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Database: UniProt
Entry: I6YV68_MELRP
LinkDB: I6YV68_MELRP
Original site: I6YV68_MELRP 
ID   I6YV68_MELRP            Unreviewed;       269 AA.
AC   I6YV68;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
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   OrderedLocusNames=MROS_1190 {ECO:0000313|EMBL:AFN74427.1};
OS   Melioribacter roseus (strain JCM 17771 / P3M-2).
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Melioribacteraceae; Melioribacter.
OX   NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN74427.1, ECO:0000313|Proteomes:UP000009011};
RN   [1] {ECO:0000313|EMBL:AFN74427.1, ECO:0000313|Proteomes:UP000009011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX   PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA   Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA   Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT   "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT   organotrophic bacterium representing a novel deep lineage within
RT   Bacteriodetes/Chlorobi group.";
RL   PLoS ONE 8:E53047-E53047(2013).
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; CP003557; AFN74427.1; -; Genomic_DNA.
DR   RefSeq; WP_014855863.1; NC_018178.1.
DR   AlphaFoldDB; I6YV68; -.
DR   STRING; 1191523.MROS_1190; -.
DR   GeneID; 78566165; -.
DR   KEGG; mro:MROS_1190; -.
DR   PATRIC; fig|1191523.3.peg.1264; -.
DR   eggNOG; COG0101; Bacteria.
DR   HOGENOM; CLU_014673_0_1_10; -.
DR   OrthoDB; 9811823at2; -.
DR   Proteomes; UP000009011; 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:UP000009011};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00171}.
FT   DOMAIN          9..104
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   DOMAIN          146..244
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   ACT_SITE        53
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   269 AA;  31036 MW;  606094CF33BE1553 CRC64;
     MGRFRLDIEY AGTRYSGWQK QKNGRTIQGK LIEAAEKIFK GERIDIQGSG RTDAGVHALN
     QVAHLEVKTM LAPEIIKMKL NDLLPADINI LEVSKAGKNF HARHDAVSRS YIYQISRRRT
     AFGKQFVWWI KDELDFEYMK RVGGLFEGMH DFASFADKDS EDKSTKALIE SIQFKEVGEL
     ILIRIVGSHF LWKMVRRIVG VLAEAGRHKL NENDVESYLN VFSREPAKYT APPSGLFLEK
     VIYEKNYQWE ELEPVINLIP TIKFGRREK
//
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