GenomeNet

Database: UniProt
Entry: A2RAF3
LinkDB: A2RAF3
Original site: A2RAF3 
ID   DCL1_ASPNC              Reviewed;        1525 AA.
AC   A2RAF3;
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 1;
DE   Includes:
DE     RecName: Full=Endoribonuclease dcl1;
DE              EC=3.1.26.-;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase dcl1;
DE              EC=3.6.4.-;
GN   Name=dcl1; ORFNames=An18g02950;
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=CAK48679.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AM270401; CAK48679.1; ALT_SEQ; Genomic_DNA.
DR   PaxDb; A2RAF3; -.
DR   PRIDE; A2RAF3; -.
DR   EnsemblFungi; CAK48679; CAK48679; An18g02950.
DR   HOGENOM; HOG000048448; -.
DR   Proteomes; UP000006706; Chromosome 8L.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR006935; Helicase/UvrB_N.
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; PF03368; Dicer_dimer; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 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; Zinc.
FT   CHAIN         1   1525       Dicer-like protein 1.
FT                                /FTId=PRO_0000306775.
FT   DOMAIN      124    305       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      439    605       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      641    731       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN     1032   1192       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1243   1394       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1428   1496       DRBM.
FT   NP_BIND     137    144       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       250    253       DEAH box.
FT   METAL      1283   1283       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1380   1380       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1383   1383       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1440   1440       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1467   1467       Zinc; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1508   1508       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1510   1510       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   SITE       1376   1376       Important for activity. {ECO:0000250}.
SQ   SEQUENCE   1525 AA;  173497 MW;  1A8FB7B056844A69 CRC64;
     MPSAHAFDMR ITSDIYKPDQ HLPMETMKVC AVTMTEDLQE DDGSSDESDN DEREDHSKTG
     VSQQRITQNA KFKALLAQRA DTGPIHDVSV THDLPDAQLS TAHLVAKQDL GIGTLDPREY
     QLELFERAKV QNTIAVLDTG SGKTLIAVLL LKHTLEKELN DRMEGKPHRI AFFLVDSVTL
     AYQQAAVLRN NLDQSVGHFF GAMGTDLWSK SVWDQHFQKN MVIVCTAEIL NQCLLNSYIK
     MSQINILIFD EAHHTKKDHP YARIIRDSYL EEVYSKRPRI FGMTASPIDT KGDIVDEATR
     LEKLLDSRIA TTSNMSLLRQ VARRPVERVW SFNKLEQPFA TSLYKHLEDR FGDMACLEGI
     FRFAWQASSE LGRWCSDRAW ARALADDVLP KLEGSVRKTA NSETSSNVPE SAYKEILRIT
     EASEIVKSYA FSSPETFGQL SPKVQVLREE LARYFGRQTE TKCIVFTQKR YTALILAELF
     QTLNIPFLRP GVLIGVRSGD LAGMNITFRQ QFISLVKFRT GEINCLFATS VAEEGLDIPD
     CNLVVRFDLY QTLIQYVQSR GRARHFNSTY ASMVERGNLE HEQRLLEVQD AEMMQSFCRT
     LPEDRLLYGF DHDLDTVLQK DEGNRTFRIK STGAKLTYHS ATAILARYAS SLQYEKEFSA
     QVTYVVLPIN GAFVCEVILP EKSPIRGLTG SPAMKKSIAK RSAAFDTCLL LRKNKLLDDH
     FNSIYHRRLP AMRNAKLAIT SKRTSQYDMI SKPSLWGRKQ GMPPKELHGT FITFLPSMQL
     SHEPAPLLLF TRERLPHFPE FPIFLDDDVE TTIITTPLEK QLLLSEKEVD ALTVFTLRVF
     RDVFHKTYDK EPEKMAYWLA PAKVQSSYLP SYDPRQILDW ESLTYVRDND SIPFSTNADP
     ESWVDLFVFD AWDGRCRFFT VGVEHSLTPS SPPPPFVARR RHMNDVMNYC LSLSKNSRAK
     FLSTCHWDQP VLRAELVRLR RNLLDKMTDT ERDVETRCFI CIEPLKVSAI PASTAFSCLA
     FPAIISRIDA YLISLQGCES LNFTVKLDLA LEAFTKDSDN TDEHRAQQIH VQRGMGRNYE
     RLEFLGDCFL KMATSIALFT QNPDDDEFDY HVNRMCLICN KNLFNAAVDK EIYKYIRSRG
     FSRHTWYPEG LKLLQGKDHS RKATTESKHA LAEKTIADVC EALIGAALLS GGPDHRFDMA
     VKAVTTLVNS PSHKAERWKD YISFYTIPKY QRRAADGAEL YLSRKIEEKL SYRFRYPTLL
     GSAFTHPSYP SAWAKVPCYQ RLEFLGDSLI DMVCVEDLFA RFPDRDPQWL TEHKMAMVSN
     KFLGALAVKL GLHTHLKYFS APLQSQITQY AEEIQTAEGE SEGAVDYWTV TKDPPKCLPD
     MVEAYVGAVF VDSDFNFEVI ERFFRDYIKP FFEDMAIYDT FANKHPTTFL HNRLTNEFGC
     VNYCLKAGEM PSIDGAPAGV LAAVIVHDVV IAEGTATSGR YAKVKASEKA LAVLDEISSA
     EFQRKFRCDC RESGDSARLD IGTAI
//
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