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Protein

Replication factor C subunit 2

Gene

rfc2

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 2 binds ATP and single-stranded DNA.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi59 – 668ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: PomBase
  • DNA binding Source: UniProtKB-KW

GO - Biological processi

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

Keywords - Biological processi

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 2
Short name:
Replication factor C2
Alternative name(s):
Activator 1 41 kDa subunit
Gene namesi
Name:rfc2
ORF Names:SPAC23D3.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC23D3.02.
PomBaseiSPAC23D3.02. rfc2.

Subcellular locationi

GO - Cellular componenti

  • Ctf18 RFC-like complex Source: PomBase
  • cytosol Source: PomBase
  • DNA replication factor C complex Source: GO_Central
  • Elg1 RFC-like complex Source: PomBase
  • nuclear chromatin Source: PomBase
  • nuclear DNA replication factor C complex Source: PomBase
  • nuclear replication fork Source: PomBase
  • nucleus Source: PomBase
  • Rad17 RFC-like complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591G → V: Not functional. 1 Publication
Mutagenesisi66 – 661T → N: Normal growth. 1 Publication
Mutagenesisi131 – 1311E → Q: Poor growth. 1 Publication
Mutagenesisi133 – 1331D → H: Not functional. 1 Publication
Mutagenesisi172 – 1721S → A: Normal growth. 1 Publication
Mutagenesisi173 – 1731R → K: Poor growth. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Replication factor C subunit 2PRO_0000121759Add
BLAST

Proteomic databases

MaxQBiQ09843.

PTM databases

SwissPalmiQ09843.

Interactioni

Subunit structurei

Heteropentamer of subunits rfc1, rfc2, rfc3, rfc4 and rfc5 that forms a complex (RFC) with PCNA in the presence of ATP. Two other complexes exist where rfc1 can be replaced by either ctf18 or elg1 to form the ctf18-RFC or the elg1-RFC complexes respectively.1 Publication

Protein-protein interaction databases

BioGridi278398. 7 interactions.
MINTiMINT-4695650.

Structurei

3D structure databases

ProteinModelPortaliQ09843.
SMRiQ09843. Positions 20-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the activator 1 small subunits family.Curated

Phylogenomic databases

HOGENOMiHOG000224154.
InParanoidiQ09843.
KOiK10755.
OMAiICFRGTF.
OrthoDBiEOG7DZ8VQ.
PhylomeDBiQ09843.

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.

Q09843-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFFAPRNKK TEQEAKKSIP WVELYRPKTL DQVSSQESTV QVLKKTLLSN
60 70 80 90 100
NLPHMLFYGS PGTGKTSTIL ALSRELFGPQ LMKSRVLELN ASDERGISII
110 120 130 140 150
REKVKSFAKT TVTNKVDGYP CPPFKIIILD EADSMTQDAQ AALRRTMESY
160 170 180 190 200
ARITRFCLIC NYMTRIIDPL SSRCSKYRFK PLDNENMVKR LEFIAADQAV
210 220 230 240 250
SMEPGVVNAL VECSGGDMRK AITFLQSAAN LHQGTPITIS SVEELAGAVP
260 270 280 290 300
YNIIRSLLDT AYTKNVSNIE TLSRDVAAEG YSTGIILSQL HDVLLKEETL
310 320 330 340
SSPVKYKIFM KLSEVDKRLN DGADETLQLL DLLSSISVVC
Length:340
Mass (Da):37,877
Last modified:February 1, 1996 - v1
Checksum:i4BE835CFEA0F996A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91237.1.
PIRiT38278. S62493.
RefSeqiNP_594540.1. NM_001019969.2.

Genome annotation databases

EnsemblFungiiSPAC23D3.02.1; SPAC23D3.02.1:pep; SPAC23D3.02.
GeneIDi2541908.
KEGGispo:SPAC23D3.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91237.1.
PIRiT38278. S62493.
RefSeqiNP_594540.1. NM_001019969.2.

3D structure databases

ProteinModelPortaliQ09843.
SMRiQ09843. Positions 20-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278398. 7 interactions.
MINTiMINT-4695650.

PTM databases

SwissPalmiQ09843.

Proteomic databases

MaxQBiQ09843.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC23D3.02.1; SPAC23D3.02.1:pep; SPAC23D3.02.
GeneIDi2541908.
KEGGispo:SPAC23D3.02.

Organism-specific databases

EuPathDBiFungiDB:SPAC23D3.02.
PomBaseiSPAC23D3.02. rfc2.

Phylogenomic databases

HOGENOMiHOG000224154.
InParanoidiQ09843.
KOiK10755.
OMAiICFRGTF.
OrthoDBiEOG7DZ8VQ.
PhylomeDBiQ09843.

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

PROiQ09843.

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...

Publicationsi

« Hide 'large scale' publications
  1. "A key role for replication factor C in DNA replication checkpoint function in fission yeast."
    Reynolds N., Fantes P.A., MacNeill S.A.
    Nucleic Acids Res. 27:462-469(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLY-59; THR-66; GLU-131; ASP-133; SER-172 AND ARG-173.
  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. "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: PROTEIN SEQUENCE OF 17-28; 46-83; 116-144; 146-152; 156-165; 179-189 AND 275-296, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiRFC2_SCHPO
AccessioniPrimary (citable) accession number: Q09843
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 119 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, Direct protein sequencing, 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.