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Database: UniProt
Entry: A0A1A0TX96_9MYCO
LinkDB: A0A1A0TX96_9MYCO
Original site: A0A1A0TX96_9MYCO 
ID   A0A1A0TX96_9MYCO        Unreviewed;       308 AA.
AC   A0A1A0TX96;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   ORFNames=A5758_23495 {ECO:0000313|EMBL:OBB63407.1};
OS   Mycobacterium sp. 852014-50255_SCH5639931.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834112 {ECO:0000313|EMBL:OBB63407.1, ECO:0000313|Proteomes:UP000092113};
RN   [1] {ECO:0000313|EMBL:OBB63407.1, ECO:0000313|Proteomes:UP000092113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=852014-50255_SCH5639931 {ECO:0000313|EMBL:OBB63407.1,
RC   ECO:0000313|Proteomes:UP000092113};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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:OBB63407.1}.
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DR   EMBL; LZSV01000038; OBB63407.1; -; Genomic_DNA.
DR   RefSeq; WP_067744889.1; NZ_LZSV01000038.1.
DR   AlphaFoldDB; A0A1A0TX96; -.
DR   STRING; 1834112.A5758_23495; -.
DR   OrthoDB; 9807829at2; -.
DR   Proteomes; UP000092113; 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   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   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          15..72
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   308 AA;  33028 MW;  C1AAFAD3C40DCEA5 CRC64;
     MTDRSMPVPE GLAGMRVDAG LARLLGLSRS AAAALAEDGG VELDGVQAGK SDRLTGGAWL
     RVRLPEAPAP VENTPVDIEG MTILYSDDDI VAVDKPAAVA AHASVGWTGP TVLGGLAAAG
     YRITTSGVPE RQGIVHRLDV GTSGVMVVAL SERAYTVLKR AFKQRTVDKR YHALVQGHPD
     PSSGTIDAPI GRHRGGEWKF AVTKDGRHSL THYDTIEAFH AASLLDVHLE TGRTHQIRVH
     FSALHHPCCG DLVYGADPKL AKRLGLERQW LHARSLSFAH PADGRRMEIV SPYPPDLQHA
     LDVLRAEG
//
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