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 06-MAR-2013, entry version 37.
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 (Chesnut blight fungus) (Endothia
OS parasitica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC Sordariomycetes; Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC Cryphonectria-Endothia 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
RT mechanism in fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12902-12906(2007).
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).
CC -!- COFACTOR: Magnesium or manganese (By similarity).
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC -!- SIMILARITY: Contains 1 Dicer dsRNA-binding fold domain.
CC -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SIMILARITY: Contains 2 RNase III domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; DQ186989; ABB00356.1; -; Genomic_DNA.
DR ProteinModelPortal; Q2VF19; -.
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 Gene3D; 1.10.1520.10; -; 3.
DR InterPro; IPR005034; Dicer_dsRNA_binding_fold.
DR InterPro; IPR006935; Helicase/UvrB_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR000999; RNase_III_dom.
DR Pfam; PF03368; dsRNA_bind; 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; SSF69065; RNase_III; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS50137; DS_RBD; FALSE_NEG.
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;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Repeat; RNA-binding.
FT CHAIN 1 1548 Dicer-like protein 1.
FT /FTId=PRO_0000306780.
FT DOMAIN 106 289 Helicase ATP-binding.
FT DOMAIN 428 589 Helicase C-terminal.
FT DOMAIN 624 718 Dicer dsRNA-binding fold.
FT DOMAIN 1051 1197 RNase III 1.
FT DOMAIN 1248 1411 RNase III 2.
FT DOMAIN 1445 1518 DRBM.
FT NP_BIND 119 126 ATP (By similarity).
FT MOTIF 232 235 DEAH box.
FT METAL 1288 1288 Magnesium or manganese (By similarity).
FT METAL 1397 1397 Magnesium or manganese (By similarity).
FT METAL 1400 1400 Magnesium or manganese (By similarity).
FT SITE 1393 1393 Important for activity (By similarity).
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
//
