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Database: UniProt
Entry: A1DE13
LinkDB: A1DE13
Original site: A1DE13 
ID   DCL1_NEOFI              Reviewed;        1538 AA.
AC   A1DE13;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   31-JUL-2019, entry version 87.
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=NFIA_075500;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC
OS   A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
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}.
DR   EMBL; DS027696; EAW17620.1; -; Genomic_DNA.
DR   RefSeq; XP_001259517.1; XM_001259516.1.
DR   SMR; A1DE13; -.
DR   STRING; 36630.CADNFIAP00007382; -.
DR   PRIDE; A1DE13; -.
DR   EnsemblFungi; EAW17620; EAW17620; NFIA_075500.
DR   GeneID; 4586299; -.
DR   KEGG; nfi:NFIA_075500; -.
DR   EuPathDB; FungiDB:NFIA_075500; -.
DR   HOGENOM; HOG000048448; -.
DR   KO; K11592; -.
DR   OMA; FNMYVQT; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000006702; 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   1538       Dicer-like protein 1.
FT                                /FTId=PRO_0000306782.
FT   DOMAIN      134    315       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      460    619       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      652    742       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN     1044   1203       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1254   1406       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1440   1508       DRBM.
FT   NP_BIND     147    154       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       260    263       DEAH box.
FT   METAL      1295   1295       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1392   1392       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1395   1395       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1452   1452       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1479   1479       Zinc; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1520   1520       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1522   1522       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   SITE       1388   1388       Important for activity. {ECO:0000250}.
SQ   SEQUENCE   1538 AA;  174902 MW;  22BFCACC1932BB46 CRC64;
     MTEQISLVDV SSSVSLKGED SSNVALLRDL FINDVAASDP AESSADVHKD EHSSDNSDND
     NEAVPKPNDF SQRRRIQNAQ FEALLSKRTD ADSNEAIDRA PIALSDDELS IAHLVEKQDL
     GNGMLDPREY QIELFERAKT QNTIAVLDTG SGKTLIAVLL LRHTILNELD NRANGKPHRV
     SFFLVDSVTL AYQQAAVLRN NIDQNVAHFF GAMGTDLWDK RTWDEHLQRN MVIVCTAEIL
     NQCLLNSYVK MDQINLLIFD EAHHAKKDHP YARIIRDSYF KAQPSQRPRV FGMTASPIDT
     KGDITEAATR LETLLDSRIA TTSKITLLRE VVSRPIEKVW AYNRLESPFA TELYKLMDTR
     YGNIKVLEGV YRFAWHASSE LGKWCSDRAW WHALADDVLP KLEGNISKLV ESNTLNAEHG
     AVFKDIIRIR EASETVKNYS FADPELPGEL SPKVQLLRME LSKHFSDTTG TKCIVFTQKR
     YTAKILNELF TVLNIPHLRP GVLIGVRPGD IGGMNVTFRQ QFLALVKFRT GEINCLFATS
     VAEEGLDIPD CNLVVRFDLY RTLIQYVQSR GRARHCTSTY AIMVEKDNAE HEGRLKEIRE
     AEKIMQRFCE TLPEDRILHG NDHDLDSLLQ EEEGRRTFTV KSTGAKLTYH SAIAILARYA
     SSLQYEKETV PQVTYVVGHV SNAYVCEVIL PEKSPIRGLT GSPAIRKAVA KQSAAFDTCL
     LLRKHRLLDD YFNSIYHRRL PAMRNAKLAI TCKRTNEYDM LLKPSIWAKQ RTTPIDKLYG
     IHISLLPSKP LSRDHRPILL LTREKLPEFP AFSIYLDEDV ETKVLSYPLK HGLQISVDEL
     QSLTTFTLRI FRDIFHKVYE HEVQKMPYWL APAKALDGPG SGTNPRDWTD WDTVSFVHNN
     DEIPFTRDLN PDSLVNRFIF DNWDGRFRYF TVAVADTLQP SDPPPPSVPR RRHMNNIMNY
     TLSLSKNSRA RFFSGCDWNQ PVLQAELVRL RRNLLDKMTT QEKEMQTECF ICAEPLRISA
     IPTSIVSTCL AFPAIISRLD SYLIALEACD ELELVIRPDF ALEAFTKDSD NTEEHRGQQI
     HFQRGMGKNY ERLEFLGDCF LKMATSIALY TQNPDDDEFD YHVNRMCLIC NKNLFNTAIK
     KQIYRYIRSR GFSRHIWYPD GLTLLHGKDH SKKLLSEGKH ALGEKTIADV CEALIGASLL
     SGGPENRFDM ATKAVTALVD SPSHRVSCWK EYITLYTMPK YQTEKPRGSE DDLARHVEEE
     LGYHFTYPRL LASAITHPSL PSTWGYRVPC YQRLEFLGDS LLDMVCVEDL FRRFPDRDPQ
     WLTEHKMAMV SNKFLGALSV KLGFHRRIMA FSNPLQAQIT HYVEEIESAQ AESRGAVDYW
     VVAKDPPKCL PDMVEAYLGA IFVDSKFDFQ VIEVFFERQI KPFFEDMSIY DTFANKHPTT
     FLHNKLTNEY GCTNYCLKAG ELPTIDGAPA GVLAAVIVHG NVISEARSSS SRYAKVKASE
     KALAVLDGLL PFEFCQKYHC GCKETQNSSS AVEIGTAI
//
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