DBP7_MAGO7
ID DBP7_MAGO7 Reviewed; 825 AA.
AC A4QX49; G4N0I4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ATP-dependent RNA helicase DBP7;
DE EC=3.6.4.13;
GN Name=DBP7; ORFNames=MGG_05810;
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).
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; CM001233; EHA52318.1; -; Genomic_DNA.
DR RefSeq; XP_003712125.1; XM_003712077.1.
DR AlphaFoldDB; A4QX49; -.
DR SMR; A4QX49; -.
DR STRING; 318829.MGG_05810T0; -.
DR EnsemblFungi; MGG_05810T0; MGG_05810T0; MGG_05810.
DR GeneID; 2684165; -.
DR KEGG; mgr:MGG_05810; -.
DR VEuPathDB; FungiDB:MGG_05810; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; A4QX49; -.
DR OMA; AVHIKAD; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000009058; Chromosome 3.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..825
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000294643"
FT DOMAIN 164..373
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 400..625
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 21..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 131..160
FT /note="Q motif"
FT MOTIF 302..305
FT /note="DEAD box"
FT COMPBIAS 80..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 825 AA; 89217 MW; 6F4FE8EFBCB786E3 CRC64;
MDDDGLLINF EVGEGPIKPQ IKFTGGRWRE RNRLQRSVKR GLTGSQSNDA VADDVGPAPA
KRQRLSEGAA PEIQRRFRPQ AQGPRSQHVS SRLFTSNPTP VTNFDEPETA PAEEPAEPAL
PSNAPLSDEA ATFAALGLSR RIAQHLSAKL ELKAPTAIQH RAVPHLVTTD EDAFLQAQTG
SGKTLAYLLP IVNRILALNQ NEDGTISKDA SKKIHRNSGL LAIVLAPTRE LCKQIATVLE
KLLRCAPWIV STTVIGGESK HSEKARIRKG INILIATPGR LKDHLDNTKV LDVSLARWLI
LDEGDRMMEM GFMDDLKEIV SKMREAPLKK INPDGIQLEP ALPTRRVTVL CSATLDHAQV
RRLGEYSLEA DKTELIKVDG TEAAKEGDEA SEAVFAAPSQ LKQSYLVVPA KLRLVTLIAL
LKSSFARRGS VMKAIIFISC ADSVDFHFDL LRSPIKEPKE AAAPPTPKKA PKDAGETPDT
PPKETKPTKP VTNHTESTVG KACYITSAAN TTITLHKLHG SLAQPVRTAT LDSFSKSKDP
SILITTDISS RGLDVPAVDL VIEYDPAFAV ADHVHRIGRT ARAGRPGKAV LFLQPGSEEG
YVGLLQKNAS TALTPQLYDS VLQAGFSSNI DLPPVTATNE DGQDTEQQKQ LDSRKQTWTS
RAEALQLHLE QRLLASDASS QASNNSGKGF NSKKGASTKL GKPAPKSSDG ATGTLLASGR
QAFRSHIRAY ATHVRDERVY FDMTQLHLGH MAKAFGLREA PGGIGAGVQR RTVKPSAANG
GGKKSTKGDD GDGLDKQDDD EAERTRRMKK MMRMVGAGAS EFNIG
