ID   RFA3_SCHPO              Reviewed;         104 AA.
AC   Q92374;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Replication factor A protein 3;
DE   AltName: Full=Single-stranded DNA-binding protein P12 subunit;
GN   Name=ssb3; ORFNames=SPCC23B6.05c;
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 [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=972 / ATCC 24843;
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 [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:P35244}.
CC   -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC       A complex (RPA). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the replication factor A protein 3 family.
CC       {ECO:0000305}.
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DR   EMBL; U59387; AAC49439.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAB51564.1; -; Genomic_DNA.
DR   PIR; T41245; T41245.
DR   RefSeq; NP_588128.1; NM_001023118.2.
DR   AlphaFoldDB; Q92374; -.
DR   SMR; Q92374; -.
DR   BioGRID; 275357; 70.
DR   DIP; DIP-29239N; -.
DR   IntAct; Q92374; 1.
DR   STRING; 4896.SPCC23B6.05c.1; -.
DR   MaxQB; Q92374; -.
DR   PaxDb; Q92374; -.
DR   EnsemblFungi; SPCC23B6.05c.1; SPCC23B6.05c.1:pep; SPCC23B6.05c.
DR   GeneID; 2538775; -.
DR   KEGG; spo:SPCC23B6.05c; -.
DR   PomBase; SPCC23B6.05c; ssb3.
DR   VEuPathDB; FungiDB:SPCC23B6.05c; -.
DR   eggNOG; ENOG502SBIR; Eukaryota.
DR   HOGENOM; CLU_141922_2_1_1; -.
DR   InParanoid; Q92374; -.
DR   OMA; HRYKEIF; -.
DR   PhylomeDB; Q92374; -.
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:Q92374; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0140445; C:chromosome, telomeric repeat region; ISO: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:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR   GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR   GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR   GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR   GO; GO:1902981; P:synthesis of RNA primer involved in mitotic DNA replication; ISO:PomBase.
DR   GO; GO:0000723; P:telomere maintenance; NAS:PomBase.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR013970; Rfa2.
DR   Pfam; PF08661; Rep_fac-A_3; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA replication; Nucleus; Reference proteome.
FT   CHAIN           1..104
FT                   /note="Replication factor A protein 3"
FT                   /id="PRO_0000097278"
SQ   SEQUENCE   104 AA;  11793 MW;  377BCF913652F1AE CRC64;
     MERPTPRVTK DMLPECSGKT VRIVGKANQV EGETAKVDSN GSFDMHLTVD NTLEPNHFYE
     FVVSVKPDSS VQLLTCVDFG TDIDMEVYQK LVLFSHKYNS LFFE