DBP10_YEAS7
ID DBP10_YEAS7 Reviewed; 995 AA.
AC A6ZXU0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=ATP-dependent RNA helicase DBP10;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 10;
GN Name=DBP10; ORFNames=SCY_0878;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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 -!- SUBUNIT: Interacts with RRP1 and associates with pre-ribosomal
CC particles. {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. DDX54/DBP10
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFW02000145; EDN60320.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZXU0; -.
DR SMR; A6ZXU0; -.
DR PRIDE; A6ZXU0; -.
DR EnsemblFungi; EDN60320; EDN60320; SCY_0878.
DR HOGENOM; CLU_003041_5_2_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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; 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 Phosphoprotein; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..995
FT /note="ATP-dependent RNA helicase DBP10"
FT /id="PRO_0000310247"
FT DOMAIN 168..340
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 418..568
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 137..165
FT /note="Q motif"
FT MOTIF 288..291
FT /note="DEAD box"
FT COMPBIAS 38..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12389"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12389"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12389"
SQ SEQUENCE 995 AA; 112961 MW; B01DDBB907B475EA CRC64;
MAGVQKRKRD LEDQDDNGSE EDDIAFDIAN EIALNDSESD ANDSDSEVEA DYGPNDVQDV
IEYSSDEEEG VNNKKKAENK DIKKKKNSKK EIAAFPMLEM SDDENNASGK TQTGDDEDDV
NEYFSTNNLE KTKHKKGSFP SFGLSKIVLN NIKRKGFRQP TPIQRKTIPL ILQSRDIVGM
ARTGSGKTAA FILPMVEKLK SHSGKIGARA VILSPSRELA MQTFNVFKDF ARGTELRSVL
LTGGDSLEEQ FGMMMTNPDV IIATPGRFLH LKVEMNLDLK SVEYVVFDEA DRLFEMGFQE
QLNELLASLP TTRQTLLFSA TLPNSLVDFV KAGLVNPVLV RLDAETKVSE NLEMLFLSSK
NADREANLLY ILQEIIKIPL ATSEQLQKLQ NSNNEADSDS DDENDRQKKR RNFKKEKFRK
QKMPAANELP SEKATILFVP TRHHVEYISQ LLRDCGYLIS YIYGTLDQHA RKRQLYNFRA
GLTSILVVTD VAARGVDIPM LANVINYTLP GSSKIFVHRV GRTARAGNKG WAYSIVAENE
LPYLLDLELF LGEKILLTPM YDSLVDVMKK RWIDEGKPEY QFQPPKLSYT KRLVLGSCPR
LDVEGLGDLY KNLMSSNFDL QLAKKTAMKA EKLYYRTRTS ASPESLKRSK EIISSGWDAQ
NAFFGKNEEK EKLDFLAKLQ NRRNKETVFE FTRNPDDEMA VFMKRRRKQL APIQRKATER
RELLEKERMA GLSHSIEDEI LKGDDGETGY TVSEDALKEF EDADQLLEAQ ENENKKKKKP
KSFKDPTFFL SHYAPAGEIQ DKQLQITNGF ANDAAQAAYD LNSDDKVQVH KQTATVKWDK
KRKKYVNTQG IDNKKYIIGE SGQKIAASFR SGRFDDWSKA RNLKPLKVGS RETSIPSNLL
EDPSQGPAAN GRTVRGKFKH KQMKAPKMPD KHRDNYYSQK KKVEKALQSG ISVKGYNNAP
GLRSELKSTE QIRKDRIIAE KKRAKNARPS KKRKF
