Q9N0F3 · SYSM_BOVIN
- ProteinSerine--tRNA ligase, mitochondrial
- GeneSARS2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids518 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Catalytic activity
- ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H+ + L-seryl-tRNA(Ser)
Pathway
Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 299-301 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: TAE | ||||||
Binding site | 330-332 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RAE | ||||||
Binding site | 345 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 352 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 418-421 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EVTS | ||||||
Binding site | 453 | L-serine (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Molecular Function | ATP binding | |
Molecular Function | serine-tRNA ligase activity | |
Molecular Function | tRNA binding | |
Biological Process | mitochondrial seryl-tRNA aminoacylation | |
Biological Process | seryl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine--tRNA ligase, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ9N0F3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-34 | Mitochondrion | ||||
Sequence: MAASIVRRLGPLVAGRGLRLRGGCVCNQSFKRSF | ||||||
Chain | PRO_0000035821 | 35-518 | Serine--tRNA ligase, mitochondrial | |||
Sequence: ATERQDRNLLYEHAREGYSALPLLDMESLCAYPEDAARALDLRKGELRSKDLPGIISTWQELRQLREQIRSLEEEKEAVTEAVRALVVNQDNSQVQQDPQYQSLRARGREIRKQLTLLYPKEAQLEEQFYLRALRLPNQTHPDVPVGDESQARVLHVVGDKPAFSFQPRGHLEIAEKLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTLNKLIHRGFTPMTVPDLLRGVVFEGCGMTPNAKPSQIYNIDPSRFEDLNLAGTAEVGLAGYFMDHSVAFRDLPIRMVCSSTCYRAETDTGKEPWGLYRVHHFTKVEMFGVTGPGLEQSSELLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVTSASNCTDFQSRRLHIMFQTEAGELQFAHTVNATGCAVPRLLIALLESYQQKDGSVLVPPALQPYLGTDRITTPTHVPLQYIGPNQPQKPRLPGQPASS | ||||||
Modified residue | 110 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 195 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 337 | N6-succinyllysine | ||||
Sequence: K |
Post-translational modification
Two N-termini starting at positions 35 and 37 have been identified by direct sequencing.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer. The tRNA molecule probably binds across the dimer.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 497-518 | Disordered | ||||
Sequence: PLQYIGPNQPQKPRLPGQPASS |
Domain
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length518
- Mass (Da)58,296
- Last updated2000-10-01 v1
- ChecksumC4411C953E842595
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 438 | in Ref. 2; AAX46747 | ||||
Sequence: Q → H |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB029947 EMBL· GenBank· DDBJ | BAA99556.1 EMBL· GenBank· DDBJ | mRNA | ||
BT021565 EMBL· GenBank· DDBJ | AAX46412.1 EMBL· GenBank· DDBJ | mRNA | ||
BT021900 EMBL· GenBank· DDBJ | AAX46747.1 EMBL· GenBank· DDBJ | mRNA | ||
BC140548 EMBL· GenBank· DDBJ | AAI40549.1 EMBL· GenBank· DDBJ | mRNA |