DBP8_YARLI
ID DBP8_YARLI Reviewed; 442 AA.
AC Q6C799;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATP-dependent RNA helicase DBP8;
DE EC=3.6.4.13;
GN Name=DBP8; OrderedLocusNames=YALI0E02552g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: ATP-binding RNA helicase involved in 40S ribosomal subunit
CC biogenesis and is required for the normal formation of 18S rRNAs
CC through pre-rRNA processing at A0, A1 and A2 sites. Required for
CC 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 box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX49/DBP8
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382131; CAG79042.1; -; Genomic_DNA.
DR RefSeq; XP_503463.1; XM_503463.1.
DR AlphaFoldDB; Q6C799; -.
DR SMR; Q6C799; -.
DR STRING; 4952.CAG79042; -.
DR EnsemblFungi; CAG79042; CAG79042; YALI0_E02552g.
DR GeneID; 2912109; -.
DR KEGG; yli:YALI0E02552g; -.
DR VEuPathDB; FungiDB:YALI0_E02552g; -.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; Q6C799; -.
DR OMA; EIKQESM; -.
DR Proteomes; UP000001300; Chromosome E.
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: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; IBA:GO_Central.
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..442
FT /note="ATP-dependent RNA helicase DBP8"
FT /id="PRO_0000232292"
FT DOMAIN 32..208
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 237..383
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 411..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..29
FT /note="Q motif"
FT MOTIF 154..157
FT /note="DEAD box"
FT COMPBIAS 411..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 442 AA; 49147 MW; 7F7789F0004F41A2 CRC64;
MSFTDLGLPE WLNESLSNMA ITKPSAIQKA CIPQIMKGKD CIGGARTGSG KTIAFAAPML
AEWSKDPCGI FGLVLTPTRE LAIQIAEQFT ALGANMNIRV ALIYGGVDMV KQSLELQKMP
HFVIATPGRL ADHIRSSGED TIRGFRRVRY VVMDEADRLL TPGFVPDLKT CMDLLPDPSK
RQTLLFTATV TDAVRALKDR TGEKGPPFIH EIASDIAVPS TLTQSYLFLP GYVREAYLWA
ILTHPDNEKK SAIIFVNRTQ TAETLRRMLM ALDVKTASLH SEMRQQERVN ALGRFRAQAA
RVLVATDVAS RGLDIPTVEM VINFDLPADA DDYIHRVGRT ARAGRKGQSV SLVTERDVTR
VTNIEERVGT KMEKYDLIED DKVVEEYLTP ASTAKRQAVL DMEAENFGER KRIQRKKAGL
DVDMKSKNKK PKRVAKGKSD KK
