GenomeNet

Database: UniProt
Entry: Q0CW42
LinkDB: Q0CW42
Original site: Q0CW42 
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   31-JUL-2019, entry version 70.
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.
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.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S.,
RA   White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C.,
RA   Denning D.W., 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-
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=EAU37054.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; CH476596; EAU37054.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001211270.1; XM_001211270.1.
DR   SMR; Q0CW42; -.
DR   STRING; 33178.CADATEAP00007720; -.
DR   PRIDE; Q0CW42; -.
DR   GeneID; 4316974; -.
DR   EuPathDB; FungiDB:ATEG_02092; -.
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: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; 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   1519       Dicer-like protein 1.
FT                                /FTId=PRO_0000306777.
FT   DOMAIN      116    297       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      431    601       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      634    724       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN     1026   1184       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1235   1387       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1421   1489       DRBM.
FT   NP_BIND     129    136       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       242    245       DEAH box.
FT   METAL      1275   1275       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1373   1373       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1376   1376       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1433   1433       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1460   1460       Zinc; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1501   1501       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1503   1503       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   SITE       1368   1368       Important for activity. {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
//
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