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seryl-tRNA synthetase (serine-tRNA ligase, SerRS, SARS)
Function:
- catalyzes the attachment of serine to tRNA(Ser)
- 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)
- aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(sec)
- biosynthesis; L-seryl-tRNA(sec) from L-serine & tRNA(sec): step 1/1
- phosphorylated upon DNA damage, probably by ATM or ATR
ATP + L-serine + tRNA(Ser)
AMP + diphosphate + L-seryl-tRNA(Ser)
ATP + L-serine + tRNA(sec)
AMP + diphosphate + L-seryl-tRNA(sec)
Structure:
- homodimer
- tRNA molecule binds across the dimer
- consists of two distinct domains, a catalytic core & a N-terminal extension that is involved in tRNA binding
- belongs to aminoacyl-tRNA synthetase-2 family, type-1 seryl-tRNA synthetase subfamily
Compartment: cytoplasm
General
amino acyl tRNA synthetase-2
phosphoprotein
Properties
SIZE: entity length = 514 aa
MW = 59 kD
COMPARTMENT: cytoplasm
MOTIF: Ser phosphorylation site {S241}
Serine binding {271-273}
ATP-binding site
NAME: ATP-binding site
SITE: 302-304
ATP-binding site
NAME: ATP-binding site
SITE: 318-318
binding site
SITE: 325-325
FOR-BINDING-OF: Serine
ATP-binding site
NAME: ATP-binding site
SITE: 391-394
binding site
SITE: 429-429
FOR-BINDING-OF: Serine
Database Correlations
OMIM 607529
UniProt P49591
PFAM correlations
Kegg hsa:6301
ENZYME 6.1.1.11
References
UniProt :accession P49591