Burgers P.M.J.;
RT "Cloning and characterization of the essential Saccharomyces cerevisiae
RT RFC4 gene encoding the 37-kDa subunit of replication factor C.";
RL J. Biol. Chem. 269:21880-21884(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION IN THE RFC COMPLEX.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7651383; DOI=10.1128/mcb.15.9.4661;
RA Cullmann G., Fien K., Kobayashi R., Stillman B.;
RT "Characterization of the five replication factor C genes of Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 15:4661-4671(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533473; DOI=10.1002/yea.320111009;
RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT than twice as many unknown as known open reading frames.";
RL Yeast 11:975-986(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [7]
RP FUNCTION, AND INTERACTION WITH CTF18.
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 [8]
RP INTERACTION WITH ELG1.
RX PubMed=12912927; DOI=10.1093/emboj/cdg406;
RA Bellaoui M., Chang M., Ou J., Xu H., Boone C., Brown G.W.;
RT "Elg1 forms an alternative RFC complex important for DNA replication and
RT genome integrity.";
RL EMBO J. 22:4304-4313(2003).
RN [9]
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 [10]
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 [11]
RP IDENTIFICATION IN THE RAD24-RFC COMPLEX, AND FUNCTION OF THE RAD24-RFC
RP COMPLEX.
RX PubMed=12604797; DOI=10.1073/pnas.0437148100;
RA Majka J., Burgers P.M.J.;
RT "Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2249-2254(2003).
RN [12]
RP IDENTIFICATION IN THE RFC COMPLEX, IDENTIFICATION IN THE RAD24-RFC COMPLEX,
RP IDENTIFICATION IN THE ELG1-RFC COMPLEX, IDENTIFICATION IN THE CTF18-RFC
RP COMPLEX, AND FUNCTION OF THE CTF18-RFC 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).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH AN ATP ANALOG; RCF1;
RP RCF2; RCF3; RCF5 AND PCNA.
RX PubMed=15201901; DOI=10.1038/nature02585;
RA Bowman G.D., O'Donnell M., Kuriyan J.;
RT "Structural analysis of a eukaryotic sliding DNA clamp-clamp loader
RT complex.";
RL Nature 429:724-730(2004).
CC -!- FUNCTION: Component of ATP-dependent clamp loader (RFC and RFC-like)
CC complexes for DNA clamps, such as the POL30/PCNA homotrimer and the
CC checkpoint clamp DDC1:MEC3:RAD17 complex. During a clamp loading
CC circle, the RFC:clamp complex binds to DNA and the recognition of the
CC double-stranded/single-stranded junction stimulates ATP hydrolysis by
CC RFC. The complex presumably provides bipartite ATP sites in which one
CC subunit 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. Component of the replication factor C (RFC or
CC activator 1) complex which loads POL30/PCNA and acts during elongation
CC of primed DNA templates by DNA polymerase delta and epsilon. RFC has an
CC essential but redundant activity in sister chromatid cohesion
CC establishment. Component of the RFC-like complex CTF18-RFC which is
CC required for efficient establishment of chromosome cohesion during S-
CC phase and may load or unload POL30/PCNA. Component of the RFC-like
CC RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17
CC complex and is involved in DNA repair pathways. Component of the RFC-
CC like ELG1-RFC complex which appears to have a role in DNA replication,
CC replication fork re-start, recombination and repair.
CC {ECO:0000269|PubMed:11486023, ECO:0000269|PubMed:12604797,
CC ECO:0000269|PubMed:15964801}.
CC -!- SUBUNIT: Replication factor C (RFC) is a heteropentamer of subunits
CC RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in
CC the presence of ATP. Component of the RAD24-RFC complex which consists
CC of RAD14, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint
CC clamp DDC1:MEC3:RAD17 complex. Component of the ELG1-RFC complex which
CC consists of ELG1, RFC2, RFC3, RFC4 and RFC5. Component of the CTF18-RFC
CC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and
CC RFC5. RFC4 interacts with ECO1. {ECO:0000269|PubMed:11389843,
CC ECO:0000269|PubMed:11486023, ECO:0000269|PubMed:12604797,
CC ECO:0000269|PubMed:12665596, ECO:0000269|PubMed:12912927,
CC ECO:0000269|PubMed:15201901, ECO:0000269|PubMed:15964801,
CC ECO:0000269|PubMed:7651383}.
CC -!- INTERACTION:
CC P40339; P49956: CTF18; NbExp=5; IntAct=EBI-15009, EBI-4560;
CC P40339; P38877: CTF8; NbExp=2; IntAct=EBI-15009, EBI-5216;
CC P40339; Q12050: ELG1; NbExp=5; IntAct=EBI-15009, EBI-32195;
CC P40339; P32641: RAD24; NbExp=2; IntAct=EBI-15009, EBI-14675;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 2760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
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DR EMBL; L20502; AAA34970.1; -; Genomic_DNA.
DR EMBL; U26030; AAC49063.1; -; Genomic_DNA.
DR EMBL; X83121; CAA58185.1; -; Genomic_DNA.
DR EMBL; Z74836; CAA99106.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10690.1; -; Genomic_DNA.
DR PIR; A53845; A53845.
DR RefSeq; NP_014547.1; NM_001183348.1.
DR PDB; 1SXJ; X-ray; 2.85 A; B=1-323.
DR PDB; 7SGZ; EM; 3.17 A; B=1-323.
DR PDB; 7SH2; EM; 3.23 A; B=1-323.
DR PDB; 7ST9; EM; 2.20 A; B=1-323.
DR PDB; 7STB; EM; 2.72 A; B=1-323.
DR PDB; 7STE; EM; 2.73 A; B=1-323.
DR PDB; 7THJ; EM; 3.80 A; B=1-323.
DR PDB; 7THV; EM; 4.00 A; B=1-323.
DR PDB; 7TI8; EM; 3.50 A; B=1-323.
DR PDB; 7TIB; EM; 3.40 A; B=1-323.
DR PDB; 7TIC; EM; 3.90 A; B=1-323.
DR PDB; 7TID; EM; 3.30 A; B=1-323.
DR PDB; 7TKU; EM; 4.00 A; B=1-323.
DR PDBsum; 1SXJ; -.
DR PDBsum; 7SGZ; -.
DR PDBsum; 7SH2; -.
DR PDBsum; 7ST9; -.
DR PDBsum; 7STB; -.
DR PDBsum; 7STE; -.
DR PDBsum; 7THJ; -.
DR PDBsum; 7THV; -.
DR PDBsum; 7TI8; -.
DR PDBsum; 7TIB; -.
DR PDBsum; 7TIC; -.
DR PDBsum; 7TID; -.
DR PDBsum; 7TKU; -.
DR AlphaFoldDB; P40339; -.
DR SMR; P40339; -.
DR BioGRID; 34308; 334.
DR ComplexPortal; CPX-1731; CTF18-RFC complex.
DR ComplexPortal; CPX-1807; Rad17 RFC-like complex.
DR ComplexPortal; CPX-422; ELG1-RFC complex.
DR ComplexPortal; CPX-545; DNA replication factor C complex.
DR DIP; DIP-2530N; -.
DR IntAct; P40339; 47.
DR MINT; P40339; -.
DR STRING; 4932.YOL094C; -.
DR MaxQB; P40339; -.
DR PaxDb; P40339; -.
DR PRIDE; P40339; -.
DR EnsemblFungi; YOL094C_mRNA; YOL094C; YOL094C.
DR GeneID; 854059; -.
DR KEGG; sce:YOL094C; -.
DR SGD; S000005454; RFC4.
DR VEuPathDB; FungiDB:YOL094C; -.
DR eggNOG; KOG0991; Eukaryota.
DR GeneTree; ENSGT00550000075050; -.
DR HOGENOM; CLU_042324_0_1_1; -.
DR InParanoid; P40339; -.
DR OMA; SCNYSSQ; -.
DR BioCyc; YEAST:G3O-33494-MON; -.
DR Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SCE-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-69091; Polymerase switching.
DR EvolutionaryTrace; P40339; -.
DR PRO; PR:P40339; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P40339; protein.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IPI:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005663; C:DNA replication factor C complex; IDA:SGD.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031389; C:Rad17 RFC-like complex; IDA:SGD.
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; IEA:UniProtKB-KW.
DR GO; GO:0090618; P:DNA clamp unloading; IDA:ComplexPortal.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:ComplexPortal.
DR GO; GO:0006272; P:leading strand elongation; IDA:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IC:ComplexPortal.
DR GO; GO:0007062; P:sister chromatid cohesion; IDA:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013748; Rep_factorC_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 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..323
FT /note="Replication factor C subunit 4"
FT /id="PRO_0000121771"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 49..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 255..260
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 282..300
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:1SXJ"
SQ SEQUENCE 323 AA; 36149 MW; 1F55F35F0713331F CRC64;
MSKTLSLQLP WVEKYRPQVL SDIVGNKETI DRLQQIAKDG NMPHMIISGM PGIGKTTSVH
CLAHELLGRS YADGVLELNA SDDRGIDVVR NQIKHFAQKK LHLPPGKHKI VILDEADSMT
AGAQQALRRT MELYSNSTRF AFACNQSNKI IEPLQSRCAI LRYSKLSDED VLKRLLQIIK
LEDVKYTNDG LEAIIFTAEG DMRQAINNLQ STVAGHGLVN ADNVFKIVDS PHPLIVKKML
LASNLEDSIQ ILRTDLWKKG YSSIDIVTTS FRVTKNLAQV KESVRLEMIK EIGLTHMRIL
EGVGTYLQLA SMLAKIHKLN NKA
