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DBP4_ASPTN
ID   DBP4_ASPTN              Reviewed;         804 AA.
AC   Q0CMM5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=ATP-dependent RNA helicase dbp4;
DE            EC=3.6.4.13;
GN   Name=dbp4; ORFNames=ATEG_05059;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU34128.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAU34128.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CH476600; EAU34128.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001214237.1; XM_001214237.1.
DR   AlphaFoldDB; Q0CMM5; -.
DR   SMR; Q0CMM5; -.
DR   STRING; 341663.Q0CMM5; -.
DR   GeneID; 4321060; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   eggNOG; KOG0343; Eukaryota.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0034512; F:box C/D RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034511; F:U3 snoRNA binding; IEA:EnsemblFungi.
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; IPR025313; DUF4217.
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; 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; 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..804
FT                   /note="ATP-dependent RNA helicase dbp4"
FT                   /id="PRO_0000310199"
FT   DOMAIN          77..251
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          277..436
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          493..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           46..74
FT                   /note="Q motif"
FT   MOTIF           199..202
FT                   /note="DEAD box"
FT   COMPBIAS        493..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..792
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         90..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   804 AA;  91077 MW;  E2A168DC14BD33FA CRC64;
     MAPANAPRNG KYAKSSQRTL KRKRVQEDLS SLVQRVEDLD LKESFKAFTD LPLSEPTLSG
     LSASHYKTLT DIQSRAVSHA LKGRDILGAA KTGSGKTLAF LIPVLENLYR KQWAEHDGLG
     ALILSPTREL AIQIFEVLRK VGRYHHFSAG LVIGGKSLKE EQERLGKMNI LVCTPGRMLQ
     HLDQTALFDT YNLQMLVLDE ADRIMDMGFQ KTVDAIIGHL PKERQTMLFS ATQTKKVSDL
     ARLSLQDPEY VAVHEAAASA TPSTLQQHYV VTPLPQKLDI LWSFIRSNLK SKTIVFLSSG
     KQVRFVYEAF RHLQPGIPLM HLHGRQKQGG RLDITTKYSQ AKHAVLFSTD VAARGLDFPA
     VDWVIQLDCP EDADTYIHRV GRTARYERDG RAVLFLDPSE EQGMLKRLEQ KKVPVEKINV
     KANKQQSIKN QLQNMCFKDP ELKYLGQKAF ISYVKSVYVQ KDKEIFKLKD LDLEEFASSL
     GLPGAPRIKF IKGDDTKERK NAPRAVAHLS SDDDESDAED DEKKSKKKDA PQVRTKYDRM
     FERRNQDVLA GHYTKLINDD GTLADPKATD EADEDNDFLS VKRRFDAGDK QLEVGGSSDE
     SGSDSEAETG KKDVKVVNID GKEPLVIDSK RREKLLKSKK KLLKFKGKGT KLIYDDEGNA
     HEIYEMEDEE QFRAKGDAKE QQARFLAAEA ERTRLADVED KELVKQKRRE KKEKRKARER
     ELLAQEEQEE MLVQLPPPED DDQGRFSPSE DEAPRPSKKQ RVQFAEPAES EEERRPKKPK
     KSTAEPKEIQ TLEDLESLAT GLLG
 
 
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