DBP10_PHANO
ID DBP10_PHANO Reviewed; 878 AA.
AC Q0UMB6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=ATP-dependent RNA helicase DBP10;
DE EC=3.6.4.13;
GN Name=DBP10; ORFNames=SNOG_07098;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX54/DBP10
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT85749.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445334; EAT85749.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001797451.1; XM_001797399.1.
DR AlphaFoldDB; Q0UMB6; -.
DR SMR; Q0UMB6; -.
DR STRING; 321614.Q0UMB6; -.
DR GeneID; 5974341; -.
DR KEGG; pno:SNOG_07098; -.
DR eggNOG; KOG0337; Eukaryota.
DR InParanoid; Q0UMB6; -.
DR OMA; MRWDKKS; -.
DR OrthoDB; 268859at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR24031:SF292; PTHR24031:SF292; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
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..878
FT /note="ATP-dependent RNA helicase DBP10"
FT /id="PRO_0000256046"
FT DOMAIN 109..281
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 349..538
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 332..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 78..106
FT /note="Q motif"
FT MOTIF 229..232
FT /note="DEAD box"
FT COMPBIAS 332..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..653
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..868
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 878 AA; 97391 MW; EDB98A3E5A1A2B37 CRC64;
MAPRASSPAL SENEFDIFDA LAGGDEAAQP MRVTADLGID LEFGSDDGSD DEAFIAAKQA
AANRKNANAP GKSGKKGGGF QAMGLNVALL KAIAQKGFKI PTPIQRKAVP LILQGDDVVG
MARTGSGKTA AFVIPMIERL KTHSAKVGAR GVIMSPSREL ALQTLKVVKE FGRGTDLRTI
LLVGGDSLEE QFNSMTTNPD IIIATPGRFL HLKVEMGLDL SSVQYIVFDE ADRLFEMGFA
AQLAEILYAL PTSRQTLLFS ATLPKSLVEF ARAGLQEPKL IRLDAESKIS PDLKSAYFTI
KSGDRDGALI HLLENVIKMP VGQTEVWKQA KEEADNLSKG KKRKRGSGNP KDAPVEESTI
IFAATKHRVE YLSTLLKAAG YPVSYVYGNL DQTARQEQVK DFRAGLTRIL VVTDVAARGY
RHATHKPRHQ LRLPFSTKNL CSSSGEDGPR WAEGLGIQPV QTCRSAISHR LTNVPWQTPS
GCLAPYQLEP SVELVNKQLT DDEDLVNLLN VAEKGERQYQ RTRNQASNQS VHRAKDLASD
SKFAETHMLF NDEMHDALRA KEDMLERIQG FRPAETVFEI GKRGTNSEAA EIMRKRRVAV
ERQKTKQAFN KANDESSGLT RPTADALPDD ELDSEDDQQA AVGDYESESD ELEVTVSQPE
SKKSGKDVWR SDEFFMSYLP KENFAEEKAY GVQGGDAGNS NFVSAARSAE MSLVNDEIQG
FADASKPRMR WDKKSKKYVS RANDEDGSKG AKMIRGESGQ KIAASFRSGR FDDWRKANKV
KMQRVGEMEA PNRSTQFNSG GPRYKHKAEK APKQADRYRD DYHVQKQRVQ EAKEKRIGHF
KDGGAKNELK DVDTVRKERR VQEKRKEKNA RPSKKRKF