DCL1_CRYPA
ID DCL1_CRYPA Reviewed; 1548 AA.
AC Q2VF19;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Dicer-like protein 1;
DE Includes:
DE RecName: Full=Endoribonuclease DCL-1;
DE EC=3.1.26.-;
DE Includes:
DE RecName: Full=ATP-dependent helicase DCL-1;
DE EC=3.6.4.-;
GN Name=DCL-1;
OS Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC Cryphonectria-Endothia species complex; Cryphonectria.
OX NCBI_TaxID=5116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=17646660; DOI=10.1073/pnas.0702500104;
RA Segers G.C., Zhang X., Deng F., Sun Q., Nuss D.L.;
RT "Evidence that RNA silencing functions as an antiviral defense mechanism in
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12902-12906(2007).
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, ECO:0000269|PubMed:17646660}.
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; DQ186989; ABB00356.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2VF19; -.
DR SMR; Q2VF19; -.
DR OMA; HMRTGVL; -.
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; 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; 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; Repeat;
KW RNA-binding; Zinc.
FT CHAIN 1..1548
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306780"
FT DOMAIN 106..289
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 428..589
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 624..718
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1051..1197
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1248..1411
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1445..1518
FT /note="DRBM"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 232..235
FT /note="DEAH box"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1397
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1400
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1489
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1393
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1548 AA; 176667 MW; 91B533E9EF72349B CRC64;
MGDPAAHEMA DLERGFSSED DAEYRSGDDE ASKFVENEPS KRGKISQKKK IEQTNFAKWM
DTNQKSLTRK AVKQSVNQDN SLAYMIRSWE GGEKIITSPR DYQMELFERA KQQNTIAVLD
TGSGKTLIAA LLLDHTVNQE LEDRAKGLPR RIAFFLVEKV ALAFQQHAVL ECNLAHSVAV
FSGESIKNTW TKGFWETQLA DHEVIVCTAE ILNQCLQYAY IRIDQINLLV FDEAHHTKKN
HPYARIIKDY YASGKDRGLR LPRIFGMTAS PVDALIDVRQ AAIELEGLLH SRIATTADPD
ALRRAVGRPK KEIIYKYNPL VKPIQTMLTF KLRPLIANNK QFSKAFAFSE AAARELGTWF
VDRMWQLFLE DEELLKLEAK TERSLSKDMA APEVVEKHRN AVRSARELIR SHEFPKPEPG
LLSSKLKTLS KLLEEYFTDS SIRCIVFVER RWTAKLLTDF FESHAAEIPG LKVGSLMGAN
AEGGSSQTSF REQIRTILSF KKGNTNCIFA TSVAEEGLDI PDCNLIIRFD ICKTMIQYIQ
SRGRARQADS TYIHLIEGGN GDHRRIMHQN AENEKLLRRF CNTQPEDRLL KGSDYDMDFF
LRQERNQRQY TIKSTGARLT YKNSLPILQA FLNTLRNQDD YAEGMDLVAD YSILSVQGGF
ICEVMMPPLS PVTSAIGKVY STKQVAKCSA AFELCFQLIQ KKFLDDHLRS KFVEKRHVMA
NARLAVSSKN KAKYDMRLKP QIWAELGVPE KLYATVLILS KPSALERPSR PLFILTRTPL
PQLKPFLLFL GPVEQEMTSD LVCQVLNCPI TPTEEDLQLL TKFTLKIFVD IFNKKYAANA
QALPYFFAPT NKDHVFLFSN LQDPRNAVDW PLLRHVADRD AEAYTGDEPE EFFQDKYIVD
PHDGARRFWL QGIRKDLTCT SPVPADVEHQ PTHRQWKRRE VPHDILHWSL TAWKATREAH
ENKWKENQPV VVGKYATLRR NFLADINETS KNPFCYFVLE PMRISPLPVD VVAMAYLLPS
IIHRIEQNLI ALDACRLLQL DIHPDLALEA LTKDSDNQGE DERMDSIQAF EPVNFQPGMG
ANYERLELLG DSFLKMATTI AVFTLIPNKD EFDYHCERMV MICNQNLFGV AKSDDLKLHE
YIRSKSFERG TWYPVLKLEF GKTHLKTLKQ MDEHRLADKS IADVCEALIG AAYMTTRKHD
DYDLAVRAVT RLVNHKQHPM TKWDDYHAAY VMPGWQTMPA NAAELDMAQK IHEATGYQFK
HPRVLRSAFR HPSRPYVFDK VPHYQRLEFL GDALFDMACV DYLFHIAPDE GPQWLTEHKM
AMVSNQFLGC LAVSLGFHKF ILHHHASIGS QIHEYVTEIT EARRAAEDAA EAAGKPRSAY
SRDYWVEAPQ PPKCIPDVLE AYVGAIFVDS KYDYSVVQQF FHAHVLPFFA SMRMYDTFAN
KHPVTFFTQY VFETFGCHAY GLHAEEMPVK DDTGLVTGKT QVVAGILLHG QVVEGAVRDS
GRYAKIAAAR KALDKLRSMT RQEFLDAYKC DCKPGEAAED ISESATAI
