DBP2_YARLI
ID DBP2_YARLI Reviewed; 552 AA.
AC Q6C4D4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=ATP-dependent RNA helicase DBP2;
DE EC=3.6.4.13;
GN Name=DBP2; OrderedLocusNames=YALI0E27715g;
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-dependent RNA helicase involved nonsense-mediated mRNA
CC decay and ribosome biogenesis through rRNA processing. {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 polysomes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382131; CAG80081.1; -; Genomic_DNA.
DR RefSeq; XP_504478.1; XM_504478.1.
DR AlphaFoldDB; Q6C4D4; -.
DR SMR; Q6C4D4; -.
DR STRING; 4952.CAG80081; -.
DR EnsemblFungi; CAG80081; CAG80081; YALI0_E27715g.
DR GeneID; 2912263; -.
DR KEGG; yli:YALI0E27715g; -.
DR VEuPathDB; FungiDB:YALI0_E27715g; -.
DR HOGENOM; CLU_003041_16_9_1; -.
DR InParanoid; Q6C4D4; -.
DR OMA; STMPKFE; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; 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:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0030515; F:snoRNA binding; IEA:EnsemblFungi.
DR GO; GO:1990120; P:messenger ribonucleoprotein complex assembly; IEA:EnsemblFungi.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IEA:EnsemblFungi.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IEA:EnsemblFungi.
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; Cytoplasm; Helicase; Hydrolase; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..552
FT /note="ATP-dependent RNA helicase DBP2"
FT /id="PRO_0000054999"
FT DOMAIN 147..322
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 350..497
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..535
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT MOTIF 116..144
FT /note="Q motif"
FT MOTIF 270..273
FT /note="DEAD box"
FT COMPBIAS 537..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 552 AA; 60710 MW; D8D6A06C722EF85C CRC64;
MSYGDDYNNN DRGYGGGRGF GGGRGGRGGS RGGRGGFGGD RGFGGDRGGY GGGGYQDNDF
GNLPKQDWDL EKLPQFEKNF YKEDPAVTER TDEEVTAFRK ENQMTLHGDG IPKPVTNFDE
AGFPPYVLKE VKQQGFEKPT AIQCQGWPMA LTGRDVIGIA STGSGKTLSY CLPAIVHINA
QPMLSHGDGP IVLVLAPTRE LAVQIQQECS KFGKSSKIRN TCVYGGVPRG QQIRDLARGV
EIVIATPGRL LDMLESGKTN LRRVTYLVLD EADRMLDMGF EPQIRKIVDQ IRPDRQTLMW
SATWPKEVQR LAHDYLKDQI QVNIGSLELS ASHNITQVVE VCTEYEKRDR LVKHLETVME
NKESKCLIFT GTKRVADDIT KFLRQDGWPA LAIHGDKQQQ ERDWVLNEFR QGKSPIMVAT
DVASRGIDVK GINFVINYDY PSNSEDYVHR IGRTGRAGTK GTAYTYFTED NRKQARDLLV
ILREAKQHID PKLEEMGGGR GGRGGWGGRG GRGGRGGRGG YRRGGYGGGG YGGGRGSDIT
GSNSAPLSNS RW
