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Database: UniProt
Entry: N1JNR7_BLUG1
LinkDB: N1JNR7_BLUG1
Original site: N1JNR7_BLUG1 
ID   N1JNR7_BLUG1            Unreviewed;       755 AA.
AC   N1JNR7;
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=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=BGHDH14_bgh04415 {ECO:0000313|EMBL:CCU82295.1};
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:CCU82295.1, ECO:0000313|Proteomes:UP000015441};
RN   [1] {ECO:0000313|EMBL:CCU82295.1, ECO:0000313|Proteomes:UP000015441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH14 {ECO:0000313|EMBL:CCU82295.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       DDX15/PRP43 sub-subfamily. {ECO:0000256|ARBA:ARBA00024333}.
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:CCU82295.1}.
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DR   EMBL; CAUH01006119; CCU82295.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1JNR7; -.
DR   STRING; 546991.N1JNR7; -.
DR   EnsemblFungi; BLGH_04576-mRNA-1; BLGH_04576-mRNA-1; BLGH_04576.
DR   eggNOG; KOG0925; Eukaryota.
DR   HOGENOM; CLU_001832_5_11_1; -.
DR   InParanoid; N1JNR7; -.
DR   OrthoDB; 3682876at2759; -.
DR   Proteomes; UP000015441; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IEA:EnsemblFungi.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0000390; P:spliceosomal complex disassembly; IEA:EnsemblFungi.
DR   CDD; cd17973; DEXHc_DHX15; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR044756; DHX15_DEXHc.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF109; ATP-DEPENDENT RNA HELICASE DHX15 HOMOLOG; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:CCU82295.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015441}.
FT   DOMAIN          100..265
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          290..472
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  85702 MW;  ADE18A997B44EC64 CRC64;
     MTEHRLADPE VSSAKRTKTN DLDPSINPYL AHYHEDEESS MKDKKDLTKW KRNRTTAKQA
     RLAEDGPNNP FNERPLSQNY FNILKTRRDL PVYKQRQEFL TMYQKSQILV FVGETGSGKT
     TQVPQYVLYD DLPHLNGKMV ACTQPRRVAA MSVAQRVADE MDVELGEEVG YNIRFEDVTG
     PKTILKYMTD GMLLREAMND HDLTRYSCII IDEAHERTLA TDLLMGLLKE IADRRPGLKI
     VIMSATLDAQ KFQKYFNEAP LLAVPGRTYP VEIFYTPEPE RDYVEAALRT VLQIHATEPE
     GDILLFLTGE EEIEDACRKI SLEADEMVRE ADAGPLKVYP LYGSLPPHQQ QKIFEPAPPP
     NRPGARPGRK VIVGTNIAET SLTIDGIVYV VDPGFSKQKV YNPRIRVESL LISPISKASA
     QQRAGRAGRT RPGKCFRLYT EHAFKTELID QTHPEILRSN LSNTVLELKK LGIVDLVHFD
     FMDPPAPETL MRALEELNYL ACLDDEGELT ALGQLASEFP LDPALAVMLI SSPEFYCSNE
     ILSLTALLSV PQIFVRPASA RKRADDMKAL FTHPDGDHLT MLNVYHAFKG EEAQRNPKEW
     CHKHYLSLRA LQSADSVREQ LKRIMTKSEL ELMSTDFTDK NYFNNIRRAL VSGFFMQVAK
     KESSGKSYKT VKDDQSVLLH PSTGLGVDSE WVLYNEFVLT TKNYVRTVTS VRPEWLLDIA
     PNYYDLSSFP NGDIKTALCK VSEKVKRRQA MKGKR
//
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