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Protein

Replication factor C subunit 5

Gene

RFC5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of ATP-dependent clamp loader (RFC and RFC-like) complexes for DNA clamps, such as the POL30/PCNA homotrimer and the checkpoint clamp DDC1:MEC3:RAD17 complex. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Component of the replication factor C (RFC or activator 1) complex which loads POL30/PCNA and acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. Component of the RFC-like RAD24-RFC complex which loads the checkpoint clamp DDC1:MEC3:RAD17 complex and is involved in DNA repair pathways. Component of the RFC-like ELG1-RFC complex which appears to have a role in DNA replication, replication fork re-start, recombination and repair.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei5ATP; via carbonyl oxygen1
Binding sitei17ATP1
Binding sitei231ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi43 – 51ATP9

GO - Molecular functioni

GO - Biological processi

  • leading strand elongation Source: SGD
  • sister chromatid cohesion Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29054-MONOMER.
ReactomeiR-SCE-110312. Translesion synthesis by REV1.
R-SCE-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SCE-110320. Translesion Synthesis by POLH.
R-SCE-174411. Polymerase switching on the C-strand of the telomere.
R-SCE-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SCE-5655862. Translesion synthesis by POLK.
R-SCE-5656121. Translesion synthesis by POLI.
R-SCE-5656169. Termination of translesion DNA synthesis.
R-SCE-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SCE-69091. Polymerase switching.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication factor C subunit 5
Short name:
Replication factor C5
Alternative name(s):
Activator 1 40 kDa subunit
Gene namesi
Name:RFC5
Ordered Locus Names:YBR087W
ORF Names:YBR0810
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR087W.
SGDiS000000291. RFC5.

Subcellular locationi

GO - Cellular componenti

  • Ctf18 RFC-like complex Source: SGD
  • DNA replication factor C complex Source: SGD
  • Elg1 RFC-like complex Source: SGD
  • nucleus Source: UniProtKB-SubCell
  • Rad17 RFC-like complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001217651 – 354Replication factor C subunit 5Add BLAST354

Proteomic databases

MaxQBiP38251.
PRIDEiP38251.

PTM databases

iPTMnetiP38251.

Interactioni

Subunit structurei

Replication factor C (RFC) is a heteropentamer of subunits RFC1, RFC2, RFC3, RFC4 and RFC5 and forms a complex with POL30/PCNA in the presence of ATP. Component of the RAD24-RFC complex which consists of RAD24, RFC2, RFC3, RFC4 and RFC5 and associates with the checkpoint clamp DDC1:MEC3:RAD17 complex. Component of the ELG1-RFC complex which consists of ELG1, RFC2, RFC3, RFC4 and RFC5. Component of the CTF18-RFC complex, which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. RFC5 interacts with ECO1.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTF18P499565EBI-15016,EBI-4560
CTF8P388772EBI-15016,EBI-5216
ELG1Q120505EBI-15016,EBI-32195
RAD24P326412EBI-15016,EBI-14675

Protein-protein interaction databases

BioGridi32793. 152 interactors.
DIPiDIP-2531N.
IntActiP38251. 14 interactors.
MINTiMINT-480383.

Structurei

Secondary structure

1354
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni5 – 8Combined sources4
Helixi13 – 15Combined sources3
Helixi20 – 27Combined sources8
Turni28 – 31Combined sources4
Beta strandi39 – 42Combined sources4
Helixi49 – 54Combined sources6
Helixi56 – 60Combined sources5
Beta strandi91 – 96Combined sources6
Helixi106 – 116Combined sources11
Turni117 – 120Combined sources4
Beta strandi136 – 141Combined sources6
Helixi148 – 160Combined sources13
Turni162 – 164Combined sources3
Beta strandi165 – 172Combined sources8
Helixi179 – 182Combined sources4
Beta strandi185 – 189Combined sources5
Helixi195 – 209Combined sources15
Helixi217 – 226Combined sources10
Helixi230 – 237Combined sources8
Helixi239 – 242Combined sources4
Turni243 – 246Combined sources4
Helixi258 – 272Combined sources15
Helixi276 – 290Combined sources15
Turni291 – 293Combined sources3
Helixi296 – 305Combined sources10
Turni306 – 309Combined sources4
Helixi315 – 333Combined sources19
Helixi338 – 353Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85E1-354[»]
ProteinModelPortaliP38251.
SMRiP38251.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38251.

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075006.
HOGENOMiHOG000224153.
InParanoidiP38251.
KOiK10756.
OMAiMGNNDRV.
OrthoDBiEOG092C317A.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

P38251-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLWVDKYRP KSLNALSHNE ELTNFLKSLS DQPRDLPHLL LYGPNGTGKK
60 70 80 90 100
TRCMALLESI FGPGVYRLKI DVRQFVTASN RKLELNVVSS PYHLEITPSD
110 120 130 140 150
MGNNDRIVIQ ELLKEVAQME QVDFQDSKDG LAHRYKCVII NEANSLTKDA
160 170 180 190 200
QAALRRTMEK YSKNIRLIMV CDSMSPIIAP IKSRCLLIRC PAPSDSEIST
210 220 230 240 250
ILSDVVTNER IQLETKDILK RIAQASNGNL RVSLLMLESM ALNNELALKS
260 270 280 290 300
SSPIIKPDWI IVIHKLTRKI VKERSVNSLI ECRAVLYDLL AHCIPANIIL
310 320 330 340 350
KELTFSLLDV ETLNTTNKSS IIEYSSVFDE RLSLGNKAIF HLEGFIAKVM

CCLD
Length:354
Mass (Da):39,942
Last modified:October 1, 1994 - v1
Checksum:i4CD403AF2AFA2961
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26031 Genomic DNA. Translation: AAC49065.1.
X78993 Genomic DNA. Translation: CAA55595.1.
Z35956 Genomic DNA. Translation: CAA85036.1.
AY693173 Genomic DNA. Translation: AAT93192.1.
BK006936 Genomic DNA. Translation: DAA07208.1.
PIRiS48257.
RefSeqiNP_009644.3. NM_001178435.3.

Genome annotation databases

EnsemblFungiiYBR087W; YBR087W; YBR087W.
GeneIDi852383.
KEGGisce:YBR087W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26031 Genomic DNA. Translation: AAC49065.1.
X78993 Genomic DNA. Translation: CAA55595.1.
Z35956 Genomic DNA. Translation: CAA85036.1.
AY693173 Genomic DNA. Translation: AAT93192.1.
BK006936 Genomic DNA. Translation: DAA07208.1.
PIRiS48257.
RefSeqiNP_009644.3. NM_001178435.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85E1-354[»]
ProteinModelPortaliP38251.
SMRiP38251.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32793. 152 interactors.
DIPiDIP-2531N.
IntActiP38251. 14 interactors.
MINTiMINT-480383.

PTM databases

iPTMnetiP38251.

Proteomic databases

MaxQBiP38251.
PRIDEiP38251.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR087W; YBR087W; YBR087W.
GeneIDi852383.
KEGGisce:YBR087W.

Organism-specific databases

EuPathDBiFungiDB:YBR087W.
SGDiS000000291. RFC5.

Phylogenomic databases

GeneTreeiENSGT00550000075006.
HOGENOMiHOG000224153.
InParanoidiP38251.
KOiK10756.
OMAiMGNNDRV.
OrthoDBiEOG092C317A.

Enzyme and pathway databases

BioCyciYEAST:G3O-29054-MONOMER.
ReactomeiR-SCE-110312. Translesion synthesis by REV1.
R-SCE-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SCE-110320. Translesion Synthesis by POLH.
R-SCE-174411. Polymerase switching on the C-strand of the telomere.
R-SCE-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SCE-5655862. Translesion synthesis by POLK.
R-SCE-5656121. Translesion synthesis by POLI.
R-SCE-5656169. Termination of translesion DNA synthesis.
R-SCE-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SCE-5696400. Dual Incision in GG-NER.
R-SCE-6782135. Dual incision in TC-NER.
R-SCE-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SCE-69091. Polymerase switching.

Miscellaneous databases

EvolutionaryTraceiP38251.
PROiP38251.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRFC5_YEAST
AccessioniPrimary (citable) accession number: P38251
Secondary accession number(s): D6VQ88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5040 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.