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TARS2 threonyl-tRNA synthetase 2, mitochondrial [ Mandrillus leucophaeus (drill) ]

Gene ID: 105534763, updated on 13-Mar-2024

Summary

Gene symbol
TARS2
Gene description
threonyl-tRNA synthetase 2, mitochondrial
See related
Ensembl:ENSMLEG00000030174
Gene type
protein coding
RefSeq status
MODEL
Organism
Mandrillus leucophaeus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Cercopithecidae; Cercopithecinae; Mandrillus
Orthologs
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Genomic context

See TARS2 in Genome Data Viewer
Location:
chromosome: Un
Exon count:
18
Annotation release Status Assembly Chr Location
100 current Mleu.le_1.0 (GCF_000951045.1) Unplaced Scaffold NW_012101354.1 (2195721..2217519, complement)

NW_012101354.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC105534762 Neighboring gene extracellular matrix protein 1 Neighboring gene regulation of nuclear pre-mRNA domain containing 2 Neighboring gene pre-mRNA processing factor 3

Genomic regions, transcripts, and products

Genomic Sequence:
NW_012101354.1 Unplaced Scaffold Reference Mleu.le_1.0

General gene information

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
PubMed 
enables threonine-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
PubMed 
Process Evidence Code Pubs
involved_in threonyl-tRNA aminoacylation IEA
Inferred from Electronic Annotation
more info
PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
PubMed 
located_in mitochondrion IEA
Inferred from Electronic Annotation
more info
PubMed 

General protein information

Preferred Names
threonine--tRNA ligase, mitochondrial
Names
threonyl-tRNA synthetase 2, mitochondrial (putative)

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Mandrillus leucophaeus Annotation Release 100 details...Open this link in a new tab

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference Mleu.le_1.0

Genomic

  1. NW_012101354.1 Reference Mleu.le_1.0

    Range
    2195721..2217519 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_011973614.1XP_011829004.1  threonine--tRNA ligase, mitochondrial isoform X3

    UniProtKB/TrEMBL
    A0A2K5Y934
    Related
    ENSMLEP00000012076.1, ENSMLET00000035502.1
    Conserved Domains (4) summary
    cd01667
    Location:61122
    TGS_ThrRS_N; TGS _ThrRS_N: ThrRS (threonyl-tRNA Synthetase) is a class II tRNA synthetase that couples threonine to its cognate tRNA. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and ...
    PLN02908
    Location:17578
    PLN02908; threonyl-tRNA synthetase
    cd00771
    Location:202483
    ThrRS_core; Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent ...
    cd00860
    Location:483574
    ThrRS_anticodon; ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is ...
  2. XM_011973613.1XP_011829003.1  threonine--tRNA ligase, mitochondrial isoform X2

    UniProtKB/TrEMBL
    A0A2K5Y939
    Related
    ENSMLEP00000012075.1, ENSMLET00000035501.1
    Conserved Domains (5) summary
    cd01667
    Location:61122
    TGS_ThrRS_N; TGS _ThrRS_N: ThrRS (threonyl-tRNA Synthetase) is a class II tRNA synthetase that couples threonine to its cognate tRNA. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and ...
    PLN02908
    Location:17626
    PLN02908; threonyl-tRNA synthetase
    smart00863
    Location:229265
    tRNA_SAD; Threonyl and Alanyl tRNA synthetase second additional domain
    cd00771
    Location:255531
    ThrRS_core; Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent ...
    cd00860
    Location:531622
    ThrRS_anticodon; ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is ...
  3. XM_011973612.1XP_011829002.1  threonine--tRNA ligase, mitochondrial isoform X1

    See identical proteins and their annotated locations for XP_011829002.1

    UniProtKB/TrEMBL
    A0A2K5Y930
    Related
    ENSMLEP00000012071.1, ENSMLET00000035497.1
    Conserved Domains (5) summary
    cd01667
    Location:61122
    TGS_ThrRS_N; TGS _ThrRS_N: ThrRS (threonyl-tRNA Synthetase) is a class II tRNA synthetase that couples threonine to its cognate tRNA. In addition to its catalytic and anticodon-binding domains, ThrRS has an N-terminal TGS domain, named after the ThrRS, GTPase, and ...
    PLN02908
    Location:17708
    PLN02908; threonyl-tRNA synthetase
    smart00863
    Location:229252
    tRNA_SAD; Threonyl and Alanyl tRNA synthetase second additional domain
    cd00771
    Location:300613
    ThrRS_core; Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent ...
    cd00860
    Location:613704
    ThrRS_anticodon; ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is ...