ID N1JIN0_BLUG1 Unreviewed; 1588 AA.
AC N1JIN0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Dicer-like protein 1 {ECO:0000256|ARBA:ARBA00020797};
GN ORFNames=BGHDH14_bgh00835 {ECO:0000313|EMBL:CCU83033.1};
OS Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS (Oidium monilioides f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU83033.1, ECO:0000313|Proteomes:UP000015441};
RN [1] {ECO:0000313|EMBL:CCU83033.1, ECO:0000313|Proteomes:UP000015441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DH14 {ECO:0000313|EMBL:CCU83033.1};
RX PubMed=21148392; DOI=10.1126/science.1194573;
RA Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT extreme parasitism.";
RL Science 330:1543-1546(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000256|PROSITE-ProRule:PRU00657}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCU83033.1}.
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DR EMBL; CAUH01007419; CCU83033.1; -; Genomic_DNA.
DR STRING; 546991.N1JIN0; -.
DR EnsemblFungi; BLGH_05892-mRNA-1; BLGH_05892-mRNA-1; BLGH_05892.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_3_1; -.
DR InParanoid; N1JIN0; -.
DR OrthoDB; 342391at2759; -.
DR Proteomes; UP000015441; 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:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; cd18034; DEXHc_dicer; 1.
DR CDD; cd00593; RIBOc; 2.
DR CDD; cd18802; SF2_C_dicer; 1.
DR Gene3D; 3.30.160.380; Dicer dimerisation domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 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 PANTHER; PTHR14950:SF62; DICER-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR14950; DICER-RELATED; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 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 {ECO:0000256|ARBA:ARBA00023118};
KW Antiviral protein {ECO:0000256|ARBA:ARBA00022721};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000015441};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00657}.
FT DOMAIN 155..337
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 483..651
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 684..774
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 1129..1240
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1291..1455
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 181461 MW; C6E6569802800558 CRC64;
MSSNHKPEAS TTPTIIARSE EDLISELSTQ PATDLRDRTR LNSACLSIKT DESSATESSK
LTPSEQYNQD NSEDSDDENK QEKPKTISES LKVAERKRRQ NAVAAEYIKN INKKLVKEAN
KQQPGDDANQ STKWLVNQSE NRKIISTPRE YQVELFNRAK QNNIIAVLDT GSGKTLIAVL
LLRHIISQEL EDRALGKNRR ISFFLVDSVQ LVFQQHAVLK ANLNSPMAMF CGDMGCDLWS
KELWENHFQE NEIIVCTAEI LRQCLHHSFI RIKDINLLIF DEAHHAKKDH AYARIIKDFF
ATQQADSCLP RIFGMTASPV DARVDVRKAA SELETILHCQ IATIDDENLF QLSYKNNGKT
EQLARYASLP PKFKTPLYQQ MYDCFFKNKI LIKPLLFSYQ ASSELGAWCS DQIWLFCLSD
NETKKLLAKA ECQGGQQNFE PELEVIEKTV SQIQNAKEII QNHVFNPPDY SDSQSWSNNL
SSKVVLLIRY LRERFERETT DKCIIFVKQR YTARVLTRLL EQERIKTKWL RVGALVGTRS
GEAGDLNTSF RDQVITMMQF RKGRLNCLIA TSVAEEGLDV PDCNLVIRFD LYTTLIQHIQ
SRGRARHANS NYIHFCEAGN QDHSRIIMEV RKNESILRDF CRMLPEDRKL TGNDITIDDI
LAKEKYNRVI KIPETGAQLN YKMSLVVLAN FVDRLPNAAD GNLQVEYIMM STLKKFQCEA
ILPESSPVRG AIGEWCSTKQ VAKCSAAFET CLKLLEGKYL DNWLIPTFSR KILPAMRNAK
LALDSKKRSA YTMRTKPKLW SITSTTPEFY VNVLVLEQPE SVGRKTQPLA LLTRSHMPQL
PSFMLHFGGG CNSLAHCISL GSIKLDADMI EQINTFTLCI FNDVFSKCYE SDSSKMPYFL
VPAKDSFTFR DHNIDPFQVV DWEAVTQMAE YQLKWSKDQW GDKSWMTEKD EFLADRFIID
PYDGSRKLYS IGVTKDYKPL DPVPPKTAPR SGARKNNDNI MEYSCSLWAK ARAQREFDVN
QRVVEAEYIS LRRNLLDEFD VLEDHTPKQC FIILEPLKIS QLSTKVVAMA YIFPALIHRI
ESYLIALEAC ELLHLEIRPD LALEAVTKDS DNSGQDDETQ INFQRGMGNN YERLEFLGDC
FLKMATSISL YGLQPENNEF AYHVDRMLLT SNKNLKDNAL KLKLYEFIRS QSFNRRAWYP
EGLVLLKGKT AKAPKSHDLA DKTIADVCEA LIGAALLSYH ETKNMDMAVR AVTELVCSEH
HRATSFSDYY KLYVKPKYQI QPSTQSQLLL ASDTEKQHPY KFRYPRLLCS AFTHSSFPRS
FNGKVPSYQR LEFLGDALLD MVCINYLFHN FPNKDPQWLT EHKMAMVSNM FLGALCVHLG
FHRHLLVFNS TFMQQIGDYI VEVTEARLQS EKEATDAGKP LDDCSPDYWI SVRQPPKCLP
DIVEAYIGAI FVDSEYDYAE VEKFFDAHIA WFFRDMSVYD TFANNHPTTF LSNFLEVSMG
CHAWSMKVGD IPNDDGGKGS IVVMVIIHGT VIAHARAESS RYAKINAAKS AMELLDGIGL
GEFRVRYECD CKPTFTGSEK PREDDSKG
//
