(data stored in ACNUC7421 zone)

SWISSPROT: Q2IMX1_ANADE

ID   Q2IMX1_ANADE            Unreviewed;       264 AA.
AC   Q2IMX1;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 97.
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=Adeh_0381 {ECO:0000313|EMBL:ABC80157.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80157.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in
CC       the anticodon stem and loop of transfer RNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_00171}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA uridine(38-40) = tRNA pseudouridine(38-40);
CC         Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-
CC         COMP:10087, 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
CC       family. {ECO:0000256|HAMAP-Rule:MF_00171,
CC       ECO:0000256|RuleBase:RU003792, ECO:0000256|SAAS:SAAS00543779}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00171}.
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; CP000251; ABC80157.1; -; Genomic_DNA.
DR   STRING; 290397.Adeh_0381; -.
DR   EnsemblBacteria; ABC80157; ABC80157; Adeh_0381.
DR   KEGG; ade:Adeh_0381; -.
DR   eggNOG; ENOG4105DI7; Bacteria.
DR   eggNOG; COG0101; LUCA.
DR   HOGENOM; HOG000248672; -.
DR   KO; K06173; -.
DR   OMA; FLYGMVR; -.
DR   Proteomes; UP000001935; Chromosome.
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   Gene3D; 3.30.70.660; -; 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   PANTHER; PTHR11142; PTHR11142; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 2.
DR   PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR   SUPFAM; SSF55120; SSF55120; 1.
DR   TIGRFAMs; TIGR00071; hisT_truA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMX1.
DR   SWISS-2DPAGE; Q2IMX1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00171,
KW   ECO:0000256|RuleBase:RU003792, ECO:0000256|SAAS:SAAS00119851};
KW   Lyase {ECO:0000313|EMBL:ABC80157.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00171,
KW   ECO:0000256|RuleBase:RU003792, ECO:0000256|SAAS:SAAS00427419}.
FT   DOMAIN       28    116       PseudoU_synth_1. {ECO:0000259|Pfam:
FT                                PF01416}.
FT   DOMAIN      162    264       PseudoU_synth_1. {ECO:0000259|Pfam:
FT                                PF01416}.
FT   ACT_SITE     71     71       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00171, ECO:0000256|PIRSR:PIRSR001430-
FT                                1}.
FT   BINDING     129    129       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00171, ECO:0000256|PIRSR:PIRSR001430-
FT                                2}.
SQ   SEQUENCE   264 AA;  28776 MW;  3A64FD8051A5DD5B CRC64;
     MPGPCASGRP AARAWYLRGV PVVKLVLEYD GTAYVGWQVQ PNGPSIQAEV ERALATLHKA
     PRRVTAAGRT DAGVHARGQV ASFREDRPLP VKAYVMGMNA VLPPDVAVRA ASLEPDGFDA
     RRSARGKRYR YVIENLPTRA PLTRLQAWQH FHPLELANVR EAAAHLVGRH DFAAFQAADC
     ACEHAVREVR RLEVLGEAGG RIEVVIEATA FVKHMVRNIV GTLVEVGRGR RAPGSMLALL
     ARGDRTEAGP TAPPQGLFLE EVFY
//

If you have problems or comments...

PBIL Back to PBIL home page