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DBP4_ENCCU
ID   DBP4_ENCCU              Reviewed;         449 AA.
AC   Q8SR01;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=ATP-dependent RNA helicase DBP4;
DE            EC=3.6.4.13;
GN   Name=DBP4; OrderedLocusNames=ECU10_1680;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GB-M1;
RX   PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA   Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA   Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT   "Identification of transcriptional signals in Encephalitozoon cuniculi
RT   widespread among Microsporidia phylum: support for accurate structural
RT   genome annotation.";
RL   BMC Genomics 10:607-607(2009).
CC   -!- FUNCTION: ATP-dependent RNA helicase required for ribosome biogenesis.
CC       Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC       Required for pre-rRNA cleavage at site A2 (By similarity).
CC       {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   -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC       ribosomal complexes (By similarity). {ECO:0000250}.
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. DDX10/DBP4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL590449; CAD25888.2; -; Genomic_DNA.
DR   RefSeq; NP_586284.1; NM_001042117.1.
DR   AlphaFoldDB; Q8SR01; -.
DR   SMR; Q8SR01; -.
DR   STRING; 284813.Q8SR01; -.
DR   PRIDE; Q8SR01; -.
DR   GeneID; 859935; -.
DR   KEGG; ecu:ECU10_1680; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_1680; -.
DR   HOGENOM; CLU_003041_1_3_1; -.
DR   InParanoid; Q8SR01; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000819; Chromosome X.
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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
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..449
FT                   /note="ATP-dependent RNA helicase DBP4"
FT                   /id="PRO_0000255999"
FT   DOMAIN          32..206
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          228..378
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT   MOTIF           154..157
FT                   /note="DEAD box"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   449 AA;  51328 MW;  82007B6DB01D3200 CRC64;
     MKFEDLKIDQ RIEKGLRENG FVSMKEVQQK VIPMALEGHD IIGSSQTGTG KTLAFLVPTL
     QRLVSLGWGG GDGLGCLVIT PTRELALQIF DVLSRIAKYT VLSTGLIMGG LEAEDELLKV
     NQMNILVCTP GRLLQHLQEN PYLSTANVQI LILDEADKMI EMGFKEVLED ILEYIPQKKQ
     TLLFSATPKA STARILKLED PRIISIYKEE GFPSQLRQYF YMMRTGDKIN YLHTFIGSNP
     EVKGIVFFST CKEVKFHCLL FERLKLRNRI FCLSGGMSQK QRIDVFKRFV KEKNGILFCT
     DLGSRGLDFP KVDVVIQYDC PCNVETYVHR VGRTARNSER GESYVYLVHG EEKLLTDIQK
     KGWIKKQEGM EDKGISEEIT EGPGVQIRCI NNMVKRLVRS SKELNEYCRK YLVTYEKFLT
     FSSKRYSEGV IRKIPALYEH FGVSRDQSH
 
 
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