DCL2_ASPOR
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 03-AUG-2022, entry version 99.
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;
OC Aspergillus subgen. Circumdati.
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., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA 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-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}.
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DR EMBL; AP007154; BAE56740.1; -; Genomic_DNA.
DR RefSeq; XP_001818742.1; XM_001818690.1.
DR AlphaFoldDB; Q2UNX5; -.
DR SMR; Q2UNX5; -.
DR STRING; 510516.Q2UNX5; -.
DR PRIDE; Q2UNX5; -.
DR EnsemblFungi; BAE56740; BAE56740; AO090001000193.
DR GeneID; 5990713; -.
DR KEGG; aor:AO090001000193; -.
DR VEuPathDB; FungiDB:AO090001000193; -.
DR HOGENOM; CLU_000907_4_6_1; -.
DR OMA; HFCAVIP; -.
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: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..1377
FT /note="Dicer-like protein 2"
FT /id="PRO_0000306789"
FT DOMAIN 23..203
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 368..531
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 561..655
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 914..1052
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1092..1275
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT MOTIF 144..147
FT /note="DEAH box"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 1257
FT /note="Important for activity"
FT /evidence="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
