ID A0A1S4CXJ3_TOBAC Unreviewed; 577 AA.
AC A0A1S4CXJ3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Replication protein A subunit {ECO:0000256|RuleBase:RU364130};
GN Name=LOC107823681 {ECO:0000313|RefSeq:XP_016505858.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016505858.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016505858.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the replication protein A complex (RPA) required
CC for DNA recombination, repair and replication. The activity of RPA is
CC mediated by single-stranded DNA binding and protein interactions.
CC Probably involved in repair of double-strand DNA breaks (DSBs) induced
CC by genotoxic stresses. {ECO:0000256|RuleBase:RU364130}.
CC -!- SUBUNIT: Heterotrimer of RPA1, RPA2 and RPA3 (canonical replication
CC protein A complex). {ECO:0000256|RuleBase:RU364130}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU364130}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000256|ARBA:ARBA00005690, ECO:0000256|RuleBase:RU364130}.
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DR RefSeq; XP_016505858.1; XM_016650372.1.
DR AlphaFoldDB; A0A1S4CXJ3; -.
DR SMR; A0A1S4CXJ3; -.
DR STRING; 4097.A0A1S4CXJ3; -.
DR PaxDb; 4097-A0A1S4CXJ3; -.
DR GeneID; 107823681; -.
DR KEGG; nta:107823681; -.
DR OMA; RARVEMY; -.
DR OrthoDB; 276920at2759; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005662; C:DNA replication factor A complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR CDD; cd04474; RPA1_DBD_A; 1.
DR CDD; cd04475; RPA1_DBD_B; 1.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 3.
DR InterPro; IPR047192; Euk_RPA1_DBD_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR NCBIfam; TIGR00617; rpa1; 1.
DR PANTHER; PTHR23273; REPLICATION FACTOR A 1, RFA1; 1.
DR PANTHER; PTHR23273:SF32; REPLICATION PROTEIN A 70 KDA DNA-BINDING SUBUNIT B-RELATED; 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; Nucleic acid-binding proteins; 3.
PE 3: Inferred from homology;
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU364130};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364130};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU364130};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364130};
KW Reference proteome {ECO:0000313|Proteomes:UP000084051};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU364130};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU364130}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..228
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT DOMAIN 263..358
FT /note="Replication protein A OB"
FT /evidence="ECO:0000259|Pfam:PF16900"
FT DOMAIN 421..566
FT /note="Replication factor A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08646"
SQ SEQUENCE 577 AA; 65348 MW; EE4318266DA66696 CRC64;
MTISAILILK FDRDEIGAVD FFFFFFFFFL DWFWRFVFLP NGLLNLFRYL IVTKCDAVSP
ALEAEYKAEV KSQDNGIVLK PKQESFKNDV KMEEIGLKPK QEIQTKSAAQ IVHEQHGNMA
PAARMAMTRR IQPLVSLNPY QGNWTIKVRV TSKGNMRTYK NARGEGCVFN VELTDEDGTQ
IQATMFNEAA RKFFDKFELG KVYYISKGTL RVANKQFKTV QNDYEMTLNE NSQVEEASNE
EAFIPETKFN FVPIDELGPY VNGRELVDVI GVVQSVSPTM SIRRKSNNET VPKRDITIAD
ETKKTVVVSL WNDLATNVGQ ELLDMSDKSP VVAIKSLKVG DFQGVSLSAL SKSNIVVNPD
LPEAKKLRYW YDSEGKETSL ASIGSGMSPS TKNGARSMYS DRVSLLHITS NPSLGEEKPV
FFSIKAYISF IKPDQTMWYR ACRTCNKKVT DAFGSGYWCE GCQKNDAECS LRYIMALKVF
DASGEAWFSA FNEHAEKILG CSADELDKLK SEEGETAYQM KLKEATWVPH LFRVSVAPQE
YNSEKRQRIT VRAVAPVDYA AESKYLLEEM SKMNISI
//
