AC MF_00176; DC Protein; auto TR HAMAP; MF_00176; -; 1; level=0 XX Names: Ser_tRNA_synth_type1 XX ID SYS DE RecName: Full=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; 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. The tRNA molecule binds across the dimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N- CC terminal extension that is involved in tRNA binding. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type-1 seryl-tRNA synthetase subfamily. XX DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no DR Pfam; PF02403; Seryl_tRNA_N; 1; trigger=no DR Pfam; PF00587; tRNA-synt_2b; 1; trigger=no DR PRINTS; PR00981; TRNASYNTHSER; 1; trigger=no DR NCBIfam; TIGR00414; SerS; 1; trigger=no XX KW Cytoplasm KW Aminoacyl-tRNA synthetase KW ATP-binding KW Ligase KW Nucleotide-binding KW Protein biosynthesis XX GO GO:0004828; F:serine-tRNA ligase activity GO GO:0005524; F:ATP binding GO GO:0016260; P:selenocysteine biosynthetic process GO GO:0006434; P:seryl-tRNA aminoacylation GO GO:0005737; C:cytoplasm XX FT From: SYS_THET2 (P34945) FT BINDING 256..258 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: R-x-E FT BINDING 345..348 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: E-x-x-S FT BINDING 225..227 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT Condition: T-x-E FT BINDING 272 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Optional; Condition: V FT BINDING 279 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT Condition: E FT BINDING 380 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT Condition: [TS] XX Size: 411-482; Related: None; Template: P0A8L1; P34945; Q46F20; P95689; P54221; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in CLOAB, ENTFA, LACPL, STRAW 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 1.37 2023/06/01 //