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

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
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

ATP-binding, DNA-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

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
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.
PRIDEiP38629.

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

WithEntry#Exp.IntActNotes
CTF18P499564EBI-15000,EBI-4560
CTF8P388772EBI-15000,EBI-5216
RAD24P326413EBI-15000,EBI-14675
RFC2P403484EBI-15000,EBI-14992

Protein-protein interaction databases

BioGridi35547. 90 interactors.
DIPiDIP-2529N.
IntActiP38629. 14 interactors.
MINTiMINT-540713.

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.
OMAiSHKLNPA.
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.

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi35547. 90 interactors.
DIPiDIP-2529N.
IntActiP38629. 14 interactors.
MINTiMINT-540713.

Proteomic databases

MaxQBiP38629.
PRIDEiP38629.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL290W; YNL290W; YNL290W.
GeneIDi855426.
KEGGisce:YNL290W.

Organism-specific databases

EuPathDBiFungiDB:YNL290W.
SGDiS000005234. RFC3.

Phylogenomic databases

GeneTreeiENSGT00550000075072.
HOGENOMiHOG000224152.
InParanoidiP38629.
KOiK10756.
OMAiSHKLNPA.
OrthoDBiEOG092C39MN.

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.

Miscellaneous databases

EvolutionaryTraceiP38629.
PROiP38629.

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 nameiRFC3_YEAST
AccessioniPrimary (citable) accession number: P38629
Secondary accession number(s): D6W0Q3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 139 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 3140 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.