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Replication factor A protein 1 (RF-A protein 1) (DNA-binding protein BUF2) (Replication protein A 69 kDa DNA-binding subunit) (Single-stranded DNA-binding protein)

 RFA1_YEAST              Reviewed;         621 AA.
P22336; D6VPL9; P38906;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
10-OCT-2018, entry version 181.
RecName: Full=Replication factor A protein 1;
Short=RF-A protein 1;
AltName: Full=DNA-binding protein BUF2;
AltName: Full=Replication protein A 69 kDa DNA-binding subunit;
AltName: Full=Single-stranded DNA-binding protein;
Name=RFA1; Synonyms=BUF2, RPA1; OrderedLocusNames=YAR007C;
ORFNames=FUN3;
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 111-129 AND
495-503.
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 PARTIAL PROTEIN SEQUENCE.
PubMed=2192864;
Heyer W.-D., Rao M.R., Erdile L.F., Kelley T.J., Kolodner R.D.;
"An essential Saccharomyces cerevisiae single-stranded DNA binding
protein is homologous to the large subunit of human RP-A.";
EMBO J. 9:2321-2329(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=7941740; DOI=10.1002/yea.320100413;
Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
"Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of
the 42 kbp SPO7-CENI-CDC15 region.";
Yeast 10:535-541(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
Storms R.K.;
"The nucleotide sequence of chromosome I from Saccharomyces
cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
[6]
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).
[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 POB3.
PubMed=16678108; DOI=10.1016/j.molcel.2006.03.025;
Vandemark A.P., Blanksma M., Ferris E., Heroux A., Hill C.P.,
Formosa T.;
"The structure of the yFACT Pob3-M domain, its interaction with the
DNA replication factor RPA, and a potential role in nucleosome
deposition.";
Mol. Cell 22:363-374(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, 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).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: As part of the replication protein A (RPA/RP-A), a
single-stranded DNA-binding heterotrimeric complex, may play an
essential role in DNA replication, recombination and repair. Binds
and stabilizes single-stranded DNA intermediates, preventing
complementary DNA reannealing and recruiting different proteins
involved in DNA metabolism. 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: Component of the heterotrimeric canonical replication
protein A complex (RPA). Interacts with POB3.
{ECO:0000269|PubMed:16678108}.
-!- INTERACTION:
P38859:DNA2; NbExp=3; IntAct=EBI-14971, EBI-5973;
Q04636:POB3; NbExp=3; IntAct=EBI-14971, EBI-27863;
P26754:RFA2; NbExp=4; IntAct=EBI-14971, EBI-14976;
P26755:RFA3; NbExp=4; IntAct=EBI-14971, EBI-14981;
P35187:SGS1; NbExp=5; IntAct=EBI-14971, EBI-17059;
Q04437:YKU80; NbExp=2; IntAct=EBI-14971, EBI-8224;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: The N-terminus is blocked.
-!- MISCELLANEOUS: Present with 4100 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the replication factor A protein 1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X59748; CAA42420.1; -; Genomic_DNA.
EMBL; M60262; AAA34994.1; -; Genomic_DNA.
EMBL; S64901; AAB27889.1; -; Genomic_DNA.
EMBL; L22015; AAC04960.1; -; Genomic_DNA.
EMBL; BK006935; DAA06989.1; -; Genomic_DNA.
PIR; S20145; S20145.
RefSeq; NP_009404.1; NM_001178211.1.
PDB; 1YNX; NMR; -; A=181-294.
PDB; 5M1X; X-ray; 1.80 A; A/B/C/D=1-132.
PDB; 5OMB; X-ray; 1.94 A; A/B=1-132.
PDB; 5OMC; X-ray; 2.38 A; A/B=1-132.
PDBsum; 1YNX; -.
PDBsum; 5M1X; -.
PDBsum; 5OMB; -.
PDBsum; 5OMC; -.
ProteinModelPortal; P22336; -.
SMR; P22336; -.
BioGrid; 31793; 318.
ComplexPortal; CPX-21; Replication Protein A complex.
DIP; DIP-2512N; -.
IntAct; P22336; 59.
MINT; P22336; -.
STRING; 4932.YAR007C; -.
iPTMnet; P22336; -.
MaxQB; P22336; -.
PaxDb; P22336; -.
PRIDE; P22336; -.
EnsemblFungi; YAR007C; YAR007C; YAR007C.
GeneID; 851266; -.
KEGG; sce:YAR007C; -.
EuPathDB; FungiDB:YAR007C; -.
SGD; S000000065; RFA1.
GeneTree; ENSGT00390000012403; -.
HOGENOM; HOG000162322; -.
InParanoid; P22336; -.
KO; K07466; -.
OMA; DMTRNKL; -.
OrthoDB; EOG092C24GU; -.
BioCyc; YEAST:G3O-28869-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-3108214; SUMOylation of DNA damage response and repair proteins.
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.
EvolutionaryTrace; P22336; -.
PRO; PR:P22336; -.
Proteomes; UP000002311; Chromosome I.
GO; GO:0000781; C:chromosome, telomeric region; IMP:SGD.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005662; C:DNA replication factor A complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:CACAO.
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; IPI:SGD.
GO; GO:0030491; P:heteroduplex formation; IDA:SGD.
GO; GO:0006312; P:mitotic recombination; IMP:SGD.
GO; GO:0006289; P:nucleotide-excision repair; IDA:SGD.
GO; GO:0016567; P:protein ubiquitination; IMP:SGD.
GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
GO; GO:0043934; P:sporulation; IMP:CACAO.
GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
GO; GO:0007004; P:telomere maintenance via telomerase; IPI:SGD.
GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:SGD.
CDD; cd04476; RPA1_DBD_C; 1.
CDD; cd04477; RPA1N; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR004365; NA-bd_OB_tRNA.
InterPro; IPR013955; Rep_factor-A_C.
InterPro; IPR007199; Rep_factor-A_N.
InterPro; IPR031657; REPA_OB_2.
InterPro; IPR004591; Rfa1.
Pfam; PF04057; Rep-A_N; 1.
Pfam; PF08646; Rep_fac-A_C; 1.
Pfam; PF16900; REPA_OB_2; 1.
Pfam; PF01336; tRNA_anti-codon; 1.
SUPFAM; SSF50249; SSF50249; 4.
TIGRFAMs; TIGR00617; rpa1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; DNA replication; DNA-binding;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 621 Replication factor A protein 1.
/FTId=PRO_0000097268.
DNA_BIND 197 284 OB.
ZN_FING 486 508 C4-type. {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 178 178 Phosphoserine; by ATM or ATR.
{ECO:0000244|PubMed:18407956}.
HELIX 10 16 {ECO:0000244|PDB:5M1X}.
HELIX 18 22 {ECO:0000244|PDB:5M1X}.
STRAND 28 33 {ECO:0000244|PDB:5M1X}.
TURN 39 41 {ECO:0000244|PDB:5M1X}.
STRAND 44 51 {ECO:0000244|PDB:5M1X}.
STRAND 53 62 {ECO:0000244|PDB:5M1X}.
HELIX 63 72 {ECO:0000244|PDB:5M1X}.
STRAND 79 90 {ECO:0000244|PDB:5M1X}.
TURN 91 94 {ECO:0000244|PDB:5M1X}.
STRAND 95 109 {ECO:0000244|PDB:5M1X}.
HELIX 120 126 {ECO:0000244|PDB:5M1X}.
HELIX 128 130 {ECO:0000244|PDB:5OMB}.
HELIX 187 189 {ECO:0000244|PDB:1YNX}.
TURN 192 194 {ECO:0000244|PDB:1YNX}.
STRAND 198 213 {ECO:0000244|PDB:1YNX}.
STRAND 218 228 {ECO:0000244|PDB:1YNX}.
STRAND 231 237 {ECO:0000244|PDB:1YNX}.
HELIX 239 248 {ECO:0000244|PDB:1YNX}.
STRAND 251 259 {ECO:0000244|PDB:1YNX}.
STRAND 261 264 {ECO:0000244|PDB:1YNX}.
TURN 267 269 {ECO:0000244|PDB:1YNX}.
STRAND 270 274 {ECO:0000244|PDB:1YNX}.
STRAND 276 280 {ECO:0000244|PDB:1YNX}.
STRAND 285 289 {ECO:0000244|PDB:1YNX}.
SEQUENCE 621 AA; 70348 MW; 7EB8DFA6910EF8A8 CRC64;
MSSVQLSRGD FHSIFTNKQR YDNPTGGVYQ VYNTRKSDGA NSNRKNLIMI SDGIYHMKAL
LRNQAASKFQ SMELQRGDII RVIIAEPAIV RERKKYVLLV DDFELVQSRA DMVNQTSTFL
DNYFSEHPNE TLKDEDITDS GNVANQTNAS NAGVPDMLHS NSNLNANERK FANENPNSQK
TRPIFAIEQL SPYQNVWTIK ARVSYKGEIK TWHNQRGDGK LFNVNFLDTS GEIRATAFND
FATKFNEILQ EGKVYYVSKA KLQPAKPQFT NLTHPYELNL DRDTVIEECF DESNVPKTHF
NFIKLDAIQN QEVNSNVDVL GIIQTINPHF ELTSRAGKKF DRRDITIVDD SGFSISVGLW
NQQALDFNLP EGSVAAIKGV RVTDFGGKSL SMGFSSTLIP NPEIPEAYAL KGWYDSKGRN
ANFITLKQEP GMGGQSAASL TKFIAQRITI ARAQAENLGR SEKGDFFSVK AAISFLKVDN
FAYPACSNEN CNKKVLEQPD GTWRCEKCDT NNARPNWRYI LTISIIDETN QLWLTLFDDQ
AKQLLGVDAN TLMSLKEEDP NEFTKITQSI QMNEYDFRIR AREDTYNDQS RIRYTVANLH
SLNYRAEADY LADELSKALL A


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