DBP2_ASHGO
ID DBP2_ASHGO Reviewed; 557 AA.
AC Q755N4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=ATP-dependent RNA helicase DBP2;
DE EC=3.6.4.13;
GN Name=DBP2; OrderedLocusNames=AFL221C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 337; 356; 367-368; 394-407
RP AND 421.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53153.2; -; Genomic_DNA.
DR RefSeq; NP_985329.2; NM_210683.2.
DR AlphaFoldDB; Q755N4; -.
DR SMR; Q755N4; -.
DR STRING; 33169.AAS53153; -.
DR EnsemblFungi; AAS53153; AAS53153; AGOS_AFL221C.
DR GeneID; 4621553; -.
DR KEGG; ago:AGOS_AFL221C; -.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_16_9_1; -.
DR InParanoid; Q755N4; -.
DR OMA; STMPKFE; -.
DR Proteomes; UP000000591; Chromosome VI.
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..557
FT /note="ATP-dependent RNA helicase DBP2"
FT /id="PRO_0000227944"
FT DOMAIN 145..320
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 348..495
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..532
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT MOTIF 114..142
FT /note="Q motif"
FT MOTIF 268..271
FT /note="DEAD box"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 557 AA; 61728 MW; F4B50BF264A09E1E CRC64;
MSYAGNRDQQ FNRSNFGGRD GDHRGQRPSD RNSYGRDGFG RGGRGGFAGR GRGRSDDRLE
LTKPDWDVES LPKFEKNFYV EHEDVQKMST DEVEQFRKEN EMKIVGHDVP KPIRTFDEAG
FPEYVLKEVK EEGFEKPTAI QCQGWPMALS GRDMIGVAAT GSGKTLSYCL PGIVHINAQP
LLSPGDGPVV LVLAPTRELA VQIQKECSKF GRSSRIRNTC VYGGVPKSQQ IRDLQRGVEI
LIATPGRLID MLEIGKTNLK RVTYLVLDEA DRMLDMGFEP QIRKIVDQIR PDRQTLMWSA
TWPKEVQQLA RDYLHDPIQV NIGSLELAAS HTITQLVEVV SDFDKRDRLV KHLEIASKDK
DSKIIIFAST KRTCDEITSY LRQDGWPALA IHGDKQQQER DWVLNEFRTG RSPIMVATDV
AARGIDVKGI NFVINYDMPG NIEDYVHRIG RTGRAGATGT AISFFTEANK TLGAQLISIM
REAKQEIPQD LLVYDRAPRG GFHPRYGGRG GRGGRGGRGG RGYGGYGGGY GGYGGGYGGG
HGGYGGKPKD SGWGNRN