GenomeNet

Database: UniProt
Entry: Q9ZVD5
LinkDB: Q9ZVD5
Original site: Q9ZVD5 
ID   AGO4_ARATH              Reviewed;         924 AA.
AC   Q9ZVD5; Q93VG2;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   18-SEP-2019, entry version 126.
DE   RecName: Full=Protein argonaute 4 {ECO:0000303|PubMed:12522258, ECO:0000303|PubMed:28229965};
DE            Short=AtAGO4 {ECO:0000303|PubMed:12522258, ECO:0000303|PubMed:28229965};
DE   AltName: Full=Protein OVEREXPRESSOR OF CATIONIC PEROXIDASE 11;
GN   Name=AGO4 {ECO:0000303|PubMed:12522258, ECO:0000303|PubMed:28229965};
GN   Synonyms=OCP11;
GN   OrderedLocusNames=At2g27040 {ECO:0000312|Araport:AT2G27040};
GN   ORFNames=T20P8.9 {ECO:0000312|EMBL:AAC77862.2};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   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
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12522258; DOI=10.1126/science.1079695;
RA   Zilberman D., Cao X., Jacobsen S.E.;
RT   "ARGONAUTE4 control of locus-specific siRNA accumulation and DNA and
RT   histone methylation.";
RL   Science 299:716-719(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=14988555; DOI=10.1126/science.1095989;
RA   Chan S.W., Zilberman D., Xie Z., Johansen L.K., Carrington J.C.,
RA   Jacobsen S.E.;
RT   "RNA silencing genes control de novo DNA methylation.";
RL   Science 303:1336-1336(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=15242620; DOI=10.1016/j.cub.2004.06.055;
RA   Zilberman D., Cao X., Johansen L.K., Xie Z., Carrington J.C.,
RA   Jacobsen S.E.;
RT   "Role of Arabidopsis ARGONAUTE4 in RNA-directed DNA methylation
RT   triggered by inverted repeats.";
RL   Curr. Biol. 14:1214-1220(2004).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16839878; DOI=10.1016/j.cell.2006.05.031;
RA   Pontes O., Li C.F., Nunes P.C., Haag J., Ream T., Vitins A.,
RA   Jacobsen S.E., Pikaard C.S.;
RT   "The Arabidopsis chromatin-modifying nuclear siRNA pathway involves a
RT   nucleolar RNA processing center.";
RL   Cell 126:79-92(2006).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NRPE1.
RX   PubMed=16839879; DOI=10.1016/j.cell.2006.05.032;
RA   Li C.F., Pontes O., El-Shami M., Henderson I.R., Bernatavichute Y.V.,
RA   Chan S.W.-L., Lagrange T., Pikaard C.S., Jacobsen S.E.;
RT   "An ARGONAUTE4-containing nuclear processing center colocalized with
RT   Cajal bodies in Arabidopsis thaliana.";
RL   Cell 126:93-106(2006).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF ASP-660; ASP-742 AND HIS-874.
RX   PubMed=16998468; DOI=10.1038/nature05198;
RA   Qi Y., He X., Wang X.J., Kohany O., Jurka J., Hannon G.J.;
RT   "Distinct catalytic and non-catalytic roles of ARGONAUTE4 in RNA-
RT   directed DNA methylation.";
RL   Nature 443:1008-1012(2006).
RN   [10]
RP   FUNCTION.
RX   PubMed=17869110; DOI=10.1016/j.cub.2007.08.039;
RA   Baumberger N., Tsai C.-H., Lie M., Havecker E., Baulcombe D.C.;
RT   "The Polerovirus silencing suppressor P0 targets ARGONAUTE proteins
RT   for degradation.";
RL   Curr. Biol. 17:1609-1614(2007).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH NRPE1.
RX   PubMed=17938239; DOI=10.1101/gad.451207;
RA   El-Shami M., Pontier D., Lahmy S., Braun L., Picart C., Vega D.,
RA   Hakimi M.A., Jacobsen S.E., Cooke R., Lagrange T.;
RT   "Reiterated WG/GW motifs form functionally and evolutionarily
RT   conserved ARGONAUTE-binding platforms in RNAi-related components.";
RL   Genes Dev. 21:2539-2544(2007).
RN   [12]
RP   FUNCTION, MUTAGENESIS OF GLU-641, AND DISRUPTION PHENOTYPE.
RX   PubMed=17993621; DOI=10.1105/tpc.107.054494;
RA   Agorio A., Vera P.;
RT   "ARGONAUTE4 is required for resistance to Pseudomonas syringae in
RT   Arabidopsis.";
RL   Plant Cell 19:3778-3790(2007).
RN   [13]
RP   FUNCTION.
RX   PubMed=18342361; DOI=10.1016/j.cell.2008.02.034;
RA   Mi S., Cai T., Hu Y., Chen Y., Hodges E., Ni F., Wu L., Li S.,
RA   Zhou H., Long C., Chen S., Hannon G.J., Qi Y.;
RT   "Sorting of small RNAs into Arabidopsis argonaute complexes is
RT   directed by the 5' terminal nucleotide.";
RL   Cell 133:116-127(2008).
RN   [14]
RP   FUNCTION.
RX   PubMed=18596098; DOI=10.1128/jvi.00719-08;
RA   Raja P., Sanville B.C., Buchmann R.C., Bisaro D.M.;
RT   "Viral genome methylation as an epigenetic defense against
RT   geminiviruses.";
RL   J. Virol. 82:8997-9007(2008).
RN   [15]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18266474; DOI=10.1371/journal.pgen.0040027;
RA   Li C.F., Henderson I.R., Song L., Fedoroff N., Lagrange T.,
RA   Jacobsen S.E.;
RT   "Dynamic regulation of ARGONAUTE4 within multiple nuclear bodies in
RT   Arabidopsis thaliana.";
RL   PLoS Genet. 4:E27-E27(2008).
RN   [16]
RP   INTERACTION WITH RDM3, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. C24;
RX   PubMed=19410546; DOI=10.1016/j.cell.2009.04.028;
RA   He X.-J., Hsu Y.-F., Zhu S., Wierzbicki A.T., Pontes O., Pikaard C.S.,
RA   Liu H.-L., Wang C.-S., Jin H., Zhu J.-K.;
RT   "An effector of RNA-directed DNA methylation in arabidopsis is an
RT   ARGONAUTE 4- and RNA-binding protein.";
RL   Cell 137:498-508(2009).
RN   [17]
RP   INTERACTION WITH RDM3.
RC   STRAIN=cv. Columbia;
RX   PubMed=19343051; DOI=10.1038/embor.2009.31;
RA   Bies-Etheve N., Pontier D., Lahmy S., Picart C., Vega D., Cooke R.,
RA   Lagrange T.;
RT   "RNA-directed DNA methylation requires an AGO4-interacting member of
RT   the SPT5 elongation factor family.";
RL   EMBO Rep. 10:649-654(2009).
RN   [18]
RP   FUNCTION, AND INTERACTION WITH NRPE1.
RX   PubMed=19377477; DOI=10.1038/ng.365;
RA   Wierzbicki A.T., Ream T.S., Haag J.R., Pikaard C.S.;
RT   "RNA polymerase V transcription guides ARGONAUTE4 to chromatin.";
RL   Nat. Genet. 41:630-634(2009).
RN   [19]
RP   INTERACTION WITH TURNIP CRINKLE VIRUS CAPSID PROTEIN P38.
RX   PubMed=20439431; DOI=10.1101/gad.1908710;
RA   Azevedo J., Garcia D., Pontier D., Ohnesorge S., Yu A., Garcia S.,
RA   Braun L., Bergdoll M., Hakimi M.A., Lagrange T., Voinnet O.;
RT   "Argonaute quenching and global changes in Dicer homeostasis caused by
RT   a pathogen-encoded GW repeat protein.";
RL   Genes Dev. 24:904-915(2010).
RN   [20]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=20173091; DOI=10.1105/tpc.109.072199;
RA   Havecker E.R., Wallbridge L.M., Hardcastle T.J., Bush M.S.,
RA   Kelly K.A., Dunn R.M., Schwach F., Doonan J.H., Baulcombe D.C.;
RT   "The Arabidopsis RNA-directed DNA methylation argonautes functionally
RT   diverge based on their expression and interaction with target loci.";
RL   Plant Cell 22:321-334(2010).
RN   [21]
RP   FUNCTION, INTERACTION WITH CHROMATIN, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=21738482; DOI=10.1371/journal.pgen.1002120;
RA   Rowley M.J., Avrutsky M.I., Sifuentes C.J., Pereira L.,
RA   Wierzbicki A.T.;
RT   "Independent chromatin binding of ARGONAUTE4 and SPT5L/KTF1 mediates
RT   transcriptional gene silencing.";
RL   PLoS Genet. 7:E1002120-E1002120(2011).
RN   [22]
RP   INTERACTION WITH SDE3.
RX   PubMed=22940249; DOI=10.1016/j.molcel.2012.07.028;
RA   Garcia D., Garcia S., Pontier D., Marchais A., Renou J.P.,
RA   Lagrange T., Voinnet O.;
RT   "Ago hook and RNA helicase motifs underpin dual roles for SDE3 in
RT   antiviral defense and silencing of nonconserved intergenic regions.";
RL   Mol. Cell 48:109-120(2012).
RN   [23]
RP   INTERACTION WITH MBD6.
RX   PubMed=28229965; DOI=10.1007/s12038-016-9658-1;
RA   Parida A.P., Sharma A., Sharma A.K.;
RT   "AtMBD6, a methyl CpG binding domain protein, maintains gene silencing
RT   in Arabidopsis by interacting with RNA binding proteins.";
RL   J. Biosci. 42:57-68(2017).
CC   -!- FUNCTION: Together with RDM3, required for transcriptional gene
CC       silencing (TGS) by DNA methylation and repressive histone
CC       modifications (H3K9me2) of several chromatin loci
CC       (PubMed:21738482). Component of the RISC complex that associate
CC       with the small interfering RNA (siRNA) pathway involved in direct
CC       cytosine methylation at endogenous DNA repeats. Forms a
CC       AGO4/NRPE1/siRNA complex in cajal body, facilitating its function
CC       in RNA-directed gene silencing of target loci. Required for CpNpG
CC       and asymmetric DNA methylation as well as histone H3 'Lys-9'
CC       methylation (H3K9me) at SUP and SN1 loci. May be not required for
CC       CpG methylation. Required for the production and maintenance of
CC       retrotransposon SN1 and Copia and ribosomal 5S 25 nucleotide
CC       siRNAs specialized in gene silencing at chromatin level. Involved
CC       in de novo methylation of FWA gene and required for the
CC       maintenance of RNA-directed DNA methylation (RdDM) triggered by
CC       inverted repeat transgenes. Interacts with miRNA miR390 and
CC       miR172, targeting respectively TAS3 and AP2 mRNAs, and mediates
CC       cleavage of miRNA targets. Associates mainly with small RNAs of 24
CC       nucleotide in length and preferentially recruits small RNAs with a
CC       5' terminal adenosine. Targeted by the turnip yellows virus (TuYV)
CC       protein P0 (via F-box-like domain) for probable proteasome
CC       degradation and thereby inactivating AGO4 function in RNA
CC       silencing. Required for resistance to the bacterial pathogen
CC       P.syringae. Works independently of the RdDM pathway in mediating
CC       resistance to P.syringae. RdDM is involved in viral genome
CC       methylation as an epigenetic defense against geminiviruses
CC       (PubMed:12522258, PubMed:14988555, PubMed:15242620,
CC       PubMed:16839878, PubMed:16839879, PubMed:16998468,
CC       PubMed:17869110, PubMed:17938239, PubMed:17993621,
CC       PubMed:18342361, PubMed:18596098, PubMed:19377477,
CC       PubMed:20173091). {ECO:0000269|PubMed:12522258,
CC       ECO:0000269|PubMed:14988555, ECO:0000269|PubMed:15242620,
CC       ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:16839879,
CC       ECO:0000269|PubMed:16998468, ECO:0000269|PubMed:17869110,
CC       ECO:0000269|PubMed:17938239, ECO:0000269|PubMed:17993621,
CC       ECO:0000269|PubMed:18342361, ECO:0000269|PubMed:18596098,
CC       ECO:0000269|PubMed:19377477, ECO:0000269|PubMed:20173091,
CC       ECO:0000269|PubMed:21738482}.
CC   -!- SUBUNIT: Interacts with NRPE1 (via C-terminus). Binding to NRPE1
CC       is required for its function in RdDM. Interacts with turnip
CC       crinkle virus (TCV) capsid protein P38; this interaction inhibits
CC       probably RNA silencing ability of AGO4. Interacts with SDE3
CC       (PubMed:16839879, PubMed:17938239, PubMed:19377477,
CC       PubMed:20439431, PubMed:22940249). Binds to RDM3 (PubMed:19410546,
CC       PubMed:19343051). Binds chromatin at loci subject to
CC       transcriptional silencing (PubMed:21738482). Interacts with MBD6
CC       (PubMed:28229965). {ECO:0000269|PubMed:16839879,
CC       ECO:0000269|PubMed:17938239, ECO:0000269|PubMed:19343051,
CC       ECO:0000269|PubMed:19377477, ECO:0000269|PubMed:19410546,
CC       ECO:0000269|PubMed:20439431, ECO:0000269|PubMed:21738482,
CC       ECO:0000269|PubMed:22940249, ECO:0000269|PubMed:28229965}.
CC   -!- INTERACTION:
CC       Q9LJF5:DRB3; NbExp=2; IntAct=EBI-2352199, EBI-10815073;
CC       Q9M548:DRM2; NbExp=2; IntAct=EBI-2352199, EBI-6923904;
CC       Q5D869:NRPE1; NbExp=3; IntAct=EBI-2352199, EBI-2352263;
CC       Q9LUJ3:RDM1; NbExp=2; IntAct=EBI-2352199, EBI-15850569;
CC       F4JW79:RDM3; NbExp=5; IntAct=EBI-2352199, EBI-2352225;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000269|PubMed:16839878}. Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:19410546}. Nucleus, Cajal body
CC       {ECO:0000269|PubMed:16839879, ECO:0000269|PubMed:18266474}.
CC       Note=Also located in AB-bodies that are distincts from the Cajal
CC       bodies and immediately adjacent to the condensed 45S ribosomal DNA
CC       (rDNA) loci (PubMed:18266474). Colocalizes with AGO4 and
CC       polymerase V in the nucleoplasm (PubMed:19410546).
CC       {ECO:0000269|PubMed:18266474, ECO:0000269|PubMed:19410546}.
CC   -!- TISSUE SPECIFICITY: Expressed in embryos, mature leaves, vascular
CC       tissue of the sepals, stamens and stigma, at the tip of the style
CC       and siliques. {ECO:0000269|PubMed:20173091}.
CC   -!- DISRUPTION PHENOTYPE: Decreased DNA cytosine methylation at CpNpG
CC       and asymmetric positions at different DNA loci corresponding to
CC       retroelements, transposons and repetitive DNA sequences
CC       (PubMed:12522258, PubMed:17993621, PubMed:21738482). Reduced
CC       H3K9me2 at IGN5 and IGN26 loci (PubMed:21738482).
CC       {ECO:0000269|PubMed:12522258, ECO:0000269|PubMed:17993621,
CC       ECO:0000269|PubMed:21738482}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000305}.
DR   EMBL; AC005623; AAC77862.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07928.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07929.1; -; Genomic_DNA.
DR   EMBL; AY035081; AAK59586.1; -; mRNA.
DR   EMBL; AY051033; AAK93710.1; -; mRNA.
DR   PIR; A84668; A84668.
DR   RefSeq; NP_001189613.1; NM_001202684.1.
DR   RefSeq; NP_565633.1; NM_128262.4.
DR   SMR; Q9ZVD5; -.
DR   BioGrid; 2598; 4.
DR   DIP; DIP-53402N; -.
DR   IntAct; Q9ZVD5; 6.
DR   MINT; Q9ZVD5; -.
DR   STRING; 3702.AT2G27040.2; -.
DR   MoonProt; Q9ZVD5; -.
DR   iPTMnet; Q9ZVD5; -.
DR   PaxDb; Q9ZVD5; -.
DR   PRIDE; Q9ZVD5; -.
DR   EnsemblPlants; AT2G27040.1; AT2G27040.1; AT2G27040.
DR   EnsemblPlants; AT2G27040.2; AT2G27040.2; AT2G27040.
DR   GeneID; 817246; -.
DR   Gramene; AT2G27040.1; AT2G27040.1; AT2G27040.
DR   Gramene; AT2G27040.2; AT2G27040.2; AT2G27040.
DR   KEGG; ath:AT2G27040; -.
DR   Araport; AT2G27040; -.
DR   TAIR; locus:2059258; AT2G27040.
DR   eggNOG; KOG1041; Eukaryota.
DR   eggNOG; ENOG410XP07; LUCA.
DR   HOGENOM; HOG000116043; -.
DR   InParanoid; Q9ZVD5; -.
DR   KO; K11593; -.
DR   OMA; CYEQMFT; -.
DR   OrthoDB; 159407at2759; -.
DR   PhylomeDB; Q9ZVD5; -.
DR   PRO; PR:Q9ZVD5; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZVD5; baseline and differential.
DR   Genevisible; Q9ZVD5; AT.
DR   GO; GO:0015030; C:Cajal body; IDA:TAIR.
DR   GO; GO:0005719; C:nuclear euchromatin; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0004521; F:endoribonuclease activity; IMP:CAFA.
DR   GO; GO:0035198; F:miRNA binding; IDA:CAFA.
DR   GO; GO:0035197; F:siRNA binding; IDA:TAIR.
DR   GO; GO:0006342; P:chromatin silencing; IMP:UniProtKB.
DR   GO; GO:0031048; P:chromatin silencing by small RNA; TAS:TAIR.
DR   GO; GO:0009816; P:defense response to bacterium, incompatible interaction; IMP:TAIR.
DR   GO; GO:0051607; P:defense response to virus; IDA:TAIR.
DR   GO; GO:0006306; P:DNA methylation; IMP:TAIR.
DR   GO; GO:0016458; P:gene silencing; IMP:UniProtKB.
DR   GO; GO:0051567; P:histone H3-K9 methylation; IMP:TAIR.
DR   GO; GO:0019048; P:modulation by virus of host morphology or physiology; IMP:TAIR.
DR   GO; GO:0070919; P:production of siRNA involved in chromatin silencing by small RNA; IMP:CAFA.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; IMP:TAIR.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0080188; P:RNA-directed DNA methylation; IMP:CAFA.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR014811; ArgoL1.
DR   InterPro; IPR032472; ArgoL2.
DR   InterPro; IPR032473; Argonaute_Mid_dom.
DR   InterPro; IPR032474; Argonaute_N.
DR   InterPro; IPR003100; PAZ_dom.
DR   InterPro; IPR036085; PAZ_dom_sf.
DR   InterPro; IPR003165; Piwi.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF08699; ArgoL1; 1.
DR   Pfam; PF16488; ArgoL2; 1.
DR   Pfam; PF16487; ArgoMid; 1.
DR   Pfam; PF16486; ArgoN; 1.
DR   Pfam; PF02170; PAZ; 1.
DR   Pfam; PF02171; Piwi; 1.
DR   SMART; SM01163; DUF1785; 1.
DR   SMART; SM00950; Piwi; 1.
DR   SUPFAM; SSF101690; SSF101690; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50821; PAZ; 1.
DR   PROSITE; PS50822; PIWI; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Host-virus interaction; Nucleus; Plant defense;
KW   Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
KW   RNA-mediated gene silencing; Transcription; Transcription regulation;
KW   Translation regulation.
FT   CHAIN         1    924       Protein argonaute 4.
FT                                /FTId=PRO_0000404667.
FT   DOMAIN      272    408       PAZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00142}.
FT   DOMAIN      577    885       Piwi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00150}.
FT   MOTIF       584    591       Nuclear localization signal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00768}.
FT   COMPBIAS     27     39       Pro-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00015}.
FT   MUTAGEN     641    641       E->K: In ago4-2; no effect on RNA
FT                                binding, but loss of slicer activity.
FT                                {ECO:0000269|PubMed:17993621}.
FT   MUTAGEN     660    660       D->A: No effect on RNA binding, but loss
FT                                of slicer activity.
FT                                {ECO:0000269|PubMed:16998468}.
FT   MUTAGEN     742    742       D->A: No effect on RNA binding, but loss
FT                                of slicer activity.
FT                                {ECO:0000269|PubMed:16998468}.
FT   MUTAGEN     874    874       H->A: No effect on RNA binding, but loss
FT                                of slicer activity.
FT                                {ECO:0000269|PubMed:16998468}.
SQ   SEQUENCE   924 AA;  102840 MW;  C0323FAE9592B147 CRC64;
     MDSTNGNGAD LESANGANGS GVTEALPPPP PVIPPNVEPV RVKTELAEKK GPVRVPMARK
     GFGTRGQKIP LLTNHFKVDV ANLQGHFFHY SVALFYDDGR PVEQKGVGRK ILDKVHQTYH
     SDLDGKEFAY DGEKTLFTYG ALPSNKMDFS VVLEEVSATR ANGNGSPNGN ESPSDGDRKR
     LRRPNRSKNF RVEISYAAKI PLQALANAMR GQESENSQEA IRVLDIILRQ HAARQGCLLV
     RQSFFHNDPT NCEPVGGNIL GCRGFHSSFR TTQGGMSLNM DVTTTMIIKP GPVVDFLIAN
     QNARDPYSID WSKAKRTLKN LRVKVSPSGQ EFKITGLSDK PCREQTFELK KRNPNENGEF
     ETTEVTVADY FRDTRHIDLQ YSADLPCINV GKPKRPTYIP LELCALVPLQ RYTKALTTFQ
     RSALVEKSRQ KPQERMTVLS KALKVSNYDA EPLLRSCGIS ISSNFTQVEG RVLPAPKLKM
     GCGSETFPRN GRWNFNNKEF VEPTKIQRWV VVNFSARCNV RQVVDDLIKI GGSKGIEIAS
     PFQVFEEGNQ FRRAPPMIRV ENMFKDIQSK LPGVPQFILC VLPDKKNSDL YGPWKKKNLT
     EFGIVTQCMA PTRQPNDQYL TNLLLKINAK LGGLNSMLSV ERTPAFTVIS KVPTIILGMD
     VSHGSPGQSD VPSIAAVVSS REWPLISKYR ASVRTQPSKA EMIESLVKKN GTEDDGIIKE
     LLVDFYTSSN KRKPEHIIIF RDGVSESQFN QVLNIELDQI IEACKLLDAN WNPKFLLLVA
     QKNHHTKFFQ PTSPENVPPG TIIDNKICHP KNNDFYLCAH AGMIGTTRPT HYHVLYDEIG
     FSADELQELV HSLSYVYQRS TSAISVVAPI CYAHLAAAQL GTFMKFEDQS ETSSSHGGIT
     APGPISVAQL PRLKDNVANS MFFC
//
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