ID A0A0S8ZC11_9PSED Unreviewed; 211 AA.
AC A0A0S8ZC11;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Dual-specificity RNA pseudouridine synthase RluA {ECO:0000256|ARBA:ARBA00039988};
DE EC=5.4.99.28 {ECO:0000256|ARBA:ARBA00038944};
DE EC=5.4.99.29 {ECO:0000256|ARBA:ARBA00038945};
DE AltName: Full=23S rRNA pseudouridine(746) synthase {ECO:0000256|ARBA:ARBA00041266};
DE AltName: Full=Ribosomal large subunit pseudouridine synthase A {ECO:0000256|ARBA:ARBA00042883};
DE AltName: Full=rRNA pseudouridylate synthase A {ECO:0000256|ARBA:ARBA00042844};
DE AltName: Full=rRNA-uridine isomerase A {ECO:0000256|ARBA:ARBA00043143};
DE AltName: Full=tRNA pseudouridine(32) synthase {ECO:0000256|ARBA:ARBA00042372};
GN ORFNames=ASE98_03785 {ECO:0000313|EMBL:KQN50959.1};
OS Pseudomonas sp. Leaf48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736221 {ECO:0000313|EMBL:KQN50959.1, ECO:0000313|Proteomes:UP000051774};
RN [1] {ECO:0000313|EMBL:KQN50959.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN50959.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN50959.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN50959.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dual specificity enzyme that catalyzes the synthesis of
CC pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32
CC in the anticodon stem and loop of transfer RNAs.
CC {ECO:0000256|ARBA:ARBA00037305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(32) in tRNA = pseudouridine(32) in tRNA;
CC Xref=Rhea:RHEA:42544, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10108,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00036184};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(746) in 23S rRNA = pseudouridine(746) in 23S rRNA;
CC Xref=Rhea:RHEA:42548, Rhea:RHEA-COMP:10109, Rhea:RHEA-COMP:10110,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.29;
CC Evidence={ECO:0000256|ARBA:ARBA00036916};
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:KQN50959.1}.
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DR EMBL; LMLH01000012; KQN50959.1; -; Genomic_DNA.
DR RefSeq; WP_060541534.1; NZ_LMLH01000012.1.
DR AlphaFoldDB; A0A0S8ZC11; -.
DR STRING; 1736221.ASE98_03785; -.
DR OrthoDB; 9807829at2; -.
DR Proteomes; UP000051774; 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; IPR006145; PsdUridine_synth_RsuA/RluA.
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; SSF55120; Pseudouridine synthase; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
PE 4: Predicted;
FT DOMAIN 15..161
FT /note="Pseudouridine synthase RsuA/RluA-like"
FT /evidence="ECO:0000259|Pfam:PF00849"
SQ SEQUENCE 211 AA; 24070 MW; 86DA7CB0011FF3B2 CRC64;
MPLSNVHIIH QDAAVLVVNK PTLLLSVPGR ADDNKDCLIT RLQENGYPEA RIVHRLDWET
SGIILLARDP DTHRELSRQF HDRETEKAYT ALCWGQPELD SGSIDLPLRY DPPTKPRHVV
DHEFGKNALT FWRVLERCGD WCRVELTPIT GRSHQLRVHM LSIGHPLLGD GLYAHEQALA
AWPRLCLHAS MLSFTHPQSG ERLRFECPAP F
//