ID A0A0R2PF76_9ACTN Unreviewed; 239 AA.
AC A0A0R2PF76;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=tRNA pseudouridine synthase {ECO:0000256|RuleBase:RU003792};
DE EC=5.4.99.12 {ECO:0000256|RuleBase:RU003792};
DE Flags: Fragment;
GN ORFNames=ABR54_06595 {ECO:0000313|EMBL:KRO35563.1};
OS Actinobacteria bacterium BACL15 MAG-120619-bin91.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetes incertae sedis;
OC ac1 cluster.
OX NCBI_TaxID=1655562 {ECO:0000313|EMBL:KRO35563.1, ECO:0000313|Proteomes:UP000053274};
RN [1] {ECO:0000313|EMBL:KRO35563.1, ECO:0000313|Proteomes:UP000053274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL15 MAG-120619-bin91 {ECO:0000313|EMBL:KRO35563.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU003792};
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000256|ARBA:ARBA00009375, ECO:0000256|RuleBase:RU003792}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRO35563.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LIAM01000084; KRO35563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2PF76; -.
DR Proteomes; UP000053274; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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|RuleBase:RU003792};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW ECO:0000256|RuleBase:RU003792}.
FT DOMAIN 1..83
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT DOMAIN 134..236
FT /note="Pseudouridine synthase I TruA alpha/beta"
FT /evidence="ECO:0000259|Pfam:PF01416"
FT ACT_SITE 42
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001430-1"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001430-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRO35563.1"
SQ SEQUENCE 239 AA; 26628 MW; 03C934FED1FE1B55 CRC64;
DGTNFSGWGK QPGRRTVQEE VEKALTTATQ SKIETIVAGR TDAGVHATGQ VIHVDVPDSL
NLDDLSYKLN RMLDTDVRIM NVTVVTGPFN ARFSALRRHY TYKILDGNQT ILPLDRLDVA
PWYRTLDVDL MNQASALMLG SHDFAAYCKF REGSTTIRTL QRFEWSRDTS GFLIGDVVAD
SFCYSMVRNL VGAVVCVADG RFGPEWIEQT LANKVRISDS LVFPACGLSL REVEYPPQS
//
