GenomeNet

Database: UniProt
Entry: A2R345
LinkDB: A2R345
Original site: A2R345 
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   31-JUL-2019, entry version 80.
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.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G.,
RA   Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K.,
RA   Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M.,
RA   Breestraat S., Caddick M.X., Contreras R., Cornell M., Coutinho P.M.,
RA   Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M.,
RA   van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S.,
RA   Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T.,
RA   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.,
RA   van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P.,
RA   van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C.,
RA   Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G.,
RA   Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U.,
RA   Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B.,
RA   Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory
RT   Aspergillus niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Dicer-like endonuclease involved in cleaving double-
CC       stranded RNA in the RNA interference (RNAi) pathway. Produces 21
CC       to 25 bp dsRNAs (siRNAs) which target the selective destruction of
CC       homologous RNAs leading to sequence-specific suppression of gene
CC       expression, called post-transcriptional gene silencing (PTGS).
CC       Part of a broad host defense response against viral infection and
CC       transposons (By 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};
DR   EMBL; AM270320; CAK46537.1; ALT_SEQ; Genomic_DNA.
DR   PaxDb; A2R345; -.
DR   PRIDE; A2R345; -.
DR   EnsemblFungi; CAK46537; CAK46537; An14g03000.
DR   HOGENOM; HOG000048683; -.
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: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   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; PF03368; Dicer_dimer; 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; Complete proteome;
KW   Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat; RNA-binding.
FT   CHAIN         1   1387       Dicer-like protein 2-1.
FT                                /FTId=PRO_0000306787.
FT   DOMAIN       26    205       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      370    535       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      565    659       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      915   1055       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1094   1277       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   NP_BIND      39     46       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       146    149       DEAH box.
FT   METAL      1133   1133       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1263   1263       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1266   1266       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1259   1259       Important for activity. {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
//
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