(data stored in ACNUC7421 zone)

SWISSPROT: B4SIF1_STRM5

ID   B4SIF1_STRM5            Unreviewed;       233 AA.
AC   B4SIF1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   OrderedLocusNames=Smal_0451 {ECO:0000313|EMBL:ACF50156.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50156.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50156.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50156.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC       {ECO:0000256|RuleBase:RU003887, ECO:0000256|SAAS:SAAS01169812}.
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DR   EMBL; CP001111; ACF50156.1; -; Genomic_DNA.
DR   RefSeq; WP_004140604.1; NC_011071.1.
DR   STRING; 391008.Smal_0451; -.
DR   EnsemblBacteria; ACF50156; ACF50156; Smal_0451.
DR   KEGG; smt:Smal_0451; -.
DR   eggNOG; ENOG4105I08; Bacteria.
DR   eggNOG; COG1187; LUCA.
DR   HOGENOM; HOG000044954; -.
DR   KO; K06183; -.
DR   OMA; QGKYHQV; -.
DR   OrthoDB; 1037615at2; -.
DR   BioCyc; SMAL391008:SMAL_RS02320-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   Gene3D; 3.10.290.10; -; 1.
DR   Gene3D; 3.30.70.1560; -; 1.
DR   InterPro; IPR042092; PsdUridine_s_RsuA/RluB/E/F_cat.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   InterPro; IPR000748; PsdUridine_synth_RsuA/RluB/E/F.
DR   InterPro; IPR018496; PsdUridine_synth_RsuA/RluB_CS.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00093; TIGR00093; 1.
DR   PROSITE; PS01149; PSI_RSU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SIF1.
DR   SWISS-2DPAGE; B4SIF1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Isomerase {ECO:0000256|RuleBase:RU003887,
KW   ECO:0000256|SAAS:SAAS00999454};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182,
KW   ECO:0000256|SAAS:SAAS00999393}.
FT   DOMAIN        1     66       S4 RNA-binding. {ECO:0000259|PROSITE:
FT                                PS50889}.
SQ   SEQUENCE   233 AA;  26010 MW;  F409BBE31A677B26 CRC64;
     MKLVKLIANL GYGSRKQVQW MFREGRVTDA DGEVLYADDQ VPHEAVRVDG EPLDPPVGLS
     IALHKPAGYT CSTKDKGRLI YDLLPPRYRD RDPVLSTVGR LDRDTSGLLL LTDDGGLLHR
     IISPKSKLPK VYEVELSDDL RGDEVALFAS GTLMLESEKT PLLPAELEVL DARRARLVLH
     EGRYHQVRRM FAATGNHVQA LHRSRVGGLD LQGLDEGQWR QLTPTDLDTL FAP
//

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