TRUD_ALISL
ID TRUD_ALISL Reviewed; 348 AA.
AC B6EKL4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=VSAL_I2510;
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238;
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178379; CAQ80194.1; -; Genomic_DNA.
DR RefSeq; WP_012550982.1; NC_011312.1.
DR AlphaFoldDB; B6EKL4; -.
DR SMR; B6EKL4; -.
DR STRING; 316275.VSAL_I2510; -.
DR EnsemblBacteria; CAQ80194; CAQ80194; VSAL_I2510.
DR KEGG; vsa:VSAL_I2510; -.
DR eggNOG; COG0585; Bacteria.
DR HOGENOM; CLU_005281_4_0_6; -.
DR OMA; LWLWVEK; -.
DR OrthoDB; 1490777at2; -.
DR Proteomes; UP000001730; Chromosome 1.
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; 3.30.2340.10; -; 1.
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 InterPro; IPR043165; TruD_insert_sf.
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..348
FT /note="tRNA pseudouridine synthase D"
FT /id="PRO_1000136827"
FT DOMAIN 158..304
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 348 AA; 39724 MW; 3A3E232EA37CE9DC CRC64;
MSDIMSTFSW LYGKPVATGK LKQLPEHFIV KEVLGYEFTG KGEHLMVKIR KTGENTKYVA
NEFAKFCGVK SKDISWAGLK DRHAVTEQWL SVHLPKSDHL NFVLFEVAHP GVEILEMTRH
HKKLRPGDLL GNSFQLIATE VTDMDDVLAR LEKVKVTGVP NYFGAQRFGH EGNNVTEARR
WGRENVRTRD NTKRSFYLSA ARSWIFNHII SQRITEGYFS LPVDGDILLD QNDRTVNENV
TSEDCIQKIK KGELSISAAL AGDNQLPTTE KALMFEQPQL DAEPDLMALI RGNRMRHERR
SIELHPENLH WSVEGDQLTL NFSLTSGSFA TVIVRELLQE IEVERTYD
