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Database: UniProt
Entry: Q1DKI1
LinkDB: Q1DKI1
Original site: Q1DKI1 
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   31-JUL-2019, entry version 81.
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; Onygenales incertae sedis; 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). {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; GG704915; EAS27978.3; -; Genomic_DNA.
DR   RefSeq; XP_001239561.2; XM_001239560.2.
DR   PRIDE; Q1DKI1; -.
DR   EnsemblFungi; EAS27978; EAS27978; CIMG_13589.
DR   GeneID; 24165216; -.
DR   KEGG; cim:CIMG_13589; -.
DR   EuPathDB; FungiDB:CIMG_13589; -.
DR   eggNOG; ENOG410INVH; Eukaryota.
DR   eggNOG; KOG0701; Eukaryota.
DR   eggNOG; COG0571; LUCA.
DR   eggNOG; COG1111; LUCA.
DR   InParanoid; Q1DKI1; -.
DR   KO; K11592; -.
DR   OMA; FNMYVQT; -.
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: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; 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; PF03368; Dicer_dimer; 1.
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; Complete proteome;
KW   Helicase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat; RNA-binding; Zinc.
FT   CHAIN         1   1500       Dicer-like protein 1.
FT                                /FTId=PRO_0000306779.
FT   DOMAIN      106    287       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      426    597       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      623    713       Dicer dsRNA-binding fold.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00657}.
FT   DOMAIN     1061   1172       RNase III 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1223   1374       RNase III 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00177}.
FT   DOMAIN     1408   1476       DRBM.
FT   NP_BIND     119    126       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       232    235       DEAH box.
FT   METAL      1263   1263       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1360   1360       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1363   1363       Magnesium or manganese. {ECO:0000250}.
FT   METAL      1420   1420       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1447   1447       Zinc; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1488   1488       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   METAL      1490   1490       Zinc. {ECO:0000250|UniProtKB:Q09884}.
FT   SITE       1356   1356       Important for activity. {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
//
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