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DBP10_NEUCR
ID   DBP10_NEUCR             Reviewed;         934 AA.
AC   Q7S9J4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=ATP-dependent RNA helicase dbp-10;
DE            EC=3.6.4.13;
GN   Name=dbp-10; ORFNames=NCU07712;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
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DR   EMBL; CM002239; EAA33062.1; -; Genomic_DNA.
DR   RefSeq; XP_962298.1; XM_957205.2.
DR   AlphaFoldDB; Q7S9J4; -.
DR   SMR; Q7S9J4; -.
DR   STRING; 5141.EFNCRP00000008050; -.
DR   PRIDE; Q7S9J4; -.
DR   EnsemblFungi; EAA33062; EAA33062; NCU07712.
DR   GeneID; 3878446; -.
DR   KEGG; ncr:NCU07712; -.
DR   VEuPathDB; FungiDB:NCU07712; -.
DR   HOGENOM; CLU_003041_5_2_1; -.
DR   InParanoid; Q7S9J4; -.
DR   OMA; MRWDKKS; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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   SMART; SM00490; HELICc; 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..934
FT                   /note="ATP-dependent RNA helicase dbp-10"
FT                   /id="PRO_0000232318"
FT   DOMAIN          130..302
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          359..513
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          21..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          851..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           99..127
FT                   /note="Q motif"
FT   MOTIF           250..253
FT                   /note="DEAD box"
FT   COMPBIAS        346..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..644
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..697
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         143..150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   934 AA;  103653 MW;  E010C55016EFAB98 CRC64;
     MPRRAASPTP SENEVDIAGA LFNNDSDFED NSSKHHTKKG AVTNSGLDLD FNDLLGNGDD
     GLPSFNGEGD DDEAFIASLT RSSQRKSSNI QGKSVKKGGG FQAMGLNAHL LRAITRKGFS
     VPTPIQRKAI PLILERKDVV GMARTGSGKT AAFVIPMIER LKGHSPRVGS RALIMSPSRE
     LALQTLKVVK ELGRGTDLKT VLLVGGDSLE EQFGMMASNP DIIIATPGRF LHLKVEMNLS
     LASIKYVVFD EADRLFEMGF ATELTEILHA LPPSRQTLLF SATLPSSLVE FARAGLQEPS
     LVRLDAETKV SPDLESAFFA VKGGEKEGAL LHLLHDVIKV PLGPPEGTKE ESDELQARKR
     KREYRPNPKE KPTEYSTIIF TATKHHVEYI ANLLKLAGFA VSYVYGSLDQ TARLIQVDNF
     RRGRTHILVV TDVAARGIDM PALANVINYD FPSQPKIFVH RVGRTARAGQ RGWAYGLVRQ
     SDVPYLLDLQ LFLGRKLIIG HDQKNPSFAA DVVVGTLKRD GVDVNIEWVE KALKESADLK
     ALKGVAAKAE KLYMKTRNSA SSQSAKRARE VTQSRGWTQL HPLFGEEAAE AQAARDDLLS
     RINRFKPQET IFELGPKGKS SRNKAAEVVR NMRSRFKERK TTNDEDDEDV DMEDAEGKPD
     GEETNAFEDF EDEEEEGEAE EAEEAEAKED PYADDSDSEM EVTVSSSMHT KKKGGPVNFQ
     DPEIFMSYTP RTTSLAEEKA YGVHSGGYSG NSFVEAARDA TMDLTNDESA KNFGLPTKSK
     MRWDKRHSKY VAVANDEDGS KGAKMIRGES GVKIAASFKS GRFDRWRKDN RLGKLPTIGE
     TEKSQLIRNF GAQPGQPRYK HKMEKAPKDA DKFRDDYHVR KKRVAEAKEK RIGKYKDGEG
     SKRELKTATD IRKARAVAEK KREKNARPAK RQKR
 
 
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