DBP7_ASPTN
ID DBP7_ASPTN Reviewed; 769 AA.
AC Q0CF43;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=ATP-dependent RNA helicase dbp7;
DE EC=3.6.4.13;
GN Name=dbp7; ORFNames=ATEG_07691;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU31953.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476604; EAU31953.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001216312.1; XM_001216312.1.
DR AlphaFoldDB; Q0CF43; -.
DR SMR; Q0CF43; -.
DR STRING; 341663.Q0CF43; -.
DR EnsemblFungi; EAU31953; EAU31953; ATEG_07691.
DR GeneID; 4322783; -.
DR eggNOG; KOG0348; Eukaryota.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000007963; 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; IPR025313; DUF4217.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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..769
FT /note="ATP-dependent RNA helicase dbp7"
FT /id="PRO_0000281708"
FT DOMAIN 175..382
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 408..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..171
FT /note="Q motif"
FT MOTIF 318..321
FT /note="DEAD box"
FT COMPBIAS 16..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 769 AA; 84769 MW; 12BE9F693305F8B2 CRC64;
MADDGMLLNF TFSDDVVKKS EPKLKGGTWR DRLSAKKIAQ HRAQPRKPSD GTAAPRPVKN
PNRIQVSGTR PAKRQRTDDD HDAGLRDHDR AGQSQHQHQH PRQFISSLFS KNPLPRNAEE
PTDEAPAEDA KPTNAPLIDG LDTFTNLGLS PTLAAHLLTK LELKAPTAIQ KASISQLLKE
ESDAFIQAET GSGKTLAYLL PLVQRIMALS HPTNRTDATS TTDAEGQPVV HRDSGLFAIV
LAPTRELCKQ ISVVLEGLLR CAHWIVAGTV IGGEKKKSEK ARLRKGLNIL VATPGRLADH
LENTQALDVS NVRWLVLDEG DRLMELGFEQ ELQGIIKKLD ARQRPSRIPG VPTKRTTILC
SATLKMNVQK LGEMSLKDAI HIKADPADED GDAKPKNDDE SAFTVPAQLK QSYAIVAAKL
RLVTLTAFLK RTFMRKGSVM KAIVFVSCAD SVDFHFEVFT RKLQDSDENA EDSDASDTKE
KPAAFTHNTI ARATAFSNPS NPVTLHRLHG SLPQHVRTST LASFARNKDA SVLVCTDVAS
RGLDLPNVDL VIEYDPAFSA EDHLHRIGRT ARLGRDGRAL IFLQPGCEEG YVEILKRGYR
DGGKALTRTN ADDILKRGFG GNVESENKDW EEKATDWQMD LERWALEKPE SLEMARRAYQ
SHIRAYATHV ASERSMFNIK ELHLGHLAKA FALRDRPSKI NVPGLRQGKD DTKKDYKAAR
APAAGKKRKT PGGRDDDDIP AAADTASAAQ KMRAKMKEHM AGASEFNLA
