DCL21_ASPNC
ID DCL21_ASPNC Reviewed; 1387 AA.
AC A2R345;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Dicer-like protein 2-1;
DE Includes:
DE RecName: Full=Endoribonuclease dcl2-1;
DE EC=3.1.26.-;
DE Includes:
DE RecName: Full=ATP-dependent helicase dcl2-1;
DE EC=3.6.4.-;
GN Name=dcl2-1; ORFNames=An14g03000;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Dicer-like endonuclease involved in cleaving double-stranded
CC RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs
CC (siRNAs) which target the selective destruction of homologous RNAs
CC leading to sequence-specific suppression of gene expression, called
CC post-transcriptional gene silencing (PTGS). Part of a broad host
CC defense response against viral infection and transposons (By
CC similarity). {ECO:0000250}.
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 helicase family. Dicer subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00657}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK46537.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270320; CAK46537.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2R345; -.
DR SMR; A2R345; -.
DR PaxDb; A2R345; -.
DR PRIDE; A2R345; -.
DR EnsemblFungi; CAK46537; CAK46537; An14g03000.
DR Proteomes; UP000006706; Chromosome 1R.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProt.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 1.10.1520.10; -; 2.
DR Gene3D; 3.30.160.380; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF69065; SSF69065; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 3: Inferred from homology;
KW Antiviral defense; Antiviral protein; ATP-binding; Helicase; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1387
FT /note="Dicer-like protein 2-1"
FT /id="PRO_0000306787"
FT DOMAIN 26..205
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 370..535
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 565..659
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 915..1055
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1094..1277
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT MOTIF 146..149
FT /note="DEAH box"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 1259
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1387 AA; 156456 MW; 68B17C1A26553265 CRC64;
MTVAATVLPA GEDAPAYRPR SYQVEMFEAS LKENIIVTMG TGSGKTHIAL LRIIKELESN
PHKLIWFLTP TVALCLQQFK FLSDNIPAVR ARTLTSLDKV ELWTEQPVWD AILKEMQVVV
STHAVLADAM SHGFVKITQL GLMIFDEAHH CMRRHPANKI MQDFYHPALE RHGAEAVPKI
LGLTASPVVR SNRQELLKIE SNLDAVCKTP RTHRSELMTH THRPHLQQIL FTPVLLDDLQ
VGSKTLKALV SAWTSLRLED DPYIKKLRKS PLDGRALQKV LESGKTYCND QLKRFATRSL
HIFEELGEWA ADYFIHASIE QLKARAGNSA DTMGWTDEEK AYLLDIVSKL PIPNIDLTHS
DPDRIPISSK FRSLLEFLDT KGEPNFSGLI FAKQRATVSV MEKLLSIHPV TKHRFRCASF
VGWSGGGSKD VLGELLDARM QRDTLSEFRT GQKNLIIATD VLEEGIDISA CSVVVCFDKP
PNLKSFVQRR GRARHRQSTY AIMFATDDES SALSKWEDLE QAMIEAYEDD ERRLREAWAL
EAINEEVVER LEVQSTGAVL TADTAVAHLN HFCAVLPRQP YASNEPEFSY EKDDADLLRG
TVTLPSCVHP GVRRIQGQRW WQTERAARKE AAFQAYKRLY EFGLLSDHLL PFKRNLELKE
TDLTNLPALV EVSEQYDPWV DWACSWSSPD VHQTRIAIKH NGDSRMCIRL TSPTSLPPVE
PMTLFWDSET IYTLDFDKPK RMKEIAAESI ENMRLATALY LQAASSRQMR PEQDFVTLFG
PDLTDLELAE WLNKHAGDEP ALEVYSRKDF PTVMGIVRDR SRYNEPMLFK RWVVSGQDDT
PIVELECDAV PKRRNLLHRQ TLAAKQPDSE TPAISSKIRL ILAENCTIDK LPYAETIFGR
FISVILDRLE ATLVATRLCE TILRDLEFSS IRHIITAITA PSAQSLTNYQ RYEFFGDSVL
KFTVSCQLFF QHPNWHEGYL SEGRDEIVQN SRLARAALDA GLDAFIMNKM FTPRKWSAPL
ISEKISLTPK QRTMSTKVLA DVVEALIGAS YIDGGFAAAH ACIHRFLPEV NLENIDRTTA
PMPKDGVTNH TLNDDHLMAH IGYTFTNKSL LVESLTHPSC QFDTTTQSYQ RLEFLGDAVL
DMAIMSTLLS HPREIPQGLM TKIKHAVVNA NLLAFFCMEF ALTEKRTNVQ VTPTGTVTLN
PSTEHIELWR FMRYQGAHLQ TARDLALSRH SSLRGSIIHG LKHSPSYPWK SLSQLNADKF
FSDIIESILG AIFIDSHGNL AECEKFLERL GLLRYLRRIL KDEVDVMHPR NIAQQMAKGE
IRFEVLRVPN EGGGGGEDDG ATYRCTVKMA GVDGVAVVVE GCLTSEEAEI TAAERAVEIL
VGRGCSL
