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Protein

Replication factor C subunit 3

Gene

RFC3

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. RFC3 supplies a catalytic site to the ATP site of RFC4.4 Publications

Miscellaneous

Present with 3140 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei20ATP1
Binding sitei28ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei148ATP1
Binding sitei206ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi16 – 19ATP4
Nucleotide bindingi53 – 61ATP9

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW

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-33280-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 3
Short name:
Replication factor C3
Alternative name(s):
Activator 1 40 kDa subunit
Gene namesi
Name:RFC3
Ordered Locus Names:YNL290W
ORF Names:N0533
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL290W
SGDiS000005234 RFC3

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
Initiator methionineiRemovedCombined sources
ChainiPRO_00001217562 – 340Replication factor C subunit 3Add BLAST339

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP38629
PaxDbiP38629
PRIDEiP38629

PTM databases

iPTMnetiP38629

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. RFC3 interacts with ECO1 and POL30/PCNA.9 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi35547, 98 interactors
DIPiDIP-2529N
IntActiP38629, 40 interactors
MINTiP38629
STRINGi4932.YNL290W

Structurei

Secondary structure

1340
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 18Combined sources4
Helixi24 – 26Combined sources3
Helixi31 – 42Combined sources12
Beta strandi49 – 52Combined sources4
Beta strandi54 – 58Combined sources5
Helixi59 – 71Combined sources13
Helixi75 – 78Combined sources4
Beta strandi79 – 82Combined sources4
Helixi90 – 94Combined sources5
Helixi96 – 102Combined sources7
Beta strandi106 – 108Combined sources3
Beta strandi112 – 116Combined sources5
Helixi119 – 121Combined sources3
Helixi124 – 136Combined sources13
Turni137 – 140Combined sources4
Beta strandi141 – 148Combined sources8
Helixi150 – 152Combined sources3
Helixi155 – 158Combined sources4
Beta strandi161 – 165Combined sources5
Helixi171 – 183Combined sources13
Turni184 – 186Combined sources3
Helixi191 – 201Combined sources11
Helixi205 – 211Combined sources7
Turni212 – 218Combined sources7
Beta strandi221 – 223Combined sources3
Helixi229 – 235Combined sources7
Helixi241 – 252Combined sources12
Helixi256 – 268Combined sources13
Turni269 – 271Combined sources3
Helixi274 – 285Combined sources12
Helixi293 – 310Combined sources18
Helixi316 – 330Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85C1-340[»]
ProteinModelPortaliP38629
SMRiP38629
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38629

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000075072
HOGENOMiHOG000224152
InParanoidiP38629
KOiK10756
OMAiCTGNPHP
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38629-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSTEKRSK ENLPWVEKYR PETLDEVYGQ NEVITTVRKF VDEGKLPHLL
60 70 80 90 100
FYGPPGTGKT STIVALAREI YGKNYSNMVL ELNASDDRGI DVVRNQIKDF
110 120 130 140 150
ASTRQIFSKG FKLIILDEAD AMTNAAQNAL RRVIERYTKN TRFCVLANYA
160 170 180 190 200
HKLTPALLSR CTRFRFQPLP QEAIERRIAN VLVHEKLKLS PNAEKALIEL
210 220 230 240 250
SNGDMRRVLN VLQSCKATLD NPDEDEISDD VIYECCGAPR PSDLKAVLKS
260 270 280 290 300
ILEDDWGTAH YTLNKVRSAK GLALIDLIEG IVKILEDYEL QNEETRVHLL
310 320 330 340
TKLADIEYSI SKGGNDQIQG SAVIGAIKAS FENETVKANV
Length:340
Mass (Da):38,204
Last modified:October 1, 1994 - v1
Checksum:i0170EDABAB5CEA52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18755 Genomic DNA Translation: AAA34969.1
U26029 Genomic DNA Translation: AAC49062.1
U23084 Genomic DNA Translation: AAC49110.1
Z71566 Genomic DNA Translation: CAA96207.1
BK006947 Genomic DNA Translation: DAA10269.1
PIRiA36988
RefSeqiNP_014109.1, NM_001183128.1

Genome annotation databases

EnsemblFungiiYNL290W; YNL290W; YNL290W
GeneIDi855426
KEGGisce:YNL290W

Similar proteinsi

Entry informationi

Entry nameiRFC3_YEAST
AccessioniPrimary (citable) accession number: P38629
Secondary accession number(s): D6W0Q3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 23, 2018
This is version 152 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

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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

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