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Database: UniProt
Entry: A0A292RGL0_9BACT
LinkDB: A0A292RGL0_9BACT
Original site: A0A292RGL0_9BACT 
ID   A0A292RGL0_9BACT        Unreviewed;       303 AA.
AC   A0A292RGL0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=CPT80_02245 {ECO:0000313|EMBL:DAA97024.1};
OS   Candidatus Gastranaerophilales bacterium HUM_9.
OC   Bacteria; Candidatus Melainabacteria; Candidatus Gastranaerophilales.
OX   NCBI_TaxID=1916320 {ECO:0000313|EMBL:DAA97024.1, ECO:0000313|Proteomes:UP000218540};
RN   [1] {ECO:0000313|EMBL:DAA97024.1, ECO:0000313|Proteomes:UP000218540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HUM_9 {ECO:0000313|EMBL:DAA97024.1};
RX   PubMed=28360330; DOI=.1126/science.aal3794;
RA   Soo R.M., Hemp J., Parks D.H., Fischer W.W., Hugenholtz P.;
RT   "On the origins of oxygenic photosynthesis and aerobic respiration in
RT   Cyanobacteria.";
RL   Science 355:1436-1440(2017).
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil.
CC       {ECO:0000256|RuleBase:RU362028}.
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|RuleBase:RU362028};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC       {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:DAA97024.1}.
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DR   EMBL; DABG01000009; DAA97024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A292RGL0; -.
DR   STRING; 1916320.GCA_002103075_00360; -.
DR   Proteomes; UP000218540; Unassembled WGS sequence.
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; cd02869; PseudoU_synth_RluA_like; 1.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006224; PsdUridine_synth_RluA-like_CS.
DR   InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   NCBIfam; TIGR00005; rluA_subfam; 1.
DR   PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR   PANTHER; PTHR21600:SF44; PSEUDOU_SYNTH_2 DOMAIN-CONTAINING PROTEIN; 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; PS01129; PSI_RLU; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU362028};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          16..80
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   ACT_SITE        140
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   303 AA;  34557 MW;  321CE7420354BC63 CRC64;
     MTNFNKFIID NSDADIRLDC YLSNILENVS RTKIQNAIKS ELVLINDKTC KPSHIIKTDD
     IITIDNSAFD EIEIKAENIP LEIVYDSNEF SIVNKPSGML THPTSTQKTG TLVNALLYKF
     KNNLSDLNGS FRKGIVHRLD KNTSGLLLVA KNNIAHEKLA KLIKDREIEK HYRAIVKGFL
     PENITINEPI GRCKTNPTRM DITPDGKPSL TEVSIIKQFL NATYVDINLK TGRTHQIRVH
     LSHIGHPVFN DTLYGFGKQK IKTEEQVLQS YKLKFVNPFN NELINIEIEP DEKINKVLKY
     LEQ
//
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