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Database: UniProt
Entry: Q5APT8
LinkDB: Q5APT8
Original site: Q5APT8 
ID   DBP3_CANAL              Reviewed;         564 AA.
AC   Q5APT8; A0A1D8PER1; Q5AP94;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   16-OCT-2019, entry version 84.
DE   RecName: Full=ATP-dependent RNA helicase DBP3;
DE            EC=3.6.4.13;
GN   Name=DBP3; OrderedLocusNames=CAALFM_C110030WA;
GN   ORFNames=CaO19.12334, CaO19.4870;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs
RT   aligned on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates
RT   allele-specific measurements and provides a simple model for repeat
RT   and indel structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: ATP-dependent RNA helicase required for 60S ribosomal
CC       subunit synthesis. Involved in efficient pre-rRNA processing,
CC       predominantly at site A3, which is necessary for the normal
CC       formation of 25S and 5.8S rRNAs (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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
DR   EMBL; CP017623; AOW26634.1; -; Genomic_DNA.
DR   RefSeq; XP_723554.1; XM_718461.1.
DR   SMR; Q5APT8; -.
DR   BioGrid; 1217962; 1.
DR   STRING; 5476.C4YD41; -.
DR   PRIDE; Q5APT8; -.
DR   GeneID; 3634868; -.
DR   KEGG; cal:CAALFM_C110030WA; -.
DR   CGD; CAL0000185988; DBP3.
DR   EuPathDB; FungiDB:C1_10030W_A; -.
DR   InParanoid; Q5APT8; -.
DR   KO; K14811; -.
DR   OrthoDB; 471730at2759; -.
DR   PRO; PR:Q5APT8; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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; 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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    564       ATP-dependent RNA helicase DBP3.
FT                                /FTId=PRO_0000232174.
FT   DOMAIN      184    356       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      385    534       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     197    204       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       155    181       Q motif.
FT   MOTIF       303    306       DEAD box.
SQ   SEQUENCE   564 AA;  63127 MW;  B0F390EF1C170626 CRC64;
     MSFSSGKFLF VFLFFFFFKN TSCSNQRKYI TKQQTMSKDK KEHKDKKRKH DNEDVEIADS
     KKQRKLEKQE KKDKKDKKDK KEKKEKKEKK HKKEKKHKDS ESSPVEPAAN DSSSSTNYTQ
     SSKLSSVSQS DIDKFLSDNE ITVEDPSSSS LRPILSFDQV QLTSAITSKL SKFDKPTPIQ
     SVSWPFLLSG KDVIGVAETG SGKTFAFGVP AINNIITTGN TKTLSVLCIS PTRELALQIY
     DNLIELTADS GVNCVAVYGG VSKDDQIRKI KTANVVVATP GRLVDLINDG AINLGKVNYL
     VLDEADRMLE KGFEEDIKTI ISNTSNSERQ TLMFTATWPK EVRELANNFM NSPVKVTVGD
     RDELSANKRI TQVVEVINKF DKEKKLIQLL RKYNANESSD NKILIFALYK KEASRIENFL
     KRNRFSVAAI HGDLSQQQRT AALSAFKSGQ SNLLLATDVA ARGLDIPNVK VVINLTFPLT
     IEDYVHRIGR TGRAGAKGTA HTLFTEDEKH LSGALCNILR GANQPVPEEL LKFGGHTKKK
     AHSVYGAFYK DVDMTKTAKK IKFD
//
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