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Database: UniProt
Entry: A1CBC9
LinkDB: A1CBC9
Original site: A1CBC9 
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   31-JUL-2019, entry version 76.
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
OS   3887 / NRRL 1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   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-
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=EAW13047.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DS027049; EAW13047.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001274473.1; XM_001274472.1.
DR   STRING; 5057.CADACLAP00001180; -.
DR   PRIDE; A1CBC9; -.
DR   GeneID; 4706314; -.
DR   KEGG; act:ACLA_014840; -.
DR   EuPathDB; FungiDB:ACLA_014840; -.
DR   HOGENOM; HOG000048448; -.
DR   KO; K11592; -.
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: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   1534       Dicer-like protein 1.
FT                                /FTId=PRO_0000306773.
FT   DOMAIN      130    311       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      456    613       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      648    738       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN     1054   1199       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1250   1402       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1436   1504       DRBM.
FT   NP_BIND     143    150       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       256    259       DEAH box.
FT   METAL      1291   1291       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1388   1388       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1391   1391       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1448   1448       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1475   1475       Zinc; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1516   1516       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1518   1518       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   SITE       1384   1384       Important for activity. {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
//
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