DBP7_YARLI
ID DBP7_YARLI Reviewed; 799 AA.
AC Q6C835;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ATP-dependent RNA helicase DBP7;
DE EC=3.6.4.13;
GN Name=DBP7; OrderedLocusNames=YALI0D23133g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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-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; CR382130; CAG81377.1; -; Genomic_DNA.
DR RefSeq; XP_503177.1; XM_503177.1.
DR AlphaFoldDB; Q6C835; -.
DR SMR; Q6C835; -.
DR STRING; 4952.CAG81377; -.
DR PRIDE; Q6C835; -.
DR EnsemblFungi; CAG81377; CAG81377; YALI0_D23133g.
DR GeneID; 2910285; -.
DR KEGG; yli:YALI0D23133g; -.
DR VEuPathDB; FungiDB:YALI0_D23133g; -.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; Q6C835; -.
DR OMA; LERIMSC; -.
DR Proteomes; UP000001300; Chromosome D.
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:0042254; P:ribosome biogenesis; IBA:GO_Central.
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; 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..799
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000256029"
FT DOMAIN 265..465
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 511..679
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 34..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 233..261
FT /note="Q motif"
FT MOTIF 391..394
FT /note="DEAD box"
FT COMPBIAS 207..221
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 278..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 306..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 799 AA; 89657 MW; F2218F307EB66C43 CRC64;
MMLNLVVADG PRQLSAREKA AKLKKSGLSF AQRKALREEE KKNAWKKEQG GITTTIEDRM
KRREQDNPPV RPKPYDKPYE KKPYEKKPFE KKPYEKKSYD KPVASKPVEE TDEEKYQRLM
EGGKRPEKER WVPQRNFRNR RDMEKAGKDQ SQDATPKHHD RDVIGTREDG SLIRRIREKT
GAKGGIKGTY VSSIFSEKKE DRIAGEDVQM EDEEEEEAEN NAESSNAALK DSTTFSGLGC
SQRLVDALVG MQLAKPTKIQ RATIPRLIQR ERDLFVQAQT GSGKTLAFVL PVLERIMSCD
DVSRETGLFA VILTPTRELT TQIYSVLETL CRKACPWIVP GIVIGGEKKK SEKARIRKGV
NILVATPGRL ADHFDNTEAL DLSQVRWVVL DEGDRLMELG FEETITKILR TIEWKSVLRG
ENYLKDIPKN LKPLPSRRVT VLCSATMKGG VTELGKSTLK DADWVSNDSV EDALAETSVE
TFSAPSQLVQ EWVVVPAKLR LVTLLGALRG DILQSSEKTN TKVIVFLSCS DSVDFHFDVL
SRDGSQINKM DTAKTAPLLL DDVSTSVYKL HGSLSQQART ATLASFAKNS TPSILLCTDV
ASRGLDLPKI THVIEYDPPF SIEDHLHRVG RTARAGQDGR ALLFLLPGAE EGYVEKLKQS
QQMKKTTYEN ILAAGFGGKG WDFAATNYHL DVERWVLGDE TALDRARRGF TSHIRAYATH
IAAEKDMFNV RMLHLGHLAK SFALREAPGK LGKKKDPEKI KVNKDGSLDE TQARKKMLDR
SRKHVYNSGE SAMGGYVLE
