位置:首页 > 蛋白库 > DBP7_CANGA
DBP7_CANGA
ID   DBP7_CANGA              Reviewed;         715 AA.
AC   Q8TFL3; Q6FLJ0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=ATP-dependent RNA helicase DBP7;
DE            EC=3.6.4.13;
GN   Name=DBP7; OrderedLocusNames=CAGL0L03047g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=12125055; DOI=10.1002/yea.890;
RA   Walsh D.W., Wolfe K.H., Butler G.;
RT   "Genomic differences between Candida glabrata and Saccharomyces cerevisiae
RT   around the MRPL28 and GCN3 loci.";
RL   Yeast 19:991-994(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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   -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY083607; AAM08097.1; -; Genomic_DNA.
DR   EMBL; CR380958; CAG61874.1; -; Genomic_DNA.
DR   RefSeq; XP_448904.1; XM_448904.1.
DR   AlphaFoldDB; Q8TFL3; -.
DR   SMR; Q8TFL3; -.
DR   STRING; 5478.XP_448904.1; -.
DR   EnsemblFungi; CAG61874; CAG61874; CAGL0L03047g.
DR   GeneID; 2890843; -.
DR   KEGG; cgr:CAGL0L03047g; -.
DR   CGD; CAL0135220; CAGL0L03047g.
DR   VEuPathDB; FungiDB:CAGL0L03047g; -.
DR   eggNOG; KOG0348; Eukaryota.
DR   HOGENOM; CLU_003041_26_2_1; -.
DR   InParanoid; Q8TFL3; -.
DR   OMA; QMGFERW; -.
DR   Proteomes; UP000002428; Chromosome L.
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:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
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   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; 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..715
FT                   /note="ATP-dependent RNA helicase DBP7"
FT                   /id="PRO_0000232253"
FT   DOMAIN          160..354
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          400..586
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           125..154
FT                   /note="Q motif"
FT   MOTIF           289..292
FT                   /note="DEAD box"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   715 AA;  79988 MW;  C43196A9DD7E8306 CRC64;
     MSDDESMVLN FSTDTAGIQR ADKVTGGRWK DRRKLQQRLG GREPVKRRAE GGDKERGDKR
     AKVDTGNAQE KKNIPKPVSK ADVNINSQIV SSLFTSNRAK QTSENKNKHN SDDKVVPSNA
     PLTDDSFEGL GVGSLVVSHL ENKMRIQKST SIQKVVIPQI LQNADKTDFF IHAQTGSGKT
     LAYLLPIFSA ILGMGDHIDR KSGCFALIIA PTRELASQIY HVTTMLANCC HYLVPCLLIG
     GERKKSEKAR LRKGCNFIIG TPGRILDHFQ NTKVIKEQMQ SSLRYVVLDE GDKLMELGFE
     ETINQIMEIV NSMDVITRKY PKLPNRIVHL LCSATKNNEV AKLSKRSLDN YKVISIGGKK
     DTMMDNTSVP DQLLQKVVIA PPKLRLITLA GVLDGIQKKP LDAGSVAKRT IVFLSCADSV
     DYHFEVFSGN DGLYKNLVGD SVRVLSKGNK ILPSIKDEEL PGIICYKLHG SLSQQMRTMT
     LKHFATDSEQ TKGKHLILFC TDVASRGLDL PDVSTVIEFD PPFAVEDHLH RIGRTARAGR
     SGEALLFLLP GEEEGYLDYI QKYHPKGWDL LDAEKDVLIK AFNDIDVARN DKEIKSTGKT
     FEWDTNATTW HLNVERRILE NEQFKEQATK GYISHVRAYA THISAEKQYF NLKGVHLGHL
     AKSFGLRDRP KAMGMNSSKD ANGNERSKPK KENAKNKMFR MARMAAKQSA DEFNY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024