DBP9_PICGU
ID DBP9_PICGU Reviewed; 586 AA.
AC A5DC85;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=ATP-dependent RNA helicase DBP9;
DE EC=3.6.4.13;
GN Name=DBP9; ORFNames=PGUG_00890;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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 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., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., 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-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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX56/DBP9
CC subfamily. {ECO:0000305}.
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DR EMBL; CH408155; EDK36792.2; -; Genomic_DNA.
DR RefSeq; XP_001487513.1; XM_001487463.1.
DR AlphaFoldDB; A5DC85; -.
DR SMR; A5DC85; -.
DR STRING; 4929.XP_001487513.1; -.
DR EnsemblFungi; EDK36792; EDK36792; PGUG_00890.
DR GeneID; 5128659; -.
DR KEGG; pgu:PGUG_00890; -.
DR VEuPathDB; FungiDB:PGUG_00890; -.
DR eggNOG; KOG0346; Eukaryota.
DR HOGENOM; CLU_003041_17_1_1; -.
DR InParanoid; A5DC85; -.
DR OMA; GYEKDFK; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
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; 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; 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..586
FT /note="ATP-dependent RNA helicase DBP9"
FT /id="PRO_0000294672"
FT DOMAIN 67..245
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 274..467
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 344..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..63
FT /note="Q motif"
FT MOTIF 191..194
FT /note="DEAD box"
FT COMPBIAS 356..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..576
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 586 AA; 66599 MW; 4F146B21B45CAC74 CRC64;
MQYHLQVEPH RCAHRTFPSP MTDAVVASEY LDESAKWENF KLDPRLLQAV YQLGFEKPTL
IQSNAIPLSL EDKRDIIAKA STGSGKTGAY SIPIIQNILS EGLSEHNIKS VILVPTKELA
NQVTKFIEKL LVYCNSITQI NLATNVSDQV VVSLLSAKPE IIISTPSRLT TVLEKHASIV
DLTTVTSLAI DEVDLMLSYG YMEDLQKLDD FLPIKRNLQT YLMSATVNDD VNDLKARFCT
KPAIIKLNDN EENQNRLVQF YARTSEFDKF LFAYVIFKLH LIKGKTLAFV NNIDRGYRLK
LFLEQFGVRC CILNSELPVN SRLHIVDEFN KNVYNLLIAS DESTEVTEQE GEDDQEDSKP
EKSKKKKGKK VDGEYGVSRG VDFRNVACVL NFDLPTTSRS YVHRVGRTAR AGKAGMALSF
VVPVKEVGKH KTATNPGAKR DEKVLARIVK SQSKNGFEIK PYQFDMTQVE GFRYRAEDAF
RAVTSAAIRE ARIRELKNEI MNSEKLKRFF EENPQDLASL RHDKELHPAK VQSQLKRVPD
YLLPESARQD PKKIGFVPFH KNKVHKNRKR KGGKKVDALK SFRQKK
