ID   RLUD_PASMU              Reviewed;         324 AA.
AC   Q9CKA6;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
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; Synonyms=sfb; OrderedLocusNames=PM1719;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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DR   EMBL; AE004439; AAK03803.1; -; Genomic_DNA.
DR   RefSeq; WP_010907302.1; NC_002663.1.
DR   AlphaFoldDB; Q9CKA6; -.
DR   SMR; Q9CKA6; -.
DR   STRING; 747.DR93_642; -.
DR   EnsemblBacteria; AAK03803; AAK03803; PM1719.
DR   KEGG; pmu:PM1719; -.
DR   PATRIC; fig|272843.6.peg.1740; -.
DR   HOGENOM; CLU_016902_4_0_6; -.
DR   OMA; AHPSPGW; -.
DR   Proteomes; UP000000809; Chromosome.
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; 3.10.290.10; -; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR006225; PsdUridine_synth_RluC/D.
DR   InterPro; IPR006224; PsdUridine_synth_RluC/D_CS.
DR   InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   Pfam; PF00849; PseudoU_synth_2; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00005; rluA_subfam; 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..324
FT                   /note="Ribosomal large subunit pseudouridine synthase D"
FT                   /id="PRO_0000162696"
FT   DOMAIN          17..90
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  36895 MW;  02FF744374469A1B CRC64;
     MAQITLSAEI QLSQLGQRLD QALAELFPDY SRSRLKTWIE QNLVHVNGDV VNVPRAKVYG
     GEQIEIVVEI DDDTRFEPEN LPLNIVYEDD DILVINKPKD FVVHPGAGNA SGTVLNALLY
     HYPAIAEVPR AGIVHRLDKD TTGLMVIAKT IPAQTKLVRD LQKRKITREY EAIACGIMTK
     GGMVDQPMAR HPTKRTHMAV HPMGKPAVTH YRIMERFRNY TRLRLRLETG RTHQIRVHMA
     HIAHPLLGDQ TYGGRPRPPK NASEELMQTL RDFKRQALHA IMLRLAHPIT GELMEWHAPL
     PTDFVELVEA LKADYQLHQD DLDY