DBP7_VANPO
ID DBP7_VANPO Reviewed; 732 AA.
AC A7TNT1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=ATP-dependent RNA helicase DBP7;
DE EC=3.6.4.13;
GN Name=DBP7; ORFNames=Kpol_1016p14;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; DS480434; EDO16074.1; -; Genomic_DNA.
DR RefSeq; XP_001643932.1; XM_001643882.1.
DR AlphaFoldDB; A7TNT1; -.
DR SMR; A7TNT1; -.
DR STRING; 436907.A7TNT1; -.
DR PRIDE; A7TNT1; -.
DR EnsemblFungi; EDO16074; EDO16074; Kpol_1016p14.
DR GeneID; 5544197; -.
DR KEGG; vpo:Kpol_1016p14; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; A7TNT1; -.
DR OMA; AVHIKAD; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000000267; 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 InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
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; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..732
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000310219"
FT DOMAIN 178..372
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 420..599
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 144..173
FT /note="Q motif"
FT MOTIF 307..310
FT /note="DEAD box"
FT COMPBIAS 9..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 732 AA; 82634 MW; 1CFB42137E3D2B3B CRC64;
MIEDDGMLLN FSTDTTEDNN DSKFNSGKVT GGRWKERRKL KMMMEGREPV KRKTFEELEN
SDMDTNKKPK SDSSGRKSYN QQSNNESVKD VVRPVVSKVN PSQVNTQIVS SLFTAARQVE
TSVNINEHDD KEEINPSNAP LAADNFDSLK IEQQLVNHLN EKMRIQKPTS IQKLVLPQLL
SSKNNDLFIH AQTGSGKTLA FALPILSKIL SMKTRVDRKS GCFAIFITPT RELATQIYHV
LSELTNCCHY LVPCLLIGGE SKKSEKARLR KGCNFIIGTP GRILDHFQNT QSVKEQLAVS
LRYVVLDEAD KLMELGFEET LTDILKLIHD ISLNTSVYPQ LPSRIMHILC SATSKGSVTK
LGNVALQNYK MISNSHVTNE LENATVPDQL LQKIAIVPPK LRLVTLAATL DSIHRKHIEQ
KKKKLDYVSR TVVFLSCSDS VNFHFEAFSS SDANHRNLVG ESARLLTKGN DILPSFDPEN
DPDFICYKLH GSLSQQIRSS TLQHFSKTNE NVKGKHLVLF CTDVASRGLD LPEIGTVIEL
DPPFAVEDHL HRIGRTARAG KHGESLLFLL PGEEEGYMEY IKPYHTKGWK LVNYTNDLLK
PSFQNVNVKR SDKETSKNVE EWDTNATTWH LNVERRVLED SSFKDIAMKG YASHIRAYAT
HISKEKKFFN VKCLHLGHLA KSFALRERPK TMGLQNTKNG GEAKKNSKES AKNKMFRLAR
MAVKQSSGEF NY
