ID A0A0N8PPU0_9BACL Unreviewed; 295 AA.
AC A0A0N8PPU0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=AN477_02365 {ECO:0000313|EMBL:KPV45261.1};
OS Alicyclobacillus ferrooxydans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV45261.1, ECO:0000313|Proteomes:UP000050482};
RN [1] {ECO:0000313|EMBL:KPV45261.1, ECO:0000313|Proteomes:UP000050482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-34 {ECO:0000313|EMBL:KPV45261.1,
RC ECO:0000313|Proteomes:UP000050482};
RA Hemp J.;
RT "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL Submitted (SEP-2015) 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:KPV45261.1}.
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DR EMBL; LJCO01000011; KPV45261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8PPU0; -.
DR STRING; 471514.AN477_02365; -.
DR PATRIC; fig|471514.4.peg.2813; -.
DR OrthoDB; 9773999at2; -.
DR Proteomes; UP000050482; 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:UniProtKB-KW.
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; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1.
DR PANTHER; PTHR21600:SF100; RNA PSEUDOURIDYLATE SYNTHASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00849; PseudoU_synth_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000050482};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 86..237
FT /note="Pseudouridine synthase RsuA/RluA-like"
FT /evidence="ECO:0000259|Pfam:PF00849"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 295 AA; 33496 MW; 807432B19F43B73C CRC64;
MLDKLPGFIV DKETQLLPFL LEKYANKGRN KVKSMLTRGQ IKVGNRVVTR HDHPLIPGDR
VSVLNTGSVQ QRELMAGVKM MYEDDDIIVI DKPPGLLSIA TEEEKERTAF RILNDYVREN
NPKSRVFIVH RLDRETSGVM LFAKSETVKQ RLQDNWKELI LERSYVVLVE GQVKEEQGTI
KNWLKESSTK TMFVSRPGDG VVAVTHYQVI EKSPLYSLLA VQLETGRKNQ IRVHMQSIGH
SVVGDRRYGG KRSPIDRLGL HARILAFTHP VTGETLRFET AIPAKFRSLV AGKKA
//
