DCL2_MAGO7
ID DCL2_MAGO7 Reviewed; 1485 AA.
AC A4RHU9; G4MTK0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 03-AUG-2022, entry version 92.
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; Synonyms=MDL2; ORFNames=MGG_12357;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION.
RX PubMed=15304480; DOI=10.1074/jbc.m408259200;
RA Kadotani N., Nakayashiki H., Tosa Y., Mayama S.;
RT "One of the two Dicer-like proteins in the filamentous fungi Magnaporthe
RT oryzae genome is responsible for hairpin RNA-triggered RNA silencing and
RT related small interfering RNA accumulation.";
RL J. Biol. Chem. 279:44467-44474(2004).
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.
CC {ECO:0000269|PubMed:15304480}.
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; CM001232; EHA55558.1; -; Genomic_DNA.
DR RefSeq; XP_003715365.1; XM_003715317.1.
DR AlphaFoldDB; A4RHU9; -.
DR SMR; A4RHU9; -.
DR STRING; 318829.MGG_12357T0; -.
DR PRIDE; A4RHU9; -.
DR EnsemblFungi; MGG_12357T0; MGG_12357T0; MGG_12357.
DR GeneID; 2683150; -.
DR KEGG; mgr:MGG_12357; -.
DR VEuPathDB; FungiDB:MGG_12357; -.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_6_1; -.
DR InParanoid; A4RHU9; -.
DR OMA; HFCAVIP; -.
DR OrthoDB; 1337630at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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; IPR014720; dsRBD_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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS50137; DS_RBD; 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..1485
FT /note="Dicer-like protein 2"
FT /id="PRO_0000306794"
FT DOMAIN 72..250
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 415..579
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 609..712
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 988..1127
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1168..1358
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1388..1469
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 193..196
FT /note="DEAH box"
FT COMPBIAS 28..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 1340
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1485 AA; 166095 MW; 4246BF379102DFFE CRC64;
MSSQDESASS SDTGEGGHVF GRENLNQSAD YGYKTGSSAS THSTTDDAIS EEPQPSGNGP
RSIIARAYQL EMFQASMQQN IIVSMDTGSG KTQVAVLRIR AELERTPPEK RVWFLAPTVA
LCAQQYEVIR SQIKVANSIV MTGDDNVDSW SDVQTWDAVL ANVRVVVCTY MILFEALSHA
FVTMDSISLL VMDEAHNCTG KFPGRLIMKR FYMPRKSAGD HVPHILGLTA SPVMKSDLSS
MEDLESSLDS VCRGPTLQRE ELFANVHQPT MTVTTYKECD LRSPVQYTRN MNNLHLAFEN
LDIAEDPYVL HLMGQRTPKS LRELDRILTK LDTYTQNQMK ALQRKSSSLF RELGQWAVDS
YIYNVVEKVS NLDARSSWLG GWLDDEQRYL HRAIQGINAL PVSAAIPAPE MTSIKLQVLL
RILRGYEGSP VGIVFVKERA TAGILSQLLA IIPDINARYK VGCMVGTSRY MSRKMNIHEV
LQQGDDLLAL EKFRSGAINL LVATSVLEEG IDVPVCNLVI CFDMPANLKS FIQRRGRARM
RESKLHLMIE EDSLVSVKDW GALEAAMKQR YENDMRELDH LAQVEEEDEM DVPPLHSRTT
AAKVTVDDAK GHLEHFCRVV TRSQQYVDAS PEYLVTTKTT AFVGGKPIPI LGVTVLLPAS
LPPNLRQAHS SRDWISERNA KKDAALQAYK MLYEAGLINE HLLPIRESDF VDREVDGRPG
LLEVQEQWNP WPCIVEAWET GLSSQTIHRR RLQLTDQDGM LMGELDALLP VPFPPISILK
LYWIQHSEHP WTISFDPDVT MSGPGSTDPS FEIQQALDQT QILLDMAFGH RFSVSEQSKA
LRFIWPNRTL KLQMIGGQPF SKKAGEAHSS DYIIRSYGRD PYIYKSWVPV KPPLELVRGY
WKAKPDEEEP PADAPWVVVK RLPKNCGFVK NSRIPIELPK EYQTSSPRRF DYIIPEQLCT
FDTVPATLVQ LGMLVPSITQ AMEPYFVAQE LLRRTALGSL DFKDIDLVMM VITSSSAGRL
TNYERVEFLG DAVLKLGAAV TCATNNLHFP EGYLSLLKDR LVSNSRLCKA ATALGLDQFI
ITRQYSLKQW RNMLTAPEPP TNTRKMSSKT LADVTEALIG AAYIEGGMSK ALRCISLMIP
NERWRSLDES RAVLYQVALN DIPLPSTLGP LEELLGYSFN KKSLLIEAIT HASYNIPGSA
GSSLERLEFL GDSVLDFVVV ARLFSVKDPA PIEHYNMHLL RTAVVNGEFL GFLAMEWRTA
ATQRSVVVRT GQGTADELET VETPGLPLFG FLRHNASGDW VRDQQLAEER HAEMAPGIRD
ALEHGQRYPW DLLARLRISK VHSDVLEAVI GAVWVDSGSL EECEKLIERV GILRYLDRAL
RDGVKILHPK EELGRVAQNN KVVYKVDKAK RAARAEVYEV SGELAEGEDV EFLCSVTVGD
RCVARVGGAV SKNDAMTKAA LEVIRVWEEA GRSWDNVGVV LEEGV
