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DBP8_PICGU
ID   DBP8_PICGU              Reviewed;         433 AA.
AC   A5DLE0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP-dependent RNA helicase DBP8;
DE            EC=3.6.4.13;
GN   Name=DBP8; ORFNames=PGUG_04091;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408159; EDK39993.2; -; Genomic_DNA.
DR   RefSeq; XP_001483362.1; XM_001483312.1.
DR   AlphaFoldDB; A5DLE0; -.
DR   SMR; A5DLE0; -.
DR   STRING; 4929.XP_001483362.1; -.
DR   EnsemblFungi; EDK39993; EDK39993; PGUG_04091.
DR   GeneID; 5125427; -.
DR   KEGG; pgu:PGUG_04091; -.
DR   VEuPathDB; FungiDB:PGUG_04091; -.
DR   eggNOG; KOG0340; Eukaryota.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   InParanoid; A5DLE0; -.
DR   OMA; EIKQESM; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000001997; 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..433
FT                   /note="ATP-dependent RNA helicase DBP8"
FT                   /id="PRO_0000294657"
FT   DOMAIN          32..208
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          247..387
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          401..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT   MOTIF           154..157
FT                   /note="DEAD box"
FT   COMPBIAS        401..424
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   433 AA;  47909 MW;  E3692CC635872602 CRC64;
     MSFKDLGVSK WLLEALAAMK IRSPTSIQAE CIPQILAGRD CIGGAKTGSG KTIAFAAPMM
     TKWSEDPFGI YGLVLTPTRE LALQIAEQFL ALGASMNIKV AVVVGGEDMV KQALEIQKSP
     HFIIATPGRL ADHILNSGDD TVGGLKRIKF LVLDEADRLL SNSFGSDLER CFKILPDASK
     RQTLLFTATV TDAVRALKDK PVPEGKKPVF IHEIVSKDQV AIPATLTISY VFVPSYVKEA
     YLHNILVSPK YEKASAIVFV NRTYTAEILR RTLRKLDIRV ASLHSEMPQS ERTNSLHRFR
     AGAARVLIAT DVASRGLDIP NVELVVNQDI PADPDDYIHR VGRTARAGKK GGSVSIVSEK
     DVERILAIEN HINKKMDLLE EVNDDKIIKE SLSIVTAAKR ESVADMEKEG FGEKRKINKR
     KREERTRDSK KRK
 
 
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