RFA1_SCHPO
ID RFA1_SCHPO Reviewed; 609 AA.
AC Q92372; Q92382;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 164.
DE RecName: Full=Replication factor A protein 1;
DE AltName: Full=Single-stranded DNA-binding protein p68 subunit;
GN Name=ssb1; Synonyms=rad11, rpa1; ORFNames=SPBC660.13c;
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 PARTIAL PROTEIN SEQUENCE.
RX PubMed=8702843; DOI=10.1074/jbc.271.34.20868;
RA Ishiai M., Sanchez J.P., Amin A.A., Murakami Y., Hurwitz J.;
RT "Purification, gene cloning, and reconstitution of the heterotrimeric
RT single-stranded DNA-binding protein from Schizosaccharomyces pombe.";
RL J. Biol. Chem. 271:20868-20878(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9111307; DOI=10.1128/mcb.17.5.2381;
RA Parker A.E., Clyne R.K., Carr A.M., Kelly T.J.;
RT "The Schizosaccharomyces pombe rad11+ gene encodes the large subunit of
RT replication protein A.";
RL Mol. Cell. Biol. 17:2381-2390(1997).
RN [3]
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).
CC -!- FUNCTION: As part of the replication protein A (RPA/RP-A), a single-
CC stranded DNA-binding heterotrimeric complex, may play an essential role
CC in DNA replication, recombination and repair. Binds and stabilizes
CC single-stranded DNA intermediates, preventing complementary DNA
CC reannealing and recruiting different proteins involved in DNA
CC metabolism. {ECO:0000250|UniProtKB:P27694}.
CC -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC A complex (RPA).
CC -!- INTERACTION:
CC Q92372; P36592: rad22; NbExp=2; IntAct=EBI-966394, EBI-966242;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
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DR EMBL; U59385; AAC49437.1; -; mRNA.
DR EMBL; U75446; AAC49694.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22533.1; -; Genomic_DNA.
DR PIR; T40625; T40625.
DR RefSeq; NP_595092.1; NM_001020999.2.
DR AlphaFoldDB; Q92372; -.
DR SMR; Q92372; -.
DR BioGRID; 277673; 27.
DR DIP; DIP-29237N; -.
DR IntAct; Q92372; 4.
DR STRING; 4896.SPBC660.13c.1; -.
DR iPTMnet; Q92372; -.
DR MaxQB; Q92372; -.
DR PaxDb; Q92372; -.
DR EnsemblFungi; SPBC660.13c.1; SPBC660.13c.1:pep; SPBC660.13c.
DR GeneID; 2541158; -.
DR KEGG; spo:SPBC660.13c; -.
DR PomBase; SPBC660.13c; ssb1.
DR VEuPathDB; FungiDB:SPBC660.13c; -.
DR eggNOG; KOG0851; Eukaryota.
DR HOGENOM; CLU_012393_2_0_1; -.
DR InParanoid; Q92372; -.
DR OMA; VRVTIWG; -.
DR PhylomeDB; Q92372; -.
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-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SPO-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-SPO-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
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-5696395; Formation of Incision Complex in GG-NER.
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-68962; Activation of the pre-replicative complex.
DR Reactome; R-SPO-69166; Removal of the Flap Intermediate.
DR PRO; PR:Q92372; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005662; C:DNA replication factor A complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0090734; C:site of DNA damage; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; EXP:PomBase.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; EXP:PomBase.
DR GO; GO:0070034; F:telomerase RNA binding; EXP:PomBase.
DR GO; GO:0042162; F:telomeric DNA binding; EXP:PomBase.
DR GO; GO:0006281; P:DNA repair; IMP:PomBase.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:1902969; P:mitotic DNA replication; IMP:PomBase.
DR GO; GO:0106112; P:negative regulation of mitotic cohesin ssDNA (lagging strand) loading; IDA:PomBase.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0006279; P:premeiotic DNA replication; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:PomBase.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR CDD; cd04477; RPA1N; 1.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR007199; Rep_factor-A_N.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR PANTHER; PTHR23273; PTHR23273; 2.
DR Pfam; PF04057; Rep-A_N; 1.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF16900; REPA_OB_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 4.
DR TIGRFAMs; TIGR00617; rpa1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA replication; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..609
FT /note="Replication factor A protein 1"
FT /id="PRO_0000097266"
FT DNA_BIND 192..278
FT /note="OB"
FT ZN_FING 477..498
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 130..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 68197 MW; 5F2E77A0E12022EA CRC64;
MAERLSVGAL RIINTSDASS FPPNPILQVL TVKELNSNPT SGAPKRYRVV LSDSINYAQS
MLSTQLNHLV AENKLQKGAF VQLTQFTVNV MKERKILIVL GLNVLTELGV MDKIGNPAGL
ETVDALRQQQ NEQNNASAPR TGISTSTNSF YGNNAAATAP APPPMMKKPA APNSLSTIIY
PIEGLSPYQN KWTIRARVTN KSEVKHWHNQ RGEGKLFSVN LLDESGEIRA TGFNDQVDAF
YDILQEGSVY YISRCRVNIA KKQYTNVQNE YELMFERDTE IRKAEDQTAV PVAKFSFVSL
QEVGDVAKDA VIDVIGVLQN VGPVQQITSR ATSRGFDKRD ITIVDQTGYE MRVTLWGKTA
IEFSVSEESI LAFKGVKVND FQGRSLSMLT SSTMSVDPDI QESHLLKGWY DGQGRGQEFA
KHSVISSTLS TTGRSAERKN IAEVQAEHLG MSETPDYFSL KGTIVYIRKK NVSYPACPAA
DCNKKVFDQG GSWRCEKCNK EYDAPQYRYI ITIAVGDHTG QLWLNVFDDV GKLIMHKTAD
ELNDLQENDE NAFMNCMAEA CYMPYIFQCR AKQDNFKGEM RVRYTVMSIN QMDWKEESKR
LINFIESAQ
