ID   DCL2_NEUCR              Reviewed;        1534 AA.
AC   Q7SCC1; Q8X079;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 4.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Dicer-like protein 2;
DE   Includes:
DE     RecName: Full=Endoribonuclease dcl-2;
DE              EC=3.1.26.-;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase dcl-2;
DE              EC=3.6.4.-;
GN   Name=dcl-2; ORFNames=B14D6.490, NCU06766;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=14993290; DOI=10.1128/mcb.24.6.2536-2545.2004;
RA   Catalanotto C., Pallotta M., ReFalo P., Sachs M.S., Vayssie L., Macino G.,
RA   Cogoni C.;
RT   "Redundancy of the two dicer genes in transgene-induced posttranscriptional
RT   gene silencing in Neurospora crassa.";
RL   Mol. Cell. Biol. 24:2536-2545(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=15767281; DOI=10.1093/nar/gki300;
RA   Nolan T., Braccini L., Azzalin G., De Toni A., Macino G., Cogoni C.;
RT   "The post-transcriptional gene silencing machinery functions independently
RT   of DNA methylation to repress a LINE1-like retrotransposon in Neurospora
RT   crassa.";
RL   Nucleic Acids Res. 33:1564-1573(2005).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=17371837; DOI=10.1128/mcb.00186-07;
RA   Choudhary S., Lee H.-C., Maiti M., He Q., Cheng P., Liu Q., Liu Y.;
RT   "A double-stranded-RNA response program important for RNA interference
RT   efficiency.";
RL   Mol. Cell. Biol. 27:3995-4005(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. Controls the
CC       expression of the non-LTR retrotransposon Tad in the African strain,
CC       Adiomopoume. {ECO:0000269|PubMed:14993290, ECO:0000269|PubMed:15767281,
CC       ECO:0000269|PubMed:17371837}.
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   -!- INDUCTION: By double-stranded RNA (dsRNA).
CC       {ECO:0000269|PubMed:17371837}.
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00657}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB91758.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA34302.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL356173; CAB91758.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002237; EAA34302.3; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_963538.3; XM_958445.3.
DR   AlphaFoldDB; Q7SCC1; -.
DR   SMR; Q7SCC1; -.
DR   STRING; 5141.EFNCRP00000006887; -.
DR   EnsemblFungi; EAA34302; EAA34302; NCU06766.
DR   GeneID; 3879662; -.
DR   KEGG; ncr:NCU06766; -.
DR   HOGENOM; CLU_000907_4_6_1; -.
DR   InParanoid; Q7SCC1; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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; IPR014720; dsRBD_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; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51327; DICER_DSRBF; 1.
DR   PROSITE; PS50137; DS_RBD; 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   2: Evidence at transcript level;
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..1534
FT                   /note="Dicer-like protein 2"
FT                   /id="PRO_0000306796"
FT   DOMAIN          65..249
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          404..575
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          597..700
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT   DOMAIN          959..1107
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1153..1353
FT                   /note="RNase III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1383..1483
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1492..1534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           192..195
FT                   /note="DEAH box"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1513..1527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1342
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            1335
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1534 AA;  172132 MW;  A5643F181EDA9FED CRC64;
     MDQDPRKDNP VEMDVDRDDS SQDPDDNESF KSALDEPLDL KELYQDALEK PSEEPSEELN
     DQVSTPAALT ARAYQLEMFE ASLKQNIIVA LFSDRVMVAD GHWQWQDSGR IWFLTPTVAL
     ARQQHRVLQS QIPSVKAIML CGQDGVDSWS EQAVWDAVLL NVRIVVSTYQ ILFDANAHSF
     VRLDSLSLIV IDEAHNCSGS HPIARLMTEA YLPAKKAGLP VPSILGLTAS PLKSNNLADI
     EKLEQVLDAV CRTPTIHREE LLAHVNRPEM LVVSYGDSGT DPTPTDLMTR FLEAYHRLDI
     SKDPDVLLLK AQRTERAREK LRQMITKKDT LAQKELRGVY NRALLVRREI GPWAADYYLT
     RTVSHMLAEL ERGEPPAQHR YIGEALRSIP IPAISKEPIQ LSPKVQTLLK VLASHQQDPV
     GIVFVKERVM VSIVTHIIST HPLTKDRYRT ASMIGTASVP GKARNHMDMT KKEDMTSLEG
     FRLGRFNLLV ATSVLEEGID VPICNLVICF DEPSNIKSFI QRRGRAREVS STLYLMVQNA
     SSESATDWHN LERLMKERYE DEMRQNAELE LLDDPRIGSY PVLEVESTGA RMTIRDARSH
     LNHFCAKVSS RSRYLQKEPY FVIRQVNPDP ASPGRRTLLQ ATVHLPASLA PDLRRHESLW
     TWTSEKLAIM DASFQAYKAL YNAGLVNENL LPTKVSDFLA DLGDDPGHIW VKTQFDPWPE
     VAYAWQESSS LYSRRLTVLV PGVENPLEFE FILPVPVPYM APLKLWWNAT SALTLITSPE
     MQEFRKQEGT SAGPDHSYAL LAMAFAHRFP IQGRQYPIRL VSTRRKLDVD GIAALEFDPR
     LYESSPQPPL VRLVDGRNMP YFVTKILPSK PPVELISKPS TDHADLPENV PYVVCKPIGK
     AVGQFIPLDA AQDQDSWTPK NGKLYRKVLP STQIRMDNFP AVFAQVGAVI PAFTRAVEMS
     LVAADLMYNR LGCLQLDNLP LITTALISSG SRGPTNYERL EFIGDTILKF CACLTASALF
     PNHHERLLSQ WKDKLVNNVR LCRASRDFGL DEYIINSAAS KKWRPKFVED YMDEMKSPIS
     AETRQMSSKM VADVVESLIG AAYMCGGMSK ALECVALLLP TPKSSQFKWQ EIELSRTQLF
     EFAPKDAILS KQLEPLEKAM DYTFNKKSLL IEAMTHPSCA GLGTNESCYE RLEFLGDAIL
     DVIVVKRLMA ETGPNELAHN DMHEHLSSVV TADIMAFLAM EWVIMQTDIN EIDPTNLDAL
     GLLPSSQSRI TPASLVSNKE DWPFWRFMRH NSPQVGATQT ATIERYLTLR DEIRDAIWKH
     NTLPWALLAR MGPQKFYSDI VESLIGAVWV DSGSWKACED VLTQMGLLPL LDHLLETKAH
     VMHPNVELQI LAPPNKRATR TEFVIISNKR GIISSGTEFL DEPSAVDDGL VSVEPYDDTP
     EHDEVFSCKL FVGGKQVADV TGAATKEEAR VRAAEKGCLV IKAERKVWNE AKAAAKEDKG
     HNTENGDANA DNGQSGEKEE VPDCRDADGD TVMN