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HAMAP rule MF_01278

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General rule information [?]

Accession MF_01278
Dates 16-APR-2007 (Created)
1-JUN-2023 (Last updated, Version 20)
Name Ser_tRNA_synth_type2
Scope(s) Archaea
Template(s) Q46AN5 (SYS2_METBF); Q58477 (SYS2_METJA); O30520 (SYS2_METMP); O27194 (SYS2_METTH); [ Recover all ]
Triggered by HAMAP; MF_01278 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier SYS2
Protein name RecName: Full=Type-2 serine--tRNA ligase;
                 EC=6.1.1.11;
AltName: Full=Seryl-tRNA synthetase;
                 Short=SerRS;
AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
Gene name Name=serS;

Comments [?]

FUNCTIONCatalyzes 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).
CATALYTIC ACTIVITY Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L- seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CATALYTIC ACTIVITY Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L- seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
case <FTGroup:1>
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 Zn(2+) ion per subunit. This ion is coordinated with 2 cysteines, 1 glutamate and a water molecule that dissociates from the zinc ion to allow the coordination of the amino group of the serine substrate, which is essential for catalysis.;
end case
PATHWAYAminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm.
DOMAINConsists of two distinct domains, a catalytic core and a N- terminal extension that is presumably involved in tRNA binding.
SIMILARITYBelongs to the class-II aminoacyl-tRNA synthetase family. Type-2 seryl-tRNA synthetase subfamily.

Keywords [?]


Gene Ontology [?]

GO:0004828; Molecular function:serine-tRNA ligase activity
GO:0005524; Molecular function:ATP binding
case <FTGroup:1>
GO:0008270; Molecular function:zinc ion binding
end case
GO:0016260; Biological process:selenocysteine biosynthetic process
GO:0006434; Biological process:seryl-tRNA aminoacylation
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

PROSITE PS50862; AA_TRNA_LIGASE_II; 1;
Pfam PF00587; tRNA-synt_2b; 1;
NCBIfam TIGR00415; SerS_MJ; 1;

Features [?]

From: SYS2_METBF (Q46AN5)
Key From To Description Tag Condition FTGroup
BINDING 336 338 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
R-x-E
BINDING 347 348 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
R-V
BINDING 353 355 /ligand="L-serine"
/ligand_id="ChEBI:CHEBI:33384"
R-x-E
BINDING 306 306 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="catalytic"
C 1
BINDING 355 355 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="catalytic"
E 1
BINDING 461 461 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_note="catalytic"
C 1
BINDING 304 304 /ligand="L-serine"
/ligand_id="ChEBI:CHEBI:33384"
A
BINDING 336 336 /ligand="L-serine"
/ligand_id="ChEBI:CHEBI:33384"
R
BINDING 400 400 /ligand="L-serine"
/ligand_id="ChEBI:CHEBI:33384"
Q
BINDING 432 432 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
E
BINDING 435 435 /ligand="L-serine"
/ligand_id="ChEBI:CHEBI:33384"
N
BINDING 468 468 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
R

Additional information [?]

Size range 500-527 amino acids
Related rules None
Fusion Nter: None Cter: None



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