TRUD_ANADF
ID TRUD_ANADF Reviewed; 349 AA.
AC A7HGV2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Anae109_3769;
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=404589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5;
RX PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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; CP000769; ABS27948.1; -; Genomic_DNA.
DR RefSeq; WP_012098576.1; NC_009675.1.
DR AlphaFoldDB; A7HGV2; -.
DR SMR; A7HGV2; -.
DR STRING; 404589.Anae109_3769; -.
DR EnsemblBacteria; ABS27948; ABS27948; Anae109_3769.
DR KEGG; afw:Anae109_3769; -.
DR eggNOG; COG0585; Bacteria.
DR HOGENOM; CLU_005281_4_0_7; -.
DR OMA; LWLWVEK; -.
DR OrthoDB; 1490777at2; -.
DR Proteomes; UP000006382; 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; 3.30.2340.10; -; 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 PROSITE; PS50984; TRUD; 1.
DR PROSITE; PS01268; UPF0024; 1.
PE 3: Inferred from homology;
KW Isomerase; Reference proteome; tRNA processing.
FT CHAIN 1..349
FT /note="tRNA pseudouridine synthase D"
FT /id="PRO_1000149840"
FT DOMAIN 150..304
FT /note="TRUD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01082"
SQ SEQUENCE 349 AA; 37581 MW; A058BA583C5DDF55 CRC64;
MTDAPLVTAE LPGSGGSLRR SPEDFRVDEV PAYLPSGAGP HLYLRVEKRG RTTRDALRTL
ARALGVPERD AGYAGLKDKD AVTTQWLSFP AARDPEPQAL ASEGLRVLEV SRHANKLRPG
HVRANRFQLA VRGGDLARAQ AAAAALAERG LPNLFGPQRF GTEGRNAEVG RALLLGDPSP
EARRAARDRF LRRLSISAYQ ALLFNRWLAE RMADGLFATA VAGDVLKKLD TGGLFTCADP
AVDGPRVQRF EVSPAGPMFG HKLRAAEGEA LAREERLLAA EGIQLSDFAR GGGEAEGTRR
AARLRVEVAL APLEDGYLAT FELPKGSYAT VVMRELMKAG AELPEADED