DBP4_YEAS7
ID DBP4_YEAS7 Reviewed; 770 AA.
AC A6ZPU3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=ATP-dependent RNA helicase DBP4;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 4;
DE AltName: Full=Helicase CA4;
DE AltName: Full=Helicase UF1;
GN Name=DBP4; Synonyms=HCA4; ORFNames=SCY_2904;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000040; EDN63303.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZPU3; -.
DR SMR; A6ZPU3; -.
DR IntAct; A6ZPU3; 1.
DR PRIDE; A6ZPU3; -.
DR EnsemblFungi; EDN63303; EDN63303; SCY_2904.
DR HOGENOM; CLU_003041_26_1_1; -.
DR Proteomes; UP000007060; 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 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; 1.
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 Phosphoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..770
FT /note="ATP-dependent RNA helicase DBP4"
FT /id="PRO_0000310202"
FT DOMAIN 72..246
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 278..437
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 705..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..69
FT /note="Q motif"
FT MOTIF 194..197
FT /note="DEAD box"
FT COMPBIAS 717..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20448"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20448"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20448"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20448"
SQ SEQUENCE 770 AA; 87183 MW; 0C9E4DED1090D09E CRC64;
MAKKNRLNTT QRKTLRQKED EYIENLKTKI DEYDPKITKA KFFKDLPISD PTLKGLRESS
FIKLTEIQAD SIPVSLQGHD VLAAAKTGSG KTLAFLVPVI EKLYREKWTE FDGLGALIIS
PTRELAMQIY EVLTKIGSHT SFSAGLVIGG KDVKFELERI SRINILIGTP GRILQHLDQA
VGLNTSNLQM LVLDEADRCL DMGFKKTLDA IVSTLSPSRQ TLLFSATQSQ SVADLARLSL
TDYKTVGTHD VMDGSVNKEA STPETLQQFY IEVPLADKLD ILFSFIKSHL KCKMIVFLSS
SKQVHFVYET FRKMQPGISL MHLHGRQKQR ARTETLDKFN RAQQVCLFAT DVVARGIDFP
AVDWVVQVDC PEDVDTYIHR VGRCARYGKK GKSLIMLTPQ EQEAFLKRLN ARKIEPGKLN
IKQSKKKSIK PQLQSLLFKD PELKYLGQKA FISYVRSIYV QKDKQVFKFD ELPTEEFAYS
LGLPGAPKIK MKGMKTIEQA KERKNAPRQL AFLSKANEDG EVIEDKSKQP RTKYDKMFER
KNQTILSEHY LNITKAQAQE DEDDDFISVK RKDHEINEAE LPALTLPTSR RAQKKALSKK
ASLASKGNAS KLIFDDEGEA HPVYELEDEE EFHKRGDAEV QKTEFLTKES AVMADIDNID
KQVAKEKKQE KKRKRLEAMR REMEAAMEEE ISGDEEEGKT VAYLGTGNLS DDMSDGDMSD
SEGHLKKKAR TVDYSHGHNP SNSVDDDIIE VEEPQTLEDL ESLTAKLIQG
