ID A0A3M8AU67_9BACL Unreviewed; 309 AA.
AC A0A3M8AU67;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=EDM57_16875 {ECO:0000313|EMBL:RNB54710.1};
OS Brevibacillus gelatini.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1655277 {ECO:0000313|EMBL:RNB54710.1, ECO:0000313|Proteomes:UP000268829};
RN [1] {ECO:0000313|EMBL:RNB54710.1, ECO:0000313|Proteomes:UP000268829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100115 {ECO:0000313|EMBL:RNB54710.1,
RC ECO:0000313|Proteomes:UP000268829};
RA Dunlap C.;
RT "Phylogenomics of Brevibacillus.";
RL Submitted (OCT-2018) 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:RNB54710.1}.
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DR EMBL; RHHS01000039; RNB54710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8AU67; -.
DR OrthoDB; 9773999at2; -.
DR Proteomes; UP000268829; 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 21..85
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 309 AA; 34969 MW; F1A68F31D97FD3B8 CRC64;
MNDTQLFERY DWNVEPEDAG ERIDKFITLQ NEDWSRSQVQ AWIKEGRVTV NGEPVKNNYK
LQTEDEVTLR VPPPKEMAIK PEPMPLEIIY EDSDVVVVNK PRGLVVHPAP GHYSGTLVNG
LLAHCKDLSG INGVLRPGIV HRIDKDTSGL LMVAKNDKAH IGLAEQLKDH SVTRTYVAIV
HGVIPHEMGT IDAPIGRDPK NRQQMAVVFE NSKPAVTHFI VLERFKEYTL VELKLETGRT
HQIRVHMKYI GYPLAGDPKY GPKNTLEIDG QALHAKTLGF THPRTQERLE FEAPMPKDLT
DLIDFLRQA
//
