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DBP8_ASPCL
ID   DBP8_ASPCL              Reviewed;         523 AA.
AC   A1CKJ0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=ATP-dependent RNA helicase dbp8;
DE            EC=3.6.4.13;
GN   Name=dbp8; ORFNames=ACLA_038790;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in 40S ribosomal subunit
CC       biogenesis and is required for the normal formation of 18S rRNAs
CC       through pre-rRNA processing at A0, A1 and A2 sites. Required for
CC       vegetative growth (By similarity). {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. DDX49/DBP8
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DS027056; EAW09664.1; -; Genomic_DNA.
DR   RefSeq; XP_001271090.1; XM_001271089.1.
DR   AlphaFoldDB; A1CKJ0; -.
DR   SMR; A1CKJ0; -.
DR   STRING; 5057.CADACLAP00003098; -.
DR   EnsemblFungi; EAW09664; EAW09664; ACLA_038790.
DR   GeneID; 4703223; -.
DR   KEGG; act:ACLA_038790; -.
DR   VEuPathDB; FungiDB:ACLA_038790; -.
DR   eggNOG; KOG0340; Eukaryota.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   OMA; EIKQESM; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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..523
FT                   /note="ATP-dependent RNA helicase dbp8"
FT                   /id="PRO_0000281710"
FT   DOMAIN          124..303
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          335..492
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           93..121
FT                   /note="Q motif"
FT   MOTIF           246..249
FT                   /note="DEAD box"
FT   BINDING         137..144
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   523 AA;  56646 MW;  9D8A71599BC586AB CRC64;
     MAPPRPEETI SEDLDESSGS SETEQPDIQT RAPKRRRLSA SSDDSYVAPA PLPTLSRIKK
     KGAEDAKPVA SAGQENPVLI RDALEIGLRE EASSFSALNV APWLVGSLTT LAVRKPTAIQ
     KACIPEILNG KDCIGGSRTG SGKTIAFSVP MLQKWAEDPL GIFGLILTPT RELALQIFEQ
     IKAISAPQSM KPVLITGGTD MRSQALALAG RPHVVVATPG RLADHIKSSG EDTVCGLKRV
     RMVVLDEADR LLSSGPGSML PDVETCLSAL PPSSERQTLL FTATVTPEVR ALKNMPRAAN
     KPPVFVTEIS SESQGTVPPT LKQTYLKVPL THREAFLHVL LSTEGNSTKP AIIFCNHTKT
     ADLLERMLRR LSHRVTSLHS LLPQSERNAN LARFRASAAR ILVATDVASR GLDIPSVSLV
     VNYDVPRNPD DYVHRVGRTA RAGRSGESVT LVGQRDVQLV LAIEARVGRQ MEEWSEEGVS
     IEGRVVRTGV LKEVGEAKRE ASGEIDEGRD VLGRKRNKLK KVR
 
 
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