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Database: UniProt
Entry: RDR1_ARATH
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ID   RDR1_ARATH              Reviewed;        1107 AA.
AC   Q9LQV2; Q8H1K9; Q9ZRX5;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=RNA-dependent RNA polymerase 1;
DE            Short=AtRDRP1;
DE            EC=2.7.7.48;
DE   AltName: Full=RNA-directed RNA polymerase 1;
GN   Name=RDR1; Synonyms=RDRP1; OrderedLocusNames=At1g14790; ORFNames=F10B6.19;
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 [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12650452; DOI=10.1094/mpmi.2003.16.3.206;
RA   Yu D., Fan B., MacFarlane S.A., Chen Z.;
RT   "Analysis of the involvement of an inducible Arabidopsis RNA-dependent RNA
RT   polymerase in antiviral defense.";
RL   Mol. Plant Microbe Interact. 16:206-216(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 479-991.
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   PubMed=9836747; DOI=10.1105/tpc.10.12.2087;
RA   Schiebel W., Pelissier T., Riedel L., Thalmeir S., Schiebel R., Kempe D.,
RA   Lottspeich F., Saenger H.L., Wassenegger M.;
RT   "Isolation of an RNA-directed RNA polymerase-specific cDNA clone from
RT   tomato.";
RL   Plant Cell 10:2087-2101(1998).
RN   [6]
RP   FUNCTION.
RX   PubMed=19308254; DOI=10.1371/journal.pone.0004971;
RA   Qi X., Bao F.S., Xie Z.;
RT   "Small RNA deep sequencing reveals role for Arabidopsis thaliana RNA-
RT   dependent RNA polymerases in viral siRNA biogenesis.";
RL   PLoS ONE 4:E4971-E4971(2009).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20190077; DOI=10.1105/tpc.109.073056;
RA   Garcia-Ruiz H., Takeda A., Chapman E.J., Sullivan C.M., Fahlgren N.,
RA   Brempelis K.J., Carrington J.C.;
RT   "Arabidopsis RNA-dependent RNA polymerases and dicer-like proteins in
RT   antiviral defense and small interfering RNA biogenesis during turnip mosaic
RT   virus infection.";
RL   Plant Cell 22:481-496(2010).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19966292; DOI=10.1073/pnas.0904086107;
RA   Wang X.B., Wu Q., Ito T., Cillo F., Li W.X., Chen X., Yu J.L., Ding S.W.;
RT   "RNAi-mediated viral immunity requires amplification of virus-derived
RT   siRNAs in Arabidopsis thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:484-489(2010).
CC   -!- FUNCTION: RNA-dependent direct polymerase involved in antiviral
CC       silencing. Required for the production of some small RNAs (mainly 21
CC       and some 22 nucleotides) derived from the crucifer-infecting
CC       tobamovirus (TMV-cg). Required for turnip mosaic virus (TuMV) silencing
CC       and accumulation of viral siRNAs. Involved in cucumber mosaic virus
CC       (CMV) silencing. Required for the biogenesis of viral secondary siRNAs,
CC       process that follows the production of primary siRNAs derived from
CC       viral RNA replication. Specifically targets the positive-strand of the
CC       3 RNA genomes of CMV and preferentially amplifies the 5'-terminal
CC       siRNAs of each viral genomic RNA. Not involved in the production of
CC       siRNAs derived from a single-stranded 336-nucleotide satellite RNA of
CC       CMV. {ECO:0000269|PubMed:12650452, ECO:0000269|PubMed:19308254,
CC       ECO:0000269|PubMed:19966292, ECO:0000269|PubMed:20190077}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48;
CC   -!- INDUCTION: By salicylic acid (SA) and infection by a crucifer-infecting
CC       tobamovirus (TMV-cg).
CC   -!- DISRUPTION PHENOTYPE: Upon viral infection, increased levels of TMV-cg,
CC       tobacco rattle virus (TRV) and CMV genomic viral RNAs. Reduced levels
CC       of TMV-cg-derived small RNAs and CMV-derived siRNAs.
CC       {ECO:0000269|PubMed:12650452, ECO:0000269|PubMed:19966292,
CC       ECO:0000269|PubMed:20190077}.
CC   -!- SIMILARITY: Belongs to the RdRP family. {ECO:0000305}.
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DR   EMBL; AY148431; AAN64409.1; -; mRNA.
DR   EMBL; AC006917; AAF79241.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29226.1; -; Genomic_DNA.
DR   EMBL; AK228731; BAF00633.1; -; mRNA.
DR   EMBL; AJ011977; CAA09894.1; -; Genomic_DNA.
DR   RefSeq; NP_172932.1; NM_101348.4.
DR   AlphaFoldDB; Q9LQV2; -.
DR   SMR; Q9LQV2; -.
DR   STRING; 3702.Q9LQV2; -.
DR   PaxDb; 3702-AT1G14790-1; -.
DR   ProteomicsDB; 235102; -.
DR   EnsemblPlants; AT1G14790.1; AT1G14790.1; AT1G14790.
DR   GeneID; 838044; -.
DR   Gramene; AT1G14790.1; AT1G14790.1; AT1G14790.
DR   KEGG; ath:AT1G14790; -.
DR   Araport; AT1G14790; -.
DR   TAIR; AT1G14790; RDR1.
DR   eggNOG; KOG0988; Eukaryota.
DR   HOGENOM; CLU_001366_3_0_1; -.
DR   InParanoid; Q9LQV2; -.
DR   OMA; CYNEGYE; -.
DR   OrthoDB; 5477883at2759; -.
DR   PhylomeDB; Q9LQV2; -.
DR   BRENDA; 2.7.7.48; 399.
DR   PRO; PR:Q9LQV2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LQV2; baseline and differential.
DR   Genevisible; Q9LQV2; AT.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0060148; P:positive regulation of post-transcriptional gene silencing; IMP:TAIR.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:TAIR.
DR   GO; GO:0009615; P:response to virus; IMP:TAIR.
DR   GO; GO:0030422; P:siRNA processing; IMP:CACAO.
DR   GO; GO:0010025; P:wax biosynthetic process; IGI:TAIR.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR   PANTHER; PTHR23079; RNA-DEPENDENT RNA POLYMERASE; 1.
DR   PANTHER; PTHR23079:SF55; RNA-DIRECTED RNA POLYMERASE; 1.
DR   Pfam; PF05183; RdRP; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
PE   2: Evidence at transcript level;
KW   Nucleotidyltransferase; Plant defense; Reference proteome; RNA-binding;
KW   RNA-directed RNA polymerase; RNA-mediated gene silencing; Transferase.
FT   CHAIN           1..1107
FT                   /note="RNA-dependent RNA polymerase 1"
FT                   /id="PRO_0000404672"
FT   CONFLICT        758
FT                   /note="P -> S (in Ref. 1; AAN64409 and 5; CAA09894)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1107 AA;  126214 MW;  F8FF97691FF82187 CRC64;
     MGKTIQVFGF PNGVSAEEVK KFLERLTGSG TVYAIKVRQP KKGGPRVYAI VQFTSERHTR
     LIITAAAERL YYGRSYLKAF EVEQDIVPKP RASLHTISGL KMFFGCQVST KKFLTLWSAQ
     DVCVSFGIGM RKLHFSFSWY QKDYRLELSY ENIWQIDLHS PQGRSSKFLV IQVIGAPKIF
     EKEDQPINLL FGIMDFYSDG SDEQWIRTTD FTSSSCIGQS TAFCLELPVH LNVPDFRENF
     ANYAEHRASS FLIESGSSYS SNANTLVPVV DPPPGFSLPF EILFKLNTLV QNACLSGPAL
     DLDFYRLLNQ KKYDRALIDH CLEKLFHLGE CCYEPAHWLR DEYKKWISKG KLPLSPTISL
     DDGLVYMYRV QVTPARVYFS GPEVNVSNRV LRHYSKYINN FLRVSFVDED LEKVRSMDLS
     PRSSTQRRTK LYDRIYSVLR DGIVIGDKKF EFLAFSSSQL RENSAWMFAP IDRITAAHIR
     AWMGDFDHIR NVAKYAARLG QSFSSSRETL NVRSDEIEVI PDVEIISLGT RYVFSDGIGK
     ISAEFARKVA RKCGLTEFSP SAFQIRYGGY KGVVAVDPNS SKKLSLRKSM SKFESENTKL
     DVLAWSKYQP CYMNRQLITL LSTLGVTDSV FEKKQREVVD RLDAILTHPL EAHEALGLMA
     PGENTNILKA LILCGYKPDA EPFLSMMLQN FRASKLLELR TKTRIFISGG RSMMGCLDET
     RTLEYGQVVV QYSDPMRPGR RFIITGPVVV AKNPCLHPGD VRVLQAVNVP ALNHMVDCVV
     FPQKGLRPHP NECSGSDLDG DIYFVCWDQE LVPPRTSEPM DYTPEPTQIL DHDVTIEEVE
     EYFANYIVND SLGIIANAHT AFADKEPLKA FSDPCIELAK KFSTAVDFPK TGVAAVIPQH
     LYVKEYPDFM EKPDKPTYES KNVIGKLFRE VKERAPPLIS IKSFTLDVAS KSYDKDMEVD
     GFEEYVDEAF YQKANYDFKL GNLMDYYGIK TEAEILSGGI MRMSKSFTKR RDAESIGRAV
     RALRKETLSL FNASEEEENE SAKASAWYHV TYHSSYWGLY NEGLNRDHFL SFAWCVYDKL
     VRIKKTNLGR RQRQETLERL DHVLRFG
//
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