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Database: UniProt
Entry: A0A0N9U5J1_SPHMC
LinkDB: A0A0N9U5J1_SPHMC
Original site: A0A0N9U5J1_SPHMC 
ID   A0A0N9U5J1_SPHMC        Unreviewed;       216 AA.
AC   A0A0N9U5J1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   ORFNames=AN936_08735 {ECO:0000313|EMBL:ALH80450.1};
OS   Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH80450.1, ECO:0000313|Proteomes:UP000058074};
RN   [1] {ECO:0000313|EMBL:ALH80450.1, ECO:0000313|Proteomes:UP000058074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EY-1 {ECO:0000313|EMBL:ALH80450.1,
RC   ECO:0000313|Proteomes:UP000058074};
RX   PubMed=26634754;
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT   Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC       {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR   EMBL; CP012700; ALH80450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N9U5J1; -.
DR   KEGG; smag:AN936_08735; -.
DR   PATRIC; fig|33050.5.peg.1816; -.
DR   Proteomes; UP000058074; Chromosome.
DR   GO; GO:0140098; F:catalytic activity, acting on RNA; IEA:UniProt.
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   GO; GO:0006364; P:rRNA processing; IEA:UniProt.
DR   Gene3D; 3.30.70.1560; Alpha-L RNA-binding motif; 1.
DR   Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 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; IPR020094; TruA/RsuA/RluB/E/F_N.
DR   NCBIfam; TIGR00093; pseudouridine synthase; 1.
DR   PANTHER; PTHR47683; PSEUDOURIDINE SYNTHASE FAMILY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47683:SF3; RIBOSOMAL LARGE SUBUNIT PSEUDOURIDINE SYNTHASE B; 1.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR   PROSITE; PS01149; PSI_RSU; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003887};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058074}.
FT   DOMAIN          45..174
FT                   /note="Pseudouridine synthase RsuA/RluA-like"
FT                   /evidence="ECO:0000259|Pfam:PF00849"
SQ   SEQUENCE   216 AA;  24507 MW;  9EB55423EB0271B3 CRC64;
     MVEEGRIALN GQVIVHPAPL LTSLEGLTVD GNPVAKPVST RLYRFHKPSG CLTAARDPKG
     RKTIYDLLPK DLPRLMPVGR LDYNTEGLLL LTNDGEFKRQ LELPASGVER TYRARAFGDI
     SQTQLEDLVE GIEIDGIRYG KIDANLERRT GRNQWIEMTL TEGKNREVRR VLEHLGLQVS
     RLIRTRYGQF TLEALDVGAV EIVPRDELFQ FRRRMG
//
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