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   03-AUG-2022, entry version 75.
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 parasitica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   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 mechanism in
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12902-12906(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, DCL-2 is involved in antiviral defense against mycoviruses
CC       like the hypovirus CHV1-EP713 and the reovirus MyRV1-Cp9B21.
CC       {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}.
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DR   EMBL; DQ186990; ABB00357.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2VF18; -.
DR   SMR; Q2VF18; -.
DR   PRIDE; Q2VF18; -.
DR   OMA; CAAYVGW; -.
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:0031047; P:gene silencing by RNA; IEA:UniProt.
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; -; 2.
DR   Gene3D; 3.30.160.380; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
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; 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; Hydrolase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding; Repeat;
KW   RNA-binding.
FT   CHAIN           1..1451
FT                   /note="Dicer-like protein 2"
FT                   /id="PRO_0000306792"
FT   DOMAIN          70..247
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          412..582
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          603..704
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT   DOMAIN          968..1111
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1153..1351
FT                   /note="RNase III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   REGION          34..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1253..1272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           190..193
FT                   /note="DEAH box"
FT   BINDING         83..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1337
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1340
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            1333
FT                   /note="Important for activity"
FT                   /evidence="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