DBP10_CANGA
ID DBP10_CANGA Reviewed; 969 AA.
AC Q6FNA2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=ATP-dependent RNA helicase DBP10;
DE EC=3.6.4.13;
GN Name=DBP10; OrderedLocusNames=CAGL0K01551g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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-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; CR380957; CAG61253.1; -; Genomic_DNA.
DR RefSeq; XP_448292.1; XM_448292.1.
DR AlphaFoldDB; Q6FNA2; -.
DR SMR; Q6FNA2; -.
DR STRING; 5478.XP_448292.1; -.
DR EnsemblFungi; CAG61253; CAG61253; CAGL0K01551g.
DR GeneID; 2890018; -.
DR KEGG; cgr:CAGL0K01551g; -.
DR CGD; CAL0134057; CAGL0K01551g.
DR VEuPathDB; FungiDB:CAGL0K01551g; -.
DR eggNOG; KOG0337; Eukaryota.
DR HOGENOM; CLU_003041_5_1_1; -.
DR InParanoid; Q6FNA2; -.
DR OMA; MRWDKKS; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; 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:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IEA:EnsemblFungi.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
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..969
FT /note="ATP-dependent RNA helicase DBP10"
FT /id="PRO_0000232312"
FT DOMAIN 146..318
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 396..543
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 115..143
FT /note="Q motif"
FT MOTIF 266..269
FT /note="DEAD box"
FT COMPBIAS 34..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..969
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 969 AA; 109562 MW; 3E2CCA59606C8401 CRC64;
MVKNLKRKER DEHESDSDEE IDIAGNLVAD GSDSESDDSS DGSDEEVQDV IEYSSDEEEP
AKPAKAVKKK VEDKSFPSLE LSDDEDEKKK VDNDDDDVNA YFSVNTDAKS KHKKGSFASF
GLSKLILVNI SKRGFRQPTP IQRKTIPLIL QNRDIVGMAR TGSGKTAAFV LPMIEKLKTH
SSKIGARAII LSPSRELAMQ THSVFKEFSR GTHLRSVLLT GGDSLEDQFG MMMTNPDVII
ATPGRFLHLK VEMNLDLKSV EYAVFDEADR LFEMGFQEQL NELLAALPSS RQTLLFSATL
PTSLVDFAKA GLVNPVLVRL DAESKISDNL EMLFLSTKND EREANLLYIL QEVIKLPLAT
PEQIKQLNDN KADDSDESAE EDEDKKRRKR KSFNRKAMPK ANELPSEKAT VVFVPTRHHV
EYLSNLLKDC GYLVSYIYGA LDQHARKSQL YNFRIGLTSI LVVTDVAARG VDIPMLANVV
NYSLPASSKI FIHRVGRTAR AGNRGWAYSI VSENELPYLL DLELFLGRKI LLTPMYEALE
RLSKEKWVAE GNDETLFQSP KISYTSRMVL GSCPRLDIEA LSELYNNLMK SNFDLDMAKK
TALKAEKLYF RTRTSASPES LKRSKEIISS GWDEQNVLFG KNLEKEKNAF LEKLQNRRNK
ETVFEFTRNP EDEMANLMHR RRRAIAPIQR KAKERKELLE KERMAGLTHA LEDEILKGDD
AEVGYTVTED TLKAFEDADT ILAEQENASK KKKKTFRDPN FFLSHYAPAN EIQDKQLELS
GGFINEAAQS AYDLNSDDKV QVHKQTATVK WDKKRKKYVN MNGIDNKKYI IGESGQKIAA
SFRSGKFDEW SKARKLAPLK TGANESSIPS NLLVDPTRGP GKSGSKLPNG KFKHKLEKAP
RLPDKKRDDY HKQKKKVESA LERGIAVKGY NNAPAFKSEL KSVAQIRKDR KTKENRHAKN
ARPSKKRKF
