ID   RDR3_ARATH              Reviewed;         992 AA.
AC   O82190;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Probable RNA-dependent RNA polymerase 3;
DE            Short=AtRDRP3;
DE            EC=2.7.7.48;
DE   AltName: Full=RNA-directed RNA polymerase 3;
GN   Name=RDR3; Synonyms=RDRP3; OrderedLocusNames=At2g19910; ORFNames=F6F22.6;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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).
CC   -!- FUNCTION: Probably involved in the RNA silencing pathway and required
CC       for the generation of small interfering RNAs (siRNAs). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the RdRP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC62125.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC005169; AAC62125.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC06942.1; -; Genomic_DNA.
DR   PIR; F84582; F84582.
DR   RefSeq; NP_179581.2; NM_127549.3.
DR   AlphaFoldDB; O82190; -.
DR   SMR; O82190; -.
DR   STRING; 3702.AT2G19910.1; -.
DR   PaxDb; O82190; -.
DR   PRIDE; O82190; -.
DR   EnsemblPlants; AT2G19910.1; AT2G19910.1; AT2G19910.
DR   GeneID; 816510; -.
DR   Gramene; AT2G19910.1; AT2G19910.1; AT2G19910.
DR   KEGG; ath:AT2G19910; -.
DR   Araport; AT2G19910; -.
DR   TAIR; locus:2052040; AT2G19910.
DR   eggNOG; KOG0988; Eukaryota.
DR   HOGENOM; CLU_008367_0_0_1; -.
DR   InParanoid; O82190; -.
DR   OrthoDB; 104603at2759; -.
DR   PhylomeDB; O82190; -.
DR   PRO; PR:O82190; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O82190; baseline and differential.
DR   GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR   InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR   PANTHER; PTHR23079; PTHR23079; 1.
DR   Pfam; PF05183; RdRP; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase; Reference proteome; RNA-binding;
KW   RNA-directed RNA polymerase; RNA-mediated gene silencing; Transferase.
FT   CHAIN           1..992
FT                   /note="Probable RNA-dependent RNA polymerase 3"
FT                   /id="PRO_0000404674"
FT   REGION          88..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  112759 MW;  1D26B05BF0F131EC CRC64;
     MMNNGCDEVS PRSEIALLGS VETMLEKIYE KHNHRLPISV ETRRKLSSIS EELALETLRK
     VFNKPYLKTL DGLIMYFVKG TVTVDGSPRL SPGESPVQSP RTPAKKSCRA SQDVSLDLET
     PSPKFMKREE NGGSKYIPPL LALGELEFKK AFLLLSYIGG ESLVEEVISG DQIRKWKDLP
     MVSYEAAVWN RLGQRYCSPK ERRRPLEGDS GMTHYYQCHV ATDGSYKFKG HLLENTGTHL
     HKVLGDDNVL TVKFDKVLGV ETYCNDLYST YKGIAKNGIM VGLRRYRFFV FKDGGKEEKK
     KDVSTKGVKC YFIRTDSTAS IDMQNPYIFA GKSMHEARMH FMHVNTLSSL PNYMSRFSLI
     LSKTKTLEVD MTGITFEQID DIHCHDQDDK DVLDKNGKPC IHSDGTGYIS EDLARMCPVN
     IFKGKSMRSN NIQSKNLNFE GQGPCGQEPP LLIQFRIFYN GYAVKGTFLT NKKLPPRTVQ
     VRPSMIKVYE DRTLSNLSTF NSLEVVTTSN PPRKARLSRN LVALLSYGGV PNDFFLNILR
     NTLEESKTIF YSERAAFKAA INYGDDQYTA DMILVGIPLD EPYLKDRLSY LLKTERNALK
     AGRFPIDESY YIMGTVDPTG ELKENEICVI LHSGQISGDV LVYRNPGLHF GDIHVLKATY
     VKALEDYVGN AKFAVFFPQK GPRSLGDEIA GGDFDGDMYF ISRNPKLLEH FKPSEPWVSS
     SKPSKIYCGR KPSELSEEEL EEELFKMFLK ARFCKRDVIG MAADCWLGIM DPFLTLGDES
     AKEKYERKKN ILKLIDIYYD ALDAPKKGAK VDLPPDLEIK NFPHYMERDP KRDFRSTSIL
     GLIFDTVDSH NAEEPPPSEI SKLWYFEDEP VPKSHMDKFT SWYENYRSEM SQAMMETDKV
     KRNQLTNEVI QRYKQDFYGA AGFEDSNKSL EELYPQALAL YNVVYDYAIQ EGVAKCTFAW
     NVAGPVLCKF YLKKTKDKSV VASTSVLKKL LG