MST1 threonine--tRNA ligase MST1 [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Official Symbol: MST1
Official Full Name: threonine--tRNA ligase MST1
Primary source: SGD:S000001677
Locus tag: YKL194C
See related: AllianceGenome:SGD:S000001677; FungiDB:YKL194C; VEuPathDB:YKL194C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables threonine-tRNA ligase activity. Involved in mitochondrial threonyl-tRNA aminoacylation. Located in mitochondrion. [provided by Alliance of Genome Resources, Jul 2025]
Orthologs: all
: Try the new Gene page
Try the new Transcripts and proteins table

Genomic context

Go to the top of the page Help

See MST1 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (77258..78646, complement)

Chromosome XI - NC_001143.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Data suggest that structural features of the anticodon-binding domain in threonine--tRNA ligase MST1 permit binding of the enlarged anticodon loop of tRNA1(Thr).
Title: The crystal structure of yeast mitochondrial ThrRS in complex with the canonical threonine tRNA.
the plasticity of the aminoacylation site in MST1 allows binding of Ser-AMP and the appropriate positioning of the hydrolytic water molecule.
Title: The mechanism of pre-transfer editing in yeast mitochondrial threonyl-tRNA synthetase.
MST1 recognizes and aminoacylates two natural tRNAs that contain anticodon loops of different size and sequence
Title: Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment.

Submit: New GeneRIF Correction

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables aminoacyl-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables catalytic activity, acting on a tRNA	IEA Inferred from Electronic Annotation more info
enables ligase activity	IEA Inferred from Electronic Annotation more info
enables nucleotide binding	IEA Inferred from Electronic Annotation more info
enables threonine-tRNA ligase activity	IBA Inferred from Biological aspect of Ancestor more info
enables threonine-tRNA ligase activity	IDA Inferred from Direct Assay more info	PubMed
enables threonine-tRNA ligase activity	IEA Inferred from Electronic Annotation more info
enables threonine-tRNA ligase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables zinc ion binding	RCA inferred from Reviewed Computational Analysis more info	PubMed

Process	Evidence Code	Pubs
involved_in mitochondrial threonyl-tRNA aminoacylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitochondrial threonyl-tRNA aminoacylation	IDA Inferred from Direct Assay more info	PubMed
involved_in tRNA aminoacylation for protein translation	IEA Inferred from Electronic Annotation more info
involved_in threonyl-tRNA aminoacylation	IEA Inferred from Electronic Annotation more info
involved_in translation	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: threonine--tRNA ligase MST1

NP_012727.1

EC 6.1.1.3

Mitochondrial threonyl-tRNA synthetase; aminoacylates both the canonical threonine tRNA tT(UGU)Q1 and the unusual threonine tRNA tT(UAG)Q2 in vitro; lacks a typical editing domain, but has pre-transfer editing activity stimulated by the unusual tRNA-Thr

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

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

Reference assembly

Genomic

NC_001143.9 Reference assembly

Range

77258..78646 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179760.1 → NP_012727.1 threonine--tRNA ligase MST1

See identical proteins and their annotated locations for NP_012727.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VX06, P07236

UniProtKB/TrEMBL

A6ZZD1, B3LQR1, G2WHJ8

Conserved Domains (2) summary

cd00771
Location:44 → 347

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:347 → 459

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 ...