DBP2_DEBHA
ID DBP2_DEBHA Reviewed; 536 AA.
AC Q6BY27;
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=DEHA2A12958g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382133; CAG84869.1; -; Genomic_DNA.
DR RefSeq; XP_456892.1; XM_456892.1.
DR AlphaFoldDB; Q6BY27; -.
DR SMR; Q6BY27; -.
DR STRING; 4959.XP_456892.1; -.
DR EnsemblFungi; CAG84869; CAG84869; DEHA2A12958g.
DR GeneID; 2899413; -.
DR KEGG; dha:DEHA2A12958g; -.
DR VEuPathDB; FungiDB:DEHA2A12958g; -.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_16_9_1; -.
DR InParanoid; Q6BY27; -.
DR OMA; STMPKFE; -.
DR OrthoDB; 638613at2759; -.
DR Proteomes; UP000000599; Chromosome A.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
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; Cytoplasm; Helicase; Hydrolase; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..536
FT /note="ATP-dependent RNA helicase DBP2"
FT /id="PRO_0000054996"
FT DOMAIN 136..311
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 326..486
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 496..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..520
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT MOTIF 105..133
FT /note="Q motif"
FT MOTIF 259..262
FT /note="DEAD box"
FT BINDING 149..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 536 AA; 58661 MW; F735FD411EC1FD15 CRC64;
MSYNNNSDSY GGGYNSYGGN SYGGGGYGGG RGGGRGGFGG RGGGRYDERV ELNTPEWDID
SLPKFEKNFY NEHPDVTARS VQDVNAFRKE HDMKCDGTDI PKPITSFDEA GFPDYVLKEV
KQQGFPKPTS IQCQGWPMAL SGRDMVGIAS TGSGKTLSYC LPSIVHINAQ PLLSPGDGPI
VLVLAPTREL AVQIQQECSK FGSSSRIRNT CVYGGAPKGQ QIRDLARGVE ICIATPGRLI
DMLETGKTNL RRVTYLVLDE ADRMLDMGFE PQIRKIVDQI RPDRQTLMWS ATWPKEVQAL
TRDYLNDPIQ VTVGSLELAA SHTITQLVEV VTEFEKRDRL IKHLETATAD PEAKCLIFAS
TKRTCDEITN YLRADGWPAL AIHGDKQQGE RDWVLKEFKT GKSPIMVATD VAARGIDVKG
ISYVINLDMP GNIEDYVHRI GRTGRAGSTG TAVSFFTDNN SKLGGDLCKI MREANQTIPP
ELMRFDRRSF GSHIRYGRGG GRGGFRGGRG RGGFRGGRGG YQSGSNSAPL GNARRY
