DCL2_NEOFI
ID DCL2_NEOFI Reviewed; 1388 AA.
AC A1D9Z6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Dicer-like protein 2;
DE Includes:
DE RecName: Full=Endoribonuclease dcl2;
DE EC=3.1.26.-;
DE Includes:
DE RecName: Full=ATP-dependent helicase dcl2;
DE EC=3.6.4.-;
GN Name=dcl2; ORFNames=NFIA_030600;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 response against viral infection and transposons (By
CC 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}.
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DR EMBL; DS027693; EAW20627.1; -; Genomic_DNA.
DR RefSeq; XP_001262524.1; XM_001262523.1.
DR AlphaFoldDB; A1D9Z6; -.
DR SMR; A1D9Z6; -.
DR STRING; 36630.CADNFIAP00002683; -.
DR EnsemblFungi; EAW20627; EAW20627; NFIA_030600.
DR GeneID; 4589127; -.
DR KEGG; nfi:NFIA_030600; -.
DR VEuPathDB; FungiDB:NFIA_030600; -.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_6_1; -.
DR OMA; CAAYVGW; -.
DR OrthoDB; 1337630at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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; 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; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1388
FT /note="Dicer-like protein 2"
FT /id="PRO_0000306795"
FT DOMAIN 23..203
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 371..537
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 564..658
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 919..1059
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1098..1281
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT MOTIF 144..147
FT /note="DEAH box"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 1263
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1388 AA; 156430 MW; C30E206A2EB2D3DB CRC64;
MASSVTACQG ASPYQPRNYQ LEMLEASMKE NIIVAMDTGS GKTHIAVLRI KAELDICPPD
KLVWFLAPTV ALCIQQHEVI ASNLPAVRTR TLTGLDKVEL WTEQSIWDAV LNGYRVIVST
HAVLADALSH GFVKMSRLAL LIFDEAHHCT RRHAANKIMR DFYHPTLTKS GPGAVPRIMG
LTASPVVRSN HQELLTVESN LDAVCRTPRV HRQELVKFTH RPHLQQIWYT PTDPAGFKSA
SQTLGALYHA WETLDIGDDP YIQRLRKSPL DDTALKKALL TGKTYCREQL RRFVDRSRHI
FEELGEWAAE YYIYASIKQL GDRVRNSYMS GDWDEAEKAY LVDFLSKIPA SEIQLALNDP
GSFRISPKFE SLLNFLDSLD EREFSGLIFV KQRATVSAMT SLLSVHPCTR ERFRCAAYVG
WSNGSASKDI LGDLLNMQLQ RDTLDDFRSG RKNLIIATDV LEEGIDISAC SVVVCYDKPP
NLKSFVQRRG RARRKQSTFA IMFPTDDASA DVSKWQDLEQ AMIEAYQDDE RQLQSVSALE
SLDEEVMERL TVESTSAVLT ADMAMAHLHH FCAVLPPQPY ADMRPVFSFE TNEDGLLKGT
VILPSCVHPK VRRTEGRRWW RTERAAMKET AFQAYKALYE FGLVNDHLLP LTKRPELKSH
DLGAMPSILE TSEQYDPWIE WAYSWSSPDI HQSRIVVRMN EGRGDELCMR LMGPTYLPPL
SPMTLFWNNS TTFTVTFEAA ERVPLVPLSS VEDMRAITAL YLKATNSRVC SSERDFTALF
APDLHHTELK GWLNAYEGCD PAMEVYSRGH NPLLMGVVRD HSRYGEPFLF RKWLVSDQNP
SCSVVELECA PFPHRRNLLH RQRLANSQVD VDEETPESAA KNPIVAADAC TIDRLPFTMA
IFGLFISAIV ERLETELIAT RLRETILRDV GFKSTDHIIT AISTPFAHAL TNYQRYEFLG
DSILKFSVSC QLFFQHPNWH EGYLSEGRAM IVQNPRLAKA ALDTGLDAYI VTKRIASRKW
SAPLISEKLE RVPAKRQMST KVLADVVEAL IGAAYMDGGH ATAQACIRRL LPEINLHAVD
TRTATRSVAP ESARHMMNER LKDHIGYTFE DESLLVEALT HPSCDYDSTT QSYQRLEYLG
DAVLDMVIVS AIFNHPIQRP QGDMTKIKHA VVNANLLAFL CMESATSEEK LDVAQTSKDS
FAVTTSQESV ELWRFMRYRG QNLNAARDAS LARHRALRDE IASSLLHAPH YPWHALSRLN
ADKFFSDIVE SVLGAIFVDS GGDLAPCEVF VERIGLMAYL RRILDQEIDV RHPRSVAQQL
AKTNIQFVLQ RVPNEEGGAS YQCSVRIEQA ELFVVTGCLT AEEAEVTAAV EAIKFLTRDE
GSTPLNTS
