DCL_GIAIC
ID DCL_GIAIC Reviewed; 754 AA.
AC A8BQJ3; Q86QW6;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Endoribonuclease Dicer-like;
DE EC=3.1.26.- {ECO:0000269|PubMed:16410517};
GN ORFNames=GL50803_103887;
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50803 / WB clone C6;
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E.J., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.33 ANGSTROMS) IN COMPLEX WITH MANGANESE, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=16410517; DOI=10.1126/science.1121638;
RA Macrae I.J., Zhou K., Li F., Repic A., Brooks A.N., Cande W.Z., Adams P.D.,
RA Doudna J.A.;
RT "Structural basis for double-stranded RNA processing by Dicer.";
RL Science 311:195-198(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH MANGANESE, SUBUNIT,
RP AND COFACTOR.
RX PubMed=17704568; DOI=10.1107/s0907444907036128;
RA MacRae I.J., Doudna J.A.;
RT "An unusual case of pseudo-merohedral twinning in orthorhombic crystals of
RT Dicer.";
RL Acta Crystallogr. D 63:993-999(2007).
CC -!- FUNCTION: Involved in cleaving double-stranded RNA in the RNA
CC interference (RNAi) pathway. It produces 21 to 23 bp dsRNAs (siRNAs)
CC which target the selective destruction of homologous RNAs.
CC {ECO:0000269|PubMed:16410517}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16410517};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16410517};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000269|PubMed:16410517, ECO:0000269|PubMed:17704568};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16410517,
CC ECO:0000269|PubMed:17704568}.
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DR EMBL; AACB02000033; EDO77862.1; -; Genomic_DNA.
DR RefSeq; XP_001705536.1; XM_001705484.1.
DR PDB; 2FFL; X-ray; 3.33 A; A/B/C/D=1-754.
DR PDB; 2QVW; X-ray; 3.00 A; A/B/C/D=1-754.
DR PDBsum; 2FFL; -.
DR PDBsum; 2QVW; -.
DR AlphaFoldDB; A8BQJ3; -.
DR SMR; A8BQJ3; -.
DR EnsemblProtists; EDO77862; EDO77862; GL50803_103887.
DR GeneID; 5698409; -.
DR KEGG; gla:GL50803_00103887; -.
DR VEuPathDB; GiardiaDB:GL50803_103887; -.
DR HOGENOM; CLU_369381_0_0_1; -.
DR InParanoid; A8BQJ3; -.
DR OMA; WADMYEE; -.
DR OrthoDB; 475946at2759; -.
DR BRENDA; 3.1.26.3; 2401.
DR EvolutionaryTrace; A8BQJ3; -.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 1.10.1520.10; -; 2.
DR InterPro; IPR041279; Dicer_N.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR11207; PTHR11207; 2.
DR Pfam; PF17895; Dicer_N; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF101690; SSF101690; 1.
DR SUPFAM; SSF69065; SSF69065; 2.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nuclease; Nucleotide-binding; Repeat; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..754
FT /note="Endoribonuclease Dicer-like"
FT /id="PRO_0000371303"
FT DOMAIN 123..251
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 298..418
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 613..734
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT BINDING 336
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16410517,
FT ECO:0000269|PubMed:17704568, ECO:0007744|PDB:2FFL,
FT ECO:0007744|PDB:2QVW"
FT BINDING 404
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16410517,
FT ECO:0000269|PubMed:17704568, ECO:0007744|PDB:2FFL,
FT ECO:0007744|PDB:2QVW"
FT BINDING 407
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16410517,
FT ECO:0000269|PubMed:17704568, ECO:0007744|PDB:2FFL,
FT ECO:0007744|PDB:2QVW"
FT BINDING 649
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16410517,
FT ECO:0000269|PubMed:17704568, ECO:0007744|PDB:2FFL,
FT ECO:0007744|PDB:2QVW"
FT BINDING 720
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16410517,
FT ECO:0000269|PubMed:17704568, ECO:0007744|PDB:2FFL,
FT ECO:0007744|PDB:2QVW"
FT BINDING 723
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16410517,
FT ECO:0000269|PubMed:17704568, ECO:0007744|PDB:2FFL,
FT ECO:0007744|PDB:2QVW"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2FFL"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2QVW"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2QVW"
FT TURN 162..166
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:2QVW"
FT TURN 218..223
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2QVW"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 265..282
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 328..354
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 360..371
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:2QVW"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 402..415
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 419..431
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 462..471
FT /evidence="ECO:0007829|PDB:2QVW"
FT TURN 472..476
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 484..495
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 498..514
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 526..540
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:2QVW"
FT TURN 565..568
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:2QVW"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:2QVW"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 589..600
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 609..618
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 629..640
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 643..645
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 646..667
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 673..682
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 686..694
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 699..707
FT /evidence="ECO:0007829|PDB:2QVW"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:2FFL"
FT HELIX 716..733
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 735..745
FT /evidence="ECO:0007829|PDB:2QVW"
FT HELIX 747..749
FT /evidence="ECO:0007829|PDB:2QVW"
SQ SEQUENCE 754 AA; 82478 MW; 27FDC93E7C78BE0A CRC64;
MHALGHCCTV VTTRGPSHWL LLLDTHLGTL PGFKVSAGRG LPAAEVYFEA GPRVSLSRTD
ATIVAVYQSI LFQLLGPTFP ASWTEIGATM PHNEYTFPRF ISNPPQFATL AFLPLLSPTS
PLDLRALMVT AQLMCDAKRL SDEYTDYSTL SASLHGRMVA TPEISWSLYV VLGIDSTQTS
LSYFTRANES ITYMRYYATA HNIHLRAADL PLVAAVRLDD LKDHQIPAPG SWDDLAPKLR
FLPPELCLLL PDEFDLIRVQ ALQFLPEIAK HICDIQNTIC ALDKSFPDCG RIGGERYFAI
TAGLRLDQGR GRGLAGWRTP FGPFGVSHTD VFQRLELLGD AVLGFIVTAR LLCLFPDASV
GTLVELKMEL VRNEALNYLV QTLGLPQLAE FSNNLVAKSK TWADMYEEIV GSIFTGPNGI
YGCEEFLAKT LMSPEHSKTV GSACPDAVTK ASKRVCMGEA GAHEFRSLVD YACEQGISVF
CSSRVSTMFL ERLRDIPAED MLDWYRLGIQ FSHRSGLSGP GGVVSVIDIM THLARGLWLG
SPGFYVEQQT DKNESACPPT IPVLYIYHRS VQCPVLYGSL TETPTGPVAS KVLALYEKIL
AYESSGGSKH IAAQTVSRSL AVPIPSGTIP FLIRLLQIAL TPHVYQKLEL LGDAFLKCSL
ALHLHALHPT LTEGALTRMR QSAETNSVLG RLTKRFPSVV SEVIIESHPK IQPDSKVYGD
TFEAILAAIL LACGEEAAGA FVREHVLPQV VADA
