AC   MF_01278;
DC   Protein; auto
TR   HAMAP; MF_01278; -; 1; level=0
XX
Names: Ser_tRNA_synth_type2
XX
ID   SYS2
DE   RecName: Full=Type-2 serine--tRNA ligase;
DE            EC=6.1.1.11;
DE   AltName: Full=Seryl-tRNA synthetase;
DE            Short=SerRS;
DE   AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
GN   Name=serS;
XX
CC   -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC       to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC       seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC       tRNA(Sec).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC         Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC         seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC         Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 Zn(2+) ion per subunit. This ion is coordinated with 2
CC       cysteines, 1 glutamate and a water molecule that dissociates from the
CC       zinc ion to allow the coordination of the amino group of the serine
CC       substrate, which is essential for catalysis.;
end case
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC       terminal extension that is presumably involved in tRNA binding.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type-2 seryl-tRNA synthetase subfamily.
XX
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no
DR   Pfam; PF00587; tRNA-synt_2b; 1; trigger=no
DR   NCBIfam; TIGR00415; SerS_MJ; 1; trigger=no
XX
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   ATP-binding
KW   Ligase
KW   Metal-binding
KW   Nucleotide-binding
KW   Protein biosynthesis
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
XX
GO   GO:0004828; F:serine-tRNA ligase activity
GO   GO:0005524; F:ATP binding
case <FTGroup:1>
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0016260; P:selenocysteine biosynthetic process
GO   GO:0006434; P:seryl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYS2_METBF (Q46AN5)
FT   BINDING         336..338
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R-x-E
FT   BINDING         347..348
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R-V
FT   BINDING         353..355
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT   Condition: R-x-E
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: C
FT   BINDING         355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: E
FT   BINDING         461
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   Group: 1; Condition: C
FT   BINDING         304
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT   Condition: A
FT   BINDING         336
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT   Condition: R
FT   BINDING         400
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT   Optional; Condition: Q
FT   BINDING         432
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: E
FT   BINDING         435
FT                   /ligand="L-serine"
FT                   /ligand_id="ChEBI:CHEBI:33384"
FT   Optional; Condition: N
FT   BINDING         468
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
XX
Size: 500-527;
Related: None;
Template: Q46AN5; Q58477; O30520; O27194;
Scope:
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
XX
# Revision 1.20 2023/06/01
//