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Protein

Replication factor C subunit 1

Gene

RFC1

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 the ATP-dependent clamp loader RFC complex for the POL30/PCNA homotrimer DNA clamp. 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. Replication factor C (RFC or activator 1) complex 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei299 – 2991ATP; via carbonyl oxygen
Binding sitei311 – 3111ATP; via amide nitrogen and carbonyl oxygen
Binding sitei456 – 4561ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi353 – 3619ATP

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • DNA repair Source: SGD
  • leading strand elongation Source: SGD
  • mismatch repair Source: SGD
  • mitotic cell cycle Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33719-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 1
Short name:
Replication factor C1
Alternative name(s):
Activator 1 95 kDa subunit
Cell division control protein 44
Gene namesi
Name:RFC1
Synonyms:CDC44
Ordered Locus Names:YOR217W
ORF Names:YOR50-7
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR217W.
SGDiS000005743. RFC1.

Subcellular locationi

GO - Cellular componenti

  • DNA replication factor C complex Source: SGD
  • nucleus Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi427 – 4271D → H in cs mutant CDC44-2; causes cell cycle arrest. 1 Publication
Mutagenesisi436 – 4361G → R in cs mutant CDC44-3/4; causes cell cycle arrest. 1 Publication
Mutagenesisi512 – 5121G → A in cs mutant CDC44-9; no effect. 1 Publication
Mutagenesisi513 – 5131D → N in cs mutants CDC44-1/5/8 and CDC44-9; causes cell cycle arrest. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 861861Replication factor C subunit 1PRO_0000121776Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381PhosphothreonineCombined sources
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei63 – 631PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38630.

PTM databases

iPTMnetiP38630.

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. Interacts with ECO1 and POL30/PCNA.5 Publications

Protein-protein interaction databases

BioGridi34612. 65 interactions.
DIPiDIP-2527N.
IntActiP38630. 13 interactions.
MINTiMINT-619267.

Structurei

Secondary structure

1
861
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi298 – 3014Combined sources
Helixi307 – 3093Combined sources
Helixi314 – 32512Combined sources
Helixi327 – 3326Combined sources
Turni333 – 3353Combined sources
Beta strandi347 – 3526Combined sources
Helixi359 – 36911Combined sources
Beta strandi373 – 3775Combined sources
Helixi385 – 3906Combined sources
Helixi392 – 3954Combined sources
Turni402 – 4065Combined sources
Beta strandi418 – 4236Combined sources
Helixi426 – 4283Combined sources
Helixi436 – 44611Combined sources
Beta strandi451 – 4566Combined sources
Helixi464 – 4663Combined sources
Turni467 – 4693Combined sources
Beta strandi470 – 4745Combined sources
Helixi480 – 49314Combined sources
Helixi502 – 5098Combined sources
Turni510 – 5123Combined sources
Helixi514 – 5218Combined sources
Helixi523 – 5275Combined sources
Helixi535 – 54410Combined sources
Turni545 – 5484Combined sources
Helixi550 – 5589Combined sources
Helixi561 – 5633Combined sources
Helixi568 – 5703Combined sources
Helixi574 – 5818Combined sources
Turni585 – 5873Combined sources
Helixi588 – 5958Combined sources
Beta strandi596 – 6027Combined sources
Helixi610 – 63122Combined sources
Helixi638 – 6403Combined sources
Helixi641 – 6488Combined sources
Helixi650 – 6545Combined sources
Helixi669 – 68719Combined sources
Turni688 – 6925Combined sources
Helixi699 – 7035Combined sources
Turni704 – 7063Combined sources
Helixi707 – 7148Combined sources
Helixi725 – 7306Combined sources
Turni731 – 7333Combined sources
Helixi737 – 74610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85A295-785[»]
ProteinModelPortaliP38630.
SMRiP38630. Positions 151-243, 298-554.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38630.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 24391BRCTPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi830 – 8345Nuclear localization signalSequence analysis
Motifi855 – 8606Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the activator 1 large subunit family.Curated
Contains 1 BRCT domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00730000111066.
HOGENOMiHOG000164552.
InParanoidiP38630.
KOiK10754.
OMAiQENYLRT.
OrthoDBiEOG092C1OUP.

Family and domain databases

Gene3Di3.40.50.10190. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR001357. BRCT_dom.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR013725. DNA_replication_fac_RFC1_C.
IPR027417. P-loop_NTPase.
IPR012178. RFC1.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF00533. BRCT. 1 hit.
PF08519. RFC1. 1 hit.
[Graphical view]
PIRSFiPIRSF036578. RFC1. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38630-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNISDFFGK NKKSVRSSTS RPTRQVGSSK PEVIDLDTES DQESTNKTPK
60 70 80 90 100
KMPVSNVIDV SETPEGEKKL PLPAKRKASS PTVKPASSKK TKPSSKSSDS
110 120 130 140 150
ASNITAQDVL DKIPSLDLSN VHVKENAKFD FKSANSNADP DEIVSEIGSF
160 170 180 190 200
PEGKPNCLLG LTIVFTGVLP TLERGASEAL AKRYGARVTK SISSKTSVVV
210 220 230 240 250
LGDEAGPKKL EKIKQLKIKA IDEEGFKQLI AGMPAEGGDG EAAEKARRKL
260 270 280 290 300
EEQHNIATKE AELLVKKEEE RSKKLAATRV SGGHLERDNV VREEDKLWTV
310 320 330 340 350
KYAPTNLQQV CGNKGSVMKL KNWLANWENS KKNSFKHAGK DGSGVFRAAM
360 370 380 390 400
LYGPPGIGKT TAAHLVAQEL GYDILEQNAS DVRSKTLLNA GVKNALDNMS
410 420 430 440 450
VVGYFKHNEE AQNLNGKHFV IIMDEVDGMS GGDRGGVGQL AQFCRKTSTP
460 470 480 490 500
LILICNERNL PKMRPFDRVC LDIQFRRPDA NSIKSRLMTI AIREKFKLDP
510 520 530 540 550
NVIDRLIQTT RGDIRQVINL LSTISTTTKT INHENINEIS KAWEKNIALK
560 570 580 590 600
PFDIAHKMLD GQIYSDIGSR NFTLNDKIAL YFDDFDFTPL MIQENYLSTR
610 620 630 640 650
PSVLKPGQSH LEAVAEAANC ISLGDIVEKK IRSSEQLWSL LPLHAVLSSV
660 670 680 690 700
YPASKVAGHM AGRINFTAWL GQNSKSAKYY RLLQEIHYHT RLGTSTDKIG
710 720 730 740 750
LRLDYLPTFR KRLLDPFLKQ GADAISSVIE VMDDYYLTKE DWDSIMEFFV
760 770 780 790 800
GPDVTTAIIK KIPATVKSGF TRKYNSMTHP VAIYRTGSTI GGGGVGTSTS
810 820 830 840 850
TPDFEDVVDA DDNPVPADDE ETQDSSTDLK KDKLIKQKAK PTKRKTATSK
860
PGGSKKRKTK A
Length:861
Mass (Da):94,903
Last modified:October 1, 1994 - v1
Checksum:iA7D9208D66DD9A98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03102 Unassigned DNA. Translation: AAC48916.1.
U26027 Genomic DNA. Translation: AAC49060.1.
X92441 Genomic DNA. Translation: CAA63180.1.
Z75125 Genomic DNA. Translation: CAA99434.1.
BK006948 Genomic DNA. Translation: DAA10989.1.
PIRiS44763.
RefSeqiNP_014860.1. NM_001183636.1.

Genome annotation databases

EnsemblFungiiYOR217W; YOR217W; YOR217W.
GeneIDi854392.
KEGGisce:YOR217W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03102 Unassigned DNA. Translation: AAC48916.1.
U26027 Genomic DNA. Translation: AAC49060.1.
X92441 Genomic DNA. Translation: CAA63180.1.
Z75125 Genomic DNA. Translation: CAA99434.1.
BK006948 Genomic DNA. Translation: DAA10989.1.
PIRiS44763.
RefSeqiNP_014860.1. NM_001183636.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85A295-785[»]
ProteinModelPortaliP38630.
SMRiP38630. Positions 151-243, 298-554.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34612. 65 interactions.
DIPiDIP-2527N.
IntActiP38630. 13 interactions.
MINTiMINT-619267.

PTM databases

iPTMnetiP38630.

Proteomic databases

MaxQBiP38630.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR217W; YOR217W; YOR217W.
GeneIDi854392.
KEGGisce:YOR217W.

Organism-specific databases

EuPathDBiFungiDB:YOR217W.
SGDiS000005743. RFC1.

Phylogenomic databases

GeneTreeiENSGT00730000111066.
HOGENOMiHOG000164552.
InParanoidiP38630.
KOiK10754.
OMAiQENYLRT.
OrthoDBiEOG092C1OUP.

Enzyme and pathway databases

BioCyciYEAST:G3O-33719-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

EvolutionaryTraceiP38630.
PROiP38630.

Family and domain databases

Gene3Di3.40.50.10190. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR001357. BRCT_dom.
IPR008921. DNA_pol3_clamp-load_cplx_C.
IPR013725. DNA_replication_fac_RFC1_C.
IPR027417. P-loop_NTPase.
IPR012178. RFC1.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF00533. BRCT. 1 hit.
PF08519. RFC1. 1 hit.
[Graphical view]
PIRSFiPIRSF036578. RFC1. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF48019. SSF48019. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRFC1_YEAST
AccessioniPrimary (citable) accession number: P38630
Secondary accession number(s): D6W2S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: September 7, 2016
This is version 155 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 2360 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.