DCL1_ASPOR
ID DCL1_ASPOR Reviewed; 1523 AA.
AC Q2U6C4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=AO090120000297;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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=BAE62891.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007166; BAE62891.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001824024.2; XM_001823972.2.
DR AlphaFoldDB; Q2U6C4; -.
DR SMR; Q2U6C4; -.
DR STRING; 510516.Q2U6C4; -.
DR Proteomes; UP000006564; Chromosome 5.
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..1523
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306776"
FT DOMAIN 123..304
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 444..617
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 640..730
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1031..1190
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1241..1392
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1426..1494
FT /note="DRBM"
FT REGION 24..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 249..252
FT /note="DEAH box"
FT BINDING 136..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1378
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1381
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1438
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1506
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1374
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1523 AA; 172531 MW; 48D0FBDC8F1C5C46 CRC64;
MPPLEVKPLA GYVRSQSLRI PSSLNLSGER TISTTEPTEG NDSSSEESGD NEQISTQRLI
SQNKRLQSAK FEALLSERAD TLTGNSGRPT LDLPDAELST ASLVAKQDAG TGMLDPREYQ
VELFERAKSQ NTIAVLDTGS GKTLIAVLLL KHIIQNELID RANGKPPRIS FFLVDSVTLA
FQQAAVLRNN LDQNVAQFFG AMGTDLWSKQ TWDHQFENNM VIVCTAEILN QCLLNSYIRM
DQINLLIFDE AHHTKKDHPY ARIIRESYLK ADPTKRPRIF GMTASPIDTK GDIIESATKL
EVLLDSKIAT TSKPNLLREV VRRPIEESWE YDKLDPPFAT KLYQILQARF GDISSLQPVF
RFTLQASSEL GPCCADRAWA YALADDVLPK LEGNVRKLAQ SISSPIPQCA LKEISRIQEA
SDIVKNHSFN SPNVPGELSP KVQLLRQKLI KYFEHPTKTK CIVFTQKRYT AKMLFDLFST
LEIPYLRPGV LIGVRSGDIV GMNVSFRQQF LALVKFRSGE INCLFATSVA EEGLDIPDCN
LVVRFDLYNT LIQYVQSRGR ARHSSSTYAS MIERYNADHA ARLVEVREAE KLMQSFCETL
PEDRILHGID SEIDSILQGE EEKRTFIIRA TGAKLTYHSA LAILARYASS LQYEKETSAQ
ATYVVLPQNN SFVCEVILPE KSPVRGLTGV PASKKSAAKQ SAAFDTCVLL RKHKLLDDHF
NSVYHRRLPA MRNARLAITS SRTNQYDMLS KPSLWGKQQG TLPEKLFATV ISFIPSEPLR
RRHRSIILLT RERLPDFPSF TIFLDDDIET IVVTESVEEA LHISSQELEY LSTFTFRIFH
DVFHKTYAEE PEKLPYWVAP AETKKSKNVS DSKSLTDWEL LHLVHENEEI PSTLHPSSEA
LINRFVFDPW DGRYRYFTMA IDNTLHPSDP PPSFLPRRKF MESIMSYTLS GSKNARAGFL
SRCNWQQPVL EVELVRLRRN LLDKMTDTEK DVETRCFVCI EPLRISAIPE EIAASCLAFP
AIINRLDAYL IALEGCKTLD LSVKPEYALE AFTKDSDNTE EHRVQQIHVQ RGMGKNYERL
EFLGDCFLKM ATSISLFVQN PDDDEFDFHV NRMCLICNKN LFNTALKKEL YQYTRSRGFS
RHTWYPDGLT LLHGRDHRKK ISAESKHALR EKTVADVCEA LIGASLLSGG LHNQFDMAVK
AVTAVVDSPN HKALCWADYT SSYMLPKYQT QSPDGYELDL GRKVEEKLGY RFKYPRLLHS
AFTHPSYPST WAKVPCYQRL EFLGDSLLDM VCVDDLFYRY PDKDPQWLTE HKMAMVSNKF
LGALAVKLGL HTHLRHFSNP LQSQITHYAE EIQAAENESQ GAVDYWLVTK DPPKCLPDMV
EAYLGAAFVD SDFQFRVVED FFQRHVKSYF HDMTIYDTFA NKHPTTFLQN RLTNEYGCTN
YCLKAGEIPV VDGGTVSVLA AVIVHEVVIA EGTASSGRYA KVKASEKALS VLENMGPSEF
REKYHCDCRT ANGSQPMDIG TAI
