AGO5_ARATH
ID AGO5_ARATH Reviewed; 997 AA.
AC Q9SJK3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein argonaute 5;
GN Name=AGO5; OrderedLocusNames=At2g27880; ORFNames=T1E2.20;
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).
RN [3]
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 for
RT degradation.";
RL Curr. Biol. 17:1609-1614(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [5]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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., Zhou H.,
RA Long C., Chen S., Hannon G.J., Qi Y.;
RT "Sorting of small RNAs into Arabidopsis argonaute complexes is directed by
RT the 5' terminal nucleotide.";
RL Cell 133:116-127(2008).
RN [6]
RP FUNCTION.
RX PubMed=18344228; DOI=10.1093/pcp/pcn043;
RA Takeda A., Iwasaki S., Watanabe T., Utsumi M., Watanabe Y.;
RT "The mechanism selecting the guide strand from small RNA duplexes is
RT different among argonaute proteins.";
RL Plant Cell Physiol. 49:493-500(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 562-699.
RX PubMed=22850669; DOI=10.1038/emboj.2012.204;
RA Frank F., Hauver J., Sonenberg N., Nagar B.;
RT "Arabidopsis Argonaute MID domains use their nucleotide specificity loop to
RT sort small RNAs.";
RL EMBO J. 31:3588-3595(2012).
CC -!- FUNCTION: Involved in RNA-mediated post-transcriptional gene silencing
CC (PTGS). Main component of the RNA-induced silencing complex (RISC) that
CC binds to a short guide RNA such as a microRNA (miRNA) or small
CC interfering RNA (siRNA). RISC uses the mature miRNA or siRNA as a guide
CC for slicer-directed cleavage of homologous mRNAs to repress gene
CC expression. Associates with siRNAs of various sizes, from 21-24
CC nucleotide in length and preferentially recruits small RNAs with a 5'
CC terminal cytosine. Probably involved in antiviral RNA silencing.
CC Associates with siRNAs derived from cucumber mosaic virus (CMV).
CC Targeted by the turnip yellows virus (TuYV) protein P0 (via F-box-like
CC domain) for probable proteasome degradation and thereby inactivating
CC AGO5 function in RNA silencing. {ECO:0000269|PubMed:17869110,
CC ECO:0000269|PubMed:18342361, ECO:0000269|PubMed:18344228}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
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DR EMBL; AC006929; AAD21514.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08055.1; -; Genomic_DNA.
DR PIR; A84678; A84678.
DR RefSeq; NP_850110.1; NM_179779.3.
DR PDB; 4G0O; X-ray; 2.19 A; A/B=562-699.
DR PDBsum; 4G0O; -.
DR AlphaFoldDB; Q9SJK3; -.
DR SMR; Q9SJK3; -.
DR BioGRID; 2684; 3.
DR STRING; 3702.AT2G27880.1; -.
DR iPTMnet; Q9SJK3; -.
DR PaxDb; Q9SJK3; -.
DR PRIDE; Q9SJK3; -.
DR ProteomicsDB; 244662; -.
DR EnsemblPlants; AT2G27880.1; AT2G27880.1; AT2G27880.
DR GeneID; 817334; -.
DR Gramene; AT2G27880.1; AT2G27880.1; AT2G27880.
DR KEGG; ath:AT2G27880; -.
DR Araport; AT2G27880; -.
DR TAIR; locus:2057851; AT2G27880.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_0_0_1; -.
DR InParanoid; Q9SJK3; -.
DR OMA; IHDEIFT; -.
DR OrthoDB; 159407at2759; -.
DR PhylomeDB; Q9SJK3; -.
DR PRO; PR:Q9SJK3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJK3; baseline and differential.
DR Genevisible; Q9SJK3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0098542; P:defense response to other organism; IEP:TAIR.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0009615; P:response to virus; IEP:TAIR.
DR GO; GO:0009616; P:RNAi-mediated antiviral immune response; IGI:TAIR.
DR CDD; cd04657; Piwi_ago-like; 1.
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; IPR045246; Piwi_ago-like.
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; SM00949; PAZ; 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 3D-structure; Magnesium; Manganese; Metal-binding; Plant defense;
KW Reference proteome; Repressor; Ribonucleoprotein; RNA-binding;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Translation regulation.
FT CHAIN 1..997
FT /note="Protein argonaute 5"
FT /id="PRO_0000194070"
FT DOMAIN 359..471
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 638..958
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..848
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 893..901
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 930..952
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT COMPBIAS 90..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 721
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 807
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 947
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT CONFLICT 402
FT /note="G -> C (in Ref. 1; AAD21514)"
FT /evidence="ECO:0000305"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:4G0O"
FT STRAND 573..578
FT /evidence="ECO:0007829|PDB:4G0O"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:4G0O"
FT HELIX 587..602
FT /evidence="ECO:0007829|PDB:4G0O"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:4G0O"
FT HELIX 622..632
FT /evidence="ECO:0007829|PDB:4G0O"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:4G0O"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:4G0O"
FT HELIX 650..658
FT /evidence="ECO:0007829|PDB:4G0O"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:4G0O"
FT STRAND 665..668
FT /evidence="ECO:0007829|PDB:4G0O"
FT HELIX 670..675
FT /evidence="ECO:0007829|PDB:4G0O"
FT HELIX 678..691
FT /evidence="ECO:0007829|PDB:4G0O"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:4G0O"
SQ SEQUENCE 997 AA; 111089 MW; BEA510811ECC3666 CRC64;
MSNRGGGGHG GASRGRGGGR RSDQRQDQSS GQVAWPGLQQ SYGGRGGSVS AGRGRGNVGR
GENTGDLTAT QVPVASAVSG GRGRGNIGDP TFSVASSSKT VSVASSSKEE SKNTEVSETM
SNLQITSTET KPEMTSLPPA SSKAVTFPVR PGRGTLGKKV MVRANHFLVQ VADRDLYHYD
VSINPEVISK TVNRNVMKLL VKNYKDSHLG GKSPAYDGRK SLYTAGPLPF DSKEFVVNLA
EKRADGSSGK DRPFKVAVKN VTSTDLYQLQ QFLDRKQREA PYDTIQVLDV VLRDKPSNDY
VSVGRSFFHT SLGKDARDGR GELGDGIEYW RGYFQSLRLT QMGLSLNIDV SARSFYEPIV
VTDFISKFLN IRDLNRPLRD SDRLKVKKVL RTLKVKLLHW NGTKSAKISG ISSLPIRELR
FTLEDKSEKT VVQYFAEKYN YRVKYQALPA IQTGSDTRPV YLPMELCQID EGQRYTKRLN
EKQVTALLKA TCQRPPDREN SIKNLVVKNN YNDDLSKEFG MSVTTQLASI EARVLPPPML
KYHDSGKEKM VNPRLGQWNM IDKKMVNGAK VTSWTCVSFS TRIDRGLPQE FCKQLIGMCV
SKGMEFKPQP AIPFISCPPE HIEEALLDIH KRAPGLQLLI VILPDVTGSY GKIKRICETE
LGIVSQCCQP RQVNKLNKQY MENVALKINV KTGGRNTVLN DAIRRNIPLI TDRPTIIMGA
DVTHPQPGED SSPSIAAVVA SMDWPEINKY RGLVSAQAHR EEIIQDLYKL VQDPQRGLVH
SGLIREHFIA FRRATGQIPQ RIIFYRDGVS EGQFSQVLLH EMTAIRKACN SLQENYVPRV
TFVIVQKRHH TRLFPEQHGN RDMTDKSGNI QPGTVVDTKI CHPNEFDFYL NSHAGIQGTS
RPAHYHVLLD ENGFTADQLQ MLTNNLCYTY ARCTKSVSIV PPAYYAHLAA FRARYYMESE
MSDGGSSRSR SSTTGVGQVI SQLPAIKDNV KEVMFYC
