ID RFA1B_ARATH Reviewed; 604 AA.
AC Q9SD82;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-NOV-2024, entry version 135.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit B;
DE Short=AtRPA70B;
DE AltName: Full=AtRPA1-5;
DE AltName: Full=Replication factor A protein 1B;
DE AltName: Full=Replication protein A 1B;
DE Short=AtRPA1B;
GN Name=RPA1B; Synonyms=RPA70B; OrderedLocusNames=At5g08020;
GN ORFNames=F13G24.220;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=15978034; DOI=10.1111/j.1742-4658.2005.04719.x;
RA Ishibashi T., Koga A., Yamamoto T., Uchiyama Y., Mori Y., Hashimoto J.,
RA Kimura S., Sakaguchi K.;
RT "Two types of replication protein A in seed plants.";
RL FEBS J. 272:3270-3281(2005).
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 (By
CC similarity). Probably involved in repair of double-strand DNA breaks
CC (DSBs) induced by genotoxic stresses (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer of RPA1, RPA2 and RPA3 (canonical replication
CC protein A complex). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants have increased sensitivity to genotoxic
CC stresses and agents that damage DNA bases (UV and methyl
CC methanesulfonate, MMS). {ECO:0000269|PubMed:15978034}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AL133421; CAB62614.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91235.1; -; Genomic_DNA.
DR PIR; T45627; T45627.
DR RefSeq; NP_196419.1; NM_120884.2.
DR AlphaFoldDB; Q9SD82; -.
DR SMR; Q9SD82; -.
DR BioGRID; 15974; 1.
DR STRING; 3702.Q9SD82; -.
DR PaxDb; 3702-AT5G08020.1; -.
DR ProteomicsDB; 236231; -.
DR EnsemblPlants; AT5G08020.1; AT5G08020.1; AT5G08020.
DR GeneID; 830696; -.
DR Gramene; AT5G08020.1; AT5G08020.1; AT5G08020.
DR KEGG; ath:AT5G08020; -.
DR Araport; AT5G08020; -.
DR TAIR; AT5G08020; RPA70B.
DR eggNOG; KOG0851; Eukaryota.
DR HOGENOM; CLU_012393_3_1_1; -.
DR InParanoid; Q9SD82; -.
DR OMA; FNSYAML; -.
DR OrthoDB; 276920at2759; -.
DR PhylomeDB; Q9SD82; -.
DR PRO; PR:Q9SD82; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SD82; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; TAS:TAIR.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR CDD; cd04474; RPA1_DBD_A; 1.
DR CDD; cd04475; RPA1_DBD_B; 1.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR FunFam; 2.40.50.140:FF:000041; Replication protein A subunit; 1.
DR FunFam; 2.40.50.140:FF:000064; Replication protein A subunit; 1.
DR FunFam; 2.40.50.140:FF:000090; Replication protein A subunit; 1.
DR FunFam; 2.40.50.140:FF:000257; Replication protein A subunit; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 4.
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; IPR007199; Rep_factor-A_N.
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; PF04057; Rep-A_N; 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; 4.
PE 3: Inferred from homology;
KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..604
FT /note="Replication protein A 70 kDa DNA-binding subunit B"
FT /id="PRO_0000422616"
FT DNA_BIND 170..256
FT /note="OB"
FT ZN_FING 468..488
FT /note="C4-type"
FT /evidence="ECO:0000255"
SQ SEQUENCE 604 AA; 67289 MW; 6DB6B37424843D47 CRC64;
MENSVTQDGI ATVLANQSLD SSSVRPEIVV QVVDLKPAGN RYTFSANDGK MKIKAMLPAT
LTSDIISGKI QNLGLIRLLE YTVNDIPGKS EEKYMLITKC EAVASALDSE IKAEIKASTG
IMLKPKHEFV AKSASQIINE QRGNAAPAAR MAMTRRVHPL VSLNPYQGSW TIKVRVTNKG
VMRTYKNARG EGCVFNVELT DEEGTQIQAT MFNAAARKFY DRFEMGKVYY ISRGSLKLAN
KQFKTVQNDY EMTLNENSEV EEASNEEMFT PETKFNFVPI DELGTYVNQK DLIDVIGVVQ
SVSPTMSIRR KNDNEMIPKR DITLADETKK TVVVSLWNDL ATGIGQELLD MADNHPVIAI
KSLKVGAFQG VSLSTISRSN VVINPNSPEA TKLKSWYDAE GKETSMSAIG SGMSSSANNG
SRSMYSDRVF LSHITSNPSL GEEKPVFFST RAYISFIKPD QTMWYRACKT CNKKVTEAMD
SGYWCESCQK KDQECSLRYI MAVKVSDSTG ETWLSAFNDE AEKIIGCTAD DLNDLKSEEG
EVNEFQTKLK EATWSSHLFR ISVSQQEYNS EKRQRITVRG VSPIDFAAET RLLLQDISKN
KTSQ
//
