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Database: UniProt
Entry: A0A1Y4NDC6_9FIRM
LinkDB: A0A1Y4NDC6_9FIRM
Original site: A0A1Y4NDC6_9FIRM 
ID   A0A1Y4NDC6_9FIRM        Unreviewed;       300 AA.
AC   A0A1Y4NDC6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=B5F09_01340 {ECO:0000313|EMBL:OUP78827.1};
OS   Erysipelatoclostridium sp. An173.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=1965571 {ECO:0000313|EMBL:OUP78827.1, ECO:0000313|Proteomes:UP000196550};
RN   [1] {ECO:0000313|Proteomes:UP000196550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An173 {ECO:0000313|Proteomes:UP000196550};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OUP78827.1}.
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DR   EMBL; NFKR01000002; OUP78827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4NDC6; -.
DR   Proteomes; UP000196550; Unassembled WGS sequence.
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:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR   Gene3D; 3.30.2350.10; Pseudouridine synthase; 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   NCBIfam; TIGR00005; rluA_subfam; 1.
DR   PANTHER; PTHR21600:SF71; LARGE SUBUNIT PSEUDOURIDINE SYNTHASE, RLUD SUBFAMILY, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR   PROSITE; PS01129; PSI_RLU; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|RuleBase:RU362028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196550}.
FT   DOMAIN          92..242
FT                   /note="Pseudouridine synthase RsuA/RluA-like"
FT                   /evidence="ECO:0000259|Pfam:PF00849"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   300 AA;  34914 MW;  24AF290FDB4FC6B0 CRC64;
     MKYQIKGDYL IIEINDDFVG MSVEQFFNYF HLSRKTIHLL KQNKQYALNN NFVTSNTLLK
     QGDSLKVLAF DQGIDYQFQS YPLTVVYEDD FILIVNKPIN TAIYPEDKNG LNTLCNYVAN
     YYLETNQYIP VRHIHRLDKD TTGLVMFCKC AFLQPKLDIM MANKEIKRTY LAIVDGIVKK
     DLIINKPISR DRHQNRMRTS NNGKKAVTKV HVLKRSFPSN YTVVKCDLQT GRKHQIRVHL
     SSINHPLLSD PLYGTNSKLI NRVALHGYKL EFNHPFFNQK ITVFADIPDD MKFIGKIDLQ
//
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