DCL1_NEUCR
ID DCL1_NEUCR Reviewed; 1584 AA.
AC Q7S8J7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Dicer-like protein 1;
DE Includes:
DE RecName: Full=Endoribonuclease dcl-1;
DE EC=3.1.26.-;
DE Includes:
DE RecName: Full=ATP-dependent helicase dcl-1;
DE EC=3.6.4.-;
GN Name=dcl-1; ORFNames=NCU08270;
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=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 [2]
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 [3]
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 [4]
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}.
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DR EMBL; CM002239; EAA32662.1; -; Genomic_DNA.
DR RefSeq; XP_961898.1; XM_956805.2.
DR AlphaFoldDB; Q7S8J7; -.
DR SMR; Q7S8J7; -.
DR STRING; 5141.EFNCRP00000008415; -.
DR PRIDE; Q7S8J7; -.
DR EnsemblFungi; EAA32662; EAA32662; NCU08270.
DR GeneID; 3878050; -.
DR KEGG; ncr:NCU08270; -.
DR VEuPathDB; FungiDB:NCU08270; -.
DR HOGENOM; CLU_000907_4_3_1; -.
DR InParanoid; Q7S8J7; -.
DR OMA; WQQYMEP; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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: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; 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; 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; 2.
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; Zinc.
FT CHAIN 1..1584
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306783"
FT DOMAIN 129..310
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 448..621
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 654..744
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1052..1207
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1258..1424
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1458..1545
FT /note="DRBM"
FT REGION 31..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 255..258
FT /note="DEAH box"
FT COMPBIAS 33..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1410
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1413
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1470
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1406
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1584 AA; 178589 MW; 3AA23008CF59F81E CRC64;
MAVATRLPFI PPEATSQIIG GDEDLIDLSQ EDVVSDNDDR GNASDVESED GVKRWTVNPE
PKPKKISAKK LADTAAFNSW IEEHQETLAR DQRKAAIEAA RVAGVDVLPA IGFDSERIIT
SPREYQVELF ERAKQQNTIA VLDTGSGKTL IAAMLLRWVI TGELEDREKG LPRRIAFFLV
DKVALVFQQH SFLTKNLDFP MEKLCGEMVE GVESKAFWKE ALEQNEVVVC TAEILSTALH
HSWIRMDQIN LLIFDEAHHT KKDHPYARII KNFYIDEQLE RRPRILGLTA SPVDAKVDPR
RAAAELEALL HSQIATAADP AALQHTICKP KTELVVEYVR GRPDSETVLN KQLRKLVGGQ
ELFKKPLNFT TSAASKLGTW CADRYWQLFF KQEDIVKLES RTERDLMKVA ALDEITEKHV
KQVREAHELV NAHTFSPAAL DPTMLSSKVI MLVRILRDQF ERGVGAQRCI IFVRQRNTAM
LLADLLQQPE IKSHIPSIAA EVLVGGGTTG SSYVNAKINF QQQNRIIRKF KLGEINCLFA
TSVAEEGLDI PDCNIVIRFD LYDTLIQCIQ SRGRARRPDS RYIQMIEKGN YEHHSRILRA
KGAEDVLRKF CEALPEDRKL TGNHMNLDYL LRKEKGKRQY TVPDTGAKLS YMQSLVCLAN
FTATLPHPPE TSLSPEYYIT TVPGGFQCEV VMPDASPIKS AVGKVHLSKG VAKCAAAFEL
CLALLKAGHL DNHLQSVFTK QLPEMRNARL AVSSKKKTEY AMRLKPELWS VRGVVTQLFA
TAFVLENPDT LGRSSRPLLL LSRSALPEVA SFPLFFGTKR FSKVRCVPIP GSVQADDTLV
EQLTRFTLKA FMDVFSKEYE ATAVNLPYFL SPMDGGHGFD FRLAKSPAHL IDRKALAYVS
ENEKVPYTFL EPDDFFQDKF VVDPYDGARK FFTHHRRHDM KPTDPVPDGI VAPNHRAWRG
LGTTHDILNY SNSLWSKSRG FMIFQADQPV VEAALISTRR DFLDDTLRDE DVEPQQCFLI
LEPMRISPIP ADVVAMLLCF PSIIHRVESN LVALDACKLL GLDLRPDLAL EAFTKDSDNS
DEHDAEKENF QTGMGDNYER LEFLGDSFLK MATTIAIYTL IPDKGEFEYH VERMLLICNK
NLFNNALEIG LEEYIRSMSF NRRQWYPEGL ILKKGKSKDA RQRHVLADKS IADVCEALIG
AAYLTGQEKG SFDMAIKAVT AMVKDKKHRM ISYGDYYAVY QKPTWQTESA NSAQRDMAKK
FSERMGYKFK HPRLLRAAFQ HPTYPSLYER LPSYQRLEFL GDALFDMVAV DYLFRKFPAA
DPQWLTEHKM AMVSNQFLCC LSFHLGFNKC IATMSPSILK DIAEYVTEIE EALETAKQEA
INAGKTADEY SRDYWVHITH ASRLPKCLSD VVEAYIGAIF VDSEYDYSVV QNFFNMHVLP
FFEDMHLYDT FANKHPVTFV ANMMAHKFRC NEWRSFAKEL DTDVTEGRGG RGGNGAVAGE
ISEINPPKVV SALLVHGKTV VHAVAASGRY AKSAMAKKAI KLLEGMSVEE FRERLGCNCK
GVPMEVDGGV PEADVDGEVH GTAV
