ID   DCL1_NEOFI              Reviewed;        1538 AA.
AC   A1DE13;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Dicer-like protein 1;
DE   Includes:
DE     RecName: Full=Endoribonuclease dcl1;
DE              EC=3.1.26.-;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase dcl1;
DE              EC=3.6.4.-;
GN   Name=dcl1; ORFNames=NFIA_075500;
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 / NRRL 181
RC   / 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027696; EAW17620.1; -; Genomic_DNA.
DR   RefSeq; XP_001259517.1; XM_001259516.1.
DR   AlphaFoldDB; A1DE13; -.
DR   SMR; A1DE13; -.
DR   STRING; 36630.CADNFIAP00007382; -.
DR   PRIDE; A1DE13; -.
DR   EnsemblFungi; EAW17620; EAW17620; NFIA_075500.
DR   GeneID; 4586299; -.
DR   KEGG; nfi:NFIA_075500; -.
DR   VEuPathDB; FungiDB:NFIA_075500; -.
DR   eggNOG; KOG0701; Eukaryota.
DR   HOGENOM; CLU_000907_4_3_1; -.
DR   OMA; WQQYMEP; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR006935; Helicase/UvrB_N.
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; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 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; Zinc.
FT   CHAIN           1..1538
FT                   /note="Dicer-like protein 1"
FT                   /id="PRO_0000306782"
FT   DOMAIN          134..315
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          460..619
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          652..742
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT   DOMAIN          1044..1203
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1254..1406
FT                   /note="RNase III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1440..1508
FT                   /note="DRBM"
FT   REGION          39..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           260..263
FT                   /note="DEAH box"
FT   COMPBIAS        43..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         147..154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1392
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1395
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1452
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q09884"
FT   BINDING         1479
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q09884"
FT   BINDING         1520
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q09884"
FT   BINDING         1522
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q09884"
FT   SITE            1388
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1538 AA;  174902 MW;  22BFCACC1932BB46 CRC64;
     MTEQISLVDV SSSVSLKGED SSNVALLRDL FINDVAASDP AESSADVHKD EHSSDNSDND
     NEAVPKPNDF SQRRRIQNAQ FEALLSKRTD ADSNEAIDRA PIALSDDELS IAHLVEKQDL
     GNGMLDPREY QIELFERAKT QNTIAVLDTG SGKTLIAVLL LRHTILNELD NRANGKPHRV
     SFFLVDSVTL AYQQAAVLRN NIDQNVAHFF GAMGTDLWDK RTWDEHLQRN MVIVCTAEIL
     NQCLLNSYVK MDQINLLIFD EAHHAKKDHP YARIIRDSYF KAQPSQRPRV FGMTASPIDT
     KGDITEAATR LETLLDSRIA TTSKITLLRE VVSRPIEKVW AYNRLESPFA TELYKLMDTR
     YGNIKVLEGV YRFAWHASSE LGKWCSDRAW WHALADDVLP KLEGNISKLV ESNTLNAEHG
     AVFKDIIRIR EASETVKNYS FADPELPGEL SPKVQLLRME LSKHFSDTTG TKCIVFTQKR
     YTAKILNELF TVLNIPHLRP GVLIGVRPGD IGGMNVTFRQ QFLALVKFRT GEINCLFATS
     VAEEGLDIPD CNLVVRFDLY RTLIQYVQSR GRARHCTSTY AIMVEKDNAE HEGRLKEIRE
     AEKIMQRFCE TLPEDRILHG NDHDLDSLLQ EEEGRRTFTV KSTGAKLTYH SAIAILARYA
     SSLQYEKETV PQVTYVVGHV SNAYVCEVIL PEKSPIRGLT GSPAIRKAVA KQSAAFDTCL
     LLRKHRLLDD YFNSIYHRRL PAMRNAKLAI TCKRTNEYDM LLKPSIWAKQ RTTPIDKLYG
     IHISLLPSKP LSRDHRPILL LTREKLPEFP AFSIYLDEDV ETKVLSYPLK HGLQISVDEL
     QSLTTFTLRI FRDIFHKVYE HEVQKMPYWL APAKALDGPG SGTNPRDWTD WDTVSFVHNN
     DEIPFTRDLN PDSLVNRFIF DNWDGRFRYF TVAVADTLQP SDPPPPSVPR RRHMNNIMNY
     TLSLSKNSRA RFFSGCDWNQ PVLQAELVRL RRNLLDKMTT QEKEMQTECF ICAEPLRISA
     IPTSIVSTCL AFPAIISRLD SYLIALEACD ELELVIRPDF ALEAFTKDSD NTEEHRGQQI
     HFQRGMGKNY ERLEFLGDCF LKMATSIALY TQNPDDDEFD YHVNRMCLIC NKNLFNTAIK
     KQIYRYIRSR GFSRHIWYPD GLTLLHGKDH SKKLLSEGKH ALGEKTIADV CEALIGASLL
     SGGPENRFDM ATKAVTALVD SPSHRVSCWK EYITLYTMPK YQTEKPRGSE DDLARHVEEE
     LGYHFTYPRL LASAITHPSL PSTWGYRVPC YQRLEFLGDS LLDMVCVEDL FRRFPDRDPQ
     WLTEHKMAMV SNKFLGALSV KLGFHRRIMA FSNPLQAQIT HYVEEIESAQ AESRGAVDYW
     VVAKDPPKCL PDMVEAYLGA IFVDSKFDFQ VIEVFFERQI KPFFEDMSIY DTFANKHPTT
     FLHNKLTNEY GCTNYCLKAG ELPTIDGAPA GVLAAVIVHG NVISEARSSS SRYAKVKASE
     KALAVLDGLL PFEFCQKYHC GCKETQNSSS AVEIGTAI