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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
 
 
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