ID A0A1S8TTI1_9CLOT Unreviewed; 305 AA.
AC A0A1S8TTI1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Pseudouridine synthase {ECO:0000256|RuleBase:RU362028};
DE EC=5.4.99.- {ECO:0000256|RuleBase:RU362028};
GN Name=rluD_2 {ECO:0000313|EMBL:OOM81024.1};
GN ORFNames=CLPUN_11840 {ECO:0000313|EMBL:OOM81024.1};
OS Clostridium puniceum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=29367 {ECO:0000313|EMBL:OOM81024.1, ECO:0000313|Proteomes:UP000190890};
RN [1] {ECO:0000313|EMBL:OOM81024.1, ECO:0000313|Proteomes:UP000190890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2619 {ECO:0000313|EMBL:OOM81024.1,
RC ECO:0000313|Proteomes:UP000190890};
RA Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA Daniel R.;
RT "Microbial solvent formation.";
RL Submitted (MAY-2016) 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:OOM81024.1}.
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DR EMBL; LZZM01000073; OOM81024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8TTI1; -.
DR STRING; 29367.CLPUN_11840; -.
DR OrthoDB; 9807829at2; -.
DR Proteomes; UP000190890; 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:OOM81024.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190890};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 15..79
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT ACT_SITE 138
FT /evidence="ECO:0000256|PIRSR:PIRSR606225-1"
SQ SEQUENCE 305 AA; 34905 MW; 59E1E85D53031962 CRC64;
MENDVFIIEE KDQGTRIDKY LAQVFVDKSR SFIQGLIEKE SVKVNDKIPK SNYKLKAFDK
IEVEFKEPEI LKIDAENIPI DILYEDKDVI VVNKAQGMVV HPAPGNYNGT LVNALLFHCK
DLSSINGVIR PGIVHRIDKD TSGVLVIAKN DEAHNKLSEQ LKDHSMKREY CALVEGRLKN
EKGTINKSLA RNKRDRLKIG IVEGGKRAVT HYEVIERYNG YTLIKCILET GRTHQIRVHM
ASIGFPLVGD PLYGFKKQRF KLNGQMLHAK TLGFIHPTQN TYVEFTTELP EYFKVLIDKL
RNELK
//
