DCL1_ASPTN
ID DCL1_ASPTN Reviewed; 1519 AA.
AC Q0CW42;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
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=ATEG_02092;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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=EAU37054.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476596; EAU37054.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001211270.1; XM_001211270.1.
DR AlphaFoldDB; Q0CW42; -.
DR SMR; Q0CW42; -.
DR STRING; 341663.Q0CW42; -.
DR PRIDE; Q0CW42; -.
DR GeneID; 4316974; -.
DR eggNOG; KOG0701; Eukaryota.
DR OrthoDB; 1337630at2759; -.
DR Proteomes; UP000007963; 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; 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..1519
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306777"
FT DOMAIN 116..297
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 431..601
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 634..724
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1026..1184
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1235..1387
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1421..1489
FT /note="DRBM"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..245
FT /note="DEAH box"
FT BINDING 129..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1373
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1376
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1501
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1503
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1368
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1519 AA; 172077 MW; 1A8FB9F68058DCCF CRC64;
MTHQNTETAS LATTKGALEP LPPDKTAGLS TGAGHEISSD ESEGSEEETG LHKDPSQRQR
QQNATFQAFL SHHAETIVNS PVKPNQAQSE LSISSLIGRN ASGTGILNPR EYQIELFERA
KVQNTIAVLD TGSGKTLIAV LLLKHVIQTE LIDRANGNPP RISFFLVDSV TLVYQQASVL
RNNLDQNVAH FFGAMGVDLW NKQTWAEHFE KNMVIVCTAE ILNQCLLNAY ITMQQINLLV
FDEAHHTKKD HPYARIIRDS YLRVPPSSRP RIFGMTASPV DTKGDVLEAA RNLEALLDSK
IATTSKLTIL RQVVNRPNEE VWIYDKLQPT FTSDLYKLME SRFGDISHLE PMFRFARHAT
SELGTWCADR VWVSALADDV LPKVEGSIGG KRQSTGLGQL PKDVHRDITR IKEASELVES
HPPNDPGAPE ALSSKVRVLW KEISQCFGQE TNTKCIVFTE KRYTAKVLFD LFTVLNVPGL
RPGVLIGVRS SDRIGMNVTF RQQILTMVRF RTGEINCLFA TAVAEEGLDI PDCNLVVRFD
LYKTLIQYVQ SRGRARHADS TYASMIEKDN ADHESILVQV NDAEKIMQSF CQLLPEDRIL
HGNDDDTDAV LDREEWEEPY TLPSTAARLT HHSAITVLAR YASSLQYEND TSAQVTYVVL
PVNDAYVCEV ILPEKSPIRG ATGMPAMKKS TAKRYAAFEA CRLLRKHRLL DEYLNSVYHR
RLPAMRNARL AITSHRTNEY KILPKSSLWN KQIGVIPGKL YGTVISLKPL TPLAREHGSM
ILFTRDRLPQ FPTFPIFLGE DVETIVLTVP VNMELQPSAD ELDYMTTFTL RIFRDVFRKT
YDKEPEKLPY WLLPAISFPC NQEADPRDVV NWEILSSVHE RDDIEYQADM PPEMLVDRFV
YDHWDGRYRY FTLAVDENLQ PSSPPPSHVA RRRHMDTIMN YSISLSKNSR AKFLSRCNWN
QPVLHAELVR LRRNLLDRMT DKERKLETRS VICIEPLKIS AIPAAIAATC LAFPAIISRL
DAYLIGLEAC KKLGLEISLE YALEALTKDS DNTHEHRSQQ VHMQRGMGKN YERLEFLGDC
FLKMATSISL FNQHPDDNEF DYHVNRMCLI CNRNLFNSAV KKELYQFIRS RGFSRDTWYP
EGLTLLQGRD HSKKIGSESK HALAEKTIAD VCEALIGAAL LTPGPQHRFD MGVRAVSAVV
DSNEHNAASW RDYISLYSIP KYQEQAPDGS EIDLCRRVEE KLGYHFRYPR LLHSAFTHPS
YPSAWARVPC YQSLEFLGDA LLDMVCVEDL FRRFPDRDPQ WLTEHKMAMV SNKFLGALAV
KLGLHTHLSY FSSALQSQIT HYAEEAQAAA SQSDVAVDYW TLTQDPPKVC LPDMVEAYLG
AVFVDSNFRF EEVEVFFQQH IKPYFHDMAI YDTFANRHPT TFLHNKLTNE YGCLNYCLKA
GEIPGADGDA STVLAAVIVH DTILTTGVAS SGRYAKVKAS ENALTELLHI DRNEFRKRYQ
CDCVQENGEH GERDVGTPI
