AGO2_DROME
ID AGO2_DROME Reviewed; 1214 AA.
AC Q9VUQ5; C7LAD2; Q2Q3Y0; Q2Q3Y1; Q2Q3Y3; Q2Q3Y4; Q2Q3Y5; Q86P07; Q8T3N2;
AC Q9VUQ6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Protein argonaute-2;
GN Name=AGO2 {ECO:0000312|EMBL:AAF49620.2}; ORFNames=CG7439;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF49620.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF49619.2}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAO39550.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO39550.1}; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Booth B., Carlson J.W.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-1214, AND VARIANTS ARG-714;
RP PRO-740; ASN-783; ALA-835; THR-854 AND GLU-866.
RC STRAIN=128, 130, 138, 140, 141, 186, 187, and 196;
RX PubMed=16546082; DOI=10.1016/j.cub.2006.01.065;
RA Obbard D.J., Jiggins F.M., Halligan D.L., Little T.J.;
RT "Natural selection drives extremely rapid evolution in antiviral RNAi
RT genes.";
RL Curr. Biol. 16:580-585(2006).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAM11104.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 449-1214, AND VARIANTS ASN-783;
RP ALA-835 AND THR-854.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Ovary {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000305}
RP PROTEIN SEQUENCE OF 506-515; 525-531; 554-557; 617-627; 662-674; 809-815
RP AND 1181-1188 (ISOFORM B), FUNCTION, AND INTERACTION WITH DCR-1.
RX PubMed=11498593; DOI=10.1126/science.1064023;
RA Hammond S.M., Boettcher S., Caudy A.A., Kobayashi R., Hannon G.J.;
RT "Argonaute2, a link between genetic and biochemical analyses of RNAi.";
RL Science 293:1146-1150(2001).
RN [7]
RP FUNCTION, AND INTERACTION WITH VIG; FMR1 AND TUDOR-SN.
RX PubMed=14508492; DOI=10.1038/nature01956;
RA Caudy A.A., Ketting R.F., Hammond S.M., Denli A.M., Bathoorn A.M.,
RA Tops B.B., Silva J.M., Myers M.M., Hannon G.J., Plasterk R.H.;
RT "A micrococcal nuclease homologue in RNAi effector complexes.";
RL Nature 425:411-414(2003).
RN [8] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH FMR1.
RX PubMed=12368261; DOI=10.1101/gad.1022002;
RA Ishizuka A., Siomi M.C., Siomi H.;
RT "A Drosophila fragile X protein interacts with components of RNAi and
RT ribosomal proteins.";
RL Genes Dev. 16:2497-2508(2002).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17178403; DOI=10.1016/j.neuron.2006.10.028;
RA Barbee S.A., Estes P.S., Cziko A.M., Hillebrand J., Luedeman R.A.,
RA Coller J.M., Johnson N., Howlett I.C., Geng C., Ueda R., Brand A.H.,
RA Newbury S.F., Wilhelm J.E., Levine R.B., Nakamura A., Parker R.,
RA Ramaswami M.;
RT "Staufen- and FMRP-containing neuronal RNPs are structurally and
RT functionally related to somatic P bodies.";
RL Neuron 52:997-1009(2006).
RN [10]
RP INTERACTION WITH CRICKET PARALYSIS VIRUS PROTEIN 1A (MICROBIAL INFECTION).
RX PubMed=20400949; DOI=10.1038/nsmb.1810;
RA Nayak A., Berry B., Tassetto M., Kunitomi M., Acevedo A., Deng C.,
RA Krutchinsky A., Gross J., Antoniewski C., Andino R.;
RT "Cricket paralysis virus antagonizes Argonaute 2 to modulate antiviral
RT defense in Drosophila.";
RL Nat. Struct. Mol. Biol. 17:547-554(2010).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF VAL-966.
RX PubMed=32504809; DOI=10.1016/j.ibmb.2020.103415;
RA Lee S., Hong J.S., Lim D.H., Lee Y.S.;
RT "Roles for Drosophila cap1 2'-O-ribose methyltransferase in the small RNA
RT silencing pathway associated with Argonaute 2.";
RL Insect Biochem. Mol. Biol. 123:103415-103415(2020).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 591-726.
RX PubMed=14625589; DOI=10.1038/nsb1016;
RA Song J.J., Liu J., Tolia N.H., Schneiderman J., Smith S.K.,
RA Martienssen R.A., Hannon G.J., Joshua-Tor L.;
RT "The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding
RT motif in RNAi effector complexes.";
RL Nat. Struct. Biol. 10:1026-1032(2003).
RN [13]
RP STRUCTURE BY NMR OF 602-740.
RX PubMed=14615801; DOI=10.1038/nature02123;
RA Lingel A., Simon B., Izaurralde E., Sattler M.;
RT "Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ
RT domain.";
RL Nature 426:465-469(2003).
RN [14]
RP STRUCTURE BY NMR OF 605-720.
RX PubMed=15156196; DOI=10.1038/nsmb777;
RA Lingel A., Simon B., Izaurralde E., Sattler M.;
RT "Nucleic acid 3'-end recognition by the Argonaute2 PAZ domain.";
RL Nat. Struct. Mol. Biol. 11:576-577(2004).
CC -!- FUNCTION: Essential for RNA interference (RNAi); double-stranded RNA
CC induces potent and specific gene silencing (PubMed:11498593,
CC PubMed:12368261, PubMed:14508492, PubMed:32504809). RNAi is mediated by
CC the RNA-induced silencing complex (RISC), a sequence-specific,
CC multicomponent nuclease that destroys or silences messenger RNAs
CC homologous to the silencing trigger (PubMed:11498593, PubMed:12368261,
CC PubMed:14508492). {ECO:0000269|PubMed:11498593,
CC ECO:0000269|PubMed:12368261, ECO:0000269|PubMed:14508492,
CC ECO:0000269|PubMed:32504809}.
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 -!- SUBUNIT: Interacts with Fmr1, Dcr-1 and vig to form the RNA-induced
CC silencing complex (RISC), a ribonucleoprotein (RNP) complex involved in
CC translation regulation, other components of the complex are RpL5, RpL11
CC and Rm62 (PubMed:11498593, PubMed:14508492, PubMed:12368261). As part
CC of the RISC complex, interacts with Tudor-SN (PubMed:14508492).
CC {ECO:0000269|PubMed:11498593, ECO:0000269|PubMed:12368261,
CC ECO:0000269|PubMed:14508492}.
CC -!- SUBUNIT: (Microbial infection) Interacts with cricket paralysis virus
CC protein 1A; this interaction may block the RISC activity.
CC {ECO:0000269|PubMed:20400949}.
CC -!- INTERACTION:
CC Q9VUQ5; Q9NFU0: Fmr1; NbExp=4; IntAct=EBI-442476, EBI-422631;
CC Q9VUQ5; Q9IJX4: ORF1; Xeno; NbExp=3; IntAct=EBI-442476, EBI-15848754;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC {ECO:0000269|PubMed:17178403}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q9VUQ5-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q9VUQ5-2; Sequence=VSP_050781;
CC -!- DOMAIN: PAZ domain provides a major contribution for nucleic acid
CC recognition. PAZ binds oligonucleotides of different lengths and has a
CC strong preference for single-stranded nucleic acids (ssRNA or SSDNA) or
CC RNA duplexes with single-stranded 3' overhangs. Can bind the
CC characteristic two-base 3' overhangs of siRNAs, indicating that it may
CC contribute to the specific and productive incorporation of siRNAs and
CC miRNAs into the RNAi pathway.
CC -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11104.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF49619.2; -; Genomic_DNA.
DR EMBL; AE014296; AAF49620.2; -; Genomic_DNA.
DR EMBL; BT003546; AAO39550.1; -; mRNA.
DR EMBL; BT099682; ACV44468.1; -; mRNA.
DR EMBL; DQ228766; ABB54719.1; -; Genomic_DNA.
DR EMBL; DQ228767; ABB54720.1; -; Genomic_DNA.
DR EMBL; DQ228768; ABB54721.1; -; Genomic_DNA.
DR EMBL; DQ228769; ABB54722.1; -; Genomic_DNA.
DR EMBL; DQ228770; ABB54723.1; -; Genomic_DNA.
DR EMBL; DQ228771; ABB54724.1; -; Genomic_DNA.
DR EMBL; DQ228772; ABB54725.1; -; Genomic_DNA.
DR EMBL; DQ228773; ABB54726.1; -; Genomic_DNA.
DR EMBL; AY094751; AAM11104.1; ALT_INIT; mRNA.
DR RefSeq; NP_648775.1; NM_140518.3. [Q9VUQ5-1]
DR RefSeq; NP_730054.1; NM_168626.3. [Q9VUQ5-2]
DR PDB; 1R6Z; X-ray; 2.80 A; A/P/Z=589-726.
DR PDB; 1T2R; NMR; -; A=602-720.
DR PDB; 1T2S; NMR; -; A=602-720.
DR PDB; 1VYN; NMR; -; A=602-740.
DR PDB; 3MJ0; X-ray; 2.31 A; A=601-723.
DR PDBsum; 1R6Z; -.
DR PDBsum; 1T2R; -.
DR PDBsum; 1T2S; -.
DR PDBsum; 1VYN; -.
DR PDBsum; 3MJ0; -.
DR AlphaFoldDB; Q9VUQ5; -.
DR BMRB; Q9VUQ5; -.
DR SMR; Q9VUQ5; -.
DR BioGRID; 65002; 70.
DR DIP; DIP-41570N; -.
DR IntAct; Q9VUQ5; 32.
DR MINT; Q9VUQ5; -.
DR STRING; 7227.FBpp0075313; -.
DR PaxDb; Q9VUQ5; -.
DR PRIDE; Q9VUQ5; -.
DR ABCD; Q9VUQ5; 1 sequenced antibody.
DR EnsemblMetazoa; FBtr0075559; FBpp0075312; FBgn0087035. [Q9VUQ5-1]
DR EnsemblMetazoa; FBtr0075560; FBpp0075313; FBgn0087035. [Q9VUQ5-2]
DR GeneID; 39683; -.
DR KEGG; dme:Dmel_CG7439; -.
DR CTD; 27161; -.
DR FlyBase; FBgn0087035; AGO2.
DR VEuPathDB; VectorBase:FBgn0087035; -.
DR eggNOG; KOG1041; Eukaryota.
DR HOGENOM; CLU_004544_7_1_1; -.
DR InParanoid; Q9VUQ5; -.
DR PhylomeDB; Q9VUQ5; -.
DR Reactome; R-DME-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-DME-426486; Small interfering RNA (siRNA) biogenesis.
DR Reactome; R-DME-426496; Post-transcriptional silencing by small RNAs.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR SignaLink; Q9VUQ5; -.
DR BioGRID-ORCS; 39683; 1 hit in 1 CRISPR screen.
DR EvolutionaryTrace; Q9VUQ5; -.
DR GenomeRNAi; 39683; -.
DR PRO; PR:Q9VUQ5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0087035; Expressed in eye disc (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9VUQ5; baseline and differential.
DR Genevisible; Q9VUQ5; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0016442; C:RISC complex; IDA:UniProtKB.
DR GO; GO:0070578; C:RISC-loading complex; IDA:FlyBase.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:FlyBase.
DR GO; GO:0070551; F:endoribonuclease activity, cleaving siRNA-paired mRNA; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:FlyBase.
DR GO; GO:0035197; F:siRNA binding; IDA:FlyBase.
DR GO; GO:0098586; P:cellular response to virus; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
DR GO; GO:0009047; P:dosage compensation by hyperactivation of X chromosome; IGI:FlyBase.
DR GO; GO:0033227; P:dsRNA transport; IMP:FlyBase.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:FlyBase.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; IMP:FlyBase.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IMP:FlyBase.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IDA:FlyBase.
DR GO; GO:0070922; P:RISC complex assembly; IDA:FlyBase.
DR GO; GO:0009616; P:RNAi-mediated antiviral immune response; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IGI:FlyBase.
DR GO; GO:0030422; P:siRNA processing; IDA:UniProtKB.
DR GO; GO:0035190; P:syncytial nuclear migration; IMP:FlyBase.
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; 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; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Magnesium; Manganese; Metal-binding;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..1214
FT /note="Protein argonaute-2"
FT /id="PRO_0000194071"
FT DOMAIN 608..717
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 885..1186
FT /note="Piwi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT REGION 1..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..686
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 1075..1076
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 1119..1127
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT REGION 1156..1178
FT /note="Interaction with guide RNA"
FT /evidence="ECO:0000255"
FT COMPBIAS 14..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 965
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 1037
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 1173
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..6
FT /note="MGKKDK -> MHFPITTPE (in isoform C)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_050781"
FT VARIANT 714
FT /note="S -> R (in strain: 186)"
FT /evidence="ECO:0000269|PubMed:16546082"
FT VARIANT 740
FT /note="S -> P (in strain: 130)"
FT /evidence="ECO:0000269|PubMed:16546082"
FT VARIANT 783
FT /note="S -> N (in strain: 138, 140 and 196)"
FT /evidence="ECO:0000269|PubMed:12537569,
FT ECO:0000269|PubMed:16546082"
FT VARIANT 835
FT /note="T -> A (in strain: 128, 130, 138, 140, 141, 186, 187
FT and 196)"
FT /evidence="ECO:0000269|PubMed:12537569,
FT ECO:0000269|PubMed:16546082"
FT VARIANT 854
FT /note="S -> T (in strain: 128, 130, 138, 140, 141, 186, 187
FT and 196)"
FT /evidence="ECO:0000269|PubMed:12537569,
FT ECO:0000269|PubMed:16546082"
FT VARIANT 866
FT /note="D -> E (in strain: 128, 130, 141, 186 and 187)"
FT /evidence="ECO:0000269|PubMed:16546082"
FT MUTAGEN 966
FT /note="V->M: Impaired conversion of the pre-RISC complex,
FT containing duplex siRNA, to the holo-RISC complex,
FT containing single-stranded guide siRNA."
FT /evidence="ECO:0000269|PubMed:32504809"
FT CONFLICT 201
FT /note="G -> D (in Ref. 3; AAO39550)"
FT /evidence="ECO:0000305"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:3MJ0"
FT HELIX 604..611
FT /evidence="ECO:0007829|PDB:3MJ0"
FT STRAND 618..621
FT /evidence="ECO:0007829|PDB:1VYN"
FT HELIX 623..625
FT /evidence="ECO:0007829|PDB:3MJ0"
FT HELIX 627..634
FT /evidence="ECO:0007829|PDB:3MJ0"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:3MJ0"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:3MJ0"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:3MJ0"
FT STRAND 658..663
FT /evidence="ECO:0007829|PDB:3MJ0"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:3MJ0"
FT STRAND 668..677
FT /evidence="ECO:0007829|PDB:3MJ0"
FT HELIX 678..683
FT /evidence="ECO:0007829|PDB:3MJ0"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:3MJ0"
FT STRAND 692..698
FT /evidence="ECO:0007829|PDB:3MJ0"
FT STRAND 705..708
FT /evidence="ECO:0007829|PDB:1T2R"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:3MJ0"
FT STRAND 713..716
FT /evidence="ECO:0007829|PDB:3MJ0"
FT TURN 717..719
FT /evidence="ECO:0007829|PDB:1T2R"
SQ SEQUENCE 1214 AA; 136850 MW; 0DC73AF09CC33F73 CRC64;
MGKKDKNKKG GQDSAAAPQP QQQQKQQQQR QQQPQQLQQP QQLQQPQQLQ QPQQQQQQQP
HQQQQQSSRQ QPSTSSGGSR ASGFQQGGQQ QKSQDAEGWT AQKKQGKQQV QGWTKQGQQG
GHQQGRQGQD GGYQQRPPGQ QQGGHQQGRQ GQEGGYQQRP PGQQQGGHQQ GRQGQEGGYQ
QRPSGQQQGG HQQGRQGQEG GYQQRPPGQQ QGGHQQGRQG QEGGYQQRPS GQQQGGHQQG
RQGQEGGYQQ RPPGQQQGGH QQGRQGQEGG YQQRPPGQQQ GGHEQGRQGQ EGGYQQRPSG
QQQGGHQQGR QGQEGGYQQR PSGQQQGGHQ QGRQGQEGGY QQRPSGQQQG GHQQGRQGQE
GGYQQRPPGQ QPNQTQSQGQ YQSRGPPQQQ QAAPLPLPPQ PAGSIKRGTI GKPGQVGINY
LDLDLSKMPS VAYHYDVKIM PERPKKFYRQ AFEQFRVDQL GGAVLAYDGK ASCYSVDKLP
LNSQNPEVTV TDRNGRTLRY TIEIKETGDS TIDLKSLTTY MNDRIFDKPM RAMQCVEVVL
ASPCHNKAIR VGRSFFKMSD PNNRHELDDG YEALVGLYQA FMLGDRPFLN VDISHKSFPI
SMPMIEYLER FSLKAKINNT TNLDYSRRFL EPFLRGINVV YTPPQSFQSA PRVYRVNGLS
RAPASSETFE HDGKKVTIAS YFHSRNYPLK FPQLHCLNVG SSIKSILLPI ELCSIEEGQA
LNRKDGATQV ANMIKYAATS TNVRKRKIMN LLQYFQHNLD PTISRFGIRI ANDFIVVSTR
VLSPPQVEYH SKRFTMVKNG SWRMDGMKFL EPKPKAHKCA VLYCDPRSGR KMNYTQLNDF
GNLIISQGKA VNISLDSDVT YRPFTDDERS LDTIFADLKR SQHDLAIVII PQFRISYDTI
KQKAELQHGI LTQCIKQFTV ERKCNNQTIG NILLKINSKL NGINHKIKDD PRLPMMKNTM
YIGADVTHPS PDQREIPSVV GVAASHDPYG ASYNMQYRLQ RGALEEIEDM FSITLEHLRV
YKEYRNAYPD HIIYYRDGVS DGQFPKIKNE ELRCIKQACD KVGCKPKICC VIVVKRHHTR
FFPSGDVTTS NKFNNVDPGT VVDRTIVHPN EMQFFMVSHQ AIQGTAKPTR YNVIENTGNL
DIDLLQQLTY NLCHMFPRCN RSVSYPAPAY LAHLVAARGR VYLTGTNRFL DLKKEYAKRT
IVPEFMKKNP MYFV
