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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: -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

Miscellaneous

Present with 2760 molecules/cell in log phase SD medium.1 Publication

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

Keywordsi

Molecular functionDNA-binding
Biological processCell cycle, DNA replication
LigandATP-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiP40339
PaxDbiP40339
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

Show more details

Protein-protein interaction databases

BioGridi34308, 288 interactors
DIPiDIP-2530N
IntActiP40339, 49 interactors
MINTiP40339
STRINGi4932.YOL094C

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
OMAiQSTWSGF
OrthoDBiEOG092C39MN

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR008921 DNA_pol3_clamp-load_cplx_C
IPR027417 P-loop_NTPase
IPR013748 Rep_factorC_C
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF08542 Rep_fac_C, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiRFC4_YEAST
AccessioniPrimary (citable) accession number: P40339
Secondary accession number(s): D6W1X4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: March 28, 2018
This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health