ExPASy Proteomics Server

Accession	MF_00176
Dates	1-JUN-2001 (Created) 25-NOV-2009 (Last updated, Version 26)

Data class

Protein

Predictors

HAMAP; MF_00176; [distribution of match scores in UniProtKB];[seed alignment for MF_00176]

Names

Ser_tRNA_synth_type1

Identifier

SYS

Protein name

RecName: Full=Seryl-tRNA synthetase; EC=6.1.1.11; AltName: Full=Seryl-tRNA(Ser/Sec) synthetase; AltName: Full=Serine--tRNA ligase; Short=SerRS;

Gene name

serS

FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also 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) (By similarity).

CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).

CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).

PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.

SUBUNIT: Homodimer. The tRNA molecule binds across the dimer (By similarity).

SUBCELLULAR LOCATION: Cytoplasm (By similarity).

DOMAIN: Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding (By similarity).

SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

PROSITE	PS50862; AA_TRNA_LIGASE_II; 1;
Pfam	PF02403; Seryl_tRNA_N; 1; PF00587; tRNA-synt_2b; 1;
PRINTS	PR00981; TRNASYNTHSER; 1;
TIGRFAMs	TIGR00414; serS; 1;

Cytoplasm, Aminoacyl-tRNA synthetase, ATP-binding, Ligase, Nucleotide-binding, Protein biosynthesis.

GO:0004828; Molecular function: serine-tRNA ligase activity.
GO:0005524; Molecular function: ATP binding.
GO:0016260; Biological process: selenocysteine biosynthetic process.
GO:0006434; Biological process: seryl-tRNA aminoacylation.
GO:0005737; Cellular component: cytoplasm.

From: SYS_THET2 (P34945)
Key		From		To		Description		Condition		FTGroup
NP_BIND		256		258		ATP (By similarity)		R-x-E
NP_BIND		345		348		ATP (By similarity)		E-x-x-S
REGION		225		227		Serine binding (By similarity)		T-x-E
BINDING (Optional)		272		272		ATP; via carbonyl oxygen and amide nitrogen (By similarity)		V
BINDING		279		279		Serine (By similarity)		E
BINDING		380		380		Serine (By similarity)		[TS]

Size range:	411-482 amino acids
Related UniRules:	None
Template:	P0A8L1 (SYS_ECOLI); P34945 (SYS_THET2); Q46F20 (SYS_METBF); P95689 (SYS_STAA8); P54221 (SYS_HALMA): [Recover all]
Scope:	Bacteria Archaea
Fusion:	Nter: None; Cter: None
Duplicate:	in CLOAB, ENTFA, LACPL, STRAW
Plasmid encoded:	None
Comments:	There are two distinct types of seryl-tRNA synthetase, as differentiated by primary sequence analysis, three-dimensional structure and substrate recognition mechanism: type 1 (MF_00176) is found in the majority of organisms (prokaryotes, eukaryotes and archaea) whereas type 2 (MF_01278) is confined to some methanogenic archaea. METBF (Methanosarcina barkeri) possesses two seryl-tRNA synthetases, one of each type.