DBP10_PICST
ID DBP10_PICST Reviewed; 931 AA.
AC A3LZT3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=ATP-dependent RNA helicase DBP10;
DE EC=3.6.4.13;
GN Name=DBP10; ORFNames=PICST_80003;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; CP000502; ABN68395.2; -; Genomic_DNA.
DR RefSeq; XP_001386424.2; XM_001386387.1.
DR AlphaFoldDB; A3LZT3; -.
DR SMR; A3LZT3; -.
DR STRING; 4924.XP_001386424.2; -.
DR EnsemblFungi; ABN68395; ABN68395; PICST_80003.
DR GeneID; 4841046; -.
DR KEGG; pic:PICST_80003; -.
DR eggNOG; KOG0337; Eukaryota.
DR HOGENOM; CLU_003041_5_2_1; -.
DR InParanoid; A3LZT3; -.
DR OMA; MRWDKKS; -.
DR OrthoDB; 268859at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
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; 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; 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; 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..931
FT /note="ATP-dependent RNA helicase DBP10"
FT /id="PRO_0000285154"
FT DOMAIN 130..302
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 372..532
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 99..127
FT /note="Q motif"
FT MOTIF 250..253
FT /note="DEAD box"
FT COMPBIAS 24..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..910
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 931 AA; 105714 MW; 8344E8A4B7098C81 CRC64;
MSDNEEDYDI ARSLTVNLED SDSDSGSDFS DEEQEVQDII SSEDEAEEQP KKKQKTAKPA
KEAFPSLELS GDEDEQDDDK DMASYFAANN PQAKKAKAGS FQSFGLSKLV LTNIAKKGYR
QPTPIQRKTI PLIMANRDVV GMARTGSGKT AAFTLPVIEK LKGHSARVGI RAIILSPSRE
LALQTYKQVK EFSKGSDLRA IVLTGGDSLE DQFSSMVSNP DIVIATPGRF LHLQVEMQLD
LKTVEYIVFD EADHLFEQGF AEQLNELLAV LPPQRQSLLF SATLPRSLVD FAKAGLSNPV
LVRLDADSKI SDQLQMAFFT TKKNEREANL LYVLQEVIKM PLGTAEQIKK LRLMDKRVND
EAEEEELENE SGSKRKYKFK KERLPSANVL PSPHSTIVFV PTKHHVEYIT TLLRDAGYLV
SYIYGTLDQH ARKNQLYQFR LGMTTVLVVT DVAARGIDIP VLANVVNYTL PGSSKIFIHR
VGRTARAGNK GWAYSIVNEK ELPYLLDLEL FLGKKILLTA MQEQKCQLLK DKQGDNYVEP
KVQYTDRLVL GSCPRLSLET FEELYENLLR NHYELSVIKE VAAKGEKLYY RTRKAASTES
VKRAKEIMDT GTWDDQHLLF GPNLEKEKEK FLAKLANRHV KETVFEFNKK GNDRDEDSLV
SFMHRRRKQL APIQRRASER RDLLQREREA GLTHGIEDEI LKAHGETGYS ASGINDVDEE
ELQNAFEDAD QLSSKSNKKN YRDDRFFISH YAPASVIQDQ QLNITSSFAN EAASATFDLD
NDDKIGNGKQ VMQWDRKKGK YINSQSTDKK FIIGESGAKI PATYRSGKFD EWKKKRNMQP
AKVGSLETEG ESKQRFKHKR NAAPKLPDKY RDDYHKQKKK VEKAVESGRD VKGYHKPGQR
SEIKSTEDIR KARLLKEKKM AKNARPSRKR K