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Database: UniProt
Entry: A0A1E1EZY7_9SPHN
LinkDB: A0A1E1EZY7_9SPHN
Original site: A0A1E1EZY7_9SPHN 
ID   A0A1E1EZY7_9SPHN        Unreviewed;       307 AA.
AC   A0A1E1EZY7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU003887};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU003887};
GN   ORFNames=SCLO_1007520 {ECO:0000313|EMBL:BAV63792.1};
OS   Sphingobium cloacae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=120107 {ECO:0000313|EMBL:BAV63792.1, ECO:0000313|Proteomes:UP000218272};
RN   [1] {ECO:0000313|EMBL:BAV63792.1, ECO:0000313|Proteomes:UP000218272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10874 {ECO:0000313|EMBL:BAV63792.1,
RC   ECO:0000313|Proteomes:UP000218272};
RA   Ootsuka M., Nishizawa T., Ohta H.;
RT   "Complete Genome Sequence of the Nonylphenol-Degrading Bacterium
RT   Sphingobium cloacae JCM 10874T.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a uridine in RNA = a pseudouridine in RNA;
CC         Xref=Rhea:RHEA:48348, Rhea:RHEA-COMP:12068, Rhea:RHEA-COMP:12069,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC         Evidence={ECO:0000256|ARBA:ARBA00000073};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RsuA family.
CC       {ECO:0000256|ARBA:ARBA00008348, ECO:0000256|RuleBase:RU003887}.
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DR   EMBL; AP017655; BAV63792.1; -; Genomic_DNA.
DR   RefSeq; WP_066514013.1; NZ_AP017655.1.
DR   AlphaFoldDB; A0A1E1EZY7; -.
DR   KEGG; sclo:SCLO_1007520; -.
DR   OrthoDB; 9807213at2; -.
DR   Proteomes; UP000218272; Chromosome.
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; IEA:UniProt.
DR   CDD; cd00165; S4; 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; 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   Pfam; PF01479; S4; 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:UP000218272};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          68..132
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   307 AA;  33530 MW;  D4A2D30DF0C348A6 CRC64;
     MEPPRKSGPR RPARPGASGK PGEGRARTGS RPPRPVPGPG KPKAAATRAA NPHPARAAAS
     AGGKAEPQRI AKLLARAGVA SRREVERMIA EGRIALDGEA VATPATLLSS LHGVTVDGVA
     VNQPAPTRLF LFHKPSGFLT TERDPRGRPT IYDKLPADLP RLMPVGRLDM TTEGLLLLTT
     DGEFKRQMEL PATGVPRTYR ARAFGDVSQN QLEDLFEGIE IDGIRYGRIE ANLERRTGRN
     QWIEMTLTEG KNREVRRVLE HLGLQVSRLI RTSYGPFHLG ELPSGAVEEV RQHDLVVFRK
     GLKGKKE
//
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