RFC2_SCHPO
ID RFC2_SCHPO Reviewed; 340 AA.
AC Q09843;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Replication factor C subunit 2;
DE Short=Replication factor C2;
DE AltName: Full=Activator 1 41 kDa subunit;
GN Name=rfc2; ORFNames=SPAC23D3.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF GLY-59; THR-66; GLU-131;
RP ASP-133; SER-172 AND ARG-173.
RX PubMed=9862966; DOI=10.1093/nar/27.2.462;
RA Reynolds N., Fantes P.A., MacNeill S.A.;
RT "A key role for replication factor C in DNA replication checkpoint function
RT in fission yeast.";
RL Nucleic Acids Res. 27:462-469(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PROTEIN SEQUENCE OF 17-28; 46-83; 116-144; 146-152; 156-165; 179-189 AND
RP 275-296, FUNCTION, AND SUBUNIT.
RX PubMed=16040599; DOI=10.1093/nar/gki728;
RA Kim J., Robertson K., Mylonas K.J.L., Gray F.C., Charapitsa I.,
RA MacNeill S.A.;
RT "Contrasting effects of Elg1-RFC and Ctf18-RFC inactivation in the absence
RT of fully functional RFC in fission yeast.";
RL Nucleic Acids Res. 33:4078-4089(2005).
CC -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC delta and epsilon requires the action of the accessory proteins PCNA
CC and activator 1. Subunit 2 binds ATP and single-stranded DNA.
CC {ECO:0000269|PubMed:16040599}.
CC -!- SUBUNIT: Heteropentamer of subunits rfc1, rfc2, rfc3, rfc4 and rfc5
CC that forms a complex (RFC) with PCNA in the presence of ATP. Two other
CC complexes exist where rfc1 can be replaced by either ctf18 or elg1 to
CC form the ctf18-RFC or the elg1-RFC complexes respectively.
CC {ECO:0000269|PubMed:16040599}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA91237.1; -; Genomic_DNA.
DR PIR; T38278; S62493.
DR RefSeq; NP_594540.1; NM_001019969.2.
DR AlphaFoldDB; Q09843; -.
DR SMR; Q09843; -.
DR BioGRID; 278398; 8.
DR ComplexPortal; CPX-546; DNA replication factor C complex.
DR STRING; 4896.SPAC23D3.02.1; -.
DR SwissPalm; Q09843; -.
DR MaxQB; Q09843; -.
DR PaxDb; Q09843; -.
DR PRIDE; Q09843; -.
DR EnsemblFungi; SPAC23D3.02.1; SPAC23D3.02.1:pep; SPAC23D3.02.
DR GeneID; 2541908; -.
DR KEGG; spo:SPAC23D3.02; -.
DR PomBase; SPAC23D3.02; rfc2.
DR VEuPathDB; FungiDB:SPAC23D3.02; -.
DR eggNOG; KOG0989; Eukaryota.
DR HOGENOM; CLU_042324_1_0_1; -.
DR InParanoid; Q09843; -.
DR OMA; KIVMVFS; -.
DR PhylomeDB; Q09843; -.
DR Reactome; R-SPO-110312; Translesion synthesis by REV1.
DR Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SPO-110320; Translesion Synthesis by POLH.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-SPO-5655862; Translesion synthesis by POLK.
DR Reactome; R-SPO-5656121; Translesion synthesis by POLI.
DR Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SPO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-69091; Polymerase switching.
DR PRO; PR:Q09843; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005663; C:DNA replication factor C complex; IBA:GO_Central.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IDA:PomBase.
DR GO; GO:0043599; C:nuclear DNA replication factor C complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0031389; C:Rad17 RFC-like complex; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0003682; F:chromatin binding; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061860; F:DNA clamp unloader activity; IC:PomBase.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IDA:PomBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IGI:PomBase.
DR GO; GO:1903460; P:mitotic DNA replication leading strand elongation; ISO:PomBase.
DR GO; GO:0070914; P:UV-damage excision repair; IDA:PomBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013748; Rep_factorC_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; DNA replication; DNA-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..340
FT /note="Replication factor C subunit 2"
FT /id="PRO_0000121759"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 59
FT /note="G->V: Not functional."
FT /evidence="ECO:0000269|PubMed:9862966"
FT MUTAGEN 66
FT /note="T->N: Normal growth."
FT /evidence="ECO:0000269|PubMed:9862966"
FT MUTAGEN 131
FT /note="E->Q: Poor growth."
FT /evidence="ECO:0000269|PubMed:9862966"
FT MUTAGEN 133
FT /note="D->H: Not functional."
FT /evidence="ECO:0000269|PubMed:9862966"
FT MUTAGEN 172
FT /note="S->A: Normal growth."
FT /evidence="ECO:0000269|PubMed:9862966"
FT MUTAGEN 173
FT /note="R->K: Poor growth."
FT /evidence="ECO:0000269|PubMed:9862966"
SQ SEQUENCE 340 AA; 37877 MW; 4BE835CFEA0F996A CRC64;
MSFFAPRNKK TEQEAKKSIP WVELYRPKTL DQVSSQESTV QVLKKTLLSN NLPHMLFYGS
PGTGKTSTIL ALSRELFGPQ LMKSRVLELN ASDERGISII REKVKSFAKT TVTNKVDGYP
CPPFKIIILD EADSMTQDAQ AALRRTMESY ARITRFCLIC NYMTRIIDPL SSRCSKYRFK
PLDNENMVKR LEFIAADQAV SMEPGVVNAL VECSGGDMRK AITFLQSAAN LHQGTPITIS
SVEELAGAVP YNIIRSLLDT AYTKNVSNIE TLSRDVAAEG YSTGIILSQL HDVLLKEETL
SSPVKYKIFM KLSEVDKRLN DGADETLQLL DLLSSISVVC
