ID   TRUD_HELAH              Reviewed;         381 AA.
AC   Q17WX3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Hac_1089;
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba;
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
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; AM260522; CAJ99853.1; -; Genomic_DNA.
DR   RefSeq; WP_011577961.1; NC_008229.1.
DR   AlphaFoldDB; Q17WX3; -.
DR   SMR; Q17WX3; -.
DR   STRING; 382638.Hac_1089; -.
DR   EnsemblBacteria; CAJ99853; CAJ99853; Hac_1089.
DR   KEGG; hac:Hac_1089; -.
DR   eggNOG; COG0585; Bacteria.
DR   HOGENOM; CLU_005281_4_0_7; -.
DR   OMA; LWLWVEK; -.
DR   OrthoDB; 1490777at2; -.
DR   BioCyc; HACI382638:HAC_RS04675-MON; -.
DR   Proteomes; UP000000775; 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; 2.
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_1000084745"
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;  44351 MW;  FC60A84F84F24A9D CRC64;
     MNLNFMPLLH AYNHASIDFH FNSSARDFCV HEVPLYEFSN KGEHAIIQVR KSGLSTLEML
     QIFSQILGVK IAELGYAGLK DKNALTTQFV SLPKKYAPLL EKNTSNFQER NLKILSLNYH
     HNKIKLGHLK GNRFFMRFKK MTPLNAHKTK QVLEQIVQFG MPNYFGSQRF GKFNDNHKEG
     LKILQNEAKF KNQKLNAFLI SSYQSYLFNS LLSKRLEISK IISDFSLKEG LEFFKQKNLN
     IHSNALKALK NQDHPFKILE GDVMCHYPYG KFFDALELEK ESERFLKKEA VPMGLLDGKK
     ALYAKNLSLE IEKEFQNHIL SDHAKTLGSR RFFWVFVENL TSKYIKEKVQ FELEFYLPKG
     SYASALLKEI KHQKGENNDE F