ID SYS_BRUAB Reviewed; 427 AA. AC Q57DM2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 02-SEP-2026, entry version 117. 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=BruAb1_0897; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella; OC Brucella melitensis group. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison to RT the highly similar genomes of Brucella melitensis and Brucella suis."; RL J. Bacteriol. 187:2715-2726(2005). 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; AE017223; AAX74262.1; -; Genomic_DNA. DR RefSeq; WP_002964015.1; NC_006932.1. DR AlphaFoldDB; Q57DM2; -. DR SMR; Q57DM2; -. DR EnsemblBacteria; AAX74262; AAX74262; BruAb1_0897. DR GeneID; 93016737; -. DR GeneID; 99643909; -. DR KEGG; bmb:BruAb1_0897; -. DR HOGENOM; CLU_023797_1_1_5; -. DR UniPathway; UPA00906; UER00895. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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 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 NCBIfam; TIGR00414; serS; 1. 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 PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..427 FT /note="Serine--tRNA ligase" FT /id="PRO_1000019626" 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 427 AA; 47548 MW; 9452FF0D8CA3F376 CRC64; MLDIKWIREN PETLDKALAK RGAAPLSSEL IALDEKRREH VGKVQAAQER RNAASKEIGK AMAAKDMGTA EKLKAEVGEL KDFLAHAEED ERRLSKELSD ALSTIPNIPL DDVPLGKDES DNVELRRIGN PHNFSFQPKE HFELGEALGY MDFERAAKLA GARFTVLKGP LARLERALGQ FMLDLHTTEH GYTEVMPPLM VRDEAVYGTG QLPKFSEDLF RTTDGRWLIP TAEVPLTNLV AEEIVDMKGL PLRFTALTPC FRSEAGSAGR DTRGMLRQHQ FLKVEMVSIT DAESSVAEHE RMTACAEEVL KRLGLPFRTV VLCTGDMGFG AQRTYDIEVW LPGQNTYREI SSCSTCGDFQ GRRMNARYRP EGEKSTRFVH TLNGSGVAVG RALIAVMENY QQEDGSIHIP EALQPYMGGL TRIEKAA //