DCL1_ASPCL
ID DCL1_ASPCL Reviewed; 1534 AA.
AC A1CBC9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
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=ACLA_014840;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW13047.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS027049; EAW13047.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001274473.1; XM_001274472.1.
DR AlphaFoldDB; A1CBC9; -.
DR SMR; A1CBC9; -.
DR STRING; 5057.CADACLAP00001180; -.
DR GeneID; 4706314; -.
DR KEGG; act:ACLA_014840; -.
DR eggNOG; KOG0701; Eukaryota.
DR OrthoDB; 1337630at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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; 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; 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..1534
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306773"
FT DOMAIN 130..311
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 456..613
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 648..738
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1054..1199
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1250..1402
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1436..1504
FT /note="DRBM"
FT REGION 36..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 256..259
FT /note="DEAH box"
FT BINDING 143..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1388
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1391
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1518
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1384
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1534 AA; 174094 MW; 200457CEAAB4115B CRC64;
MSSDLISQAE SISNIEILRA LFITDTHTTV GDVAVPSAEP GVEHDQISPG ESDEEIEENI
SDQNNSSSQK RLQNAQFEAL LTRRAEDTSN ENIDRVPLNL SDNELSIAHL VAKQDVGGGL
LDPREYQIEL FERAKAQNTI AVLDTGSGKT LIAVLLLRHV LQNELNDRAN GKPHRVSFFL
VDSVTLAYQQ AAVLRNNIDQ NVAHFFGAMG TDLWDRQVWE EHLQQNMVIV CTAEILNQCL
LNSHVRMNQI NLLIFDEAHH TKKDHPYARI IRDSYFKASP PQRPRIFGMT ASPIDTKGDI
IAAATRLETL LDSRIATTSK ITLLRQVVSR PIEKVWAYDR LESPFKTNLH KLMENRFGNV
KALEGVFRFA WYASSELGRW CSDRAWLYAL ADDVLPKLEG HVNKLAESTA AATERDMAFK
EITLIKEASN IVKAHTFNDP EFPGELSPKV RLLQTELSKH FSHAPETKCI IFTQKRYTAK
TLHELFTILS IPHLRPGVLI GVRSGDIGGM NITFRQQFLA LVKFRKGEIN CLFATSVAEE
GLDIPDCNLV VRFDLYHTLI QYVQSRGRAR HYHSTYASMV EKDNSDHEAR LREVREAEKT
MQNFCETLPE DRILHGNDHD LDSLLQHEEG RRTFTVKSTG ARLTYHSAIA ILARYASSLQ
YEKETTPQAT YVVQSVGNTY VCEVILPEKS PIRGLTGSPA IRKSIAKQSA AFDTCLLLRR
HKLLDDFFKS IYHKRLPAMR NAKLAITSKK TNQYDMLLKP SIWRRHQGIL PSKLYGTILS
LLPSEPLSRE HQPILVLTRE KLPDFPAFPI YLDEDIETKV VPRSLDTGME LSAEELRALT
TFTLRIFRDV FHKVYEQESE KLPYWLAPAE PLDANGREPG PRGIIDWKTV TFVQENDEIV
FSRDLAPESL VNRFMFDKWD GRSRFFTIKV MEGLRAADPP PSSVPRRRHM DNIMSYCLSL
SKNSRARFLA GCHWDQPVLQ AELVRLRRNL LDKLTTEEKK IQTECFICAE PLKISAIPPS
IASTCLAFPA IITRLDSYLI SIEACDELDL VIRSDYALEA VTKDSDNTEE HRGQQIHFQR
GMGKNYERLE FLGDCFLKMA TSIALFTQNP DDDEFDYHVN RMCLICNKNL FNTAKKRQIY
RYIRSRSFSR HVWYPDGLTL LQGKDHSKKM LSQAKHALGE KTIADVCEAL IGACLLSGGP
EHRFDMGVKA VSVFVDSPSH AVSRWKEYIG LYKPPNYQVR KAEGAETNLA LQVEEKLGYH
FRYPRLLCSA VTHPSTPSTW YFRVPCYQRL EFLGDSLLDM VCVEDLFHRF PDRDPQWLTE
HKMAMVSNKF LGALAVKLGF HKHIKAFSNP LQAQITYYVE EIETAEAESE GAVDYWVVAK
DPPKCLPDMV EAYLGAIFVD SDFSFEVIEA FFQAQIKPYF QDMSIYDTFA NKHPTTFLHN
RLANEFGCTN YCLKAGEMPA IDGMPAGVLA AVIVHNSVVS EATASSSRYA KIRASERALV
VLDGLLPYEF RQRYNCNCQV VGNPASAPDI GTAI
