DBP9_CANAL
ID DBP9_CANAL Reviewed; 574 AA.
AC Q5A4P9; A0A1D8PPR3; O93990;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=ATP-dependent RNA helicase DBP9;
DE EC=3.6.4.13;
GN Name=DBP9; OrderedLocusNames=CAALFM_C601890CA;
GN ORFNames=Ca20C1.02, CaO19.10896, CaO19.3393;
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=1161;
RA Oliver K., Harris D., Barrell B.G., Rajandream M.A.;
RT "Candida albicans strain 1161 genome pilot sequencing project.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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-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. DDX56/DBP9
CC subfamily. {ECO:0000305}.
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DR EMBL; AL033391; CAA21924.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30125.1; -; Genomic_DNA.
DR RefSeq; XP_716703.2; XM_711610.2.
DR AlphaFoldDB; Q5A4P9; -.
DR SMR; Q5A4P9; -.
DR STRING; 237561.Q5A4P9; -.
DR GeneID; 3641598; -.
DR KEGG; cal:CAALFM_C601890CA; -.
DR CGD; CAL0000180288; orf19.10896.
DR VEuPathDB; FungiDB:C6_01890C_A; -.
DR HOGENOM; CLU_003041_17_1_1; -.
DR InParanoid; Q5A4P9; -.
DR OMA; GYEKDFK; -.
DR OrthoDB; 973872at2759; -.
DR PRO; PR:Q5A4P9; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005730; C:nucleolus; 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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 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..574
FT /note="ATP-dependent RNA helicase DBP9"
FT /id="PRO_0000232337"
FT DOMAIN 46..224
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 235..455
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 324..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..42
FT /note="Q motif"
FT MOTIF 170..173
FT /note="DEAD box"
FT COMPBIAS 324..339
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 332
FT /note="D -> N (in Ref. 1; CAA21924)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="K -> N (in Ref. 1; CAA21924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 65186 MW; DFE1513342D3E826 CRC64;
MSTSASSSYL DDETTWDSFN LDPRLLQAID QLGFSNPTLI QSSAIPLALE EKRDIIAKAS
TGSGKTAAYC IPIVNNLLTD DSSQGIKSII LVPTRELSNQ VFQFVEKLLT FSTNKINVLN
LSSSYSDQVL NSLLVNKPEI IISTPAKLIQ ILEKNEKNID LSTVKNLTID EVDLVLSFGY
LDDLKKLESY LPVKKNLQTF LMSATVNDDL DDLKQRYCTK PAILKLNEDS ANQNNLVQYY
AKTTEFDKFL LAYVIFKLNL IKGKTIAFVN NIDRGYRLKL FLEQFGIRCC ILNSELPINS
RLHIVEEFNK NVYHLLIATD ETNELNEEQD DDEDGDEDTK DKGNAETKPK KSKKSKFKQD
KEYGVSRGVD FRNVACVLNF DLPTSSKAYI HRIGRTARAG KAGMALSFVL PLSEFGKHKT
ASLASAKKDE KVLGRIVKQQ SKNGFEIKPY QFDMKQVEGF RYRADDAFRA VTQTAVREAR
VKELKNELIN SEKLKRFFEE NPQDLASLRH DKELHPARIQ SQLKNVPQYL LPESARQDVK
NIGFVPFHKN KIHKHRKGKG KGRKKVDPLK SFRK
