RFC5_YEAST
ID RFC5_YEAST Reviewed; 354 AA.
AC P38251; D6VQ88;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Replication factor C subunit 5;
DE Short=Replication factor C5;
DE AltName: Full=Activator 1 40 kDa subunit;
GN Name=RFC5; OrderedLocusNames=YBR087W; ORFNames=YBR0810;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP CHARACTERIZATION.
RX PubMed=8559655; DOI=10.1093/nar/23.24.4986;
RA Gary S.L., Burgers P.M.J.;
RT "Identification of the fifth subunit of Saccharomyces cerevisiae
RT replication factor C.";
RL Nucleic Acids Res. 23:4986-4991(1995).
RN [7]
RP FUNCTION, AND INTERACTION WITH RAD24.
RX PubMed=10913172; DOI=10.1128/mcb.20.16.5888-5896.2000;
RA Naiki T., Shimomura T., Kondo T., Matsumoto K., Sugimoto K.;
RT "Rfc5, in cooperation with rad24, controls DNA damage checkpoints
RT throughout the cell cycle in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 20:5888-5896(2000).
RN [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION, AND 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 [12]
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 [13]
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 [14]
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH AN ATP ANALOG; RCF1;
RP RCF2; RCF3; RCF4 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:10913172, ECO:0000269|PubMed:11486023,
CC ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12665596,
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 RAD24, 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. RFC5 interacts with ECO1. {ECO:0000269|PubMed:10913172,
CC ECO:0000269|PubMed:11389843, ECO:0000269|PubMed:11486023,
CC ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12665596,
CC ECO:0000269|PubMed:12912927, ECO:0000269|PubMed:15201901,
CC ECO:0000269|PubMed:15964801, ECO:0000269|PubMed:7651383}.
CC -!- INTERACTION:
CC P38251; P49956: CTF18; NbExp=4; IntAct=EBI-15016, EBI-4560;
CC P38251; P38877: CTF8; NbExp=2; IntAct=EBI-15016, EBI-5216;
CC P38251; Q12050: ELG1; NbExp=4; IntAct=EBI-15016, EBI-32195;
CC P38251; P32641: RAD24; NbExp=4; IntAct=EBI-15016, EBI-14675;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 5040 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; U26031; AAC49065.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55595.1; -; Genomic_DNA.
DR EMBL; Z35956; CAA85036.1; -; Genomic_DNA.
DR EMBL; AY693173; AAT93192.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07208.1; -; Genomic_DNA.
DR PIR; S48257; S48257.
DR RefSeq; NP_009644.3; NM_001178435.3.
DR PDB; 1SXJ; X-ray; 2.85 A; E=1-354.
DR PDB; 7SGZ; EM; 3.17 A; E=1-354.
DR PDB; 7SH2; EM; 3.23 A; E=1-354.
DR PDB; 7ST9; EM; 2.20 A; E=1-354.
DR PDB; 7STB; EM; 2.72 A; E=1-354.
DR PDB; 7STE; EM; 2.73 A; E=1-354.
DR PDB; 7THJ; EM; 3.80 A; E=1-354.
DR PDB; 7THV; EM; 4.00 A; E=1-354.
DR PDB; 7TI8; EM; 3.50 A; E=1-354.
DR PDB; 7TIB; EM; 3.40 A; E=1-354.
DR PDB; 7TIC; EM; 3.90 A; E=1-354.
DR PDB; 7TID; EM; 3.30 A; E=1-354.
DR PDB; 7TKU; EM; 4.00 A; E=1-354.
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; P38251; -.
DR SMR; P38251; -.
DR BioGRID; 32793; 316.
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-2531N; -.
DR IntAct; P38251; 15.
DR MINT; P38251; -.
DR STRING; 4932.YBR087W; -.
DR iPTMnet; P38251; -.
DR MaxQB; P38251; -.
DR PaxDb; P38251; -.
DR PRIDE; P38251; -.
DR EnsemblFungi; YBR087W_mRNA; YBR087W; YBR087W.
DR GeneID; 852383; -.
DR KEGG; sce:YBR087W; -.
DR SGD; S000000291; RFC5.
DR VEuPathDB; FungiDB:YBR087W; -.
DR eggNOG; KOG2035; Eukaryota.
DR GeneTree; ENSGT00550000075006; -.
DR HOGENOM; CLU_042324_5_0_1; -.
DR InParanoid; P38251; -.
DR OMA; LMCEACK; -.
DR BioCyc; YEAST:G3O-29054-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; P38251; -.
DR PRO; PR:P38251; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38251; protein.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IPI: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:ComplexPortal.
DR GO; GO:0031389; C:Rad17 RFC-like complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
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..354
FT /note="Replication factor C subunit 5"
FT /id="PRO_0000121765"
FT BINDING 5
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 43..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 148..160
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:1SXJ"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 195..209
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 258..272
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:1SXJ"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 315..333
FT /evidence="ECO:0007829|PDB:1SXJ"
FT HELIX 338..353
FT /evidence="ECO:0007829|PDB:1SXJ"
SQ SEQUENCE 354 AA; 39942 MW; 4CD403AF2AFA2961 CRC64;
MSLWVDKYRP KSLNALSHNE ELTNFLKSLS DQPRDLPHLL LYGPNGTGKK TRCMALLESI
FGPGVYRLKI DVRQFVTASN RKLELNVVSS PYHLEITPSD MGNNDRIVIQ ELLKEVAQME
QVDFQDSKDG LAHRYKCVII NEANSLTKDA QAALRRTMEK YSKNIRLIMV CDSMSPIIAP
IKSRCLLIRC PAPSDSEIST ILSDVVTNER IQLETKDILK RIAQASNGNL RVSLLMLESM
ALNNELALKS SSPIIKPDWI IVIHKLTRKI VKERSVNSLI ECRAVLYDLL AHCIPANIIL
KELTFSLLDV ETLNTTNKSS IIEYSSVFDE RLSLGNKAIF HLEGFIAKVM CCLD
