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Protein

Replication factor C subunit 4

Gene

RFC4

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.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei12ATP; via carbonyl oxygen1
Binding sitei24ATP; via amide nitrogen1
Binding sitei145ATP1
Binding sitei203ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi49 – 57ATP9

GO - Molecular functioni

GO - Biological processi

  • leading strand elongation Source: SGD
  • mismatch repair 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-33494-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 4
Short name:
Replication factor C4
Alternative name(s):
Activator 1 37 kDa subunit
Gene namesi
Name:RFC4
Ordered Locus Names:YOL094C
ORF Names:O0923
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL094C.
SGDiS000005454. RFC4.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001217711 – 323Replication factor C subunit 4Add BLAST323

Proteomic databases

MaxQBiP40339.
PRIDEiP40339.

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 RAD14, 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. RFC4 interacts with ECO1.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTF18P499566EBI-15009,EBI-4560
CTF8P388772EBI-15009,EBI-5216
ELG1Q120504EBI-15009,EBI-32195
RAD24P326412EBI-15009,EBI-14675

Protein-protein interaction databases

BioGridi34308. 98 interactors.
DIPiDIP-2530N.
IntActiP40339. 18 interactors.
MINTiMINT-540691.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 14Combined sources4
Helixi20 – 22Combined sources3
Helixi28 – 38Combined sources11
Beta strandi45 – 48Combined sources4
Helixi55 – 67Combined sources13
Helixi68 – 70Combined sources3
Helixi71 – 74Combined sources4
Beta strandi75 – 78Combined sources4
Helixi86 – 90Combined sources5
Helixi92 – 98Combined sources7
Beta strandi109 – 115Combined sources7
Helixi116 – 118Combined sources3
Helixi121 – 125Combined sources5
Helixi128 – 133Combined sources6
Turni134 – 137Combined sources4
Beta strandi138 – 145Combined sources8
Helixi147 – 149Combined sources3
Helixi152 – 155Combined sources4
Beta strandi158 – 162Combined sources5
Helixi168 – 182Combined sources15
Helixi188 – 198Combined sources11
Helixi202 – 216Combined sources15
Beta strandi217 – 219Combined sources3
Helixi221 – 228Combined sources8
Helixi233 – 240Combined sources8
Helixi245 – 254Combined sources10
Turni255 – 260Combined sources6
Helixi263 – 275Combined sources13
Helixi282 – 300Combined sources19
Helixi306 – 319Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85B1-323[»]
ProteinModelPortaliP40339.
SMRiP40339.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40339.

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075050.
HOGENOMiHOG000224155.
InParanoidiP40339.
KOiK10755.
OMAiMIISGMP.
OrthoDBiEOG092C39MN.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

P40339-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTLSLQLP WVEKYRPQVL SDIVGNKETI DRLQQIAKDG NMPHMIISGM
60 70 80 90 100
PGIGKTTSVH CLAHELLGRS YADGVLELNA SDDRGIDVVR NQIKHFAQKK
110 120 130 140 150
LHLPPGKHKI VILDEADSMT AGAQQALRRT MELYSNSTRF AFACNQSNKI
160 170 180 190 200
IEPLQSRCAI LRYSKLSDED VLKRLLQIIK LEDVKYTNDG LEAIIFTAEG
210 220 230 240 250
DMRQAINNLQ STVAGHGLVN ADNVFKIVDS PHPLIVKKML LASNLEDSIQ
260 270 280 290 300
ILRTDLWKKG YSSIDIVTTS FRVTKNLAQV KESVRLEMIK EIGLTHMRIL
310 320
EGVGTYLQLA SMLAKIHKLN NKA
Length:323
Mass (Da):36,149
Last modified:February 1, 1995 - v1
Checksum:i1F55F35F0713331F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20502 Genomic DNA. Translation: AAA34970.1.
U26030 Genomic DNA. Translation: AAC49063.1.
X83121 Genomic DNA. Translation: CAA58185.1.
Z74836 Genomic DNA. Translation: CAA99106.1.
BK006948 Genomic DNA. Translation: DAA10690.1.
PIRiA53845.
RefSeqiNP_014547.1. NM_001183348.1.

Genome annotation databases

EnsemblFungiiYOL094C; YOL094C; YOL094C.
GeneIDi854059.
KEGGisce:YOL094C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20502 Genomic DNA. Translation: AAA34970.1.
U26030 Genomic DNA. Translation: AAC49063.1.
X83121 Genomic DNA. Translation: CAA58185.1.
Z74836 Genomic DNA. Translation: CAA99106.1.
BK006948 Genomic DNA. Translation: DAA10690.1.
PIRiA53845.
RefSeqiNP_014547.1. NM_001183348.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85B1-323[»]
ProteinModelPortaliP40339.
SMRiP40339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34308. 98 interactors.
DIPiDIP-2530N.
IntActiP40339. 18 interactors.
MINTiMINT-540691.

Proteomic databases

MaxQBiP40339.
PRIDEiP40339.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL094C; YOL094C; YOL094C.
GeneIDi854059.
KEGGisce:YOL094C.

Organism-specific databases

EuPathDBiFungiDB:YOL094C.
SGDiS000005454. RFC4.

Phylogenomic databases

GeneTreeiENSGT00550000075050.
HOGENOMiHOG000224155.
InParanoidiP40339.
KOiK10755.
OMAiMIISGMP.
OrthoDBiEOG092C39MN.

Enzyme and pathway databases

BioCyciYEAST:G3O-33494-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

EvolutionaryTraceiP40339.
PROiP40339.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR027417. P-loop_NTPase.
IPR013748. Rep_factorC_C.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF08542. Rep_fac_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRFC4_YEAST
AccessioniPrimary (citable) accession number: P40339
Secondary accession number(s): D6W1X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 142 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 2760 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.