(data stored in ACNUC7421 zone)

SWISSPROT: D6XWF6_BACIE

ID   D6XWF6_BACIE            Unreviewed;       483 AA.
AC   D6XWF6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=ATP-dependent RNA helicase DbpA {ECO:0000256|HAMAP-Rule:MF_00965};
DE            EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_00965};
GN   Name=dbpA {ECO:0000256|HAMAP-Rule:MF_00965};
GN   OrderedLocusNames=Bsel_0254 {ECO:0000313|EMBL:ADH97798.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97798.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97798.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DEAD-box RNA helicase involved in the assembly of the
CC       50S ribosomal subunit. Has an RNA-dependent ATPase activity, which
CC       is specific for 23S rRNA, and a 3' to 5' RNA helicase activity
CC       that uses the energy of ATP hydrolysis to destabilize and unwind
CC       short rRNA duplexes. {ECO:0000256|HAMAP-Rule:MF_00965}.
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         Evidence={ECO:0000256|HAMAP-Rule:MF_00965};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00965}.
CC   -!- DOMAIN: Contains an N-terminal domain that binds non-specifically
CC       to RNA and a C-terminal domain that binds specifically and tightly
CC       to hairpin 92 of 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00965}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DbpA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00965}.
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DR   EMBL; CP001791; ADH97798.1; -; Genomic_DNA.
DR   RefSeq; WP_013171227.1; NC_014219.1.
DR   STRING; 439292.Bsel_0254; -.
DR   EnsemblBacteria; ADH97798; ADH97798; Bsel_0254.
DR   KEGG; bse:Bsel_0254; -.
DR   eggNOG; COG0513; LUCA.
DR   HOGENOM; HOG000268809; -.
DR   KO; K05592; -.
DR   OMA; RNPIRIL; -.
DR   OrthoDB; 626183at2; -.
DR   BioCyc; BSEL439292:G1GLR-278-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0034459; F:ATP-dependent 3'-5' RNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR   CDD; cd00079; HELICc; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_00965; DEAD_helicase_DbpA; 1.
DR   InterPro; IPR005580; DbpA/CsdA_RNA-bd_dom.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR028619; DEAD_helicase_DbpA.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF03880; DbpA; 1.
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; 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;
DR   PRODOM; D6XWF6.
DR   SWISS-2DPAGE; D6XWF6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00965};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00965};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_00965,
KW   ECO:0000313|EMBL:ADH97798.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00965};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00965};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00965};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00965}.
FT   DOMAIN        4     32       Q_MOTIF. {ECO:0000259|PROSITE:PS51195}.
FT   DOMAIN       35    205       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      231    380       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   REGION      406    483       Involved in 23S rRNA binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00965}.
FT   MOTIF         4     32       Q motif. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00552}.
SQ   SEQUENCE   483 AA;  54022 MW;  C3FE62910D999A63 CRC64;
     MTHDSFQAFG LSDEIVRALN ELNMTMPTDV QKQVIPLAME NKDVLVTSQT GTGKTASYAI
     PICDTVDWEE NRPQALILSP TRELAVQIQE DITNIGRFRR IKATALYGQE PVNKQKLELK
     QKTHVVVGTP GRVLDHIKKG TLMLNRIEHL VIDEADQMLD MGFIDQVEAI LASLPKERTT
     SLFSATMRNE IRALAGRHMN APDQIAIKQE TVAADTIDQS VIHVTNKEKL QLLQDVTVVE
     NPDSCLIFCN TQESVDLLET SLNKEGYRAR KIHGGLPQKE RFSVMEAFKR GSFRYLIATN
     VAARGIDIDS VSLVINYDVP FEKESYVHRT GRTGRAGKAG KAITFVNNRE KSAIRELERY
     TGIIIPLAKA PSPDEVKRAR NTFYEKLNTA PVRKEKKSAN LNKEIMTLYV NGGKKKKLRA
     PDFVGTLTSI DGIDADDIGI ITIQETSTTI DIFNGKGPLA LKELKERTVK GKRLKVREAR
     NRS
//

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