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Database: UniProt
Entry: A5DBI5
LinkDB: A5DBI5
Original site: A5DBI5 
ID   DBP5_PICGU              Reviewed;         482 AA.
AC   A5DBI5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-OCT-2019, entry version 60.
DE   RecName: Full=ATP-dependent RNA helicase DBP5;
DE            EC=3.6.4.13;
GN   Name=DBP5; ORFNames=PGUG_00640;
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 associated with the nuclear
CC       pore complex and essential for mRNA export from the nucleus. May
CC       participate in a terminal step of mRNA export through the removal
CC       of proteins that accompany mRNA through the nucleopore complex.
CC       May also be involved in early transcription (By similarity).
CC       {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   -!- SUBUNIT: Associates with the nuclear pore complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nuclear
CC       pore complex. Nucleus membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC       Note=Nuclear pore complex cytoplasmic fibrils. {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. DDX19/DBP5
CC       subfamily. {ECO:0000305}.
DR   EMBL; CH408155; EDK36542.1; -; Genomic_DNA.
DR   RefSeq; XP_001487263.1; XM_001487213.1.
DR   SMR; A5DBI5; -.
DR   STRING; 4929.XP_001487263.1; -.
DR   PRIDE; A5DBI5; -.
DR   EnsemblFungi; EDK36542; EDK36542; PGUG_00640.
DR   GeneID; 5128846; -.
DR   KEGG; pgu:PGUG_00640; -.
DR   eggNOG; KOG0332; Eukaryota.
DR   eggNOG; ENOG410XRGX; LUCA.
DR   InParanoid; A5DBI5; -.
DR   KO; K18655; -.
DR   OMA; CKLYGLM; -.
DR   OrthoDB; 608788at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Cytoplasm; Helicase; Hydrolase;
KW   Membrane; mRNA transport; Nuclear pore complex; Nucleotide-binding;
KW   Nucleus; Protein transport; Reference proteome; RNA-binding;
KW   Translocation; Transport.
FT   CHAIN         1    482       ATP-dependent RNA helicase DBP5.
FT                                /FTId=PRO_0000294633.
FT   DOMAIN      125    292       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      303    480       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     138    145       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        92    120       Q motif.
FT   MOTIF       239    242       DEAD box.
SQ   SEQUENCE   482 AA;  53642 MW;  81522A39654E416F CRC64;
     MPEEPVDSDA SKLLESLSIN KQGDSAPIKD EKPVVESENK VSDEQNSEPT KEPETKTETE
     NNDSNLISSS YEVQVKLADL QADPNSPLYS VKSFEELGLS PELLKGLYAM KFNKPSKIQE
     KALPLLISNP PKNMIGQSQS GTGKTAAFSL TMLSRVDVND PNTQCICLSP TRELARQTLE
     VITTMGKFTK VTTQLVVPQA MEKNQGTQAH IVVGTPGTLL DMIKRKLLRT GKVKVFVLDE
     ADNMLDGQGL AAQCIRVKKV LPTSCQLVLF SATFPTEVRK YAEKFVPNAN SLELKQEELN
     VDAIKQLYMD CDSEKHKAEV LSELYGLLTI GSSIIFVKTK ATANYLYAKM KSEGHACSIL
     HSDLDNSERD KLIDDFREGR SKVLITTNVL ARGIDIASVS MVVNYDIPVD KDDKPDPSTY
     LHRIGRTGRF GRVGVAVSFV HDKKSYEDLE QIRSYFNDIE MTRVPTDDWD EVEKIVKKVL
     KK
//
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