RFA1D_ARATH
ID RFA1D_ARATH Reviewed; 629 AA.
AC Q9FME0;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit D;
DE Short=AtRPA70D;
DE AltName: Full=AtRPA1-4;
DE AltName: Full=Replication factor A protein 1D;
DE AltName: Full=Replication protein A 1D;
DE Short=AtRPA1D;
GN Name=RPA1D; Synonyms=RPA70D; OrderedLocusNames=At5g61000; ORFNames=MSL3.14;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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}.
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DR EMBL; AB008269; BAB10649.1; -; Genomic_DNA.
DR EMBL; AB006696; BAB10649.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED97409.1; -; Genomic_DNA.
DR EMBL; BT003950; AAO41995.1; -; mRNA.
DR RefSeq; NP_200908.1; NM_125493.4.
DR AlphaFoldDB; Q9FME0; -.
DR SMR; Q9FME0; -.
DR STRING; 3702.AT5G61000.1; -.
DR PaxDb; Q9FME0; -.
DR PRIDE; Q9FME0; -.
DR ProteomicsDB; 236994; -.
DR EnsemblPlants; AT5G61000.1; AT5G61000.1; AT5G61000.
DR GeneID; 836221; -.
DR Gramene; AT5G61000.1; AT5G61000.1; AT5G61000.
DR KEGG; ath:AT5G61000; -.
DR Araport; AT5G61000; -.
DR TAIR; locus:2173527; AT5G61000.
DR eggNOG; KOG0851; Eukaryota.
DR HOGENOM; CLU_012393_3_1_1; -.
DR InParanoid; Q9FME0; -.
DR OMA; YEMEISL; -.
DR OrthoDB; 1189265at2759; -.
DR PhylomeDB; Q9FME0; -.
DR PRO; PR:Q9FME0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FME0; baseline and differential.
DR Genevisible; Q9FME0; AT.
DR GO; GO:0005662; C:DNA replication factor A complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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: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 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.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..629
FT /note="Replication protein A 70 kDa DNA-binding subunit D"
FT /id="PRO_0000422618"
FT DNA_BIND 194..280
FT /note="OB"
FT ZN_FING 492..512
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 112..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 70264 MW; BA8839DFEF531784 CRC64;
MQTSVTPDAI STVLSNPSFD SSSDRSEIVV QVVDLKPIGN RYTFSANDGK TKVKAMFTAS
LTPEIISGKI QNLGLIRLID FTVNDISSKS TKYFLVTKCE AVGSVLDSEI NLDSKSGEEE
AREPKKQKLE HSPVSPLNDV VSTGITLKPK QEFVAKSASQ IMSEQRGNAA PAARMAMTRR
VHPLVSLNPY QGNWTIKVRV TNKGVMRNYK NARGEGCVFN VELTDEEGTQ IQATMFNDAA
RKFFDRFQLG KVYYISRGSL KLANKQFKTV QNDYEMTLNE NSEVEEASSE EMFIPETKFN
FVPIEELGLY VNQKELIDLI GVVQSVSPTM SIRRRTDNEM IPKRDITLAD ESRKTVVVSL
WNDLATGIGQ ELLDMADQSP VIAIKSLKVG DFQGVSLSTI SRSNVVINPE SPEAKKLKSW
FDSEGKEISM SSIGSGMSPS AKNGSRSLYT DRVLLSHITS NPSLFEEKPV FFSTRAYISF
IKPDQTMWYQ ACKTCNKKVT EALDSGYWCE GCQRKYEECS LRYIMAVKVT DSSGETWISS
FNDEAEKILG CSADELNKLK SEEGEVNEYQ TKLKEATWSS HVFRVSVTQN EYNGEKRQRV
TVKGVAPLDF AAETRLLLQD ISNKNKTSQ
