ID A0A0L6ZDB9_9CLOT Unreviewed; 307 AA.
AC A0A0L6ZDB9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:KOA20965.1};
GN ORFNames=CLHOM_05530 {ECO:0000313|EMBL:KOA20965.1};
OS Clostridium homopropionicum DSM 5847.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121318 {ECO:0000313|EMBL:KOA20965.1, ECO:0000313|Proteomes:UP000037043};
RN [1] {ECO:0000313|Proteomes:UP000037043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5847 {ECO:0000313|Proteomes:UP000037043};
RA Poehlein A., Beck M., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R.,
RA Duerre P.;
RT "Genome sequence of the strict anaerobe Clostridium homopropionicum LuHBu1
RT (DSM 5847T).";
RL Submitted (AUG-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:KOA20965.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LHUR01000011; KOA20965.1; -; Genomic_DNA.
DR RefSeq; WP_052220148.1; NZ_LHUR01000011.1.
DR AlphaFoldDB; A0A0L6ZDB9; -.
DR STRING; 36844.SAMN04488501_104167; -.
DR PATRIC; fig|1121318.3.peg.556; -.
DR Proteomes; UP000037043; 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:KOA20965.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037043};
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 307 AA; 34957 MW; D596D604E700BE24 CRC64;
MELRKIIVDK EAENTRLDVF LSKIFEDKSR SYIQKLIEGS HILVNNKEKK SNYKLNNNDI
ITIELPEVQE LVVEAENIPL DILYEDEDVV VINKPQGIVV HPAPGNYKGT LVNALLYHCE
DLSGINGVAR PGIVHRIDKD TSGILVIAKN DKAHNKLAEQ LKNHSMIREY IALVEGRIKQ
DKGVVDKPIG RNPKDRLKMG IVSGGKRAVT HYEVIERFEK NTLIKCILET GRTHQIRLHM
SHIGYPIVGD PVYGIKKQKF NLRGQMLHAK KLGFIHPSTG EYMEFESSLP EYFTHILDLL
SNKENKN
//