ID A0A1Y5RPF3_9RHOB Unreviewed; 339 AA.
AC A0A1Y5RPF3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN Name=rluD {ECO:0000313|EMBL:SLN22411.1};
GN ORFNames=PSJ8397_00903 {ECO:0000313|EMBL:SLN22411.1};
OS Pseudooctadecabacter jejudonensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooctadecabacter.
OX NCBI_TaxID=1391910 {ECO:0000313|EMBL:SLN22411.1, ECO:0000313|Proteomes:UP000193623};
RN [1] {ECO:0000313|EMBL:SLN22411.1, ECO:0000313|Proteomes:UP000193623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8397 {ECO:0000313|EMBL:SLN22411.1,
RC ECO:0000313|Proteomes:UP000193623};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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 -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(1911/1915/1917) in 23S rRNA =
CC pseudouridine(1911/1915/1917) in 23S rRNA; Xref=Rhea:RHEA:42524,
CC Rhea:RHEA-COMP:10097, Rhea:RHEA-COMP:10098, ChEBI:CHEBI:65314,
CC ChEBI:CHEBI:65315; EC=5.4.99.23;
CC Evidence={ECO:0000256|ARBA:ARBA00036882};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000256|ARBA:ARBA00010876, ECO:0000256|RuleBase:RU362028}.
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DR EMBL; FWFT01000001; SLN22411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RPF3; -.
DR OrthoDB; 9807829at2; -.
DR Proteomes; UP000193623; 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, ECO:0000313|EMBL:SLN22411.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193623};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 13..74
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 141
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 339 AA; 36520 MW; B0FCED5B9967F0BD CRC64;
MNVEFQIGEA PPARMDKALA RDVPEGAALS RSRLARLLAE GAVRVNGVVV TDPRARATEG
DAVRISVEVA DDYHVAAEDI PLDVVFEDAE LIVVNKPTGM VVHPAPGTPG GTLVNALLHH
CGDSLSGVGG EKRPGIVHRI DKETSGLLVA AKTDRAHHGL AAQFEAHTVE RHYRAICYGV
PDSTDPRVRG VKGASFEAGN ILKLQTQLAR HKHDRQKQQV VWHNGRHAVT RARIVESYGT
PPTAALLDCW LETGRTHQIR VHLAHAGHGL IGDPTYGGRR RLSEKAIGAR GIEAVRAFSR
QALHAATLGF EHPVSGEMIR FEAPMPQDMR DLVAALGGC
//
