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Database: UniProt/TrEMBL
Entry: B2FRR8_STRMK
LinkDB: B2FRR8_STRMK
Original site: B2FRR8_STRMK 
ID   B2FRR8_STRMK            Unreviewed;       329 AA.
AC   B2FRR8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   01-OCT-2014, entry version 37.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003886};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003886};
GN   Name=rluD {ECO:0000313|EMBL:CAQ47158.1};
GN   OrderedLocusNames=Smlt3747 {ECO:0000313|EMBL:CAQ47158.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ47158.1, ECO:0000313|Proteomes:UP000008840};
RN   [1] {ECO:0000313|EMBL:CAQ47158.1, ECO:0000313|Proteomes:UP000008840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a {ECO:0000313|EMBL:CAQ47158.1,
RC   ECO:0000313|Proteomes:UP000008840};
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N.,
RA   Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R.,
RA   Rutter S., Quail M.A., Rajandream M.A., Harris D., Churcher C.,
RA   Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by
RT   drug resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase rluA family.
CC       {ECO:0000256|RuleBase:RU004243}.
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DR   EMBL; AM743169; CAQ47158.1; -; Genomic_DNA.
DR   RefSeq; YP_001973446.1; NC_010943.1.
DR   STRING; 522373.Smlt3747; -.
DR   EnsemblBacteria; CAQ47158; CAQ47158; Smlt3747.
DR   GeneID; 6393188; -.
DR   KEGG; sml:Smlt3747; -.
DR   PATRIC; 23702949; VBISteMal45202_3526.
DR   eggNOG; COG0564; -.
DR   HOGENOM; HOG000275919; -.
DR   KO; K06180; -.
DR   OMA; HTIVNTD; -.
DR   OrthoDB; EOG6P070X; -.
DR   BioCyc; SMAL522373:GJE8-3624-MONOMER; -.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   Gene3D; 3.10.290.10; -; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom.
DR   InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR   InterPro; IPR006224; PsdUridine_synth_RluC/D_CS.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluD.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00005; rluA_subfam; 1.
DR   PROSITE; PS01129; PSI_RLU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008840};
KW   Isomerase {ECO:0000256|RuleBase:RU003886};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008840}.
SQ   SEQUENCE   329 AA;  36414 MW;  E781B2EB0BF61A18 CRC64;
     MSEQPSESAR QAIVPDTAAG RRFDAVVAEL FPEYSRSRLT EWIKAGEVLL DGAQVRPRDP
     LRGGEVVTLN VVLETQTDAQ PEDIPLDVLF EDEHLLVINK PVGLVVHPGA GNHSGTLVNA
     LLFRDPSVAV LPRAGIVHRL DKDTSGVMVV AKTLEAQTAL VEQLAARDVH RQYLAIVMGA
     LVAGGTADAP IDRHPRDRLK MAVREDGKEA ITHYRLRERF RAHTALECRL ETGRTHQIRV
     HMAHVRHPII GDPLYGGALK LPKGASDELV AALRGFKRQA LHAETLEFTH PITGELVRNT
     APVPEDMLHL MKVLREDSEA FAARERDRW
//
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