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Database: UniProt
Entry: A1D9Z6
LinkDB: A1D9Z6
Original site: A1D9Z6 
ID   DCL2_NEOFI              Reviewed;        1388 AA.
AC   A1D9Z6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-OCT-2019, entry version 80.
DE   RecName: Full=Dicer-like protein 2;
DE   Includes:
DE     RecName: Full=Endoribonuclease dcl2;
DE              EC=3.1.26.-;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase dcl2;
DE              EC=3.6.4.-;
GN   Name=dcl2; ORFNames=NFIA_030600;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC
OS   A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
DR   EMBL; DS027693; EAW20627.1; -; Genomic_DNA.
DR   RefSeq; XP_001262524.1; XM_001262523.1.
DR   STRING; 36630.CADNFIAP00002683; -.
DR   EnsemblFungi; EAW20627; EAW20627; NFIA_030600.
DR   GeneID; 4589127; -.
DR   KEGG; nfi:NFIA_030600; -.
DR   EuPathDB; FungiDB:NFIA_030600; -.
DR   HOGENOM; HOG000048683; -.
DR   OMA; PTVALCE; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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   1388       Dicer-like protein 2.
FT                                /FTId=PRO_0000306795.
FT   DOMAIN       23    203       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      371    537       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      564    658       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      919   1059       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1098   1281       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   NP_BIND      36     43       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       144    147       DEAH box.
FT   METAL      1137   1137       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1267   1267       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1270   1270       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1263   1263       Important for activity. {ECO:0000250}.
SQ   SEQUENCE   1388 AA;  156430 MW;  C30E206A2EB2D3DB CRC64;
     MASSVTACQG ASPYQPRNYQ LEMLEASMKE NIIVAMDTGS GKTHIAVLRI KAELDICPPD
     KLVWFLAPTV ALCIQQHEVI ASNLPAVRTR TLTGLDKVEL WTEQSIWDAV LNGYRVIVST
     HAVLADALSH GFVKMSRLAL LIFDEAHHCT RRHAANKIMR DFYHPTLTKS GPGAVPRIMG
     LTASPVVRSN HQELLTVESN LDAVCRTPRV HRQELVKFTH RPHLQQIWYT PTDPAGFKSA
     SQTLGALYHA WETLDIGDDP YIQRLRKSPL DDTALKKALL TGKTYCREQL RRFVDRSRHI
     FEELGEWAAE YYIYASIKQL GDRVRNSYMS GDWDEAEKAY LVDFLSKIPA SEIQLALNDP
     GSFRISPKFE SLLNFLDSLD EREFSGLIFV KQRATVSAMT SLLSVHPCTR ERFRCAAYVG
     WSNGSASKDI LGDLLNMQLQ RDTLDDFRSG RKNLIIATDV LEEGIDISAC SVVVCYDKPP
     NLKSFVQRRG RARRKQSTFA IMFPTDDASA DVSKWQDLEQ AMIEAYQDDE RQLQSVSALE
     SLDEEVMERL TVESTSAVLT ADMAMAHLHH FCAVLPPQPY ADMRPVFSFE TNEDGLLKGT
     VILPSCVHPK VRRTEGRRWW RTERAAMKET AFQAYKALYE FGLVNDHLLP LTKRPELKSH
     DLGAMPSILE TSEQYDPWIE WAYSWSSPDI HQSRIVVRMN EGRGDELCMR LMGPTYLPPL
     SPMTLFWNNS TTFTVTFEAA ERVPLVPLSS VEDMRAITAL YLKATNSRVC SSERDFTALF
     APDLHHTELK GWLNAYEGCD PAMEVYSRGH NPLLMGVVRD HSRYGEPFLF RKWLVSDQNP
     SCSVVELECA PFPHRRNLLH RQRLANSQVD VDEETPESAA KNPIVAADAC TIDRLPFTMA
     IFGLFISAIV ERLETELIAT RLRETILRDV GFKSTDHIIT AISTPFAHAL TNYQRYEFLG
     DSILKFSVSC QLFFQHPNWH EGYLSEGRAM IVQNPRLAKA ALDTGLDAYI VTKRIASRKW
     SAPLISEKLE RVPAKRQMST KVLADVVEAL IGAAYMDGGH ATAQACIRRL LPEINLHAVD
     TRTATRSVAP ESARHMMNER LKDHIGYTFE DESLLVEALT HPSCDYDSTT QSYQRLEYLG
     DAVLDMVIVS AIFNHPIQRP QGDMTKIKHA VVNANLLAFL CMESATSEEK LDVAQTSKDS
     FAVTTSQESV ELWRFMRYRG QNLNAARDAS LARHRALRDE IASSLLHAPH YPWHALSRLN
     ADKFFSDIVE SVLGAIFVDS GGDLAPCEVF VERIGLMAYL RRILDQEIDV RHPRSVAQQL
     AKTNIQFVLQ RVPNEEGGAS YQCSVRIEQA ELFVVTGCLT AEEAEVTAAV EAIKFLTRDE
     GSTPLNTS
//
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