RFC5_SCHPO
ID RFC5_SCHPO Reviewed; 358 AA.
AC O94697;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Replication factor C subunit 5;
DE Short=Replication factor C5;
GN Name=rfc5; ORFNames=SPBC83.14c;
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 1-10; 25-47; 80-126; 130-141; 183-220; 241-273 AND
RP 310-324, 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; CU329671; CAB36876.1; -; Genomic_DNA.
DR PIR; T40703; T40703.
DR RefSeq; NP_595646.1; NM_001021540.2.
DR AlphaFoldDB; O94697; -.
DR SMR; O94697; -.
DR BioGRID; 276748; 11.
DR ComplexPortal; CPX-546; DNA replication factor C complex.
DR STRING; 4896.SPBC83.14c.1; -.
DR MaxQB; O94697; -.
DR PaxDb; O94697; -.
DR EnsemblFungi; SPBC83.14c.1; SPBC83.14c.1:pep; SPBC83.14c.
DR GeneID; 2540215; -.
DR KEGG; spo:SPBC83.14c; -.
DR PomBase; SPBC83.14c; rfc5.
DR VEuPathDB; FungiDB:SPBC83.14c; -.
DR eggNOG; KOG2035; Eukaryota.
DR HOGENOM; CLU_042324_5_0_1; -.
DR InParanoid; O94697; -.
DR OMA; LMCEACK; -.
DR PhylomeDB; O94697; -.
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:O94697; -.
DR Proteomes; UP000002485; Chromosome II.
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:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003689; F:DNA clamp loader activity; ISO:PomBase.
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:0070914; P:UV-damage excision repair; IDA:PomBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA replication; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..358
FT /note="Replication factor C subunit 5"
FT /id="PRO_0000121764"
SQ SEQUENCE 358 AA; 40403 MW; 32AA2E1EC473AF43 CRC64;
MLWLDQYRPK TLASLDYHKQ LSERLISLSS TNEFPHLLVY GPSGAGKKTR VVAILRELYG
PGSEKLKIDQ RTFLTPSSKK LQINIVSSLH HLEITPSDVG NYDRVIMQEL LKDVAQSAQV
DLQAKKIFKV VVINVADELT RDAQAALRRT MEKYSNNIRL ILIANSTSKI IEPIRSRTLM
VRVAAPTPEE IILVMSKILT AQGLEAPDSL LNNIANNCDR NLRKAILLLE TVHAKSPGNK
QLIDTGAQLP LPDWQTFIQQ VGDSMLQEQS PARILAVRSM LYDLLSHCIP PTTILKELLS
FFLSKVDTKL HPYLIQAAAN YEHRTRMGNK SIFHLEAFVA YFMKVYAMLQ LGMELPSY
