ID   TRUD_CAMJJ              Reviewed;         372 AA.
AC   A1W165;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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};
GN   OrderedLocusNames=CJJ81176_1450;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) 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; CP000538; EAQ72518.1; -; Genomic_DNA.
DR   RefSeq; WP_002869188.1; NC_008787.1.
DR   AlphaFoldDB; A1W165; -.
DR   SMR; A1W165; -.
DR   STRING; 354242.CJJ81176_1450; -.
DR   EnsemblBacteria; EAQ72518; EAQ72518; CJJ81176_1450.
DR   KEGG; cjj:CJJ81176_1450; -.
DR   eggNOG; COG0585; Bacteria.
DR   HOGENOM; CLU_005281_4_0_7; -.
DR   OMA; LWLWVEK; -.
DR   Proteomes; UP000000646; 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   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..372
FT                   /note="tRNA pseudouridine synthase D"
FT                   /id="PRO_1000084732"
FT   DOMAIN          160..330
FT                   /note="TRUD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
SQ   SEQUENCE   372 AA;  43500 MW;  403B3A12F1562C32 CRC64;
     MNLEEENTIF KPLYSLKHSP INAYFSKNSD DFVVRERPLY EFSGKGEHLI LHINKKDLTT
     NEALKILSET SGVKIRDFGY AGLKDKQGST FQYLSMPKKF ESFLSNFSHP KLKILEIFTH
     ENKLRIGHLK GNTFFIRLKK VLPSDALKLE QALMNLDKQG FTNYFGYQRF GKFGDNYKEG
     LEILHGKKMK NVKMKEFLIS AFQSELFNRY LSKRVELSHF ANDFSEKELI QIYKISKEEA
     KELKKQEQFF KLLKGEVLGH YPFGKCFLCE DLSAELGRFK ARDISAMGLL IGAKAYETGE
     GLALNLENEI FKDTLEFKAK MQGSRRFMWG YLEELKWRYD EEKAHFCIEF FLQKGSYATV
     VLEEILHKNL FE