ID A0A0F3MAA1_ORITS Unreviewed; 283 AA.
AC A0A0F3MAA1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:KJV52417.1};
GN ORFNames=GILLIAM_01442 {ECO:0000313|EMBL:SPR07347.1}, OTSGILL_1556
GN {ECO:0000313|EMBL:KJV52417.1};
OS Orientia tsutsugamushi str. Gilliam.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=1359184 {ECO:0000313|EMBL:KJV52417.1, ECO:0000313|Proteomes:UP000033769};
RN [1] {ECO:0000313|EMBL:KJV52417.1, ECO:0000313|Proteomes:UP000033769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gilliam {ECO:0000313|EMBL:KJV52417.1,
RC ECO:0000313|Proteomes:UP000033769};
RA Daugherty S.C., Su Q., Abolude K., Beier-Sexton M., Carlyon J.A.,
RA Carter R., Day N.P., Dumler S.J., Dyachenko V., Godinez A., Kurtti T.J.,
RA Lichay M., Mullins K.E., Ott S., Pappas-Brown V., Paris D.H., Patel P.,
RA Richards A.L., Sadzewicz L., Sears K., Seidman D., Sengamalay N.,
RA Stenos J., Tallon L.J., Vincent G., Fraser C.M., Munderloh U.,
RA Dunning-Hotopp J.C.;
RT "Genome Sequencing of Rickettsiales.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000244959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gilliam {ECO:0000313|Proteomes:UP000244959};
RA Batty M. E., Batty M E.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SPR07347.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gilliam {ECO:0000313|EMBL:SPR07347.1};
RA Keele B.F.;
RL Submitted (MAR-2018) 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; LANO01000024; KJV52417.1; -; Genomic_DNA.
DR EMBL; LS398551; SPR07347.1; -; Genomic_DNA.
DR RefSeq; WP_047220706.1; NZ_LS398551.1.
DR PATRIC; fig|1359184.3.peg.1089; -.
DR Proteomes; UP000033769; Unassembled WGS sequence.
DR Proteomes; UP000244959; Chromosome i.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:SPR07347.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244959};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00171}.
FT DOMAIN 6..66
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT DOMAIN 181..283
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 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT ECO:0000256|PIRSR:PIRSR001430-2"
SQ SEQUENCE 283 AA; 31999 MW; 0D7C1961968EA627 CRC64;
MLRYKAIVEY DGTNFVGWQR QQNGLSIQQL LEDKISTFTK QTVNLIAAGR TDAGVHALGQ
VVHFDLIAPN NSKDLACINK ETDNKEVSKQ NNTTTTIDSL KMLPCRYNAY KLMSAVNYLL
KPHRIILTSC EITTLQFHAR FSAKARHYKY RIINRAVPSV IEQNRTWWIK PPLNVIDMID
ASQHLIGKHD FTSFRSSACQ SKSPLKTLTK IEVDTTNYPE IQIYFSAPSF LHHMVRNIVG
TLVYIGLCKI SPAAIKTILF AKNRAMAGPT APSSGLYFIK VDY
//