ID A0A0Q4RLX2_9BURK Unreviewed; 344 AA.
AC A0A0Q4RLX2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN ORFNames=ASF16_18890 {ECO:0000313|EMBL:KQO14318.1};
OS Acidovorax sp. Leaf78.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736237 {ECO:0000313|EMBL:KQO14318.1, ECO:0000313|Proteomes:UP000051234};
RN [1] {ECO:0000313|Proteomes:UP000051234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 -!- 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}.
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:KQO14318.1}.
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DR EMBL; LMLZ01000026; KQO14318.1; -; Genomic_DNA.
DR RefSeq; WP_056173911.1; NZ_LMLZ01000026.1.
DR AlphaFoldDB; A0A0Q4RLX2; -.
DR STRING; 1736237.ASF16_18890; -.
DR OrthoDB; 9785808at2; -.
DR Proteomes; UP000051234; 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 49..109
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 344 AA; 37128 MW; 4F1075E3CC21199E CRC64;
MSSAVQAVQA GESDLLAEET DESEDSGGLA EDVASELRTM TVAIAQHGAR LDRALVELVP
EFSRSYLQQL LSQGMVSLQG APALKASAKV KAGDQVVLEM RPTLQSQAFR PEPMDIDVVY
EDAHLLVVNK PAGLVVHPAP GNWSGTLLNG LLARDEKALL VPRAGIVHRL DKDTSGLMVV
ARDRATMDAL VALIAERQVK RQYVALAHGA WSGPKTRAVN APIGRDPRNR LRMAVVDLAV
HAGKAARTDI RWLDGAEQGC WVQCTLHTGR THQIRVHMAS LKHPLVGDVL YGGAPVKAMQ
RQALHAYRLA FAHPVTGEAL EFMAPVPEDM RQALAAWGLG YNAP
//
