ID   DCL1_COCIM              Reviewed;        1500 AA.
AC   Q1DKI1; I9NPP4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Dicer-like protein 1;
DE   Includes:
DE     RecName: Full=Endoribonuclease DCL1;
DE              EC=3.1.26.-;
DE   Includes:
DE     RecName: Full=ATP-dependent helicase DCL1;
DE              EC=3.6.4.-;
GN   Name=DCL1; ORFNames=CIMG_13589;
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; GG704915; EAS27978.3; -; Genomic_DNA.
DR   RefSeq; XP_001239561.2; XM_001239560.2.
DR   AlphaFoldDB; Q1DKI1; -.
DR   SMR; Q1DKI1; -.
DR   STRING; 246410.Q1DKI1; -.
DR   PRIDE; Q1DKI1; -.
DR   EnsemblFungi; EAS27978; EAS27978; CIMG_13589.
DR   GeneID; 24165216; -.
DR   KEGG; cim:CIMG_13589; -.
DR   VEuPathDB; FungiDB:CIMG_13589; -.
DR   InParanoid; Q1DKI1; -.
DR   OMA; WQQYMEP; -.
DR   OrthoDB; 1337630at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IPR038248; Dicer_dimer_sf.
DR   InterPro; IPR005034; Dicer_dimerisation_dom.
DR   InterPro; IPR006935; Helicase/UvrB_N.
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; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 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; 2.
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; Helicase; Hydrolase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Repeat; RNA-binding; Zinc.
FT   CHAIN           1..1500
FT                   /note="Dicer-like protein 1"
FT                   /id="PRO_0000306779"
FT   DOMAIN          106..287
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          426..597
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          623..713
FT                   /note="Dicer dsRNA-binding fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT   DOMAIN          1061..1172
FT                   /note="RNase III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1223..1374
FT                   /note="RNase III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT   DOMAIN          1408..1476
FT                   /note="DRBM"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           232..235
FT                   /note="DEAH box"
FT   COMPBIAS        27..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         119..126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         1263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1360
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1363
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         1420
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q09884"
FT   BINDING         1447
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q09884"
FT   BINDING         1488
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q09884"
FT   BINDING         1490
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q09884"
FT   SITE            1356
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1500 AA;  170580 MW;  E6DD0401A9C33351 CRC64;
     MEEPQRINDE PNDSVVPDPA GPSEPAESDS EDEHTHPNNA DEPSIRRKQN LRFKELLSAR
     AEEITAEDIK EVIKATKDDE LSMSNLLAKQ DFASVIHDPR EYQVELFEKA KKDNIIAVLD
     TGSGKTLIAV LLLKHIIEQE LIDRSAEKPH RVSFFLVDSV TLVFQQAAVL QNNINQRVDK
     FCGAMETDLW NGETWERHLA KNMVIVCTAE VLYQCLLHAF VKMENINLLI FDEAHNAKKD
     HPYARIVKDF YLKDGNAKRP KIFGMTASPV DAKMDVVKAA RNLETLLNSQ IATASNLSLL
     RQSVPRPNEE VWSYDRLDQP FETRLYKELR SRFGDLRALE KLFTFSLKAS SNLGAWCADW
     VWSYALTEES LPKLEGRAAR TAMGNLPIAK IVRPEAEIQR IREASEIIRS HKFGDPAVRP
     ELLSPKVRRL HHELLKYFER HTDTKCIVFT EQRHTARILC DLFSRIGTKH LRPGVLIGVR
     SDASGGMNIS FRQQVLAVVS FRKGEVNCLF ATSVAEEGLD IPDCNLIVRF DLASTLTQYI
     QSRGRARHMN STFAHLVERD NFVHRESVNH LQSSEEIMKR FCISLPKDRI LNSDDVDALY
     ESDRNRKSYT VQTTGAKLTY SSSLVVLAHF ANSLQYEKET STVVSYYHRF TKNAFVCEVV
     LPEKSPIRGI VGKPASKKLI AKQSAAFETC LLLRKHGLLD DHFVSTYHKR LPAMRNARLA
     ISSKKSNQYD MKVKPKLWET SRGIIPTSLN IVVLGFRPRR LLHREYHPLV LLTREKLPHF
     PEFPLYLEDD IECDVICSSI SSGFQVSSHD LEVLTTFTLR IFQDIFHKVY DRDVGMMTYW
     LAPLNLSCDI SSSASRDLLD WGILQFVFDN PEIPWSSSNS AAFFANRFVY DRWDGRYRYF
     THGIDPSLRP SDPPPSSMAR RRHMGNIMDY CLSLFKNARK KFLENCDWTQ PVIKAEIIQL
     RRNLLDKRTN KEKIKEGDYY ICLEPLTISA IPASVAAFAF AFPAIISRIE SYLIALEACQ
     ELDLPISPEL ALEALTKDSD NTDEHRAQQI HFQRGMGKNY ERLEFLGDCF LKMATSISLF
     AMNPDNDEYD FHVKRMCLVC NQNLFKTAVR FKLYAFIRSQ SFSRRGWYPG GLTLLQGKGQ
     SKGATENKHA LADKTIADVC EALIGACCLL ASKNHRFDIA VKAVTALVSS DDHNVLNWEQ
     YSRLYSIPKY QTAVVDAAEL DLAAQVKKKL GYDFKYPKLL RSAFTHPSYP SAWARVPCYQ
     RLEFLGDALL DMACVEHIYH KHPDKDPQWL TEHKMAMVSN KFLGSVAVRL GLHSHLNHFS
     TSLQSQITNY VEEIEAAELE SGDPPDAWTL TSDPPKCLPD MVEAYIGAIF IDSGFSFEVV
     EEFFQKFLKK HFEDMTIYDT YANKHPTTYL HNRLAIDFGC SNYCLKAGEV PYVDGPGTRV
     LAAVIVHDEV VAEGVASSSR YAKLKASEAA LSKLEGLPPF RFREIYGCNC QAGQSEAGNE