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Database: UniProt
Entry: A5DAC8
LinkDB: A5DAC8
Original site: A5DAC8 
ID   DBP3_PICGU              Reviewed;         534 AA.
AC   A5DAC8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   31-JUL-2019, entry version 59.
DE   RecName: Full=ATP-dependent RNA helicase DBP3;
DE            EC=3.6.4.13;
GN   Name=DBP3; ORFNames=PGUG_00233;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM
OS   1539 / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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
RC   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.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J., Harris D.,
RA   Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E.,
RA   Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J.,
RA   Santos M.C., Schmitzberger F.F., Sherlock G., Shah P.,
RA   Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I.,
RA   Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W.,
RA   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-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; CH408155; EDK36135.2; -; Genomic_DNA.
DR   RefSeq; XP_001486856.1; XM_001486806.1.
DR   SMR; A5DAC8; -.
DR   STRING; 4929.XP_001486856.1; -.
DR   PRIDE; A5DAC8; -.
DR   EnsemblFungi; EDK36135; EDK36135; PGUG_00233.
DR   GeneID; 5129457; -.
DR   KEGG; pgu:PGUG_00233; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   InParanoid; A5DAC8; -.
DR   KO; K14811; -.
DR   OMA; AYGAFFK; -.
DR   OrthoDB; 471730at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:EnsemblFungi.
DR   GO; GO:0000464; P:endonucleolytic cleavage in ITS1 upstream of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
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    534       ATP-dependent RNA helicase DBP3.
FT                                /FTId=PRO_0000294618.
FT   DOMAIN      160    330       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      359    504       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     173    180       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       131    157       Q motif.
FT   MOTIF       278    281       DEAD box.
FT   COMPBIAS      4     73       Lys-rich.
SQ   SEQUENCE   534 AA;  59650 MW;  7A60C9F740994725 CRC64;
     MGSKRKHESG DVEVKKPKHD NEVKGKEKKE KKEKKEKKEK KEKKEKKEKK EKKEKKEKNE
     KKEKKEKKAK KEKTEETEET DSTVSTVSSS SSGYTQAAEL TALPQSEIDE FLQTNEVTVE
     DPHKLGFRPI LSFDHVQLQS KIAPIVTKFP KPTPIQSASW PYLLNGDDVV GVAETGSGKT
     FAFGVPAINN IITDNKKGLR VLCISPTREL ALQIYDNLTM LTKNCGLTCV AIYGGVPKDQ
     QIKAVKTASV VVATPGRLVD LLNDGAVDLS TIDYLVLDEA DRMLEKGFEE DIKNIIGCTN
     KQRQTLMFTA TWPKEVRELA ATFMNKAVKV SIGNRDELAA NKRITQTVEV MDPRDKERRL
     LQLLRQYGSD QKILVFALYK KEATRVEAML RRSGFNVAAI HGDLSQQQRT SALDSFKRGD
     SNLLLATDVA ARGLDIPNVK VVINLTFPLT VEDYVHRIGR TGRAGQTGIA HTLFTEHEKH
     LSGALMNVLR GAGQPVPDEL LKFGGHTKKK SHSAYGAFFK DVDMTKTAKK IKFE
//
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