DCL1_PHANO
ID DCL1_PHANO Reviewed; 1522 AA.
AC Q0UI93;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Dicer-like protein 1;
DE Includes:
DE RecName: Full=Endoribonuclease DCL1;
DE EC=3.1.26.-;
DE Includes:
DE RecName: Full=ATP-dependent helicase DCL1;
DE EC=3.6.4.-;
GN Name=DCL1; ORFNames=SNOG_08521;
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=EAT83689.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445337; EAT83689.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001798832.1; XM_001798780.1.
DR AlphaFoldDB; Q0UI93; -.
DR SMR; Q0UI93; -.
DR STRING; 321614.Q0UI93; -.
DR PRIDE; Q0UI93; -.
DR GeneID; 5975731; -.
DR KEGG; pno:SNOG_08521; -.
DR InParanoid; Q0UI93; -.
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:0003677; F:DNA binding; IEA:InterPro.
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; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
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; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 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; Zinc.
FT CHAIN 1..1522
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306784"
FT DOMAIN 76..258
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 408..576
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 600..700
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 995..1166
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1222..1373
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1409..1478
FT /note="DRBM"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 202..205
FT /note="DEAH box"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1492
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1355
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1522 AA; 175115 MW; BE255EF8D0BB8DDD CRC64;
MTWAGDVEEQ DDYFSCSDVS TSGDRRKRAP QTVTQEEVDQ ATSKIANEGQ LSIRDILASQ
DTAVRITNPR DYQMELFLRA KMQNTIAVLD TGTGKTHIAT LLLRHVLEEE LENRAKGCAH
KMAFFLVDSV NLVFQQANVL RCGLDQGVEG ISGAMGQSLF QKQTWDKLFA VNMVIVCTAQ
VLVDCMMHSF MSISRMNLLI FDEAHHAKSN HPYARVMKDY YAHELDTSKR PRIFAMTASP
VDVKGQSAEH VREAARELET LLHSRIATTS DSALARNSIT RPEEEVAVYT RLRNEFETPL
HQKVKAKYGD VAPFRKLFIT AKLHASELGR WASDMYWSFA FADEQSRKLQ IREELKYNRS
KRDWSAAELD AQMARLKEAT AFVQQYEIGA PTLSEQDLSS KVMKLQYWLN LYYERTTLAR
CIVFVEKRHT AQLLKLIFDH IGGPNLHCDV LVGINNRAGE ENVSLRSQIL TLQKFRRGEL
NCLFATSVAE EGLDIPQCNL VVRFDLYRTM IGYVQSRGRA RHRNSKYLHM LEAENKEHTE
RLMNARHDEN IMREFCKDLT HDRQLGDVEQ EKAELIALED KLFPSYTDEK SGAKLTYRSS
LSILSHFVAT YPSPDHNTMA QPTYVVNPKI SDDPRDPQRN GFVCEVILPE HCPIISMVGQ
VYSRKTIAKC SAAFKMCIEL RRKDHLNEFL LPTISKYLPA MRNALLAVSE KKKGNYAMVI
KPTFWKQDRD TVPESLHLTI IDADRGLDRP HQPLAMLTRR PFPQLPSFPI YLTDCRPSNI
VSQSLHIPIS LTPELLEMFT RFTLRIFEDI YNKVYDYDVS KMSYWMLPVI EHRVASVRSM
SNPQEVLDMD QIRKVYNEPF WKWSPQSRTD DLIDRYFVDP MNGGRRYYSD RLAPHLKPQD
PVPANVPRQN HKFMKNILDF SDSKWMKSRD ITRWHQDQPV LQVEKIPFRR NHLANVEDKE
KKELANLETY ICPEPLHISN LATPFVVMCY VLPAIIHRFE SYLIALDACD VLDLKVSPAL
ALEALTKDSD NSEEHGEEKI NFKSGMGPNY ERLEFLGDCF LKVATSLSVF VQQPEENEFE
FHVRRMLMLC NQNLMETAVG KKKLYKYVRT DAFSRRNWYP EGLKLLRGKG LKKTEEDWLN
VTHNLGDKSV ADVCEAFIGA AFMQHHKGGQ WTPNDWDEAV KAVKLFANSD DHLMEKWTDY
YAAYTKPKYQ TAGATATQLD LAHKIEMKHP YRFRYPRLLR SAFIHPSQPF MWENIPSYQR
LEFLGDSLLD MAFIMHLFYK YPDKDPQWLT EHKTPMVSNK FLGAVCVKLG WHTHMKQNTA
ILSSQIRDYV YEVEEAEREA NGAVDYWVSV SEPPKCLADV IEAFVAAIFV DSEFDFNVVQ
KFFDLHLKPF FLDMTLDAYE NFASNHPTTR LSRLLSINFG CSEWRMGALE TETLIPGKGK
AIAAMVMIHD KVHFHSLGQS GRYARVRASH AALEKLEGLP PYEFRSKYGC DCVDEGEGEA
GVDEAAVSKK VELMREAIGP SI
