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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)DescriptionActionsGraphical viewLength
Binding sitei299ATP; via carbonyl oxygen1
Binding sitei311ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei456ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi353 – 361ATP9

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)DescriptionActionsGraphical viewLength
Mutagenesisi427D → H in cs mutant CDC44-2; causes cell cycle arrest. 1 Publication1
Mutagenesisi436G → R in cs mutant CDC44-3/4; causes cell cycle arrest. 1 Publication1
Mutagenesisi512G → A in cs mutant CDC44-9; no effect. 1 Publication1
Mutagenesisi513D → N in cs mutants CDC44-1/5/8 and CDC44-9; causes cell cycle arrest. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001217761 – 861Replication factor C subunit 1Add BLAST861

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38PhosphothreonineCombined sources1
Modified residuei40PhosphoserineCombined sources1
Modified residuei63PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38630.
PRIDEiP38630.

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 interactors.
DIPiDIP-2527N.
IntActiP38630. 13 interactors.
MINTiMINT-619267.

Structurei

Secondary structure

1861
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi298 – 301Combined sources4
Helixi307 – 309Combined sources3
Helixi314 – 325Combined sources12
Helixi327 – 332Combined sources6
Turni333 – 335Combined sources3
Beta strandi347 – 352Combined sources6
Helixi359 – 369Combined sources11
Beta strandi373 – 377Combined sources5
Helixi385 – 390Combined sources6
Helixi392 – 395Combined sources4
Turni402 – 406Combined sources5
Beta strandi418 – 423Combined sources6
Helixi426 – 428Combined sources3
Helixi436 – 446Combined sources11
Beta strandi451 – 456Combined sources6
Helixi464 – 466Combined sources3
Turni467 – 469Combined sources3
Beta strandi470 – 474Combined sources5
Helixi480 – 493Combined sources14
Helixi502 – 509Combined sources8
Turni510 – 512Combined sources3
Helixi514 – 521Combined sources8
Helixi523 – 527Combined sources5
Helixi535 – 544Combined sources10
Turni545 – 548Combined sources4
Helixi550 – 558Combined sources9
Helixi561 – 563Combined sources3
Helixi568 – 570Combined sources3
Helixi574 – 581Combined sources8
Turni585 – 587Combined sources3
Helixi588 – 595Combined sources8
Beta strandi596 – 602Combined sources7
Helixi610 – 631Combined sources22
Helixi638 – 640Combined sources3
Helixi641 – 648Combined sources8
Helixi650 – 654Combined sources5
Helixi669 – 687Combined sources19
Turni688 – 692Combined sources5
Helixi699 – 703Combined sources5
Turni704 – 706Combined sources3
Helixi707 – 714Combined sources8
Helixi725 – 730Combined sources6
Turni731 – 733Combined sources3
Helixi737 – 746Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85A295-785[»]
ProteinModelPortaliP38630.
SMRiP38630.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38630.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini153 – 243BRCTPROSITE-ProRule annotationAdd BLAST91

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi830 – 834Nuclear localization signalSequence analysis5
Motifi855 – 860Nuclear localization signalSequence analysis6

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

CDDicd00027. BRCT. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SXJX-ray2.85A295-785[»]
ProteinModelPortaliP38630.
SMRiP38630.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP38630.

Proteomic databases

MaxQBiP38630.
PRIDEiP38630.

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

CDDicd00027. BRCT. 1 hit.
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: November 30, 2016
This is version 158 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.