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Database: UniProt
Entry: Q59PR3
LinkDB: Q59PR3
Original site: Q59PR3 
ID   DBP8_CANAL              Reviewed;         440 AA.
AC   Q59PR3; A0A1D8PT34;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   16-OCT-2019, entry version 83.
DE   RecName: Full=ATP-dependent RNA helicase DBP8;
DE            EC=3.6.4.13;
GN   Name=DBP8; OrderedLocusNames=CAALFM_CR05630WA;
GN   ORFNames=CaO19.13973, CaO19.6652;
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-binding RNA helicase involved in 40S ribosomal
CC       subunit biogenesis and is required for the normal formation of 18S
CC       rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required
CC       for 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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX49/DBP8
CC       subfamily. {ECO:0000305}.
DR   EMBL; CP017630; AOW31279.1; -; Genomic_DNA.
DR   RefSeq; XP_711718.1; XM_706626.1.
DR   SMR; Q59PR3; -.
DR   BioGrid; 1229284; 1.
DR   STRING; 5476.C4YM09; -.
DR   PRIDE; Q59PR3; -.
DR   GeneID; 3646692; -.
DR   KEGG; cal:CAALFM_CR05630WA; -.
DR   CGD; CAL0000181153; DBP8.
DR   EuPathDB; FungiDB:CR_05630W_A; -.
DR   InParanoid; Q59PR3; -.
DR   KO; K14778; -.
DR   OrthoDB; 744428at2759; -.
DR   PRO; PR:Q59PR3; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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; 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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    440       ATP-dependent RNA helicase DBP8.
FT                                /FTId=PRO_0000232283.
FT   DOMAIN       32    208       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      247    387       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      45     52       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         1     29       Q motif.
FT   MOTIF       154    157       DEAD box.
SQ   SEQUENCE   440 AA;  48832 MW;  5A2483E47C9368DB CRC64;
     MSFNDLGVAK WLSESLDAMK IYTPTAIQSA CIPAILKGHD CIGGAKTGSG KTIAFAAPML
     TQWSEDPFGI FGLILTPTRE LALQIAEQFA ALGANMNIKV AVVVGGEDFV QQTLALQRKP
     HFVIATPGRL ADHILNSGEE TISGLRRVKY LVLDEADRLL SNSFGSDLQR CFDVLPTSDK
     RQTLLFTATI TDAVRALKEK PPTPGKPPVF MHEVETVDKV AIPSTLQISY VFVPSYVKEA
     YLNSILHLEQ FKDSTAVIFV NRTTTAEVLR RMLRKLDFRV ASLHSEMPQS ERTNSLHRFK
     AGAARILIAT DVASRGLDIP TVELVINFDI PADPDDFIHR VGRTARAGRK GDAVSIIGEK
     DIDRIQSIEE RINKKMELLE DVNDDNVIKE SLSATSVAKR ESLMEMDKEN FGERKKINRK
     KHGLDKVKPE RVTKPKKSKK
//
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