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Database: UniProt
Entry: K4PSJ9_SHEON
LinkDB: K4PSJ9_SHEON
Original site: K4PSJ9_SHEON 
ID   K4PSJ9_SHEON            Unreviewed;       237 AA.
AC   K4PSJ9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   OrderedLocusNames=SO_3583 {ECO:0000313|EMBL:AFV73583.1};
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586 {ECO:0000313|EMBL:AFV73583.1, ECO:0000313|Proteomes:UP000008186};
RN   [1] {ECO:0000313|EMBL:AFV73583.1, ECO:0000313|Proteomes:UP000008186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1 {ECO:0000313|EMBL:AFV73583.1,
RC   ECO:0000313|Proteomes:UP000008186};
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA   Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA   Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-516 in
CC       16S ribosomal RNA. {ECO:0000256|ARBA:ARBA00037590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(516) in 16S rRNA = pseudouridine(516) in 16S rRNA;
CC         Xref=Rhea:RHEA:38867, Rhea:RHEA-COMP:10089, Rhea:RHEA-COMP:10090,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00036749};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC       {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR   EMBL; AE014299; AFV73583.1; -; Genomic_DNA.
DR   RefSeq; WP_011073403.1; NC_004347.2.
DR   RefSeq; YP_007001394.1; NC_004347.2.
DR   AlphaFoldDB; K4PSJ9; -.
DR   STRING; 211586.SO_3583; -.
DR   PaxDb; 211586-SO_3583; -.
DR   KEGG; son:SO_3583; -.
DR   eggNOG; COG1187; Bacteria.
DR   HOGENOM; CLU_024979_1_2_6; -.
DR   OrthoDB; 9807213at2; -.
DR   PhylomeDB; K4PSJ9; -.
DR   BioCyc; SONE211586:G1GMP-3343-MONOMER; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProt.
DR   GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central.
DR   CDD; cd02553; PseudoU_synth_RsuA; 1.
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   Gene3D; 3.10.290.10; RNA-binding S4 domain; 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   InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR   NCBIfam; TIGR00093; pseudouridine synthase; 1.
DR   PANTHER; PTHR47683:SF4; PSEUDOURIDINE SYNTHASE; 1.
DR   PANTHER; PTHR47683; PSEUDOURIDINE SYNTHASE FAMILY PROTEIN-RELATED; 1.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR   PROSITE; PS01149; PSI_RSU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003887};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008186};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          6..64
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
SQ   SEQUENCE   237 AA;  26835 MW;  A6604AAFCAC10C71 CRC64;
     MQSKRGRLDR YLATKLQIHR KAVRALLLAE RVYVNGIPAK ALDLQVDEFS HIVFDGHILQ
     ANQPIYLMMH KPVGVVSATK DKEHQTVIDL LACEARHELH IAGRLDLNSS GLLLLTNDSR
     WSEALMSPEQ KVDKVYRVIL ANPLSEEYIA AFAQGMYFAF EDITTQPAKL VILDSHLAEV
     TLMEGKYHQI KPMFGRFRNP VVELHRLSIG DITLDEALSP GESRMLTVEE VASIWPR
//
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