ID   DCL2_ASPTN              Reviewed;        1377 AA.
AC   Q0CEI2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 78.
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=ATEG_07902;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU32164.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH476604; EAU32164.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001216523.1; XM_001216523.1.
DR   AlphaFoldDB; Q0CEI2; -.
DR   STRING; 341663.Q0CEI2; -.
DR   PRIDE; Q0CEI2; -.
DR   GeneID; 4322847; -.
DR   eggNOG; KOG0701; Eukaryota.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000007963; 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: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_0000306790"
FT   DOMAIN          23..203
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          367..544
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          563..657
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT   DOMAIN          916..1056
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1090..1274
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         1129
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1260
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            1256
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1377 AA;  155084 MW;  2ED8ACB6EEC6588D CRC64;
     MASLSDQDLE MGLFCPRNYQ TEMFEASLQE NIIVAMDTGS GKTHVALLRI MNELETRRPQ
     KLIWFLAPTV ALCFQQHDVI TKNLPAVKSR TLTGQDKVEL WTEQAIWDAI LKDMQVVVST
     HAVLADAMSN GFVRVSQLGL LIFDEAHHCM RRHPANRIMQ DFYHPTLVKQ GPDAVPGILG
     LTASPVVRTN SQELSMIESN MNAICKTPRA HRQELLTHTH RPHLQQIWYT PVNIDDPTSG
     TRTLRALIHA WETIDLEDDP YVKQLRRSTF DGKALQKALL TRKTYCNESL RRFVERSCHI
     FQELGGWAVD YFIHASIRRL REKIDDSALM LDWDNEEKEY LASFLSNIAT IQSDPPRRPE
     DFIPSPKLEA LISFLSSTDD STFSGLIFAK QRATVTVLAT LLSVHPLTKD RFRCAAFVGW
     SGGGNRKDLI GELLSMQMQR DTLSEFRSGQ KNLIVATDVL EEGIDISACS VVICYDKPAN
     VKSFVQRRGR ARRKESTFAI LFSTDDELCD LRKWQLLEEA MIEAYQDDER KRCEALALET
     MAEVVTERFE VESTGAVLTA DTAVARLHHF CSILPQQPYV DNRPELSFEY DGTGRRRGTF
     KLPSCVHPDV RRTRGEKWWT TERAATKEAA FQTCKRLYEF GLLNDHLLPL TRKPELRLTD
     FGGLPSIIEV AEQYDPWTDW AYSWSSPDIH QSRIRVQLNG NPEYQLSMSL MGPTVLPALD
     AMTLFWDSQN IFTLAFDAAQ RVPLVPGDVI EHMRAITALY LQAPSSRSIR EERDYVALFG
     PDLPHTELGA WLLKNGGNDT ALDVYSRQVA SPTMGIVRDR TRYDEPLLFK KWVVTEDGDV
     AVVEMECHSL PKRRNLLQRQ TLAQGEIVTT AVDTAPAKAR IIPATACTID RLPFTDTIFG
     LFISAILDRL EATLIATRLC ETILQDVQFS STRHVITAIS APTAQSPTDY QRYEFFGDSV
     LKFTVSCQLY MQHPNWPEGY LSEGRDEIVQ NNRLARAALD VGLDAFILTR RFTPRKWTAP
     LISEKAVEVA GKRPLSSKVL ADVVESLIGA AYMDGGQAKA HTCIRRLLPE IEICPITPPP
     VHESAPHVMN DSLKQHLGYT FVNEALLVEA LTHPSCRSDA STQSYQRLEF LGDAVLDMVV
     VHAMAHHAVE CPQGEMTMIK HALTNANLLA FFCMEFVVAQ EHTDVDAVPA AGGFALRSEQ
     KPIELWRFMR SEALDLNNAR ETVLHRHSQL RAEIVHALHH GAQYPWQALS QLNADKFFSD
     IVESILGAIF VDSRGDLDVC AMFVERIGLL PYLRRILADR VDVMHPRHTA QRLSKGEALF
     TAKRVVDGSG NASYRCVVKR NKEEIVVVEG CLSSEEAEVK AANATIGILR ANAVNLV