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Database: UniProt
Entry: Q2VF19
LinkDB: Q2VF19
Original site: Q2VF19 
ID   DCL1_CRYPA              Reviewed;        1548 AA.
AC   Q2VF19;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   14-MAY-2014, entry version 43.
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;
OS   Cryphonectria parasitica (Chesnut blight fungus) (Endothia
OS   parasitica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC   Cryphonectria-Endothia complex; Cryphonectria.
OX   NCBI_TaxID=5116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=17646660; DOI=10.1073/pnas.0702500104;
RA   Segers G.C., Zhang X., Deng F., Sun Q., Nuss D.L.;
RT   "Evidence that RNA silencing functions as an antiviral defense
RT   mechanism in fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12902-12906(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).
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC   -!- SIMILARITY: Contains 1 Dicer dsRNA-binding fold domain.
CC   -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 2 RNase III domains.
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DR   EMBL; DQ186989; ABB00356.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q2VF19; -.
DR   OMA; DICKTMI; -.
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:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 1.10.1520.10; -; 3.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR006935; Helicase/UvrB_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   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; 2.
DR   SUPFAM; SSF69065; SSF69065; 3.
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;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Repeat; RNA-binding.
FT   CHAIN         1   1548       Dicer-like protein 1.
FT                                /FTId=PRO_0000306780.
FT   DOMAIN      106    289       Helicase ATP-binding.
FT   DOMAIN      428    589       Helicase C-terminal.
FT   DOMAIN      624    718       Dicer dsRNA-binding fold.
FT   DOMAIN     1051   1197       RNase III 1.
FT   DOMAIN     1248   1411       RNase III 2.
FT   DOMAIN     1445   1518       DRBM.
FT   NP_BIND     119    126       ATP (By similarity).
FT   MOTIF       232    235       DEAH box.
FT   METAL      1288   1288       Magnesium or manganese (By similarity).
FT   METAL      1397   1397       Magnesium or manganese (By similarity).
FT   METAL      1400   1400       Magnesium or manganese (By similarity).
FT   SITE       1393   1393       Important for activity (By similarity).
SQ   SEQUENCE   1548 AA;  176667 MW;  91B533E9EF72349B CRC64;
     MGDPAAHEMA DLERGFSSED DAEYRSGDDE ASKFVENEPS KRGKISQKKK IEQTNFAKWM
     DTNQKSLTRK AVKQSVNQDN SLAYMIRSWE GGEKIITSPR DYQMELFERA KQQNTIAVLD
     TGSGKTLIAA LLLDHTVNQE LEDRAKGLPR RIAFFLVEKV ALAFQQHAVL ECNLAHSVAV
     FSGESIKNTW TKGFWETQLA DHEVIVCTAE ILNQCLQYAY IRIDQINLLV FDEAHHTKKN
     HPYARIIKDY YASGKDRGLR LPRIFGMTAS PVDALIDVRQ AAIELEGLLH SRIATTADPD
     ALRRAVGRPK KEIIYKYNPL VKPIQTMLTF KLRPLIANNK QFSKAFAFSE AAARELGTWF
     VDRMWQLFLE DEELLKLEAK TERSLSKDMA APEVVEKHRN AVRSARELIR SHEFPKPEPG
     LLSSKLKTLS KLLEEYFTDS SIRCIVFVER RWTAKLLTDF FESHAAEIPG LKVGSLMGAN
     AEGGSSQTSF REQIRTILSF KKGNTNCIFA TSVAEEGLDI PDCNLIIRFD ICKTMIQYIQ
     SRGRARQADS TYIHLIEGGN GDHRRIMHQN AENEKLLRRF CNTQPEDRLL KGSDYDMDFF
     LRQERNQRQY TIKSTGARLT YKNSLPILQA FLNTLRNQDD YAEGMDLVAD YSILSVQGGF
     ICEVMMPPLS PVTSAIGKVY STKQVAKCSA AFELCFQLIQ KKFLDDHLRS KFVEKRHVMA
     NARLAVSSKN KAKYDMRLKP QIWAELGVPE KLYATVLILS KPSALERPSR PLFILTRTPL
     PQLKPFLLFL GPVEQEMTSD LVCQVLNCPI TPTEEDLQLL TKFTLKIFVD IFNKKYAANA
     QALPYFFAPT NKDHVFLFSN LQDPRNAVDW PLLRHVADRD AEAYTGDEPE EFFQDKYIVD
     PHDGARRFWL QGIRKDLTCT SPVPADVEHQ PTHRQWKRRE VPHDILHWSL TAWKATREAH
     ENKWKENQPV VVGKYATLRR NFLADINETS KNPFCYFVLE PMRISPLPVD VVAMAYLLPS
     IIHRIEQNLI ALDACRLLQL DIHPDLALEA LTKDSDNQGE DERMDSIQAF EPVNFQPGMG
     ANYERLELLG DSFLKMATTI AVFTLIPNKD EFDYHCERMV MICNQNLFGV AKSDDLKLHE
     YIRSKSFERG TWYPVLKLEF GKTHLKTLKQ MDEHRLADKS IADVCEALIG AAYMTTRKHD
     DYDLAVRAVT RLVNHKQHPM TKWDDYHAAY VMPGWQTMPA NAAELDMAQK IHEATGYQFK
     HPRVLRSAFR HPSRPYVFDK VPHYQRLEFL GDALFDMACV DYLFHIAPDE GPQWLTEHKM
     AMVSNQFLGC LAVSLGFHKF ILHHHASIGS QIHEYVTEIT EARRAAEDAA EAAGKPRSAY
     SRDYWVEAPQ PPKCIPDVLE AYVGAIFVDS KYDYSVVQQF FHAHVLPFFA SMRMYDTFAN
     KHPVTFFTQY VFETFGCHAY GLHAEEMPVK DDTGLVTGKT QVVAGILLHG QVVEGAVRDS
     GRYAKIAAAR KALDKLRSMT RQEFLDAYKC DCKPGEAAED ISESATAI
//
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