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DCL2_COCIM
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   03-AUG-2022, entry version 91.
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; Onygenaceae; 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., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   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-stranded
CC       RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs
CC       (siRNAs) which target the selective destruction of homologous RNAs
CC       leading to sequence-specific suppression of gene expression, called
CC       post-transcriptional gene silencing (PTGS). Part of a broad host
CC       defense response against viral infection and transposons (By
CC       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}.
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DR   EMBL; GG704914; EAS34409.3; -; Genomic_DNA.
DR   RefSeq; XP_001245992.2; XM_001245991.2.
DR   AlphaFoldDB; Q1DW80; -.
DR   STRING; 246410.Q1DW80; -.
DR   EnsemblFungi; EAS34409; EAS34409; CIMG_05433.
DR   GeneID; 4562885; -.
DR   KEGG; cim:CIMG_05433; -.
DR   VEuPathDB; FungiDB:CIMG_05433; -.
DR   InParanoid; Q1DW80; -.
DR   OMA; HFCAVIP; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000001261; 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:0031047; P:gene silencing by RNA; IEA:UniProt.
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   Gene3D; 3.40.50.300; -; 2.
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; 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; 2.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   3: Inferred from homology;
KW   Antiviral defense; Antiviral protein; ATP-binding; Helicase; Hydrolase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Repeat; RNA-binding.
FT   CHAIN           1..1435
FT                   /note="Dicer-like protein 2"
FT                   /id="PRO_0000306791"
FT   DOMAIN          54..234
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          400..564
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          591..684
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT   DOMAIN          956..1099
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1141..1323
FT                   /note="RNase III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   MOTIF           175..178
FT                   /note="DEAH box"
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1178
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1312
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            1305
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
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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