DBP4_DEBHA
ID DBP4_DEBHA Reviewed; 766 AA.
AC Q6BXG0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ATP-dependent RNA helicase DBP4;
DE EC=3.6.4.13;
GN Name=DBP4; OrderedLocusNames=DEHA2B03322g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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-dependent RNA helicase required for ribosome biogenesis.
CC Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC Required for pre-rRNA cleavage at site A2 (By similarity).
CC {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: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC ribosomal complexes (By similarity). {ECO:0000250}.
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. DDX10/DBP4
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382134; CAG85100.2; -; Genomic_DNA.
DR RefSeq; XP_457109.2; XM_457109.1.
DR AlphaFoldDB; Q6BXG0; -.
DR SMR; Q6BXG0; -.
DR STRING; 4959.XP_457109.2; -.
DR PRIDE; Q6BXG0; -.
DR EnsemblFungi; CAG85100; CAG85100; DEHA2B03322g.
DR GeneID; 2913044; -.
DR KEGG; dha:DEHA2B03322g; -.
DR VEuPathDB; FungiDB:DEHA2B03322g; -.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; Q6BXG0; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000000599; Chromosome B.
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 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; 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..766
FT /note="ATP-dependent RNA helicase DBP4"
FT /id="PRO_0000232198"
FT DOMAIN 77..251
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 265..437
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 46..74
FT /note="Q motif"
FT MOTIF 199..202
FT /note="DEAD box"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 766 AA; 86824 MW; 3BC6ED32F0C4F268 CRC64;
MGKKQNNRKV VKSQRKSHRE KEEETLAKLQ ERIDAYDPVV DEKSISQFSD LPISEETARG
LKEASFASLT DIQKKTIPIS LKGEDVMGTA KTGSGKTLAF LIPTIESLIR NKITEYDGLA
ALIISPTREL AVQIFEVLVK IGKHNNFSAG LVTGGKDVKY EKERVSKMNI LVGTPGRISQ
HLNESVGMET SNLQVLVLDE ADRCLDMGFK KQIDNILGHL PPTRQTLLFS ATQSDSVKDL
ARLSLANPKR VGISSDQELS ATPESLEQYY IKIPLDEKLD VLWSFIKSHL KSKILVFFSS
SKQVQYAYET FRTLQPGISL LKLYGRHKQT SRMETTMKFS QAQHACLFAT DIVARGLDFP
AIDWVVQIDC PEDAATYVHR VGRAARFGRA GKSLMMLLPS EENGMLKRLN NNKIELKFMN
IKQKNKKTIR PQLQSLCFQD PMIKNLGQRA FISYFRSVYV QKDKDIFKID ELPSDKFARS
LGLPGAPKIK FKGGSDNKEK KNMSRQLAAL SKSNNEGDVV PEEDKKVRTK YDRMFERKNQ
TILSDHYLNL TGSKADTAEK SDDDDEDFMA VKRQDHELRD DELPDLSIPV SKRSAKKALS
KKASVAGKGN ANKLKFDDDG VAHAIYELED EEDFKKQGDA RVQKDTFLNK ETELMNNADI
EDKLTAKEKR QEKKRKRKEM EKNMRQESDD EDENIQTVVS IGGDDIDLDR DLEHSSADED
VPEPKKPKWF DNDKNVNKDE DDGVVEYDEP QTLEDLEALT SKLLEH
