RFC4_SCHPO
ID RFC4_SCHPO Reviewed; 342 AA.
AC O94449;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Replication factor C subunit 4;
DE Short=Replication factor C4;
GN Name=rfc4; ORFNames=SPAC1687.03c;
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 [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 [2]
RP PROTEIN SEQUENCE OF 14-46; 51-67; 85-96; 112-119; 122-150; 162-174;
RP 178-186; 196-238; 267-286; 291-299 AND 333-342, 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. {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; CAA22597.1; -; Genomic_DNA.
DR PIR; T37746; T37746.
DR RefSeq; NP_593121.1; NM_001018517.2.
DR AlphaFoldDB; O94449; -.
DR SMR; O94449; -.
DR BioGRID; 279239; 7.
DR ComplexPortal; CPX-546; DNA replication factor C complex.
DR STRING; 4896.SPAC1687.03c.1; -.
DR MaxQB; O94449; -.
DR PaxDb; O94449; -.
DR PRIDE; O94449; -.
DR EnsemblFungi; SPAC1687.03c.1; SPAC1687.03c.1:pep; SPAC1687.03c.
DR GeneID; 2542790; -.
DR KEGG; spo:SPAC1687.03c; -.
DR PomBase; SPAC1687.03c; rfc4.
DR VEuPathDB; FungiDB:SPAC1687.03c; -.
DR eggNOG; KOG0991; Eukaryota.
DR HOGENOM; CLU_042324_0_1_1; -.
DR InParanoid; O94449; -.
DR OMA; SCNYSSQ; -.
DR PhylomeDB; O94449; -.
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:O94449; -.
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; IEA:InterPro.
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: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; Cell cycle; Direct protein sequencing; DNA replication;
KW DNA-binding; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..342
FT /note="Replication factor C subunit 4"
FT /id="PRO_0000121770"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 37655 MW; BD3504BC2E2F60ED CRC64;
MSNAVSSSVF GEKNNSVAYE LPWVEKYRPI VLDDIVGNEE TIDRLKVIAK EGNMPHLVIS
GMPGIGKTTS ILCLAHALLG PAYKEGVLEL NASDERGIDV VRNRIKAFAQ KKVILPPGRH
KIIILDEADS MTAGAQQALR RTMEIYSNTT RFALACNQSN KIIEPIQSRC AILRYSRLTD
QQVLQRLLNI CKAEKVNYTD DGLAALIMTA EGDMRQAVNN LQSTVAGFGL VNGENVFRVA
DQPSPVAIHA MLTACQSGNI DVALEKLQGI WDLGFSAVDI VTNMFRVVKT MDSIPEFSRL
EMLKEIGQTH MIILEGVQTL LQLSGLVCRL AKSQMKPESF II
