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Database: UniProt
Entry: Q7S8J7
LinkDB: Q7S8J7
Original site: Q7S8J7 
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   18-SEP-2019, entry version 115.
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
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   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.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   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.,
RA   Paulsen I., 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.,
RA   Macino G., Cogoni C.;
RT   "Redundancy of the two dicer genes in transgene-induced
RT   posttranscriptional 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
RT   independently of DNA methylation to repress a LINE1-like
RT   retrotransposon in Neurospora 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-
CC       stranded RNA in the RNA interference (RNAi) pathway. Produces 21
CC       to 25 bp dsRNAs (siRNAs) which target the selective destruction of
CC       homologous RNAs leading to sequence-specific suppression of gene
CC       expression, called post-transcriptional gene silencing (PTGS).
CC       Part of a broad host defense response against viral infection and
CC       transposons. Controls the expression of the non-LTR
CC       retrotransposon Tad in the African strain, Adiomopoume.
CC       {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}.
DR   EMBL; CM002239; EAA32662.1; -; Genomic_DNA.
DR   RefSeq; XP_961898.1; XM_956805.2.
DR   EnsemblFungi; EAA32662; EAA32662; NCU08270.
DR   GeneID; 3878050; -.
DR   KEGG; ncr:NCU08270; -.
DR   EuPathDB; FungiDB:NCU08270; -.
DR   HOGENOM; HOG000048448; -.
DR   InParanoid; Q7S8J7; -.
DR   KO; K11592; -.
DR   OMA; FNMYVQT; -.
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; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; IBA:GO_Central.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 2.
DR   Gene3D; 3.30.160.380; -; 1.
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; PF03368; Dicer_dimer; 1.
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; Complete proteome;
KW   Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat; RNA-binding; Zinc.
FT   CHAIN         1   1584       Dicer-like protein 1.
FT                                /FTId=PRO_0000306783.
FT   DOMAIN      129    310       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      448    621       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      654    744       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN     1052   1207       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1258   1424       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1458   1545       DRBM.
FT   NP_BIND     142    149       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       255    258       DEAH box.
FT   METAL      1298   1298       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1410   1410       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1413   1413       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1470   1470       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1516   1516       Zinc; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1557   1557       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1559   1559       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   SITE       1406   1406       Important for activity. {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
//
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