TRUD_CAMJE
ID TRUD_CAMJE Reviewed; 372 AA.
AC Q9PMK3; Q0P8F8;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=Cj1457c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35565.1; -; Genomic_DNA.
DR PIR; H81291; H81291.
DR RefSeq; WP_002851259.1; NC_002163.1.
DR RefSeq; YP_002344839.1; NC_002163.1.
DR AlphaFoldDB; Q9PMK3; -.
DR SMR; Q9PMK3; -.
DR IntAct; Q9PMK3; 33.
DR STRING; 192222.Cj1457c; -.
DR PaxDb; Q9PMK3; -.
DR PRIDE; Q9PMK3; -.
DR EnsemblBacteria; CAL35565; CAL35565; Cj1457c.
DR GeneID; 905745; -.
DR KEGG; cje:Cj1457c; -.
DR PATRIC; fig|192222.6.peg.1437; -.
DR eggNOG; COG0585; Bacteria.
DR HOGENOM; CLU_005281_4_0_7; -.
DR OMA; LWLWVEK; -.
DR Proteomes; UP000000799; 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; Reference proteome; tRNA processing.
FT CHAIN 1..372
FT /note="tRNA pseudouridine synthase D"
FT /id="PRO_0000152492"
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; 43445 MW; BDA9F771F0A2D3C7 CRC64;
MNLEEENTIF KPLYSLKHSP INAYFSKNSD DFVVRERPLY EFSGKGEHLI LHINKKDLTT
NEALKILSEA SGVKIRDFGY AGLKDKQGST FQYLSMPKKF ESFLSNFSHP KLKILEIFTH
ENKLRIGHLK GNSFFIRLKK VLPSDALKLE QALMNLDKQG FANYFGYQRF GKFGDNYKEG
LEILRGKKMK NVKMKEFLIS AFQSELFNRY LSKRVELSHF ANDFSEKELI QIYKISKEEA
KELKKQEQFF KLLKGEVLGH YPFGKCFLCE DLSAELGRFK ARDISAMGLL IGAKAYETGE
GLALNLENEI FKDTLEFKAK MQGSRRFMWG YLEELKWRYD EEKAHFCIEF FLQKGSYATV
VLEEILHKNL FE