DBP10_CANAL
ID DBP10_CANAL Reviewed; 908 AA.
AC Q5ANB2; A0A1D8PK49;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=ATP-dependent RNA helicase DBP10;
DE EC=3.6.4.13;
GN Name=DBP10; OrderedLocusNames=CAALFM_C305160CA;
GN ORFNames=CaO19.13412, CaO19.5991;
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-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. DDX54/DBP10
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017625; AOW28531.1; -; Genomic_DNA.
DR RefSeq; XP_723201.1; XM_718108.1.
DR AlphaFoldDB; Q5ANB2; -.
DR SMR; Q5ANB2; -.
DR STRING; 237561.Q5ANB2; -.
DR PRIDE; Q5ANB2; -.
DR GeneID; 3635229; -.
DR KEGG; cal:CAALFM_C305160CA; -.
DR CGD; CAL0000186628; orf19.13412.
DR VEuPathDB; FungiDB:C3_05160C_A; -.
DR eggNOG; KOG0337; Eukaryota.
DR HOGENOM; CLU_003041_5_1_1; -.
DR InParanoid; Q5ANB2; -.
DR OMA; MRWDKKS; -.
DR OrthoDB; 268859at2759; -.
DR PRO; PR:Q5ANB2; -.
DR Proteomes; UP000000559; Chromosome 3.
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; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR012541; DBP10_C.
DR InterPro; IPR033517; DDX54/DBP10.
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; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR24031:SF292; PTHR24031:SF292; 1.
DR Pfam; PF08147; DBP10CT; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM01123; DBP10CT; 1.
DR SMART; SM00487; DEXDc; 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..908
FT /note="ATP-dependent RNA helicase DBP10"
FT /id="PRO_0000232311"
FT DOMAIN 130..301
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 373..533
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 99..127
FT /note="Q motif"
FT MOTIF 249..252
FT /note="DEAD box"
FT COMPBIAS 23..38
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 908 AA; 103561 MW; CA20D4A7D93C712C CRC64;
MSDDEAFDIA GSLALKDEDD YSDSSSNEGE DFQDEIIPSD DEKEPSPPPK KKSKPNPQAF
PSLELSDNEG NNDDDDDDDS KINSYFINNN PTAKKAKAGS FASFGLTKFI LANIAKKGYK
QPTPIQRKTI PLIMEGRDVV GMARTGSGKT AAFVLPLIER LKSRQPGGVR AVILSPSREL
ALQTYKQVKE FSHGTNLQSI VLIGGDSLEE DFSKMMTKPD IIVCTPGRFL HLKVEMQYDL
MTVQYIVFDE ADRLFEMGFA EQLNELLASL PSNRQSLLFS ATLPRSLVDF AKAGLTNPVL
VRLDAESKIS DQLQMAYFTT KKNEREANLL YILQEVIKMP LGSEEQIKKL KDMDKRKIDS
DSEDDDDDEE RKKGKKRYKF KKERLPPANR LPSPHSTIVF VPTKHHVEYV TKLLRDAGYL
VSYIYGTLDQ HARKNQLYQF RVGLTNVLVV TDVAARGIDI PVLANVINFT LPASSKIFIH
RVGRTARAGN KGWAYSIVNE KELPYLLDLE LFLGKKILLT SMHEAKVEML KKSSTGTFIP
PVVNYTERLV LGSVPRVDLE TFQELYENLL RNNYEIKVLK DVAAKGEKLY HRTRQPASQE
SLKRSKEIIE SSWDDQHLLF GENLEKQKDA FLAKLQDRNS KQTVFELKGS DESLVEFMNR
RRRQLAPIQR KAKERKELLA KERLAGLTHG IEDEILRADG ENGYGVDEDE LQEAFEDADK
KKSFRDPQFF LSHYAPASVI QDQQLSLSTS FANEAQAATF DLDNDDKIQT NKQVMRWDKK
KGKYINSKST DKKYIISENG TKIPASFRSG KFDEWRKQRN LKPTSTVEDD SNKRFKHKQQ
RAPKLPDKFR DDYHKQKKKV EKAIESGVNV KGFHTPQQEI KSTEQIRKAR LLKEKRKAKN
ARPSKKRK
