RFA1E_ARATH
ID RFA1E_ARATH Reviewed; 784 AA.
AC F4JSG3; O49671;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit E;
DE Short=AtRPA70E;
DE AltName: Full=AtRPA1-1;
DE AltName: Full=Replication factor A protein 1E;
DE AltName: Full=Replication protein A 1E;
DE Short=AtRPA1E;
GN Name=RPA1E; Synonyms=RPA70E; OrderedLocusNames=At4g19130;
GN ORFNames=T18B16.100;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-784.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 (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 -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16702.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78915.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021687; CAA16702.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161550; CAB78915.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84147.1; -; Genomic_DNA.
DR EMBL; AF439837; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T04434; T04434.
DR RefSeq; NP_567576.2; NM_118032.2.
DR AlphaFoldDB; F4JSG3; -.
DR SMR; F4JSG3; -.
DR STRING; 3702.AT4G19130.1; -.
DR PaxDb; F4JSG3; -.
DR PRIDE; F4JSG3; -.
DR EnsemblPlants; AT4G19130.1; AT4G19130.1; AT4G19130.
DR GeneID; 827651; -.
DR Gramene; AT4G19130.1; AT4G19130.1; AT4G19130.
DR KEGG; ath:AT4G19130; -.
DR Araport; AT4G19130; -.
DR TAIR; locus:2134766; AT4G19130.
DR eggNOG; KOG0851; Eukaryota.
DR HOGENOM; CLU_012393_3_0_1; -.
DR InParanoid; F4JSG3; -.
DR OMA; FTHATSF; -.
DR PRO; PR:F4JSG3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JSG3; baseline and differential.
DR Genevisible; F4JSG3; 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:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
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 InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR23273; PTHR23273; 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; SSF50249; 4.
DR TIGRFAMs; TIGR00617; rpa1; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..784
FT /note="Replication protein A 70 kDa DNA-binding subunit E"
FT /id="PRO_0000422619"
FT DNA_BIND 241..327
FT /note="OB"
FT ZN_FING 532..558
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 114..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 643
FT /note="R -> C (in Ref. 3; AF439837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 85992 MW; 507E62118F205CB8 CRC64;
MEVSLTAGAI GKIMNGEVTT EADMIPVLQV TDLKQIMAQQ DPTRERFRMV LSDGTYLHQG
MLGTDLNNLV KEGTLQPGSI VRLTRFVGDV IKGRRIVIVP QLEVLKQISD IIGHPVPGGK
HNDQRGADSG IKFNTTEQQG SGIRQVNNIE PGRSNAAISP QVGGTGSSVP ASTTPSTRAY
SNPSSGNGVT RQDYARDPPT SYPHQPQPPP PMYANRGPVA RNEAPPKIIP VNALSPYSGR
WTIKARVTNK AALKQYSNPR GEGKVFNFDL LDADGGEIRV TCFNAVADQF YDQIVVGNLY
LISRGSLRPA QKNFNHLRND YEIMLDNAST IKQCYEEDAA IPRHQFHFRT IGDIESMENN
CIVDVIGIVS SISPTVTITR KNGTATPKRS LQLKDMSGRS VEVTMWGDFC NAEGQRLQSL
CDSGVFPVLA VKAGRISEFN GKTVSTIGSS QLFIDPDFVE AEKLKNWFER EGKSVPCISL
SREFSGSGKV DVRKTISQIK DEKLGTSEKP DWITVSATIL YLKFDNFCYT ACPIMNGDRP
CSKKVTDNGD GTWRCEKCDK SVDECDYRYI LQLQIQDHTD LTCVTAFQEA GEEIMGISAK
DLYYVKNEHK DEEKFEDIIR KVAFTKYNFK LKVKEETFSD EQRVKATVVK VDKLNYSADT
RTMLGAMDKL RTRDANSLPI NPEGSDYNAD VVNTGIGSSG TRDPSSVQRR DFGLHAHQSG
QSGNHYSGGG ATTSCNVCGN SGHVSAKCPG ATKPQEQGQY MGGSYRGTTG SYGGGLPRQH
VGSY
