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Database: UniProt
Entry: Q0CEI2
LinkDB: Q0CEI2
Original site: Q0CEI2 
ID   DCL2_ASPTN              Reviewed;        1377 AA.
AC   Q0CEI2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   31-JUL-2019, entry version 68.
DE   RecName: Full=Dicer-like protein 2;
DE   Includes:
DE     RecName: Full=Endoribonuclease dcl2;
DE              EC=3.1.26.-;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase dcl2;
DE              EC=3.6.4.-;
GN   Name=dcl2; ORFNames=ATEG_07902;
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=EAU32164.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; CH476604; EAU32164.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001216523.1; XM_001216523.1.
DR   STRING; 33178.CADATEAP00000498; -.
DR   PRIDE; Q0CEI2; -.
DR   GeneID; 4322847; -.
DR   EuPathDB; FungiDB:ATEG_07902; -.
DR   HOGENOM; HOG000048683; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
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; PF00270; DEAD; 1.
DR   Pfam; PF03368; Dicer_dimer; 1.
DR   Pfam; PF00271; Helicase_C; 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.
FT   CHAIN         1   1377       Dicer-like protein 2.
FT                                /FTId=PRO_0000306790.
FT   DOMAIN       23    203       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      367    544       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      563    657       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      916   1056       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1090   1274       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   NP_BIND      36     43       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       144    147       DEAH box.
FT   METAL      1129   1129       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1260   1260       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1263   1263       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1256   1256       Important for activity. {ECO:0000250}.
SQ   SEQUENCE   1377 AA;  155084 MW;  2ED8ACB6EEC6588D CRC64;
     MASLSDQDLE MGLFCPRNYQ TEMFEASLQE NIIVAMDTGS GKTHVALLRI MNELETRRPQ
     KLIWFLAPTV ALCFQQHDVI TKNLPAVKSR TLTGQDKVEL WTEQAIWDAI LKDMQVVVST
     HAVLADAMSN GFVRVSQLGL LIFDEAHHCM RRHPANRIMQ DFYHPTLVKQ GPDAVPGILG
     LTASPVVRTN SQELSMIESN MNAICKTPRA HRQELLTHTH RPHLQQIWYT PVNIDDPTSG
     TRTLRALIHA WETIDLEDDP YVKQLRRSTF DGKALQKALL TRKTYCNESL RRFVERSCHI
     FQELGGWAVD YFIHASIRRL REKIDDSALM LDWDNEEKEY LASFLSNIAT IQSDPPRRPE
     DFIPSPKLEA LISFLSSTDD STFSGLIFAK QRATVTVLAT LLSVHPLTKD RFRCAAFVGW
     SGGGNRKDLI GELLSMQMQR DTLSEFRSGQ KNLIVATDVL EEGIDISACS VVICYDKPAN
     VKSFVQRRGR ARRKESTFAI LFSTDDELCD LRKWQLLEEA MIEAYQDDER KRCEALALET
     MAEVVTERFE VESTGAVLTA DTAVARLHHF CSILPQQPYV DNRPELSFEY DGTGRRRGTF
     KLPSCVHPDV RRTRGEKWWT TERAATKEAA FQTCKRLYEF GLLNDHLLPL TRKPELRLTD
     FGGLPSIIEV AEQYDPWTDW AYSWSSPDIH QSRIRVQLNG NPEYQLSMSL MGPTVLPALD
     AMTLFWDSQN IFTLAFDAAQ RVPLVPGDVI EHMRAITALY LQAPSSRSIR EERDYVALFG
     PDLPHTELGA WLLKNGGNDT ALDVYSRQVA SPTMGIVRDR TRYDEPLLFK KWVVTEDGDV
     AVVEMECHSL PKRRNLLQRQ TLAQGEIVTT AVDTAPAKAR IIPATACTID RLPFTDTIFG
     LFISAILDRL EATLIATRLC ETILQDVQFS STRHVITAIS APTAQSPTDY QRYEFFGDSV
     LKFTVSCQLY MQHPNWPEGY LSEGRDEIVQ NNRLARAALD VGLDAFILTR RFTPRKWTAP
     LISEKAVEVA GKRPLSSKVL ADVVESLIGA AYMDGGQAKA HTCIRRLLPE IEICPITPPP
     VHESAPHVMN DSLKQHLGYT FVNEALLVEA LTHPSCRSDA STQSYQRLEF LGDAVLDMVV
     VHAMAHHAVE CPQGEMTMIK HALTNANLLA FFCMEFVVAQ EHTDVDAVPA AGGFALRSEQ
     KPIELWRFMR SEALDLNNAR ETVLHRHSQL RAEIVHALHH GAQYPWQALS QLNADKFFSD
     IVESILGAIF VDSRGDLDVC AMFVERIGLL PYLRRILADR VDVMHPRHTA QRLSKGEALF
     TAKRVVDGSG NASYRCVVKR NKEEIVVVEG CLSSEEAEVK AANATIGILR ANAVNLV
//
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