DBP7_ASHGO
ID DBP7_ASHGO Reviewed; 710 AA.
AC Q754J2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=ATP-dependent RNA helicase DBP7;
DE EC=3.6.4.13;
GN Name=DBP7; OrderedLocusNames=AFR082C;
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.
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-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}.
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DR EMBL; AE016819; AAS53453.1; -; Genomic_DNA.
DR RefSeq; NP_985629.1; NM_210983.1.
DR AlphaFoldDB; Q754J2; -.
DR SMR; Q754J2; -.
DR STRING; 33169.AAS53453; -.
DR PRIDE; Q754J2; -.
DR EnsemblFungi; AAS53453; AAS53453; AGOS_AFR082C.
DR GeneID; 4621872; -.
DR KEGG; ago:AGOS_AFR082C; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; Q754J2; -.
DR OMA; AVHIKAD; -.
DR Proteomes; UP000000591; Chromosome VI.
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:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
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 InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; 2.
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..710
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000227949"
FT DOMAIN 167..361
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 396..588
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..163
FT /note="Q motif"
FT MOTIF 296..299
FT /note="DEAD box"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 710 AA; 77952 MW; 3D51B4B2D511308A CRC64;
MSDNDGLMLM NFTTESGPDN ASSHRRVKVT GGKWKERRKL KMKLEGRPLR PKRPAAAVEE
APAAAVPEGS AIEPAAKRPR GRNERAPKDV PPQPANAQVV SSLFTSTRAI TTSVNDHERA
SNDVAPSNAP LLQDTFEALG VRGTLLEHLT GKMKIQKPTK IQKMAIPEVL NGKADLFLHA
QTGSGKTLAF LLPVLQTLLS LEQRIDRHSG CFAMIVTPTR ELAAQIYGVI STLAQCCHYL
VPCLLVGGER KKSEKARLRK GANFIVGTPG RMLDHLQNTK VAREQLPHSL RYLILDEGDK
LMELGFEETL KSILEIVHSV ACDNTRFPRL PQRIVHVLCS ATRQGTVSKL GDIALTDPKV
IAASDSTTDV STVPDQLLQK IAIVPPKLRL VTLCAAISEL SRKAPTETTT RTIVFISCAD
SVDFHYDVFS GLGGSHRDLV PGTVRELAAG SRALPCFSAD SPPNTVFYKL HGSLPQAVRV
ATLRHFSSDA AATRGKHLVL FCTDVASRGL DLPRVSTVIE MDPPFAVEDH LHRIGRTARA
GVAGESLLFL LPGEEEGYME HIRAHHPRGW ELLRYDRDLL APAFAAPVAR SDRPTTATDA
AWDSNATTWH LNVERRVLED PSAKDLAIKG YTSHIRAYAT HISQEKRFFN VRCLHLGHLA
KAFGLRERPK GMAAHRGKPA TPKPKQDDAR TKMLRMARQA VAQSNSEFNY
