ID SYS_BACC2 Reviewed; 424 AA. AC B7IS31; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 04-NOV-2026, entry version 84. DE RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176}; DE EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; DE Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176}; DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176}; GN Name=serS {ECO:0000255|HAMAP-Rule:MF_00176}; GN OrderedLocusNames=BCG9842_B5302; OS Bacillus cereus (strain G9842). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC Bacillus; Bacillus cereus group. OX NCBI_TaxID=405531; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G9842; RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., RA Ravel J., Sutton G.; RT "Genome sequence of Bacillus cereus G9842."; RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases. 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). {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + CC diphosphate + H(+); 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00176}; CC -!- CATALYTIC ACTIVITY: CC Reaction=tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + CC diphosphate + H(+); 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 Evidence={ECO:0000255|HAMAP-Rule:MF_00176}; CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N- CC terminal extension that is involved in tRNA binding. CC {ECO:0000255|HAMAP-Rule:MF_00176}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00176}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001186; ACK98137.1; -; Genomic_DNA. DR RefSeq; WP_000884174.1; NC_011772.1. DR SMR; B7IS31; -. DR GeneID; 67464609; -. DR KEGG; bcg:BCG9842_B5302; -. DR HOGENOM; CLU_023797_1_1_9; -. DR OMA; AACDQTM; -. DR UniPathway; UPA00906; UER00895. DR CDD; cd00770; SerRS_core; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 1. DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. DR InterPro; IPR002317; Ser-tRNA-ligase_type_1. DR InterPro; IPR015866; Ser-tRNA-synth_1_N. DR InterPro; IPR042103; SerRS_1_N_sf. DR InterPro; IPR033729; SerRS_core. DR InterPro; IPR010978; tRNA-bd_arm. DR PANTHER; PTHR43697:SF1; SERINE--TRNA LIGASE; 1. DR PANTHER; PTHR43697; SERYL-TRNA SYNTHETASE; 1. DR Pfam; PF02403; Seryl_tRNA_N; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1. DR PRINTS; PR00981; TRNASYNTHSER. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF46589; tRNA-binding arm; 1. DR NCBIfam; TIGR00414; serS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProtKB-ARBA. DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016260; P:L-selenocysteine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR AlphaFoldDB; B7IS31; -. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..424 FT /note="Serine--tRNA ligase" FT /id="PRO_1000199466" FT BINDING 231..233 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 262..264 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 285 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 349..352 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 385 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" SQ SEQUENCE 424 AA; 48808 MW; 767F90DF04711C96 CRC64; MLDIKFLRTN FEEVKAKLQH RGEDLTDFGR FEELDTRRRE LLVQTEELKS KRNEVSQQIS VLKREKKDAE ALILEMREVG EKVKDFDNEL RTVEEDLERL MLSIPNIPHE SAPVGETEDD NVVARTWGEV KEFTFEPKPH WDLATDLGIL DFERAGKVTG SRFVFYKGAG ARLERALISF MLDLHTDEHG YEEVLPPYMV NRASMTGTGQ LPKFEEDAFR IESEDYFLIP TAEVPVTNMH RDEILNKEQL PIRYAAFSSC FRSEAGSAGR DTRGLIRQHQ FNKVELVKFV KPEDSYEELE KLTNDAERVL QLLELPYRVM SMCTGDLGFT AAKKYDIEVW IPSYGTYREI SSCSNFEAFQ ARRANIRFRR EPNGKPEHVH TLNGSGLAIG RTVAAILENY QQEDGTIIIP EVLRPYMGGK TVIK //