DCL2_PHANO
ID DCL2_PHANO Reviewed; 1399 AA.
AC Q0UL22;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
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=SNOG_07542;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT85008.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445335; EAT85008.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001797877.1; XM_001797825.1.
DR AlphaFoldDB; Q0UL22; -.
DR SMR; Q0UL22; -.
DR STRING; 321614.Q0UL22; -.
DR GeneID; 5974770; -.
DR KEGG; pno:SNOG_07542; -.
DR eggNOG; KOG0701; Eukaryota.
DR InParanoid; Q0UL22; -.
DR OrthoDB; 1337630at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016442; C:RISC complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
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..1399
FT /note="Dicer-like protein 2"
FT /id="PRO_0000306797"
FT DOMAIN 18..194
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 364..549
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 562..656
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 897..1054
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1094..1270
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1301..1370
FT /note="DRBM"
FT MOTIF 139..142
FT /note="DEAH box"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1133
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 1252
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1399 AA; 157596 MW; 375777F3770D6455 CRC64;
MADSHDAPFR LRSYQAEMVE ESMQSNIICV MDTGSGKTHI AIDRTRAELE ICRPDKIVWF
LAPTVTLCEQ QFAVFKSNLP GYGIQLLSGK DNLDHWTDQG VWDDVLLNIR IVLSTHQVLL
DALSHGFVKM RNLSLLIFDE AHHCSLKHPA HRIMSDFYKP RIGTELPRIL GLSASPIKTA
KVTSEDLQQI ERNLCATVKT PKLHRSELLR YVHRPHLMRI DYPVEPQDLQ SNMLSFLKSA
YTNYDLQKDP WVSELLQQRQ QGHDVTKNIH KVFIGGKTYC RDQLRSLALK AEAMSQELGM
SVMDWYLRGC ITQFSKMVHM SDSQLLDWSA DEKRHLLEIL RTLPSIDLNS HDIPPMSLGS
MSHKLQLLIK FLVAEAKHDP EFTCLVFVEQ RVWVACIAEV LAIHPETRDL LRVGTFVGES
ENSKRKANIA SISEPRNQQA TLENFRAGKL NLILATSVLE EGIDVSSCHL VVCFESPKNL
KSFVQRRGRA RKEESKYVIF VPQAGRRRDP ESWQSLEEGM KAAYLDDLRQ VKLATEKEQQ
SETGHRNFEV KSTGALLTLD NASQHLHHFC SILGAGPYID NRPQFEFTEI RPGVITARVI
LPLTVDPEVR TACALDTWAT EKMAKQDAAF EAYKALYVAG LVNDNLLPAR QEADDELSEL
QIPDHRPSLV PVSPTLDPWP LFARHQQQNP HVYYRTRLTL HTVDDKPKHL ILLTPKILPD
IPELLLYWNS STKLKIESSW LHDVVLNDEE ISELKSVTYK ILYSVFHNRM ELNRRDFVWL
VAPCDESGLL DSRIWLSEWR QHTCLATELI AQNSDWSLWG LVNQKGDARK YTPRSTSMNN
QLWLLQLMQL PKRRDFLHPV LESANINDAY TKTDEMAAKD CIVDPVPAPY SVFALLLPSI
LHRFGMAIIA ETLRTTLLGP VALDSAHSLL LTRALKSSAA DGNDNYQRLE FLGDCILKFI
ATVHLMAANP KWPESHLTAK KGRIVSNGFL ARATIAAGLD RFMITKSFTG AKWAPRYAGD
LLAETGPAVK EERSSKLIAD IIESLIGACY TVGGFEKAVL CVQTLLPLEP WISVPAANSI
LHEAAPAEAD LMGLDVLETL IGYTFKKKPL LLEALTHASF SGPHVHCSYE RLEFLGDAVL
DYIISKRLHA HSPELSHQKM HAIRTATVNA SFLAFRLFET TIDEETINKT SMRPESQKRA
IWQFLRSGSP SLNANRDNAL RQHEQVRDEI IIGLNEAARF PWHLFALTDP PKFLSDMVES
VIGAVYIDSL GDILTCEAIV RRLGILDCLD HILCNGVDCL HPKERLGHLA VDKGVQYARV
GMNTEPNEGD KMYKCQVKVG GEDVGDVAEG LKRLNAETVA AWKAVGVLES RKDSAIEIVS
DVEEFFDADD GGGISLDDP
