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Database: UniProt
Entry: Q2U6C4
LinkDB: Q2U6C4
Original site: Q2U6C4 
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   31-JUL-2019, entry version 86.
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.
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.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., 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-
CC       stranded RNA in the RNA interference (RNAi) pathway. Produces 21
CC       to 25 bp dsRNAs (siRNAs) which target the selective destruction of
CC       homologous RNAs leading to sequence-specific suppression of gene
CC       expression, called post-transcriptional gene silencing (PTGS).
CC       Part of a broad host defense response against viral infection and
CC       transposons (By 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};
DR   EMBL; AP007166; BAE62891.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001824024.2; XM_001823972.2.
DR   PRIDE; Q2U6C4; -.
DR   HOGENOM; HOG000048448; -.
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: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   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; PF03368; Dicer_dimer; 1.
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; Complete proteome;
KW   Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat; RNA-binding; Zinc.
FT   CHAIN         1   1523       Dicer-like protein 1.
FT                                /FTId=PRO_0000306776.
FT   DOMAIN      123    304       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      444    617       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      640    730       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN     1031   1190       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1241   1392       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1426   1494       DRBM.
FT   NP_BIND     136    143       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       249    252       DEAH box.
FT   METAL      1281   1281       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1378   1378       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1381   1381       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1438   1438       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1465   1465       Zinc; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1506   1506       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1508   1508       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   SITE       1374   1374       Important for activity. {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
//
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