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   24-JAN-2024, entry version 95.
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 A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
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., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., 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-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; DS027693; EAW20627.1; -; Genomic_DNA.
DR   RefSeq; XP_001262524.1; XM_001262523.1.
DR   AlphaFoldDB; A1D9Z6; -.
DR   SMR; A1D9Z6; -.
DR   STRING; 331117.A1D9Z6; -.
DR   EnsemblFungi; EAW20627; EAW20627; NFIA_030600.
DR   GeneID; 4589127; -.
DR   KEGG; nfi:NFIA_030600; -.
DR   VEuPathDB; FungiDB:NFIA_030600; -.
DR   eggNOG; KOG0701; Eukaryota.
DR   HOGENOM; CLU_000907_4_6_1; -.
DR   OMA; CCVNLIR; -.
DR   OrthoDB; 342391at2759; -.
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; cd18034; DEXHc_dicer; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   CDD; cd18802; SF2_C_dicer; 1.
DR   Gene3D; 3.30.160.380; Dicer dimerisation domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 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   PANTHER; PTHR14950; DICER-RELATED; 1.
DR   PANTHER; PTHR14950:SF37; ENDORIBONUCLEASE DICER; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 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..1388
FT                   /note="Dicer-like protein 2"
FT                   /id="PRO_0000306795"
FT   DOMAIN          23..203
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          371..537
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          564..658
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT   DOMAIN          919..1059
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1098..1281
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         1137
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            1263
FT                   /note="Important for activity"
FT                   /evidence="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
//