ID   DCL22_ASPNC             Reviewed;        1362 AA.
AC   A2QX45;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Dicer-like protein 2-2;
DE   Includes:
DE     RecName: Full=Endoribonuclease dcl2-2;
DE              EC=3.1.26.-;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase dcl2-2;
DE              EC=3.6.4.-;
GN   Name=dcl2-2; ORFNames=An11g07590;
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00657}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK40801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM270243; CAK40801.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001394728.2; XM_001394691.2.
DR   AlphaFoldDB; A2QX45; -.
DR   SMR; A2QX45; -.
DR   EnsemblFungi; CAK40801; CAK40801; An11g07590.
DR   GeneID; 4984978; -.
DR   Proteomes; UP000006706; Chromosome 7R.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; 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; PS50142; RNASE_3_2; 2.
PE   3: Inferred from homology;
KW   Antiviral defense; Antiviral protein; ATP-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..1362
FT                   /note="Dicer-like protein 2-2"
FT                   /id="PRO_0000306788"
FT   DOMAIN          30..197
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          343..505
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          536..630
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT   DOMAIN          889..1033
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1075..1258
FT                   /note="RNase III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   MOTIF           139..142
FT                   /note="DEAH box"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1362 AA;  153885 MW;  D233E94793C21EB3 CRC64;
     MTSSTDYHAD STPGTTSNME LRIREYQLEM LNESLKRNLI VVMPTGTGKT QVAILRILAD
     IDKGNSDKFV WLLCPTVALS EQQYIQYATV FLPSGAEDKA IWDNALSGIK IAVSTYQVLY
     DALSHGFVKL SQMSLLIFDE AHHCKKDHVA NKIMQVHYHK QHQSGVQNLP KILGLTASPI
     LSDLSSLEIV ESNLGSICKT PRQYYAQLLQ FTNRPLILPR LPTYTIPNCS VKAPILEKLC
     GILSSEDEVP SSSKMKSKQL KHIRRFMQTS ESINQELGIW AATEYMRKSI MHFKESMRMG
     AEKTNISNYG KDFAMEILTR LGKLQDCSPA IQPEEISPMC QCLLDELSKA YREGFCGLVF
     VTQRATVLAL KWLIENHPLT SHLFTCGTFI GMSTTQYSKT ELGNLHDIRN QTETLEKFRQ
     GSLNLIITTD ALEEGIDVPA CNTVLNFNCQ LSLKSFIQRR GRARRENSQF IIIMEDESGP
     RYLKRLEMEE IELVQKLQNA ERRQIPANEL DFDKYERISL SLDIDRTGAQ LIMREAVGYL
     YNFCSKLPAQ LYVSNKPLFT YERNNYGRFR AVVKLPSNLD PSLQSFSSSR SWSRLKYARE
     DAALQAYKAL YQAGLVNDYL VPTQVSDHLE GDIIFRSHYS IQNQLDPWQD IALLWKLDSQ
     LYAHNLRIIR PEEDEIHLHM ILPTQLDTTI HIPLFIDYCT TYTAILTPGH PITTDISLCQ
     QVTNLIFQSV YRDHCSRRNL DYAFLLVPEL EETKLIEFLE RYSGSVSLTE LLNQEATPSA
     LGLLRSHTRP SRPLLVEPWV AGECFLPDEL SISSFDAKVK YMTNRRNFLS HGNLAAGKST
     NCEARIGLEA NVKSMSVRDF FVDKLPSMFA QVALFTPSIS HEVEVYMIAQ ILRQELSLRS
     VTPWQRIDLL AIAIRPTSIE HRATFRLLAF IGDAFMKYLF AMQLFLHHHL WHEGLLSSLK
     QRNLSDAGLA HAIHQSGLGK FLISKHLNGK RWVPPLVSGI EPASNEARQR SIGAATLADM
     TKAVVGAAFT DGGLNQAAAC ASVMFPKLKS WNASSLHDGT YSKTRPENAV ASTAIVDMEE
     LLGYTFTDKS LAVESMTHPS CTGLVQTTSY RRLSFLGASV LEWIVVSYLH RHAQVMNPQR
     MQSLKSAFTN NTFLTFIAIT FHQVREQNHI DVDDEHNVHK NVTTCSIRLW DFLRLHSDAL
     STELSDFVQK SSEKADAIKH ELWEQRFYPW VRLRALGDMR VLSDIIQSIF GAVFIDSQAT
     LASCDALAEK LGIVPLLEHF ISHQITTDHP KDTLQAILPG RKVSYQICVD KVHPGTLRCS
     ALADSSEIAS VEGQMNDEVI KMQAAETAVR LLRKGFALSE TS
//