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Database: UniProt
Entry: Q1DW80
LinkDB: Q1DW80
Original site: Q1DW80 
ID   DCL2_COCIM              Reviewed;        1435 AA.
AC   Q1DW80; J3KG17;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   19-FEB-2014, entry version 52.
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=CIMG_05433;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; mitosporic Onygenales; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J.,
RA   Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E.,
RA   Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M.,
RA   Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J.,
RA   Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens
RT   Coccidioides and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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).
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC   -!- SIMILARITY: Contains 1 Dicer dsRNA-binding fold domain.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 2 RNase III domains.
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DR   EMBL; GG704914; EAS34630.2; -; Genomic_DNA.
DR   RefSeq; XP_001246213.1; XM_001246212.1.
DR   GeneID; 4563993; -.
DR   KEGG; cim:CIMG_05654; -.
DR   OrthoDB; EOG76QFRP; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
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:0006200; P:ATP catabolic process; IEA:GOC.
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:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 1.10.1520.10; -; 3.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR014720; dsRNA-bd_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   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; SM00358; DSRM; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF69065; SSF69065; 3.
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; 2.
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   1435       Dicer-like protein 2.
FT                                /FTId=PRO_0000306791.
FT   DOMAIN       54    234       Helicase ATP-binding.
FT   DOMAIN      400    564       Helicase C-terminal.
FT   DOMAIN      591    684       Dicer dsRNA-binding fold.
FT   DOMAIN      956   1099       RNase III 1.
FT   DOMAIN     1141   1323       RNase III 2.
FT   NP_BIND      67     74       ATP (By similarity).
FT   MOTIF       175    178       DEAH box.
FT   METAL      1178   1178       Magnesium or manganese (By similarity).
FT   METAL      1309   1309       Magnesium or manganese (By similarity).
FT   METAL      1312   1312       Magnesium or manganese (By similarity).
FT   SITE       1305   1305       Important for activity (By similarity).
SQ   SEQUENCE   1435 AA;  162531 MW;  A7633F0AFD7D44FD CRC64;
     MSAHTTAEQS PKRRRIHLDN DSKMHFSSIL EDGTSKSQEA LLPPRRARGY QLEMLSESLR
     QNIIVAMDTG SGKTEIAILR IQRELERCPA HKFVWFMAPT VALVEQQHSA ISKQLPAFQT
     RLLTGAANVS HWSTKKIWDD ILLNIRIVIS TPQVLLDALS NGFVDLHTIS LLVFDEAHHC
     VRDAPANRIM RDFYHYHRQE EGTDGLPHIL GLTASPTTRA RQTDLEVLEI NLNAVCVTPK
     MHREEMMQFV HMPEYRSIEY QPDVQNFSSI VEKLSVIINE LDIENDPFVK FMRRRNDLKS
     RQRLLDALEN KKTPCLDQLK RCLRRSRVIH RELGPWASER FLTRCIMGLK SKQTNASGPQ
     WADWDREDNS YMLNVLSQVV SSTEMGVQNP PDELSRKVHK LIDFLVLEHV NGSIGIVFAE
     ERTIVIMLAQ LLSLHPRTKH IKTTAFLGSS ASVSRKSDIT ELHNPIDQST AIDDLRTGKK
     DLIIATAVLE EGIDVPICDL VICFDLPKDL RSFIQRRGRA RKKGSKFALF LHSEDRATSS
     ELHLMEKTMK QLYLENKRAL EHIQYLENVE EEGYDGFRVA STGALLTLSN ARNHLSHFCG
     TLSAEFIATD PEFVLEGDDT TGFSAKVILP SFLDPKLREF RGILLWKTEK MAKRDASFQA
     YVALYEAGLV NDYLMPAHHH IDDEDGLEQV EKRPSFAKAL GSLNPWAAIA KKWREAKHFY
     QNLIEISAGA QAFPPMVMVL PVELPCDISF RLFWNEHSTL LVSVKRGGQD FAADLIRLAA
     DTTSILLSSL FSQKMVPGSL DFSWLFLPQM ESIPSAIREW CDSVTGTISL HDIRDCDMAG
     FENPGLVRPM DNTARPCTFE KLVWRKYVPA ETSDGASLSE QVTYDREVPH IEGRVWPKRT
     DFLHRLEPSN TSKAHHTAKC FYPANNCSVD RLPVEYSQFA LFIPCLIHSI ENYFIANELA
     QTILHPVGFS NLSLVLTAIS SSAAREASNY QRLEFLGDSL LKLHTSIQLA ADHPLWPEGR
     LTMRKGNIVS NGYLANAALQ TGLDKFILTK PFTGAKWRPS YNTDHINTGD MTEPTREMST
     KVLADVVEAL IGAANIDGGE NKILNCLKIF IPDIKWSPLN ECVNILHHQE DSFSDENNNM
     LSEIEGLVGY TFKKKPLLLA AVTHPSSKGS GHSYQRLEFV GDSILDIIVV QELFESPRCF
     HHFDMHLMRT ALVNADFLAF LCMNAYREED RGEAVENSKR RVTVAMTKRR AYLWGFMKHS
     ASWDIVNAQQ RAAKQYEKLH EEIDEKLRSS KTYPWTLLCR LDAAKFFSDI VESILGAIFI
     DSQGSMPACR IFLERIGLIP YLKRVLSEDL DLMHPKERLG LLAGTLSVKY ETKRTQGVEP
     QRWECAARVG DEEVVRVDCR VSRVDAETTA AEAAVAILKT RKLQSEASNK VAECD
//
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