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RFA1B_ARATH
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   03-AUG-2022, entry version 123.
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.AT5G08020.1; -.
DR   PaxDb; Q9SD82; -.
DR   PRIDE; Q9SD82; -.
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; locus:2142808; AT5G08020.
DR   eggNOG; KOG0851; Eukaryota.
DR   HOGENOM; CLU_012393_3_1_1; -.
DR   InParanoid; Q9SD82; -.
DR   OMA; YRLLINM; -.
DR   OrthoDB; 1189265at2759; -.
DR   PhylomeDB; Q9SD82; -.
DR   PRO; PR:Q9SD82; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9SD82; baseline and differential.
DR   Genevisible; Q9SD82; AT.
DR   GO; GO:0005662; C:DNA replication factor A complex; IBA:GO_Central.
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:0006281; P:DNA repair; TAS:TAIR.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
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:0010224; P:response to UV-B; IMP:TAIR.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR   CDD; cd04476; RPA1_DBD_C; 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; 2.
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; SSF50249; 4.
DR   TIGRFAMs; TIGR00617; rpa1; 1.
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
 
 
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