ID   TRUD_HELP2              Reviewed;         381 AA.
AC   B6JME7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=tRNA pseudouridine synthase D {ECO:0000255|HAMAP-Rule:MF_01082};
DE            EC=5.4.99.27 {ECO:0000255|HAMAP-Rule:MF_01082};
DE   AltName: Full=tRNA pseudouridine(13) synthase {ECO:0000255|HAMAP-Rule:MF_01082};
DE   AltName: Full=tRNA pseudouridylate synthase D {ECO:0000255|HAMAP-Rule:MF_01082};
DE   AltName: Full=tRNA-uridine isomerase D {ECO:0000255|HAMAP-Rule:MF_01082};
GN   Name=truD {ECO:0000255|HAMAP-Rule:MF_01082}; OrderedLocusNames=HPP12_0923;
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12;
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil-13 in
CC       transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01082}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(13) in tRNA = pseudouridine(13) in tRNA;
CC         Xref=Rhea:RHEA:42540, Rhea:RHEA-COMP:10105, Rhea:RHEA-COMP:10106,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.27;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01082};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC       {ECO:0000255|HAMAP-Rule:MF_01082}.
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DR   EMBL; CP001217; ACJ08075.1; -; Genomic_DNA.
DR   RefSeq; WP_001052370.1; NC_011498.1.
DR   AlphaFoldDB; B6JME7; -.
DR   SMR; B6JME7; -.
DR   EnsemblBacteria; ACJ08075; ACJ08075; HPP12_0923.
DR   KEGG; hpp:HPP12_0923; -.
DR   HOGENOM; CLU_005281_4_0_7; -.
DR   OMA; LWLWVEK; -.
DR   OrthoDB; 1490777at2; -.
DR   Proteomes; UP000008198; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.2350.20; -; 1.
DR   HAMAP; MF_01082; TruD; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR001656; PsdUridine_synth_TruD.
DR   InterPro; IPR020119; PsdUridine_synth_TruD_CS.
DR   InterPro; IPR011760; PsdUridine_synth_TruD_insert.
DR   InterPro; IPR042214; TruD_catalytic.
DR   Pfam; PF01142; TruD; 1.
DR   PIRSF; PIRSF037016; Pseudouridin_synth_euk_prd; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1.
DR   PROSITE; PS50984; TRUD; 1.
DR   PROSITE; PS01268; UPF0024; 1.
PE   3: Inferred from homology;
KW   Isomerase; tRNA processing.
FT   CHAIN           1..381
FT                   /note="tRNA pseudouridine synthase D"
FT                   /id="PRO_1000136840"
FT   DOMAIN          160..335
FT                   /note="TRUD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
SQ   SEQUENCE   381 AA;  43971 MW;  CD86D1E033012FC3 CRC64;
     MNLNFMPLLH AYNHASIDFH FNSSARDFCV HEVPLYEFSN TGEHAVIQVR KSGLSTLEML
     QIFSQILGVK IAELGYAGLK DKNALTTQFI SLPKKYAPLL EKNTHNLQER NLKILSLNYH
     HNKIKLGHLK GNRFFMRFKK MTPLNAQKTK QVLEQIARFG MPNYFGSQRF GKFNDNHKEG
     LKILQNQTKF AHQKLNAFLI SSYQSYLFNA LLSKRLEISK IISAFSLKEN LEFFKQNNLS
     VNSNALKALK NQAHPFKILE GDVMCHYPYG KFFDALELGK EGERFLNKEA APTGLLDGKK
     ALYAKNLSFE IEKEFQHNLL SSHAKTLGSR RFFWVFAENV TSQYMKEKAQ FELGFYLPKG
     SYASALLKKI KHEKGEKYDK F