ID SYS_RICCN Reviewed; 425 AA. AC Q92GA7; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 04-NOV-2026, entry version 113. 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}; OrderedLocusNames=RC1216; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; OC spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). 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; AE006914; AAL03754.1; -; Genomic_DNA. DR PIR; H97851; H97851. DR RefSeq; WP_010977781.1; NC_003103.1. DR AlphaFoldDB; Q92GA7; -. DR SMR; Q92GA7; -. DR GeneID; 928366; -. DR KEGG; rco:RC1216; -. DR PATRIC; fig|272944.4.peg.1394; -. DR HOGENOM; CLU_023797_1_1_5; -. DR OMA; AACDQTM; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000000816; Chromosome. 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; Reference proteome. FT CHAIN 1..425 FT /note="Serine--tRNA ligase" FT /id="PRO_0000122109" FT BINDING 228..230 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 259..261 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 282 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 346..349 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" FT BINDING 382 FT /ligand="L-serine" FT /ligand_id="ChEBI:CHEBI:33384" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176" SQ SEQUENCE 425 AA; 48465 MW; 66404AB8FE3726A9 CRC64; MLNIKWIREN KELFDEKLSQ RFIEPMSSKI AMLDGEKRKI TSLIQEFQHA RKVKSKILGN MASKSGEEFE GLQRDVKHIN EKLEALEQDL NNNNELNELL NMFPNIPDDE VPYGMDESMN KLVRTYGETN PNALNKQHFE LGIKLNLMDF EQTAKISGTR FVTLKGDLAK LERALINFMI DVHTKEWDFF EISPPVLVRD NAMYNAGQLP KFAEESFATT NGYRLIPTAE VSLVNMVADT IIPREKLPIR YVAYTPCFRS EAGSSGRDTR GMIRLHQFGK VELVSITTPE ESTNEHEYIT NASETILQKL NLPYRVMLLC TGDMGFAAKK TYDIEVWLPG QKQYREIASC SNCGDFQARR MKARYKEFGS NETTLVHTLN ASGLPIGRTM VAILENYQNE DGSITIPDVL INYMGGLQKI IAYSE //