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
