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Replication factor A protein 2 (RF-A protein 2) (DNA-binding protein BUF1) (Replication protein A 36 kDa subunit)

 RFA2_YEAST              Reviewed;         273 AA.
P26754; D6W0N3; P38905;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
05-JUL-2017, entry version 162.
RecName: Full=Replication factor A protein 2;
Short=RF-A protein 2;
AltName: Full=DNA-binding protein BUF1;
AltName: Full=Replication protein A 36 kDa subunit;
Name=RFA2; Synonyms=BUF1; OrderedLocusNames=YNL312W; ORFNames=N0368;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 100-118;
150-172 AND 184-196.
STRAIN=ATCC 208353 / W303-1A;
PubMed=1885001; DOI=10.1101/gad.5.9.1589;
Brill S.J., Stillman B.;
"Replication factor-A from Saccharomyces cerevisiae is encoded by
three essential genes coordinately expressed at S phase.";
Genes Dev. 5:1589-1600(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 5-16.
PubMed=8355713; DOI=10.1128/MCB.13.9.5749;
Luche R.M., Smart W.C., Marion T., Tillman M., Sumrada R.A.,
Cooper T.G.;
"Saccharomyces cerevisiae BUF protein binds to sequences participating
in DNA replication in addition to those mediating transcriptional
repression (URS1) and activation.";
Mol. Cell. Biol. 13:5749-5761(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=S288c / FY1676;
PubMed=7502583; DOI=10.1002/yea.320111109;
Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
"Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV
identifies six known genes, a new member of the hexose transporter
family and ten new open reading frames.";
Yeast 11:1077-1085(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
CELL CYCLE-DEPENDENT PHOSPHORYLATION.
PubMed=2200738; DOI=10.1101/gad.4.6.968;
Din S., Brill S.J., Fairman M.P., Stillman B.;
"Cell-cycle-regulated phosphorylation of DNA replication factor A from
human and yeast cells.";
Genes Dev. 4:968-977(1990).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
INTERACTION WITH MCM10.
PubMed=15494305; DOI=10.1016/j.molcel.2004.09.017;
Ricke R.M., Bielinsky A.-K.;
"Mcm10 regulates the stability and chromatin association of DNA
polymerase-alpha.";
Mol. Cell 16:173-185(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-122, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Binds to single-stranded sequences participating in DNA
replication in addition to those mediating transcriptional
repression (URS1) and activation (CAR1). Stimulates the activity
of a cognate strand exchange protein (SEP1). It cooperates with T-
AG and DNA topoisomerase I to unwind template DNA containing the
simian virus 40 origin of DNA replication.
-!- SUBUNIT: Heterotrimer of 69, 36, and 13 kDa chains. The DNA-
binding activity may reside exclusively on the 69 kDa subunit.
Interacts with MCM10. {ECO:0000269|PubMed:15494305}.
-!- INTERACTION:
P22336:RFA1; NbExp=4; IntAct=EBI-14976, EBI-14971;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: Phosphorylated in a cell cycle-dependent manner with
phosphorylation increasing at the entry in S phase and
dephosphorylation occurring at mitosis.
-!- PTM: The N-terminus is blocked.
-!- MISCELLANEOUS: Present with 6080 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the replication factor A protein 2 family.
{ECO:0000305}.
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EMBL; X59749; CAA42421.1; -; Genomic_DNA.
EMBL; S64861; AAB27888.1; -; Genomic_DNA.
EMBL; Z46259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z71588; CAA96241.1; -; Genomic_DNA.
EMBL; BK006947; DAA10249.1; -; Genomic_DNA.
PIR; B37281; B37281.
RefSeq; NP_014087.1; NM_001183150.1.
ProteinModelPortal; P26754; -.
SMR; P26754; -.
BioGrid; 35527; 370.
DIP; DIP-2518N; -.
IntAct; P26754; 10.
MINT; MINT-643412; -.
STRING; 4932.YNL312W; -.
iPTMnet; P26754; -.
MaxQB; P26754; -.
PRIDE; P26754; -.
EnsemblFungi; YNL312W; YNL312W; YNL312W.
GeneID; 855404; -.
KEGG; sce:YNL312W; -.
EuPathDB; FungiDB:YNL312W; -.
SGD; S000005256; RFA2.
GeneTree; ENSGT00390000010045; -.
HOGENOM; HOG000248662; -.
InParanoid; P26754; -.
KO; K10739; -.
OMA; SNPGMGE; -.
OrthoDB; EOG092C4EW3; -.
BioCyc; YEAST:G3O-33299-MONOMER; -.
Reactome; R-SCE-110312; Translesion synthesis by REV1.
Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-SCE-110320; Translesion Synthesis by POLH.
Reactome; R-SCE-5651801; PCNA-Dependent Long Patch Base Excision Repair.
Reactome; R-SCE-5655862; Translesion synthesis by POLK.
Reactome; R-SCE-5656121; Translesion synthesis by POLI.
Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-SCE-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-SCE-5696400; Dual Incision in GG-NER.
Reactome; R-SCE-6782135; Dual incision in TC-NER.
Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-SCE-68962; Activation of the pre-replicative complex.
Reactome; R-SCE-69166; Removal of the Flap Intermediate.
PRO; PR:P26754; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0000781; C:chromosome, telomeric region; IMP:SGD.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
GO; GO:0005662; C:DNA replication factor A complex; IDA:SGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
GO; GO:0006281; P:DNA repair; IMP:SGD.
GO; GO:0006260; P:DNA replication; IMP:SGD.
GO; GO:0006265; P:DNA topological change; IDA:SGD.
GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:SGD.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:SGD.
GO; GO:0045184; P:establishment of protein localization; IMP:SGD.
GO; GO:0030491; P:heteroduplex formation; IDA:SGD.
GO; GO:0006312; P:mitotic recombination; IPI:SGD.
GO; GO:0006289; P:nucleotide-excision repair; IDA:SGD.
GO; GO:0016567; P:protein ubiquitination; IPI:SGD.
GO; GO:0007131; P:reciprocal meiotic recombination; IPI:SGD.
GO; GO:0000722; P:telomere maintenance via recombination; IPI:SGD.
GO; GO:0007004; P:telomere maintenance via telomerase; IMP:SGD.
GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:SGD.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR004365; NA-bd_OB_tRNA.
InterPro; IPR014646; Rfa2/RPA32.
InterPro; IPR014892; RPA_C.
InterPro; IPR011991; WHTH_DNA-bd_dom.
Pfam; PF08784; RPA_C; 1.
Pfam; PF01336; tRNA_anti-codon; 1.
PIRSF; PIRSF036949; RPA32; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF50249; SSF50249; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; DNA replication;
DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 273 Replication factor A protein 2.
/FTId=PRO_0000097275.
DNA_BIND 69 157 OB.
COMPBIAS 1 30 Gly/Ser-rich.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:18407956}.
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


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