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Database: UniProt
Entry: Q2UNX5
LinkDB: Q2UNX5
Original site: Q2UNX5 
ID   DCL2_ASPOR              Reviewed;        1377 AA.
AC   Q2UNX5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-OCT-2019, entry version 89.
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=AO090001000193;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007154; BAE56740.1; -; Genomic_DNA.
DR   RefSeq; XP_001818742.1; XM_001818690.1.
DR   SMR; Q2UNX5; -.
DR   PRIDE; Q2UNX5; -.
DR   EnsemblFungi; BAE56740; BAE56740; AO090001000193.
DR   GeneID; 5990713; -.
DR   KEGG; aor:AO090001000193; -.
DR   HOGENOM; HOG000048683; -.
DR   OMA; PTVALCE; -.
DR   Proteomes; UP000006564; Chromosome 2.
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   1377       Dicer-like protein 2.
FT                                /FTId=PRO_0000306789.
FT   DOMAIN       23    203       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      368    531       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      561    655       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      914   1052       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1092   1275       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      1131   1131       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1261   1261       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1264   1264       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1257   1257       Important for activity. {ECO:0000250}.
SQ   SEQUENCE   1377 AA;  155787 MW;  2C2DB98A99F36658 CRC64;
     MAQLNGSNGT GLLYKPRQYQ YEMFEASLKE NIIVAMDTGT GKTQIALLRI AHQLEGGGPR
     KLTWFLTPTV ALCLQQYEVI RSHLPAVRAC TITGLDKVER WKSQYIWDEL LKDKQVVVST
     HAVLFEALTH GFVRISQLGL LIFDEAHHCM RRHPANMIML DFYHPTLRKH GRDSVPCILG
     LTASPVVRSK SQEMKTLESN LDSICKTPQV HKQELTTYAH RPELLPIICK AIDEGPGGRA
     LQALEHAWDT ADIDGDPDAI PQNGSLLNGS GEYKALMVRK TLCNEQIKRF VDRSRHIFAE
     LGEWAADYYI CTSVEQLRTT IRDQSLTMDW EDEERAYLSN FLSKLPVAEV QANLADPNNF
     TMSPKLAALI NFLDKFDDPE FSGLIFVKQR VTVSVLARLL SLHPQTRDRF RCAAYVGMSV
     GSCRQDMVGD WHNAKKQRGT MDDFRSGRKN LIVTTSVLEE GIDVTACRVV VCFDKPANLK
     SFIQRRGRAR QQKSTYAIMF STADEHGDLR RWQILEQAMV EAYQDEERRL REAEAQEAVD
     ENVPEMITVE ATGAVITPDS VVTHLYHFCA VLPEERYVDN RPEFSFEKDR QGLIKGTVIL
     PSCVHPKVRR IQGKLWWKSE RAAVKETAFQ AYRALYEFGL LNDHLLPLTK NPEMRPTDHT
     TLPSLLDVSE QYDPWTDWAN SWSCPDVHQM RIALESNGHP ADGLIMKLIG PTNLPPLAPI
     TLFWDRDTRL TLSFDVPERI TTVTDNCIAN MRTVTALYIQ APRSRNLLNN DDFVTLFGPD
     LPSTELADWL LRNAGYETAH EAYSRGTMPG AMGIIRDLSR YDEPFFCHRW IESETGLIEI
     ECRPIPRRRN FLHPPALDNG QADAIVESEH GSAKVHMVAA ESCTVDKLPV STAIFGLFIP
     HIVDRLESTL IANRLCATIL CDVGFADIQH VITAIMAPSA QGVTNYQRYE FLGDSILKYI
     VSCQLFFQNL NWPEGFLTEG RTTIVQNPRL TRAALDAGLD SFIITKALTP RRWIAPLIST
     RVGAAPVKRQ MSAKVLADVI EALIGAAYLD GGHSKAQICT HCFLPEVNRQ PLDIPSLITQ
     TEHGRTARHI IDGDLQRHLG YTFKNEDLLI EALTHPSCQH DQTTQSYQRL EFLGDAILDM
     VIVPIIFQYS NKISPGDMTL IKHAVVNANL LGFFCMEFSI EQDKTKVEKT PDGRFAVKSE
     TQHVELWRFM RFNSLDLQTS RDAALDRHRR LRNKILTSLY HGPSYPWQSL SQLYADKFFS
     DIVESVLGAI YVDSGGDLSA CERFLEQIGL LSYVRRVLLD GINVTHPRNI AQRLSKGDAL
     FNLRRVSDEK GRSMYRCTVT MNDAQIVLVE GCQCGEEAEV RAANETIEFL QRRQEVV
//
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