DBP6_LODEL
ID DBP6_LODEL Reviewed; 663 AA.
AC A5E726;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP-dependent RNA helicase DBP6;
DE EC=3.6.4.13;
GN Name=DBP6; ORFNames=LELG_05415;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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 -!- SUBUNIT: Associated with pre-ribosomal particles. {ECO:0000250}.
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. DDX51/DBP6
CC subfamily. {ECO:0000305}.
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DR EMBL; CH981532; EDK47234.1; -; Genomic_DNA.
DR RefSeq; XP_001523569.1; XM_001523519.1.
DR AlphaFoldDB; A5E726; -.
DR SMR; A5E726; -.
DR STRING; 379508.A5E726; -.
DR EnsemblFungi; EDK47234; EDK47234; LELG_05415.
DR GeneID; 5230558; -.
DR KEGG; lel:LELG_05415; -.
DR VEuPathDB; FungiDB:LELG_05415; -.
DR eggNOG; KOG0350; Eukaryota.
DR HOGENOM; CLU_003041_15_2_1; -.
DR InParanoid; A5E726; -.
DR OMA; HLEWLVI; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001996; 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; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..663
FT /note="ATP-dependent RNA helicase DBP6"
FT /id="PRO_0000294660"
FT DOMAIN 264..448
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 485..642
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 222..250
FT /note="Q motif"
FT MOTIF 384..387
FT /note="DEAD box"
FT COMPBIAS 59..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 277..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 663 AA; 75231 MW; 6DFEE6430932E193 CRC64;
MFGVRYDPEE SLLTPTLYHN GRFLPNLKKR KRRVQDHDVV DDDVVVFDND KDEEEMNKEK
KEEEEEEEEE EEETDNSEGE SEKSESGSES ESESESESES DVDGKHMKEE LEDKDDAMEV
DTIIEDNEYS GKHKSIFDKF KLSVTRTVND DVVHSSRDEE EDFQKQSGSR EKEKEEVVET
QDLAPLPQPQ LPRDRKLNSS TQHSANLDWL TTPEYIAIAD TKPFSEFPLS PFMHENLESL
GFENAFAVQV GVLSKLLPEI QANKLRPDAF GDVLVNASTG SGKTLAYSIP IIESLKDRVV
PRVRAIVLVP TKPLINQVRA TMLQLALGTN LNIVSLKNDI SIREESERLI ELVPDVVIST
PGRLVEHLAM DSISLSSLRY LVVDEADRLL NQSFQNWSQI LISKIHLQQV YDVANVWSLK
VQKFIFSATL TTDAGKLASL DFHNPRLLIV NDSQRLVNEL FSVPAMLSEY KLNFGVAKSS
LKPLILAKFL IAQEKLSDVL VFTKSNESSI RLCTLLQAIF DRICLQEKVK VGFMNLTNNR
TSLRSKILKD FTSQKINILV ATDLIARGLD VTSIKDVVNY DLLNSSREYV HRVGRTARAN
QAGNAYNLVF GKGEEKWFKT ISSEVSRNND VKDVEVNLKQ LISDEDEKLY QEALQSLQDQ
VRK
