DCL1_MAGO7
ID DCL1_MAGO7 Reviewed; 1591 AA.
AC A4RKC3; G4MTF7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
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; Synonyms=MDL1; ORFNames=MGG_01541;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
RN [2]
RP FUNCTION.
RX PubMed=15304480; DOI=10.1074/jbc.m408259200;
RA Kadotani N., Nakayashiki H., Tosa Y., Mayama S.;
RT "One of the two Dicer-like proteins in the filamentous fungi Magnaporthe
RT oryzae genome is responsible for hairpin RNA-triggered RNA silencing and
RT related small interfering RNA accumulation.";
RL J. Biol. Chem. 279:44467-44474(2004).
CC -!- FUNCTION: Dicer-like endonuclease which seems not to be involved in
CC cleaving double-stranded RNA in the RNA interference (RNAi) pathway,
CC contrary to its DCL2 counterpart. {ECO:0000269|PubMed:15304480}.
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; CM001232; EHA54708.1; -; Genomic_DNA.
DR RefSeq; XP_003714515.1; XM_003714467.1.
DR AlphaFoldDB; A4RKC3; -.
DR SMR; A4RKC3; -.
DR STRING; 318829.MGG_01541T0; -.
DR EnsemblFungi; MGG_01541T0; MGG_01541T0; MGG_01541.
DR GeneID; 2679399; -.
DR KEGG; mgr:MGG_01541; -.
DR VEuPathDB; FungiDB:MGG_01541; -.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_3_1; -.
DR InParanoid; A4RKC3; -.
DR OMA; WQQYMEP; -.
DR OrthoDB; 1337630at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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;
KW Reference proteome; Repeat; RNA-binding; Zinc.
FT CHAIN 1..1591
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306781"
FT DOMAIN 115..298
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 439..607
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 639..729
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1050..1190
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1243..1406
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1440..1514
FT /note="DRBM"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..245
FT /note="DEAH box"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1392
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1395
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1388
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1591 AA; 180666 MW; BFB08E2247DD9A84 CRC64;
MEVHDGLKSP DKAAKSRYDD DRIDQDSEDE AVRLVANPDP SKPRKISERK RADQAAFESW
VNDNKIRLSL PSATKSRRSG IRELFSSDET LETRPTRTRP RERVIEGPRE YQIELFERAK
QKNTIAVLDT GTGKTLIAIL LIRHIIELEL GARWQGREKR ITFFLVDKVA LVRQQTDHIR
ANLDFPVTGL HGDTVRNLWY SKEYFEKLLQ EQEVVVCTAE ILYRCLHRSY LNISQVSLVV
FDEAHHAKKN HVYARIIKDF YLMEEDCQKR PRIFGMTASP IDTKDTCISY ERATHELESL
LHSEIATISD RDLLKVIGSR PQEVRKSYAR VLRQENTELC NQLRELVGNH PLFKQTFDSA
EFAVTELGAW CADKLWELCF REEAVSTLDG RVEGSRARDP DEVGESSHEV SNAREALSLV
QQWSFSPPED GSLSTKTHKL IEILAECFSQ ASAGNAIQCI VFVKRRDTAV LLNALCEQAE
IRTKIPDLKG AFLIGAGRGG NAAFTTTRQQ EQTVSRFRDG EINCLFATSI AEEGLDIPGC
NVVIRFDLHG TTIQYIQSRG RARMRNSWFI HMTEFGNPEH NRRWFQDRVN EQKMRDFCLS
LPKDRIMEKA EVDDVLRGDQ SQKIFVVPGS KASLTFKQSL VVLAEFVATL PARPDEILSV
DYTVVPVFGG FQGEVYLPAS SPLRSAMGGV YRSKQLAKCA AAYAMCIQLY NSNYLDDHLK
STLAKVLPAM RNARLAVSSK KRKSYNMRTK PVLWSEVGPL TELYAMVLSL AQPGAAYYHS
RPILLLTRKP LPEIAQFPLF FGKGSSRRSN VRCIPLAHPW SPTTTQVEGI CAFTLCIFRD
IFSKDFQASG TDMPYFLAPS TGIEHGTDLS SLVNPERIID WATVHRTTTT DRVPYNFNEP
DEFFQDKYVS DPFDGSRKFF MRKVRRDLKP QDKVPEGVPA PSKWRAVEHT ILNYSVSLWK
KSRAGHNSRQ DQPVVEAELA PLRRNLLDET DGENSTGPQT CYLVLETLLI SQIPVDTVVM
AYTFPAIIYR LENSLISLEA CQNLGLDIPI DIALIAMTKD SDNSDDHDEA PINFQSGMGQ
NYERLEFLGD CFLKMATSIA LYTLVEGDEF EYHVERMLDI CNKNLLNWAL ESNLQEHIRS
KSFNRRTWYP PGLKLLKGKK TEVDDEHALG DKSIADVCEA LIGAAYLTAQ AQSSPNFDLA
VKAVTVMTHS KTHTMQAWSD YYASYQCPEW LSTPPSQTQL ELCSQIKNKM GYRFKNPRLL
RCAFMHPSYP RQYENIPSYQ RLEFLGDSLL DMVCVDYLFK KHPDKDPQWL TEHKMAMVSN
QFFGCVAVGL GFHRHLIHMQ PALGGSITEW AELVTKKREE ARQLAVRRGQ REEDYARDFW
IEVHHPPKCL PDILEAYVGA LFVDTGYDYS AVVGFFDRHI KPYFADMSIY DMYSSKHPVT
HITSIITTQF GCSSFRLMVH EIPDDVQGEG LVTGAVKVVA ACMIHGEVRC HAVAASGRYA
KLAVAKQAVA IYEDMSPTEF RLRHGCNCKP EDGDGDHGVL VDHRADCEPE EPLRKQDPPA
KSVVDVDGKT IAEMRLRHSK QMNDQEECLS W
