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Database: UniProt
Entry: A0A0M2HN37_9MICO
LinkDB: A0A0M2HN37_9MICO
Original site: A0A0M2HN37_9MICO 
ID   A0A0M2HN37_9MICO        Unreviewed;       306 AA.
AC   A0A0M2HN37;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE            EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN   Name=rluD {ECO:0000313|EMBL:KJL45875.1};
GN   ORFNames=RS81_00028 {ECO:0000313|EMBL:KJL45875.1};
OS   Microbacterium ketosireducens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL45875.1, ECO:0000313|Proteomes:UP000033956};
RN   [1] {ECO:0000313|EMBL:KJL45875.1, ECO:0000313|Proteomes:UP000033956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL45875.1,
RC   ECO:0000313|Proteomes:UP000033956};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-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:KJL45875.1}.
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DR   EMBL; JYIZ01000010; KJL45875.1; -; Genomic_DNA.
DR   RefSeq; WP_045274046.1; NZ_JYIZ01000010.1.
DR   AlphaFoldDB; A0A0M2HN37; -.
DR   STRING; 92835.RS81_00028; -.
DR   PATRIC; fig|92835.4.peg.31; -.
DR   OrthoDB; 9807829at2; -.
DR   Proteomes; UP000033956; 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   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; 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   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:KJL45875.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033956};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          88..242
FT                   /note="Pseudouridine synthase RsuA/RluA-like"
FT                   /evidence="ECO:0000259|Pfam:PF00849"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ   SEQUENCE   306 AA;  33117 MW;  622CDC01B1125E74 CRC64;
     MESRSLPVPD GLDGTRVDAA LAKMLGFSRT FAADVAEAGG VVMDGRTLAK SDKLRGGAWL
     DVSWAPKEEP RVIPVEVPDL RIVYDDDDIV VVDKPSGVAA HPSLGWEGPT VLGALAAGGF
     RIATTGAAER QGVVHRLDVG TSGLMVVAKT ESAYTALKRA FKEREVEKIY HAVVQGHPDP
     LTGTIDAPIG RHPNHSWKFA VIPDGKDSVT HYETLEAFPG ASLLEIHLET GRTHQIRVHM
     AAHRHPCVGD PLYGADPKLS ARLGLIRQWL HAHELSFEHP ATGEWVTFRS EYPADLAHAL
     EVLRGD
//
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