ID G8UQG2_TANFA Unreviewed; 252 AA.
AC G8UQG2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=tRNA pseudouridine synthase A {ECO:0000256|HAMAP-Rule:MF_00171};
DE EC=5.4.99.12 {ECO:0000256|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000256|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA pseudouridylate synthase I {ECO:0000256|HAMAP-Rule:MF_00171};
DE AltName: Full=tRNA-uridine isomerase I {ECO:0000256|HAMAP-Rule:MF_00171};
GN Name=truA {ECO:0000256|HAMAP-Rule:MF_00171,
GN ECO:0000313|EMBL:AEW21300.1};
GN OrderedLocusNames=BFO_0025 {ECO:0000313|EMBL:AEW21300.1};
OS Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS 5666 / FDC 338) (Bacteroides forsythus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Tannerella.
OX NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW21300.1, ECO:0000313|Proteomes:UP000005436};
RN [1] {ECO:0000313|Proteomes:UP000005436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC {ECO:0000313|Proteomes:UP000005436};
RA Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA Shetty J., Torralba M., Gill S., Nelson K.;
RT "Complete sequence of Tannerella forsythia ATCC 43037.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the
CC anticodon stem and loop of transfer RNAs. {ECO:0000256|HAMAP-
CC Rule:MF_00171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA;
CC Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00171,
CC ECO:0000256|RuleBase:RU003792};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00171}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000256|ARBA:ARBA00009375, ECO:0000256|HAMAP-Rule:MF_00171,
CC ECO:0000256|RuleBase:RU003792}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00171}.
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DR EMBL; CP003191; AEW21300.1; -; Genomic_DNA.
DR RefSeq; WP_014223513.1; NC_016610.1.
DR AlphaFoldDB; G8UQG2; -.
DR STRING; 203275.BFO_0025; -.
DR GeneID; 34757471; -.
DR KEGG; tfo:BFO_0025; -.
DR PATRIC; fig|203275.8.peg.26; -.
DR eggNOG; COG0101; Bacteria.
DR HOGENOM; CLU_014673_0_1_10; -.
DR Proteomes; UP000005436; 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 CDD; cd02570; PseudoU_synth_EcTruA; 1.
DR Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR HAMAP; MF_00171; TruA; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR NCBIfam; TIGR00071; hisT_truA; 1.
DR PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR PANTHER; PTHR11142:SF0; TRNA PSEUDOURIDINE SYNTHASE-LIKE 1; 1.
DR Pfam; PF01416; PseudoU_synth_1; 2.
DR PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00171};
KW Reference proteome {ECO:0000313|Proteomes:UP000005436};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00171}.
FT DOMAIN 9..105
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT DOMAIN 145..245
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT ACT_SITE 52
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT ECO:0000256|PIRSR:PIRSR001430-1"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT ECO:0000256|PIRSR:PIRSR001430-2"
SQ SEQUENCE 252 AA; 28896 MW; 91A077DC23757A1A CRC64;
MNRYFIWLAY KGTNYCGWQR QPNGLSVQQC VEDVLETVLR RPVPLTGAGR TDAGVHARRM
AAHFDVPKAL DDTERLAGKL NRMLPQDIAI ARIVPVRADA HARFDALSRR YQYLVSEKKD
PFDYETVCCM SLRGMDFGAM NEVAKTLYDY TDFTSFSKLH TDVKTNNCRI DEARWEKDGT
RWGFTIQADR FLRNMVRAMV GTMFEVGRGK RSVDDFRRLI EAKDRCRAGT SAPPEGLTLI
DIDYPDDLFT VD
//
