ID   DCL2_ASPFU              Reviewed;        1388 AA.
AC   Q4WA22;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
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=AFUA_4G02930;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL84441.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAHF01000016; EAL84441.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_746479.1; XM_741386.1.
DR   AlphaFoldDB; Q4WA22; -.
DR   SMR; Q4WA22; -.
DR   STRING; 746128.CADAFUBP00009739; -.
DR   GeneID; 3503874; -.
DR   KEGG; afm:AFUA_4G02930; -.
DR   eggNOG; KOG0701; Eukaryota.
DR   HOGENOM; CLU_000907_4_6_1; -.
DR   InParanoid; Q4WA22; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016442; C:RISC complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
DR   GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
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..1388
FT                   /note="Dicer-like protein 2"
FT                   /id="PRO_0000306786"
FT   DOMAIN          23..203
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          368..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          906..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;  156878 MW;  1710B5AFB4B420A3 CRC64;
     MASTVSTCQD ASPYQPRNYQ LEMLEASMKE NIIVAMDTGS GKTHIAVLRI KAELDICSPD
     KVVWFLAPTV ALCIQQHEVI ASNLPAVRTR TLTGLDKVEL WTDQSIWDAV LNGYRVIVST
     HAVLADALSH GFVKMSQLAL LIFDEAHHCT RRHAANKIMQ DFYHPTLTKS GPAAVPRIMG
     LTASPVVRSN HQELLMVESN LDAVCRTPRL HRQELLKFTH RPHLQQIWYT PTDPAGFRSA
     SLTLGALYHA WENLDIGDDP YIQRLRKSPL DDRALKKALL TGKTYCREQL RRFVDRSRHI
     FEELGEWAAE YYIYASIKQL RDRVRDSYMS GDWDEAEKAY LVDFLSKIPT SDIHFALNDP
     DGFRISPKFE SLLNFLDSSD QREFSGLIFV KQRVTVSAMT SLLSVHPYTR ERFRCAAYVG
     WSNSSASKDI LGDLLNMQLQ RDTLDDFRSG RKNLIIATDV LEEGIDLSAC SVVVCYDKPP
     NLKSFIQRRG RARRKQSTFA IMFPTDDTSA DVSRWQDLEQ AMIEAYQDDE RQLQSVSALE
     SLDEEVMERL TGDSTSAVLT ADMAMAHLHH FCAVLPPQPY VDMRPVFSFE TNEDGLLKGT
     VILPSCVHPK VRRTEGRRWW RTERAAMKET AFQAYKSLYE FGLVNDHLLP LTKKPELKTH
     DLGSMPSILE TSEQYDPWIE WAYSWSSPDI HQSRIVVKMN EGRGDELCMR LIGPEYLPPL
     SPMTLFWNSS TTFTVTFKAA ERVPLVPLSS VEDMRAITAL YLKATSSRVC SAERDFMALF
     APDLHHTELK GWLDTYEGSD PAMEVYSRGH NPLLMGVVRD HSRYGEPFLF RKWLVSHQNP
     SCSIVELECA PFPHRRNFLR RQTLANSQVD VDEAIPDSAA KNPIVAAEAC TIDRLPFTMA
     IFGLFISAIV EQLEIELIAT RLRDTILRDV SFKSTDHIIT AISTPLAHRL TNYQRYEFLG
     DSILKFSVSC QLFFQHPNWH EGYLSEGRDM IVQNPRLAKA ALDTGLDAYI VTKRLASRKW
     SAPLISEKLG RVPAKRQMST KVLADVVEAL IGAAYVDGGH STAQACIRRF LPEINLHAVD
     TRTAARSVAP ESARHMMNDR LKDHIGYTFE DESLLVEALT HPSCDYDSTT QSYQRLEYLG
     DAVLDMVIVS AIFNHRIQRP QGDMTKIKHA VVNANLLAFL CMEFAISEEK LDVAQTSKDS
     FAVTSSQESV ELWRFMRYRG QGLKAARDAS LARHRALRDE IASSLLQAPH YPWHALSRLN
     ADKFFSDIIE SVLGAIFVDS GGNLAPCEVF VEQIGLMAYL RRILDHGIDV RHPRSVVQQL
     AKTNIQFVLQ RVPTEEGGAS YQCSVQMEQA ELFVVTGCLT AEEAEVTAAV EAIKFLTRDE
     GSTPLNKS