ID   AGO1_LEIBR              Reviewed;         898 AA.
AC   G8XR08;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Protein argonaute 1 {ECO:0000303|PubMed:21060810};
DE            Short=LbrAGO1 {ECO:0000303|PubMed:23217017};
GN   Name=AGO1 {ECO:0000303|PubMed:21060810};
OS   Leishmania braziliensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660 {ECO:0000312|EMBL:ACI22628.1};
RN   [1] {ECO:0000312|EMBL:ACI22628.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=MHOM/BR/75/M2903 {ECO:0000312|EMBL:ACI22628.1};
RX   PubMed=21060810; DOI=10.1371/journal.ppat.1001161;
RA   Lye L.F., Owens K., Shi H., Murta S.M., Vieira A.C., Turco S.J.,
RA   Tschudi C., Ullu E., Beverley S.M.;
RT   "Retention and loss of RNA interference pathways in trypanosomatid
RT   protozoans.";
RL   PLoS Pathog. 6:e1001161-e1001161(2010).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=MHOM/BR/75/M2903 {ECO:0000269|PubMed:23217017};
RX   PubMed=23217017; DOI=10.1111/mmi.12117;
RA   Atayde V.D., Shi H., Franklin J.B., Carriero N., Notton T., Lye L.F.,
RA   Owens K., Beverley S.M., Tschudi C., Ullu E.;
RT   "The structure and repertoire of small interfering RNAs in Leishmania
RT   (Viannia) braziliensis reveal diversification in the trypanosomatid RNAi
RT   pathway.";
RL   Mol. Microbiol. 87:580-593(2013).
CC   -!- FUNCTION: Involved in RNA-mediated gene silencing (RNAi) of mobile
CC       elements and repeats including retroposons SLACS (Spliced Leader
CC       Associated Conserved Sequence), TATE (Telomere-Associated Transposable
CC       Element) and TAS-like sequences (Telomere Associated Sequence), and a
CC       family of 74-nucleotide long tandem repeats, CIR74 (PubMed:21060810,
CC       PubMed:23217017). Predominantly binds to siRNAs derived from SLACS and
CC       TATE transposable elements and to a lesser extent to siRNAs from TAS-
CC       like and CIR74 elements (PubMed:23217017).
CC       {ECO:0000269|PubMed:21060810, ECO:0000269|PubMed:23217017}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23217017}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces RNAi activity
CC       (PubMed:21060810, PubMed:23217017). Levels of mobile elements TATE,
CC       SLACS, TAS-like and repeat element CIR74 siRNAs are reduced
CC       (PubMed:23217017). {ECO:0000269|PubMed:21060810,
CC       ECO:0000269|PubMed:23217017}.
CC   -!- SIMILARITY: Belongs to the argonaute family. {ECO:0000305}.
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DR   EMBL; EU780587; ACI22628.1; -; Genomic_DNA.
DR   SMR; G8XR08; -.
DR   VEuPathDB; TriTrypDB:LbrM.11.0360; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_110008400; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR032472; ArgoL2.
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; PF16488; ArgoL2; 1.
DR   Pfam; PF02170; PAZ; 1.
DR   SMART; SM00949; PAZ; 1.
DR   SMART; SM00950; Piwi; 1.
DR   SUPFAM; SSF101690; SSF101690; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; RNA-binding; RNA-mediated gene silencing.
FT   CHAIN           1..898
FT                   /note="Protein argonaute 1"
FT                   /id="PRO_0000453673"
FT   DOMAIN          282..427
FT                   /note="PAZ"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          542..883
FT                   /note="Piwi"
FT                   /evidence="ECO:0000255"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   898 AA;  100596 MW;  5E0B81DB77FCAB9A CRC64;
     MLALNAGSQY PGRGRGRGRG DGGNRVHKHD GINRYHGGFR GGRGGGGGGF RDGDMRECRE
     RESWAVSAAQ ANARTLARVP VPVETNCFPI DLSEGRFHNY IVSFEFLENA TDMAGDMWKI
     SLQNELLRTI RKNRTAEKRT RTSAEVEDLC VCTGQAILAP AKLSVEDGFS IECTRKEKVS
     RNNTEERHYR VRIRYDGEVS LKLPEHAQWV NKIIAFGLAD TYSEHIGSDY VDMKSTVERG
     GDLVTMDAIS LNALRIVKQS GSTTAMMDVL QLDVSTKAST KTKCSDEMRR LRQQNPQGFR
     RAVNEALVGI SVTTVFGEPT FLKVKAIDFN ILASSPTMFK TNPEETFVEY FKRKYDAIID
     PTLPMLYCIF ADRTKMSRRM PYPADSLLLN KLNEAQLSKL PILCSIYPNE RMKRIKAALE
     RVLASPLMIT VLQQYGVRIQ PQFVKVSGRV LPAPTIYVPS GPNMFNRINT AEYTGQAGFA
     LGLKDLQHPS QPCEFKTLLM DEYFMHGNIT HWLQKYNVAL PSPRKTSFDS AAQRITEGPG
     TFAMVKLRTK EAGAYNNFKE RFARSSIVSQ MAVVDLTRNV PQMITQQVAA KIGQLCFVAD
     VDEAGKSFAC RPLLIVGAVV GTAMNTMLEK YKSINVRLYT ITFVAFLANG KSWKPYCMHH
     QVKGEEHVLY EDSDAASSHM SSTTLTVRRQ NANEVLNNRF PDFLKEVTAH FKLNGKGSKG
     TMVLYRGAMT DAEVGFTANM DLVMEQVLPN WDTATVVVHP RSHFRMAWDP TTVFPHETAS
     AYAGLSNVPR GFSTTDCRII LADSDPYTPV DSFYLSAANC TLGHAANTYY LVQKRAASIS
     LMDLQKLTYN MCYMYPNKPD ALPLPLPIKC AYEYARKYGS LKSVKELPTR MRPTMHYL