RFA2_SCHPO
ID RFA2_SCHPO Reviewed; 279 AA.
AC Q92373;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Replication factor A protein 2;
DE AltName: Full=Single-stranded DNA-binding protein P30 subunit;
GN Name=ssb2; ORFNames=SPCC1753.01c, SPCC584.06c;
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 [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: Binds to single-stranded sequences.
CC -!- SUBUNIT: Heterotrimer of 68, 30, and 12 kDa chains.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner.
CC Hypophosphorylated in G1, becomes phosphorylated at the G1/S boundary,
CC it is maintained in this state through the M phase.
CC -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC {ECO:0000305}.
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DR EMBL; U59386; AAC49438.1; -; mRNA.
DR EMBL; CU329672; CAA21823.1; -; Genomic_DNA.
DR PIR; T41124; T41124.
DR RefSeq; NP_588227.2; NM_001023217.2.
DR AlphaFoldDB; Q92373; -.
DR SMR; Q92373; -.
DR BioGRID; 275362; 5.
DR DIP; DIP-29238N; -.
DR IntAct; Q92373; 1.
DR STRING; 4896.SPCC1753.01c.1; -.
DR iPTMnet; Q92373; -.
DR MaxQB; Q92373; -.
DR PaxDb; Q92373; -.
DR EnsemblFungi; SPCC1753.01c.1; SPCC1753.01c.1:pep; SPCC1753.01c.
DR GeneID; 2538781; -.
DR KEGG; spo:SPCC1753.01c; -.
DR PomBase; SPCC1753.01c; ssb2.
DR VEuPathDB; FungiDB:SPCC1753.01c; -.
DR eggNOG; KOG3108; Eukaryota.
DR HOGENOM; CLU_051033_0_1_1; -.
DR InParanoid; Q92373; -.
DR OMA; EIASHFI; -.
DR PhylomeDB; Q92373; -.
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:Q92373; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000781; C:chromosome, telomeric region; IBA:GO_Central.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
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: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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR040260; RFA2-like.
DR InterPro; IPR014646; Rfa2/RPA32.
DR InterPro; IPR014892; RPA_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13989; PTHR13989; 1.
DR Pfam; PF08784; RPA_C; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PIRSF; PIRSF036949; RPA32; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA replication; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..279
FT /note="Replication factor A protein 2"
FT /id="PRO_0000097274"
FT DNA_BIND 80..140
FT /note="OB"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 30391 MW; C43C94A732E2EA9B CRC64;
MAYDAFGKPG YGPDFNSAFS PGMGGGAGFN EYDQSSQPSV DRQQGAGNKL RPVTIKQILN
ASQVHADAEF KIDGVEVGQV TFVGVLRNIH AQTTNTTYQI EDGTGMIEVR HWEHIDALSE
LATDTYVRVY GNIKIFSGKI YIASQYIRTI KDHNEVHFHF LEAIAVHLHF TQKANAVNGA
NAPGYGTSNA LGYNNISSNG AANSLEQKLA EYSLTPAQMT VMQAIHSAPE TNEGVHVRQL
AQSVGPGIDL TAVTDFLQQE GIIYTTIDEN HFKSVLQDQ
