DBP4_CANAL
ID DBP4_CANAL Reviewed; 765 AA.
AC Q5AF95; A0A1D8PLM9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=ATP-dependent RNA helicase DBP4;
DE EC=3.6.4.13;
GN Name=DBP4; Synonyms=HCA4; OrderedLocusNames=CAALFM_C402830CA;
GN ORFNames=CaO19.10227, CaO19.2712;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017626; AOW29049.1; -; Genomic_DNA.
DR RefSeq; XP_720463.1; XM_715370.1.
DR AlphaFoldDB; Q5AF95; -.
DR SMR; Q5AF95; -.
DR STRING; 237561.Q5AF95; -.
DR PRIDE; Q5AF95; -.
DR GeneID; 3637911; -.
DR KEGG; cal:CAALFM_C402830CA; -.
DR CGD; CAL0000199884; HCA4.
DR VEuPathDB; FungiDB:C4_02830C_A; -.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; Q5AF95; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 973872at2759; -.
DR PRO; PR:Q5AF95; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0034512; F:box C/D RNA binding; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0034511; F:U3 snoRNA binding; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; 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; 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 Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..765
FT /note="ATP-dependent RNA helicase DBP4"
FT /id="PRO_0000232196"
FT DOMAIN 79..253
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 267..439
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 655..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 48..76
FT /note="Q motif"
FT MOTIF 201..204
FT /note="DEAD box"
FT COMPBIAS 709..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 765 AA; 86722 MW; 60092246ECD3F7AE CRC64;
MAKNLKKGKK VFNKSTRKIN RLKEEEELAK LQERINNYDP KTDEASVSQF SDLPITENTL
KGLKEATFVS LTDIQKKTIP IALKGEDLMG TARTGSGKTL AFLIPVIESL IRNKITEYDG
LAALIVSPTR ELAVQIFEVL TKIGKYNTFS AGLVTGGKDV QFEKERVSRM NILVGTPGRI
SQHLNEAVGM ETSNLQVLVL DEADRCLDMG FKKQIDNILG HLPTTRQTLL FSATQSESVN
DLARLSLTNP NKIGVSSDQE VSATPESLEQ YYVKVPLDEK LDVLWSFIKS HLKSKILVFF
SSSKQVQYTY ETFRTLQPGI SLMKLYGRHK QTSRLETTMK FSQAQHACLF ATDIVARGLD
FPAIDWVVQV DCPEDAATYV HRVGRSARFG RKGKSLLMLL PSEEEGMLKR LKIHKIEPKL
MNIKQKSKKS IRPQLQSLCF KDPVMKNLGQ RAFIAYFKSV HIQKDKDVFK VEELPAESYA
ASLGLPGAPK IKIKGGESNK EKKNASRKLI ALAKTDADGE VQTGNEKVRT KYDRMFERKN
QTILSDHYLN MTGNKVNSDG ESEDEDFMTV KRKDHELKEE ELPDLTIPVS KRQAKKALSR
KATLASKGNP TKLKFDDDGV AHAIYELEDE DDFIKAGDAK KQKEEFVNKE RETMKISDIT
DKEVERQKRQ EKKRKRKEIE RRMREEEEED FDNEQTVVTL GAPDLDRDLQ YDNGSDVEEP
VSKKPKWFEG GDDDKSKNTN DGFVEYDEPE TLEDLESLTA RLIGN
