RFA2_YEAST
ID RFA2_YEAST Reviewed; 273 AA.
AC P26754; D6W0N3; P38905;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Replication factor A protein 2;
DE Short=RF-A protein 2;
DE AltName: Full=DNA-binding protein BUF1;
DE AltName: Full=Replication protein A 36 kDa subunit;
GN Name=RFA2; Synonyms=BUF1; OrderedLocusNames=YNL312W; ORFNames=N0368;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 100-118; 150-172
RP AND 184-196.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=1885001; DOI=10.1101/gad.5.9.1589;
RA Brill S.J., Stillman B.;
RT "Replication factor-A from Saccharomyces cerevisiae is encoded by three
RT essential genes coordinately expressed at S phase.";
RL Genes Dev. 5:1589-1600(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 5-16.
RX PubMed=8355713; DOI=10.1128/mcb.13.9.5749-5761.1993;
RA Luche R.M., Smart W.C., Marion T., Tillman M., Sumrada R.A., Cooper T.G.;
RT "Saccharomyces cerevisiae BUF protein binds to sequences participating in
RT DNA replication in addition to those mediating transcriptional repression
RT (URS1) and activation.";
RL Mol. Cell. Biol. 13:5749-5761(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=7502583; DOI=10.1002/yea.320111109;
RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV
RT identifies six known genes, a new member of the hexose transporter family
RT and ten new open reading frames.";
RL Yeast 11:1077-1085(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP CELL CYCLE-DEPENDENT PHOSPHORYLATION.
RX PubMed=2200738; DOI=10.1101/gad.4.6.968;
RA Din S., Brill S.J., Fairman M.P., Stillman B.;
RT "Cell-cycle-regulated phosphorylation of DNA replication factor A from
RT human and yeast cells.";
RL Genes Dev. 4:968-977(1990).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP INTERACTION WITH MCM10.
RX PubMed=15494305; DOI=10.1016/j.molcel.2004.09.017;
RA Ricke R.M., Bielinsky A.-K.;
RT "Mcm10 regulates the stability and chromatin association of DNA polymerase-
RT alpha.";
RL Mol. Cell 16:173-185(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Binds to single-stranded sequences participating in DNA
CC replication in addition to those mediating transcriptional repression
CC (URS1) and activation (CAR1). Stimulates the activity of a cognate
CC strand exchange protein (SEP1). It cooperates with T-AG and DNA
CC topoisomerase I to unwind template DNA containing the simian virus 40
CC origin of DNA replication.
CC -!- SUBUNIT: Heterotrimer of 69, 36, and 13 kDa chains. The DNA-binding
CC activity may reside exclusively on the 69 kDa subunit. Interacts with
CC MCM10. {ECO:0000269|PubMed:15494305}.
CC -!- INTERACTION:
CC P26754; P22336: RFA1; NbExp=4; IntAct=EBI-14976, EBI-14971;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner with
CC phosphorylation increasing at the entry in S phase and
CC dephosphorylation occurring at mitosis.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 6080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC {ECO:0000305}.
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DR EMBL; X59749; CAA42421.1; -; Genomic_DNA.
DR EMBL; S64861; AAB27888.1; -; Genomic_DNA.
DR EMBL; Z46259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z71588; CAA96241.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10249.1; -; Genomic_DNA.
DR PIR; B37281; B37281.
DR RefSeq; NP_014087.1; NM_001183150.1.
DR PDB; 6I52; EM; 4.70 A; B=32-182.
DR PDBsum; 6I52; -.
DR AlphaFoldDB; P26754; -.
DR SMR; P26754; -.
DR BioGRID; 35527; 389.
DR ComplexPortal; CPX-21; Replication protein A complex.
DR DIP; DIP-2518N; -.
DR IntAct; P26754; 21.
DR MINT; P26754; -.
DR STRING; 4932.YNL312W; -.
DR iPTMnet; P26754; -.
DR MaxQB; P26754; -.
DR PaxDb; P26754; -.
DR PRIDE; P26754; -.
DR EnsemblFungi; YNL312W_mRNA; YNL312W; YNL312W.
DR GeneID; 855404; -.
DR KEGG; sce:YNL312W; -.
DR SGD; S000005256; RFA2.
DR VEuPathDB; FungiDB:YNL312W; -.
DR eggNOG; KOG3108; Eukaryota.
DR GeneTree; ENSGT00940000168634; -.
DR HOGENOM; CLU_051033_0_0_1; -.
DR InParanoid; P26754; -.
DR OMA; TYKIDDG; -.
DR BioCyc; YEAST:G3O-33299-MON; -.
DR Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-SCE-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR Reactome; R-SCE-69166; Removal of the Flap Intermediate.
DR PRO; PR:P26754; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P26754; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IMP:SGD.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0005662; C:DNA replication factor A complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; IDA:ComplexPortal.
DR GO; GO:0006265; P:DNA topological change; IDA:SGD.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:SGD.
DR GO; GO:0045184; P:establishment of protein localization; IMP:SGD.
DR GO; GO:0030491; P:heteroduplex formation; IDA:SGD.
DR GO; GO:0006312; P:mitotic recombination; IPI:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IPI:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IPI:SGD.
DR GO; GO:0000723; P:telomere maintenance; IC:ComplexPortal.
DR GO; GO:0000722; P:telomere maintenance via recombination; IPI:SGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:SGD.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:SGD.
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 3D-structure; Direct protein sequencing; DNA replication; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..273
FT /note="Replication factor A protein 2"
FT /id="PRO_0000097275"
FT DNA_BIND 69..157
FT /note="OB"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956"
SQ SEQUENCE 273 AA; 29936 MW; F6087501E4E28CC1 CRC64;
MATYQPYNEY SSVTGGGFEN SESRPGSGES ETNTRVNTLT PVTIKQILES KQDIQDGPFV
SHNQELHHVC FVGVVRNITD HTANIFLTIE DGTGQIEVRK WSEDANDLAA GNDDSSGKGY
GSQVAQQFEI GGYVKVFGAL KEFGGKKNIQ YAVIKPIDSF NEVLTHHLEV IKCHSIASGM
MKQPLESASN NNGQSLFVKD DNDTSSGSSP LQRILEFCKK QCEGKDANSF AVPIPLISQS
LNLDETTVRN CCTTLTDQGF IYPTFDDNNF FAL
