GenomeNet

Database: UniProt
Entry: Q0UI93
LinkDB: Q0UI93
Original site: Q0UI93 
ID   DCL1_PHANO              Reviewed;        1522 AA.
AC   Q0UI93;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   31-JUL-2019, entry version 78.
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=SNOG_08521;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173)
OS   (Glume blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Phaeosphaeriaceae; Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing
RT   and EST analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(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 (By 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   -!- SEQUENCE CAUTION:
CC       Sequence=EAT83689.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; CH445337; EAT83689.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001798832.1; XM_001798780.1.
DR   PRIDE; Q0UI93; -.
DR   GeneID; 5975731; -.
DR   KEGG; pno:SNOG_08521; -.
DR   InParanoid; Q0UI93; -.
DR   KO; K11592; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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; 1.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   3: Inferred from homology;
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   1522       Dicer-like protein 1.
FT                                /FTId=PRO_0000306784.
FT   DOMAIN       76    258       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      408    576       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      600    700       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      995   1166       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1222   1373       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1409   1478       DRBM.
FT   NP_BIND      89     96       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       202    205       DEAH box.
FT   METAL      1262   1262       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1359   1359       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1362   1362       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1421   1421       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1449   1449       Zinc; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1490   1490       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1492   1492       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   SITE       1355   1355       Important for activity. {ECO:0000250}.
SQ   SEQUENCE   1522 AA;  175115 MW;  BE255EF8D0BB8DDD CRC64;
     MTWAGDVEEQ DDYFSCSDVS TSGDRRKRAP QTVTQEEVDQ ATSKIANEGQ LSIRDILASQ
     DTAVRITNPR DYQMELFLRA KMQNTIAVLD TGTGKTHIAT LLLRHVLEEE LENRAKGCAH
     KMAFFLVDSV NLVFQQANVL RCGLDQGVEG ISGAMGQSLF QKQTWDKLFA VNMVIVCTAQ
     VLVDCMMHSF MSISRMNLLI FDEAHHAKSN HPYARVMKDY YAHELDTSKR PRIFAMTASP
     VDVKGQSAEH VREAARELET LLHSRIATTS DSALARNSIT RPEEEVAVYT RLRNEFETPL
     HQKVKAKYGD VAPFRKLFIT AKLHASELGR WASDMYWSFA FADEQSRKLQ IREELKYNRS
     KRDWSAAELD AQMARLKEAT AFVQQYEIGA PTLSEQDLSS KVMKLQYWLN LYYERTTLAR
     CIVFVEKRHT AQLLKLIFDH IGGPNLHCDV LVGINNRAGE ENVSLRSQIL TLQKFRRGEL
     NCLFATSVAE EGLDIPQCNL VVRFDLYRTM IGYVQSRGRA RHRNSKYLHM LEAENKEHTE
     RLMNARHDEN IMREFCKDLT HDRQLGDVEQ EKAELIALED KLFPSYTDEK SGAKLTYRSS
     LSILSHFVAT YPSPDHNTMA QPTYVVNPKI SDDPRDPQRN GFVCEVILPE HCPIISMVGQ
     VYSRKTIAKC SAAFKMCIEL RRKDHLNEFL LPTISKYLPA MRNALLAVSE KKKGNYAMVI
     KPTFWKQDRD TVPESLHLTI IDADRGLDRP HQPLAMLTRR PFPQLPSFPI YLTDCRPSNI
     VSQSLHIPIS LTPELLEMFT RFTLRIFEDI YNKVYDYDVS KMSYWMLPVI EHRVASVRSM
     SNPQEVLDMD QIRKVYNEPF WKWSPQSRTD DLIDRYFVDP MNGGRRYYSD RLAPHLKPQD
     PVPANVPRQN HKFMKNILDF SDSKWMKSRD ITRWHQDQPV LQVEKIPFRR NHLANVEDKE
     KKELANLETY ICPEPLHISN LATPFVVMCY VLPAIIHRFE SYLIALDACD VLDLKVSPAL
     ALEALTKDSD NSEEHGEEKI NFKSGMGPNY ERLEFLGDCF LKVATSLSVF VQQPEENEFE
     FHVRRMLMLC NQNLMETAVG KKKLYKYVRT DAFSRRNWYP EGLKLLRGKG LKKTEEDWLN
     VTHNLGDKSV ADVCEAFIGA AFMQHHKGGQ WTPNDWDEAV KAVKLFANSD DHLMEKWTDY
     YAAYTKPKYQ TAGATATQLD LAHKIEMKHP YRFRYPRLLR SAFIHPSQPF MWENIPSYQR
     LEFLGDSLLD MAFIMHLFYK YPDKDPQWLT EHKTPMVSNK FLGAVCVKLG WHTHMKQNTA
     ILSSQIRDYV YEVEEAEREA NGAVDYWVSV SEPPKCLADV IEAFVAAIFV DSEFDFNVVQ
     KFFDLHLKPF FLDMTLDAYE NFASNHPTTR LSRLLSINFG CSEWRMGALE TETLIPGKGK
     AIAAMVMIHD KVHFHSLGQS GRYARVRASH AALEKLEGLP PYEFRSKYGC DCVDEGEGEA
     GVDEAAVSKK VELMREAIGP SI
//
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