GenomeNet

Database: UniProt
Entry: Q2VF18
LinkDB: Q2VF18
Original site: Q2VF18 
ID   DCL2_CRYPA              Reviewed;        1451 AA.
AC   Q2VF18;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   16-OCT-2019, entry version 66.
DE   RecName: Full=Dicer-like protein 2;
DE   Includes:
DE     RecName: Full=Endoribonuclease DCL-2;
DE              EC=3.1.26.-;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase DCL-2;
DE              EC=3.6.4.-;
GN   Name=DCL-2;
OS   Cryphonectria parasitica (Chestnut blight fungus) (Endothia
OS   parasitica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC   Cryphonectria-Endothia species 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, DCL-2 is involved in antiviral
CC       defense against mycoviruses like the hypovirus CHV1-EP713 and the
CC       reovirus MyRV1-Cp9B21. {ECO:0000269|PubMed:17646660}.
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}.
DR   EMBL; DQ186990; ABB00357.1; -; Genomic_DNA.
DR   PRIDE; Q2VF18; -.
DR   OMA; EKCISGP; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 1.10.1520.10; -; 1.
DR   Gene3D; 3.30.160.380; -; 1.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_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   InterPro; IPR036389; RNase_III_sf.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF03368; Dicer_dimer; 1.
DR   Pfam; PF00271; Helicase_C; 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; 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   1451       Dicer-like protein 2.
FT                                /FTId=PRO_0000306792.
FT   DOMAIN       70    247       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      412    582       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      603    704       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      968   1111       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1153   1351       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   NP_BIND      83     90       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       190    193       DEAH box.
FT   METAL      1192   1192       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1337   1337       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1340   1340       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1333   1333       Important for activity. {ECO:0000250}.
SQ   SEQUENCE   1451 AA;  163401 MW;  37EB50AAC8CE3127 CRC64;
     MAYYTDSSSS ESEDFEDVIN QVVAEEDITG AAWYDGHLSE EDSPGGKPRP KEQLPKDIVK
     MDARAYQLEM LEASLKENII CAMDTGSGKT HVAILRIKAE LEEMPEGQVV WFLTPTVSLC
     AQQYAVVKAQ IPSVQTKIVT GADKVDSWSS TTWDGALLNV KVIITTPQVL LDALLHGFVN
     ISSLALMVFD EAHHCNKNHA YSRVMKEFYW ESKTKHEPVP RILGLTASPV VRSDISSLKR
     LESTLDAVCR SPTRHREELI ANSQRPALFS IIYNPKLQPY AAGFSESLTK LMAARNKLNI
     LEDPYVVSLR AEISDRSRRK LEKAIKEKRT YVQDTMKSFC RRSMEMAKEL GAWAADWFIS
     EAIRLFLAGI YRQGASSKSF RDAEVIFLAR VFQDANIEPP PPLTTHSGLS EKVQRIIEVL
     LNYDKDARAI CFVKERATTV VLSHILTTHP EVSSKFRIGT MVGTSFVPGV KRDFLDLPET
     GGSQCLEAFR EGRKNMLVAT SVLEEGIDVP ACNLIICFDK PNNLRAFIQR RGRARMRQSH
     LYLFVEDEAE ADWEALEAQM KLQYEDEKRE HERLEAIENS EALDYPEELR VESTGARLTI
     NDAKSHLQHF VSTLASRKFV QTQPDYLIEK VSQGYQPGDQ PLLKATVLLP VSVPQALRQV
     TSSRTWVSEK NACMDAAFQA YKALYEAGLV DDHLLPLRDR LELELEVRPG MREVRGLYNP
     WLSIAAACTQ GDVPLCRRAL KVSDGNNSEL CEFELAIPVA LPEMKPMVVW WDHRAQLTLR
     IDSDAVMADT DVRHADQTTI NQQDHTSVLL SLAYGHRNMT IRDDCILRLV SKSGPLSMEQ
     LGQVEFAPGL VTANGSSYLV RDERDQSRHP YYFESVLPSK PPAESIRKVY RGFDEDPTEA
     TYLSVRKWPK KTGFFHRPCS PQHSPSTKPY AYILPAETTT VDRIPLVYAQ MGLLMPSLVC
     YTELYLVAAE LSRKVLAPLR ISNVSMLVEA ICAKSARTPE NYERIEFLGD SILKTCITVN
     LAATKLHLPE GILSLMKDRL VSNARLCRAA CDAELDQFLV TQQLVTKGWQ PPYMSDLAKQ
     DQEPESKRIL SPKTLADVVE ALIGVSFVDG GLPKALECIR LFIPESQPRP FSEVRDILFG
     AAEPKGMKLP ADLQLLEQLI EYSFCEKALL VEAVTHPSYN VSGTVACYDR LEFIGDAILD
     YIIVEEVFAL EPALENWQMH LLRTALVNAD ILGFLIMEWS YKQMGFEVCR ANEGDSDSKS
     SGDSTSDKAS PRLEQTEVPI PLWSFMRQSS AELTMEREIT KARFEELRDP ILEAMRSGTH
     YPWALFARLH AQKFYSDFFE ALVGAIWVDA GPGFDACRAF VARSGVLPYL KRLLRDQVHV
     LHPKEELGRL AGRERVEYVV KETLKDDGDG KEWACEVRVG GRYVTDVTGC LFKEESRVKA
     ATQACEILKR K
//
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