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AGO_GIAIB
ID   AGO_GIAIB               Reviewed;         899 AA.
AC   C6LTG5;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Protein argonaute {ECO:0000250|UniProtKB:Q86QW7};
GN   Name=Ago {ECO:0000250|UniProtKB:Q86QW7}; ORFNames=GL50581_2062;
OS   Giardia intestinalis (strain ATCC 50581 / GS clone H7) (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=598745;
RN   [1] {ECO:0000312|EMBL:EET00696.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50581 / GS clone H7 {ECO:0000312|EMBL:EET00696.1};
RX   PubMed=19696920; DOI=10.1371/journal.ppat.1000560;
RA   Franzen O., Jerlstrom-Hultqvist J., Castro E., Sherwood E., Ankarklev J.,
RA   Reiner D.S., Palm D., Andersson J.O., Andersson B., Svard S.G.;
RT   "Draft genome sequencing of giardia intestinalis assemblage B isolate GS:
RT   is human giardiasis caused by two different species?";
RL   PLoS Pathog. 5:E1000560-E1000560(2009).
CC   -!- FUNCTION: Plays an essential role in growth and, with Dicer, also
CC       involved in microRNA (miRNA)-mediated translational repression. The RNA
CC       interference pathway is implicated in antigenic variation having a role
CC       in regulation of variant-specific surface protein (VSP)-coding gene
CC       expression. Several VSP genes are transcribed but only transcripts
CC       encoding the VSP to be expressed accumulate. Antisense RNAs
CC       corresponding to the silenced VSP genes are detected (By similarity).
CC       {ECO:0000250|UniProtKB:Q86QW7}.
CC   -!- SUBUNIT: Interacts with miR2. Highly specific binding to the mRNA m7G-
CC       cap. May be a component of the RNA-induced silencing complex (RISC), a
CC       sequence-specific, multicomponent nuclease that destroys or silences
CC       messenger RNAs homologous to the silencing trigger (By similarity).
CC       {ECO:0000250|UniProtKB:Q86QW7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86QW7}.
CC   -!- DOMAIN: PAZ domain is absent, but Ago is capable of binding small RNAs
CC       in the same way as the other Argonaute proteins.
CC       {ECO:0000250|UniProtKB:Q86QW7}.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC       {ECO:0000255}.
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DR   EMBL; ACGJ01002264; EET00696.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6LTG5; -.
DR   SMR; C6LTG5; -.
DR   PRIDE; C6LTG5; -.
DR   EnsemblProtists; EET00696; EET00696; GL50581_2062.
DR   VEuPathDB; GiardiaDB:GL50581_2062; -.
DR   OMA; LDRWAVI; -.
DR   OrthoDB; 220258at2759; -.
DR   Proteomes; UP000002488; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR003165; Piwi.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF02171; Piwi; 1.
DR   SMART; SM00950; Piwi; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS50822; PIWI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Developmental protein; Differentiation; RNA-binding;
KW   RNA-mediated gene silencing; Translation regulation.
FT   CHAIN           1..899
FT                   /note="Protein argonaute"
FT                   /id="PRO_0000405234"
FT   DOMAIN          555..878
FT                   /note="Piwi"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00150"
FT   REGION          107..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  100571 MW;  FB16130660F91C9D CRC64;
     MTTDIVTSRI NFYPYTVLPS AKPVYQYDLS IQVSTQGYNL DNADSYRALE KFCEQQDTAL
     GNDPARSLFY SLIVDFPSSD SRPISSFYSQ TDLGSRPVTH TVEFLSTQKP KRRGGRAGGM
     RGNRGGPSTT SVQALVKVTR VRQMDPLDLM SMKTLLNILL RRTFESSLGM LNIRSGFYDL
     NRTSTHNIQV DGRGFDICWI PGFRLTTATL YGKLGLQVLP ETTKVRSKSM CELLNENRGS
     LHPNALAAIT VMAMHNGRVF RIHSIVRGQS VVSPLAEGSD TDYFTYYSAK YKDKIDSAAL
     SLLKQDDYCN SVLQRDKFIL KLTPLKKTHN GKVVRSCNVP SSLCIIISDN EIAPYGVSKL
     STNKTAVALS TMSPDALLEK ATEFANQLID NAELQSVLGD YGFRFTSQPL ELDTFVCKPP
     KLMMDTLSRE LTVEDDSGGV FRSLIQSPGV SSIYYANNGQ PAVGMPHWAL MVPRYLKNDY
     ARRLKQELTQ RIRSLAGATA STVEEPLLIA VDVNEQRRDM YRIEPYKDAF ESLLVKLNTQ
     YPDTKNSELI SRIQLVVVVI PGPKQYSGGL YKEVKRFYTD KGIVTQCLLT PRLSRDGPEW
     YDQAILNGLC QQIYAKAGGA VWAPALPKDN AYSTSTMLCA LDVSRPKKTV GRPTEVPAST
     AGFISTYEGS FEYIYSQKKN LMPNRLNQGG EVQQQTLMKT FIKNSCEVYS AFNSSLPDRI
     VIFRDGVSDG QISTVLETEI NSLYEYLCQR YREANRPMCD LKVIVAQKTC AMRLAAVSNT
     DLRPGFYILN HSPDNKQKGS EFIMASQAIV HGTTPKPIRY KLIFDSTEAS MDNSSFKQLI
     ELTNTMAYGY VNWPQAISLP HILHMAHLLS KFCGEILGNG RDLLESQAIF GLQYRPFFI
 
 
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