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Database: UniProt
Entry: A1C9M6
LinkDB: A1C9M6
Original site: A1C9M6 
ID   DCL2_ASPCL              Reviewed;        1389 AA.
AC   A1C9M6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-OCT-2019, entry version 73.
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=ACLA_055980;
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}.
DR   EMBL; DS027048; EAW13550.1; -; Genomic_DNA.
DR   RefSeq; XP_001274976.1; XM_001274975.1.
DR   STRING; 5057.CADACLAP00005115; -.
DR   PRIDE; A1C9M6; -.
DR   EnsemblFungi; EAW13550; EAW13550; ACLA_055980.
DR   GeneID; 4707091; -.
DR   KEGG; act:ACLA_055980; -.
DR   EuPathDB; FungiDB:ACLA_055980; -.
DR   HOGENOM; HOG000048683; -.
DR   OMA; PTVALCE; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000006701; 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   1389       Dicer-like protein 2.
FT                                /FTId=PRO_0000306785.
FT   DOMAIN       23    203       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      368    537       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      564    658       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN      920   1060       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1099   1282       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      1138   1138       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1268   1268       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1271   1271       Magnesium or manganese. {ECO:0000250}.
FT   SITE       1264   1264       Important for activity. {ECO:0000250}.
SQ   SEQUENCE   1389 AA;  156806 MW;  EA8AAF2FA35F7D55 CRC64;
     MSSAVPTNSD AAAYQARNYQ LEMLEASMKE NIIVAMDTGS GKTHIAVLRI KAELDSCPPD
     KIIWFLAPTV ALCTQQHKVI ASNLPAVQTR TLTGLDKVEL WTEQAIWDAI LKDVRVVVST
     YAVLADALSH GFMRMSRLAL IIFDEAHHCM RKHAANKIMQ DFYHPTVSKF GPSAVPRIMG
     LTASPVVRSN REELFTIETN LDAVCKTPRA HRQELLKFSH RPELKQLLYE PPDPMGLQVS
     SQTLRALIEA WETLDIEDDP YVKRLRKSSL DGGALEKALM TGKTFCREQL KRFVDRSRHI
     FEELGEWAAD YYIYTSIQHL KTRVQTSYMT GDWDEAERAY LVSFLSKLPA ADIQITLSDA
     ACLRISPKLE ALIGFLDAMD DPEFSGLIFV KQRATVSVMT DLLAVHPRTR ERFRSAAYVG
     WSNSSGSKDF LGNLLSMHGQ LSTLDDFRSG HKNLIIATDV LEEGIDISAC SVVVCYDKPP
     NLKSFVQRRG RARQKQSTYA IMFPAEDSAF DLAKWQTLEQ AMIEAYQDDE RHLQSAIELE
     RVNEEVVERF TVESTSAVLT ADTAMAHLHH FCAVLPSQPY VDMRPVFSVE TDIANLRRGI
     VILPNCVHPK VRRSEGQRWW RTERAAMKEA AFQAYKSLYE FGLVNDNLLP LTNKPELKVN
     KLGSIPSIME ASEQYDPWVD WAYSWSSPDI HQSRVVVRLN GAKDRELCMR LAGPTVLPPL
     APMTLFWDSE TTFTVAFEAP ERVPHVPLSS VEDMRTSTVV YLQATSSRLL STKQDFTALF
     GPDLPHTDLK AWLQMYEGNE PAVEVYSRRR DPMLMGVVRD CSRYNEPLLF RRWVESGDSP
     TTSVVEMECD PFPRRRNLLH RQTLATKKLE NDKEDTPEPV NKMRTVAADQ CTIDRLPFSN
     AILGLFISVV VQQLETELIA TKLYETILRD VGFTSTQHII TAISAPSAQA LTNYQRYEFL
     GDSILKFSVS CQLFFKHPNW HEGYLSEGRD EIVQNPRLTK AALDTGLDAF VITKMFTPRK
     WSAPLISERL ERVAGKRQVS SKVLADVVEA LIGAAYMDGG HAAAQACIRR FLPEINLHSL
     DTRTLSRSVA PEGARQTIHD RLKRHISYTF ENESLLVEAL THPSCDYDAS TQSYQRLEFL
     GDAVLDMIIV SAIFNHPVQM PQGHMTKIKH ALVNANLLAF LCMEFAIPEE RASVEQISTL
     QFEVISNEEL VELWRFMRYR GLDLNNARDA SLARHRALRD EILHSLQHDP HYPWQALSRL
     SADKFFSDIM ESILGAIFVD SGGDLAPCEA FVERIGLMSY LRRILDENIE VTHPRNVAQQ
     LAKSNIQFLA QRMPDEEGGA SYQCAVRIEE VEAFVVRGCL TAEEAEVTAA IDAIDLLMER
     VNGSASVAS
//
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