RFA1_YEAST
ID RFA1_YEAST Reviewed; 621 AA.
AC P22336; D6VPL9; P38906;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Replication factor A protein 1;
DE Short=RF-A protein 1;
DE AltName: Full=DNA-binding protein BUF2;
DE AltName: Full=Replication protein A 69 kDa DNA-binding subunit;
DE AltName: Full=Single-stranded DNA-binding protein;
GN Name=RFA1; Synonyms=BUF2, RPA1; OrderedLocusNames=YAR007C; ORFNames=FUN3;
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 111-129 AND
RP 495-503.
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 PARTIAL PROTEIN SEQUENCE.
RX PubMed=2192864; DOI=10.1002/j.1460-2075.1990.tb07404.x;
RA Heyer W.-D., Rao M.R., Erdile L.F., Kelley T.J., Kolodner R.D.;
RT "An essential Saccharomyces cerevisiae single-stranded DNA binding protein
RT is homologous to the large subunit of human RP-A.";
RL EMBO J. 9:2321-2329(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [6]
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 [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 POB3.
RX PubMed=16678108; DOI=10.1016/j.molcel.2006.03.025;
RA Vandemark A.P., Blanksma M., Ferris E., Heroux A., Hill C.P., Formosa T.;
RT "The structure of the yFACT Pob3-M domain, its interaction with the DNA
RT replication factor RPA, and a potential role in nucleosome deposition.";
RL Mol. Cell 22:363-374(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. 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: Component of the heterotrimeric canonical replication protein
CC A complex (RPA). Interacts with POB3. {ECO:0000269|PubMed:16678108}.
CC -!- INTERACTION:
CC P22336; P38859: DNA2; NbExp=3; IntAct=EBI-14971, EBI-5973;
CC P22336; Q04636: POB3; NbExp=3; IntAct=EBI-14971, EBI-27863;
CC P22336; P26754: RFA2; NbExp=4; IntAct=EBI-14971, EBI-14976;
CC P22336; P26755: RFA3; NbExp=4; IntAct=EBI-14971, EBI-14981;
CC P22336; P35187: SGS1; NbExp=5; IntAct=EBI-14971, EBI-17059;
CC P22336; Q04437: YKU80; NbExp=2; IntAct=EBI-14971, EBI-8224;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 4100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
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DR EMBL; X59748; CAA42420.1; -; Genomic_DNA.
DR EMBL; M60262; AAA34994.1; -; Genomic_DNA.
DR EMBL; S64901; AAB27889.1; -; Genomic_DNA.
DR EMBL; L22015; AAC04960.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06989.1; -; Genomic_DNA.
DR PIR; S20145; S20145.
DR RefSeq; NP_009404.1; NM_001178211.1.
DR PDB; 1YNX; NMR; -; A=181-294.
DR PDB; 5M1X; X-ray; 1.80 A; A/B/C/D=1-132.
DR PDB; 5OMB; X-ray; 1.94 A; A/B=1-132.
DR PDB; 5OMC; X-ray; 2.38 A; A/B=1-132.
DR PDB; 6I52; EM; 4.70 A; C=442-619.
DR PDBsum; 1YNX; -.
DR PDBsum; 5M1X; -.
DR PDBsum; 5OMB; -.
DR PDBsum; 5OMC; -.
DR PDBsum; 6I52; -.
DR AlphaFoldDB; P22336; -.
DR BMRB; P22336; -.
DR SMR; P22336; -.
DR BioGRID; 31793; 347.
DR ComplexPortal; CPX-21; Replication protein A complex.
DR DIP; DIP-2512N; -.
DR IntAct; P22336; 59.
DR MINT; P22336; -.
DR STRING; 4932.YAR007C; -.
DR iPTMnet; P22336; -.
DR MaxQB; P22336; -.
DR PaxDb; P22336; -.
DR PRIDE; P22336; -.
DR EnsemblFungi; YAR007C_mRNA; YAR007C; YAR007C.
DR GeneID; 851266; -.
DR KEGG; sce:YAR007C; -.
DR SGD; S000000065; RFA1.
DR VEuPathDB; FungiDB:YAR007C; -.
DR eggNOG; KOG0851; Eukaryota.
DR GeneTree; ENSGT00390000012403; -.
DR HOGENOM; CLU_012393_2_0_1; -.
DR InParanoid; P22336; -.
DR OMA; VRVTIWG; -.
DR BioCyc; YEAST:G3O-28869-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 EvolutionaryTrace; P22336; -.
DR PRO; PR:P22336; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P22336; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IMP:SGD.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005662; C:DNA replication factor A complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA: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:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
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; IPI:SGD.
DR GO; GO:0030491; P:heteroduplex formation; IDA:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IMP:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IMP:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0043934; P:sporulation; IMP:CACAO.
DR GO; GO:0000723; P:telomere maintenance; IC:ComplexPortal.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IPI:SGD.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:SGD.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR CDD; cd04477; RPA1N; 1.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR007199; Rep_factor-A_N.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR PANTHER; PTHR23273; PTHR23273; 1.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF16900; REPA_OB_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 4.
DR TIGRFAMs; TIGR00617; rpa1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; DNA replication;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..621
FT /note="Replication factor A protein 1"
FT /id="PRO_0000097268"
FT DNA_BIND 197..284
FT /note="OB"
FT ZN_FING 486..508
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 178
FT /note="Phosphoserine; by ATM or ATR"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:5M1X"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:5M1X"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:5M1X"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5M1X"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:5M1X"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:5M1X"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:5M1X"
FT STRAND 79..90
FT /evidence="ECO:0007829|PDB:5M1X"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:5M1X"
FT STRAND 95..109
FT /evidence="ECO:0007829|PDB:5M1X"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:5M1X"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:5OMB"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1YNX"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1YNX"
FT STRAND 198..213
FT /evidence="ECO:0007829|PDB:1YNX"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:1YNX"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:1YNX"
FT HELIX 239..248
FT /evidence="ECO:0007829|PDB:1YNX"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:1YNX"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1YNX"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:1YNX"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:1YNX"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1YNX"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:1YNX"
SQ 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
