TRUD_SYNC1
ID TRUD_SYNC1 Reviewed; 398 AA.
AC Q3A6I8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=Pcar_0760;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) 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; CP000142; ABA88019.1; -; Genomic_DNA.
DR RefSeq; WP_011340463.1; NC_007498.2.
DR AlphaFoldDB; Q3A6I8; -.
DR SMR; Q3A6I8; -.
DR STRING; 338963.Pcar_0760; -.
DR EnsemblBacteria; ABA88019; ABA88019; Pcar_0760.
DR KEGG; pca:Pcar_0760; -.
DR eggNOG; COG0585; Bacteria.
DR HOGENOM; CLU_005281_4_0_7; -.
DR OMA; LWLWVEK; -.
DR OrthoDB; 1490777at2; -.
DR Proteomes; UP000002534; 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; Reference proteome; tRNA processing.
FT CHAIN 1..398
FT /note="tRNA pseudouridine synthase D"
FT /id="PRO_0000230143"
FT DOMAIN 151..360
FT /note="TRUD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
SQ SEQUENCE 398 AA; 44480 MW; 3A886529EDB84307 CRC64;
MANYLTAKLP GIGGSIKTCP DDFLVEELPL YPTCGEGEHL YLEVEKRGMT TFELLKRLSR
ALQVNERAMG YAGLKDAQAT TRQFISVTDC SAEQALALQL QDIRILSARR HRNKLRLGHL
AGNRFTITIR DIDSDALEKA RDILHVLQMT GVPNFFGEQR YGALGNSHLI GQAIVQKNFS
QAAAHIIGDP DKIIHPEWRQ GAILYAENRL EEAEQALPRR MRNERNLVRS LRQGRSAEKA
VRRLPGKLLR LYLSAYQSHL FDRLVSMRLE SLETLWTGDI AYKHDNGACF LVTDAALEQP
RADRFEISPT APLFGHKVMM AEAQAGILEQ ALLAKEGITP DDFRLGAGLS MPGERRPLRI
PISETASNQQ GNELELSFSL PKGSFATTVL HEVMKTDV
