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Protein

Replication factor C subunit 1

Gene

rfc1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 1 is essential for cell cycle progression. It may associate with components of the DNA replication machinery and serve to enhance the efficiency of DNA replication.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei362 – 3621ATP; via carbonyl oxygenBy similarity
Binding sitei374 – 3741ATP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei519 – 5191ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi416 – 4238ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: PomBase
  • DNA clamp loader activity Source: InterPro

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • DNA strand elongation involved in DNA replication Source: PomBase
  • mitotic DNA replication leading strand elongation Source: PomBase
  • UV-damage excision repair Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-110312. Translesion synthesis by REV1.
R-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-110320. Translesion Synthesis by POLH.
R-SPO-174411. Polymerase switching on the C-strand of the telomere.
R-SPO-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SPO-5655862. Translesion synthesis by POLK.
R-SPO-5656121. Translesion synthesis by POLI.
R-SPO-5656169. Termination of translesion DNA synthesis.
R-SPO-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-69091. Polymerase switching.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication factor C subunit 1
Short name:
Replication factor C1
Gene namesi
Name:rfc1
ORF Names:SPBC23E6.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC23E6.07c.
PomBaseiSPBC23E6.07c. rfc1.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: PomBase
  • nuclear DNA replication factor C complex Source: PomBase
  • nuclear replication fork Source: PomBase
  • nucleolus Source: UniProtKB-SubCell
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 934934Replication factor C subunit 1PRO_0000121775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO60182.

PTM databases

iPTMnetiO60182.

Interactioni

Subunit structurei

Heteropentamer of subunits rfc1, rfc2, rfc3, rfc4 and rfc5 that forms a complex (RFC) with PCNA in the presence of ATP. Interacts with cdc24.1 Publication

Protein-protein interaction databases

BioGridi276954. 6 interactions.
IntActiO60182. 1 interaction.
MINTiMINT-4677876.

Structurei

3D structure databases

ProteinModelPortaliO60182.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini236 – 32691BRCTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000164552.
InParanoidiO60182.
KOiK10754.
OMAiTHAIFST.
OrthoDBiEOG7BGHVG.
PhylomeDBiO60182.

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.

O60182-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSDIRSFF GGGNAQKKPK VSPTPTSPKP KRSLKKKRIV LSDDEDGTIE
60 70 80 90 100
NSKVPASKSK VQKRNESEDI SHSLPSIVHE DDKLVGSDGV STTPDEYFEQ
110 120 130 140 150
QSTRSRSKPR IISNKETTTS KDVVHPVKTE NFANDLDTTS DSKPVVHQTR
160 170 180 190 200
ATRKPAQPKA EKSTTSKSKS HTTTATTHTS RSSKSKGLPR FSDEVSQALK
210 220 230 240 250
NVPLIDVDSM GVMAPGTFYE RAATTQTPGS KPVPEGNSDC LSGISFVITG
260 270 280 290 300
ILETLTRQEA TDLIKQYGGK VTGAPSVRTD FILLGENAGP RKVETIKQHK
310 320 330 340 350
IPAINEDGLF YLITHLPASG GTGAAAQAAQ QKKEQEEKKI LETVARMDDS
360 370 380 390 400
NKKESQPSQI WTSKYAPTSL KDICGNKGVV QKLQKWLQDY HKNRKSNFNK
410 420 430 440 450
PGPDGLGLYK AVLLSGPPGI GKTTAAHLVA KLEGYDVLEL NASDTRSKRL
460 470 480 490 500
LDEQLFGVTD SQSLAGYFGT KANPVDMAKS RLVLIMDEID GMSSGDRGGV
510 520 530 540 550
GQLNMIIKKS MIPIICICND RAHPKLRPLD RTTFDLRFRR PDANSMRSRI
560 570 580 590 600
MSIAYREGLK LSPQAVDQLV QGTQSDMRQI INLLSTYKLS CSEMTPQNSQ
610 620 630 640 650
AVIKNSEKHI VMKPWDICSR YLHGGMFHPS SKSTINDKLE LYFNDHEFSY
660 670 680 690 700
LMVQENYLNT TPDRIRQEPP KMSHLKHLEL ISSAANSFSD SDLVDSMIHG
710 720 730 740 750
PQQHWSLMPT HALMSCVRPA SFVAGSGSRQ IRFTNWLGNN SKTNKLYRML
760 770 780 790 800
REIQVHMRLK VSANKLDLRQ HYIPILYESL PVKLSTGHSD VVPEIIELMD
810 820 830 840 850
EYYLNREDFD SITELVLPAD AGEKLMKTIP TAAKSAFTRK YNSSSHPIAF
860 870 880 890 900
FGSSDVLPMK GSAQREVPDV EDAIEAEDEM LEEASDSEAA NEEDIDLSKD
910 920 930
KFISVPKKPK KRTKAKAEAS SSSSTSRRSR KKTA
Length:934
Mass (Da):103,489
Last modified:August 1, 1998 - v1
Checksum:i4700EB0639C24F89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18875.1.
AB027931 Genomic DNA. Translation: BAA87235.1.
PIRiT39941.
RefSeqiNP_596607.1. NM_001022528.2.

Genome annotation databases

EnsemblFungiiSPBC23E6.07c.1; SPBC23E6.07c.1:pep; SPBC23E6.07c.
GeneIDi2540426.
KEGGispo:SPBC23E6.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA18875.1.
AB027931 Genomic DNA. Translation: BAA87235.1.
PIRiT39941.
RefSeqiNP_596607.1. NM_001022528.2.

3D structure databases

ProteinModelPortaliO60182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276954. 6 interactions.
IntActiO60182. 1 interaction.
MINTiMINT-4677876.

PTM databases

iPTMnetiO60182.

Proteomic databases

MaxQBiO60182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC23E6.07c.1; SPBC23E6.07c.1:pep; SPBC23E6.07c.
GeneIDi2540426.
KEGGispo:SPBC23E6.07c.

Organism-specific databases

EuPathDBiFungiDB:SPBC23E6.07c.
PomBaseiSPBC23E6.07c. rfc1.

Phylogenomic databases

HOGENOMiHOG000164552.
InParanoidiO60182.
KOiK10754.
OMAiTHAIFST.
OrthoDBiEOG7BGHVG.
PhylomeDBiO60182.

Enzyme and pathway databases

ReactomeiR-SPO-110312. Translesion synthesis by REV1.
R-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-110320. Translesion Synthesis by POLH.
R-SPO-174411. Polymerase switching on the C-strand of the telomere.
R-SPO-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-SPO-5655862. Translesion synthesis by POLK.
R-SPO-5656121. Translesion synthesis by POLI.
R-SPO-5656169. Termination of translesion DNA synthesis.
R-SPO-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-69091. Polymerase switching.

Miscellaneous databases

PROiO60182.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Fission yeast cdc24 is a replication factor C- and proliferating cell nuclear antigen-interacting factor essential for S-phase completion."
    Tanaka H., Tanaka K., Murakami H., Okayama H.
    Mol. Cell. Biol. 19:1038-1048(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH CDC24.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 461-645, SUBCELLULAR LOCATION.
    Strain: ATCC 38364 / 968.
  4. "Contrasting effects of Elg1-RFC and Ctf18-RFC inactivation in the absence of fully functional RFC in fission yeast."
    Kim J., Robertson K., Mylonas K.J.L., Gray F.C., Charapitsa I., MacNeill S.A.
    Nucleic Acids Res. 33:4078-4089(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRFC1_SCHPO
AccessioniPrimary (citable) accession number: O60182
Secondary accession number(s): Q9US97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: August 1, 1998
Last modified: June 8, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.