ID RLUD_VIBPA Reviewed; 325 AA. AC Q87S65; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Ribosomal large subunit pseudouridine synthase D; DE EC=5.4.99.23; DE AltName: Full=23S rRNA pseudouridine(1911/1915/1917) synthase; DE AltName: Full=rRNA pseudouridylate synthase D; DE AltName: Full=rRNA-uridine isomerase D; GN Name=rluD; OrderedLocusNames=VP0559; OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=223926; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIMD 2210633; RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1; RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.; RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism RT distinct from that of V. cholerae."; RL Lancet 361:743-749(2003). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil at CC positions 1911, 1915 and 1917 in 23S ribosomal RNA. {ECO:0000250}. 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 -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000305}. 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; BA000031; BAC58822.1; -; Genomic_DNA. DR RefSeq; NP_796938.1; NC_004603.1. DR RefSeq; WP_005460300.1; NC_004603.1. DR AlphaFoldDB; Q87S65; -. DR SMR; Q87S65; -. DR GeneID; 1188027; -. DR KEGG; vpa:VP0559; -. DR PATRIC; fig|223926.6.peg.531; -. DR eggNOG; COG0564; Bacteria. DR HOGENOM; CLU_016902_4_0_6; -. DR Proteomes; UP000002493; Chromosome 1. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0120159; F:rRNA pseudouridine synthase activity; IEA:UniProtKB-EC. 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; Reference proteome; RNA-binding; rRNA processing. FT CHAIN 1..325 FT /note="Ribosomal large subunit pseudouridine synthase D" FT /id="PRO_0000162703" FT DOMAIN 18..91 FT /note="S4 RNA-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182" FT ACT_SITE 139 FT /evidence="ECO:0000250" SQ SEQUENCE 325 AA; 36604 MW; D3359215265F1156 CRC64; MAQQIVLTNT VKDSQLGQRL DQAIAELFAD FSRSRLKEWL LDGKVQVNGE VVTKPRTKVM GGEEITLQAE LEDEERWEAQ DIPLDIVYED DDIIVINKPR DFVVHPGAGT PDGTVLNALL HHYPDIAEVP RAGIVHRLDK DTTGLMVVAK TVPAQTRLVR ALQKRNITRE YEAIAIGRMT AGGKVDQPIG RHSTKRTLMA VAPLGKPAVT HYRVAEHFRE HTRIRLRLET GRTHQIRVHM SYLQHPLLGD TAYGGRARIP TGASQELTDM IRGFDRQALH AVMLRFEHPI TGEELEFHAP VPDDMVAMTE ALRKDTEEYG LPDEF //