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Protein

Replication factor C subunit 2

Gene

RFC2

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. RFC2 binds ATP and single-stranded DNA.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281ATP; via carbonyl oxygen
Binding sitei32 – 321ATP
Binding sitei171 – 1711ATP
Binding sitei229 – 2291ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi65 – 739ATP

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • purine nucleotide binding Source: SGD

GO - Biological processi

  • DNA replication checkpoint Source: SGD
  • 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-31701-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 2
Short name:
Replication factor C2
Alternative name(s):
Activator 1 41 kDa subunit
Gene namesi
Name:RFC2
Ordered Locus Names:YJR068W
ORF Names:J1808
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR068W.
SGDiS000003829. RFC2.

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: SGD
  • Rad17 RFC-like complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Replication factor C subunit 2PRO_0000121760Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP40348.

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. RFC2 interacts with ECO1.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTF18P499562EBI-14992,EBI-4560
CTF8P388772EBI-14992,EBI-5216
ELG1Q120503EBI-14992,EBI-32195
RAD24P326413EBI-14992,EBI-14675
RFC3P386294EBI-14992,EBI-15000

Protein-protein interaction databases

BioGridi33825. 51 interactions.
DIPiDIP-2528N.
IntActiP40348. 29 interactions.
MINTiMINT-480404.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 304Combined sources
Turni36 – 383Combined sources
Helixi46 – 527Combined sources
Beta strandi61 – 644Combined sources
Helixi71 – 8818Combined sources
Beta strandi91 – 955Combined sources
Beta strandi97 – 993Combined sources
Helixi103 – 1064Combined sources
Helixi109 – 1157Combined sources
Helixi125 – 1284Combined sources
Beta strandi135 – 1395Combined sources
Helixi142 – 1443Combined sources
Helixi147 – 15913Combined sources
Turni160 – 1634Combined sources
Beta strandi164 – 1718Combined sources
Helixi173 – 1753Combined sources
Helixi178 – 1836Combined sources
Beta strandi184 – 1885Combined sources
Helixi194 – 20613Combined sources
Turni207 – 2093Combined sources
Helixi214 – 22310Combined sources
Helixi228 – 23710Combined sources
Helixi239 – 2457Combined sources
Helixi253 – 2608Combined sources
Helixi266 – 27611Combined sources
Helixi280 – 29213Combined sources
Helixi300 – 31011Combined sources
Beta strandi312 – 3143Combined sources
Helixi316 – 33318Combined sources
Helixi339 – 35214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85D1-353[»]
ProteinModelPortaliP40348.
SMRiP40348. Positions 26-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40348.

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074917.
HOGENOMiHOG000224154.
InParanoidiP40348.
KOiK10755.
OMAiMETYSGV.
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.

P40348-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEGFGPNKK RKISKLAAEQ SLAQQPWVEK YRPKNLDEVT AQDHAVTVLK
60 70 80 90 100
KTLKSANLPH MLFYGPPGTG KTSTILALTK ELYGPDLMKS RILELNASDE
110 120 130 140 150
RGISIVREKV KNFARLTVSK PSKHDLENYP CPPYKIIILD EADSMTADAQ
160 170 180 190 200
SALRRTMETY SGVTRFCLIC NYVTRIIDPL ASRCSKFRFK ALDASNAIDR
210 220 230 240 250
LRFISEQENV KCDDGVLERI LDISAGDLRR GITLLQSASK GAQYLGDGKN
260 270 280 290 300
ITSTQVEELA GVVPHDILIE IVEKVKSGDF DEIKKYVNTF MKSGWSAASV
310 320 330 340 350
VNQLHEYYIT NDNFDTNFKN QISWLLFTTD SRLNNGTNEH IQLLNLLVKI

SQL
Length:353
Mass (Da):39,742
Last modified:February 1, 1995 - v1
Checksum:i59B2C4223B0D13BF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121K → R in AAS56246 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28499 Genomic DNA. Translation: BAA05858.1.
U26028 Genomic DNA. Translation: AAC49061.1.
Z49568 Genomic DNA. Translation: CAA89596.1.
L47993 Genomic DNA. Translation: AAB39294.1.
AY557920 Genomic DNA. Translation: AAS56246.1.
BK006943 Genomic DNA. Translation: DAA08855.1.
PIRiS45531.
RefSeqiNP_012602.3. NM_001181726.3.

Genome annotation databases

EnsemblFungiiYJR068W; YJR068W; YJR068W.
GeneIDi853531.
KEGGisce:YJR068W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28499 Genomic DNA. Translation: BAA05858.1.
U26028 Genomic DNA. Translation: AAC49061.1.
Z49568 Genomic DNA. Translation: CAA89596.1.
L47993 Genomic DNA. Translation: AAB39294.1.
AY557920 Genomic DNA. Translation: AAS56246.1.
BK006943 Genomic DNA. Translation: DAA08855.1.
PIRiS45531.
RefSeqiNP_012602.3. NM_001181726.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85D1-353[»]
ProteinModelPortaliP40348.
SMRiP40348. Positions 26-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33825. 51 interactions.
DIPiDIP-2528N.
IntActiP40348. 29 interactions.
MINTiMINT-480404.

Proteomic databases

MaxQBiP40348.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR068W; YJR068W; YJR068W.
GeneIDi853531.
KEGGisce:YJR068W.

Organism-specific databases

EuPathDBiFungiDB:YJR068W.
SGDiS000003829. RFC2.

Phylogenomic databases

GeneTreeiENSGT00550000074917.
HOGENOMiHOG000224154.
InParanoidiP40348.
KOiK10755.
OMAiMETYSGV.
OrthoDBiEOG092C39MN.

Enzyme and pathway databases

BioCyciYEAST:G3O-31701-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

EvolutionaryTraceiP40348.
PROiP40348.

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 nameiRFC2_YEAST
AccessioniPrimary (citable) accession number: P40348
Secondary accession number(s): D6VWN9, E9P8U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 141 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 4610 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.