ID   RLUD_BUCAI              Reviewed;         312 AA.
AC   P57481;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 110.
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=BU401;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13104.1; -; Genomic_DNA.
DR   RefSeq; NP_240218.1; NC_002528.1.
DR   RefSeq; WP_009874359.1; NC_002528.1.
DR   AlphaFoldDB; P57481; -.
DR   SMR; P57481; -.
DR   STRING; 563178.BUAP5A_394; -.
DR   EnsemblBacteria; BAB13104; BAB13104; BAB13104.
DR   KEGG; buc:BU401; -.
DR   PATRIC; fig|107806.10.peg.415; -.
DR   eggNOG; COG0564; Bacteria.
DR   HOGENOM; CLU_016902_4_0_6; -.
DR   Proteomes; UP000001806; 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; 3.30.2350.10; 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..312
FT                   /note="Ribosomal large subunit pseudouridine synthase D"
FT                   /id="PRO_0000162684"
FT   DOMAIN          18..87
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  35840 MW;  6AC32A7F9260D890 CRC64;
     MKKIQLNSIA SSCSLSGQRL DLVLSKLFRE YSRSYLKKLI IMNQVLVNES IVNQPDKKIL
     GGETLTIHPF SKDLLVDIPE NIFLDIVYED SDILIINKPA GLVVHPGSGN KSGTILNALL
     YHYKNSKDLP RAGIVHRLDK DTSGLMVIAK NIFSYNHLLL LLKEKKIIRE YEGIVHGKMI
     AGGTINKPIM RHYNRRTCMM VHHLGKPSVT HYKVLSRFKF HTHIAIRLET GRTHQIRVHM
     LHIKYPLVGD PCYSGFKIQS NYRKDKKTNK IYKFPRQALH ANHLSLHHPI KKNVMSWTVP
     LPQDIQELLL KI
//