ID C3PNS7_RICAE Unreviewed; 330 AA. AC C3PNS7; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00140}; DE EC=6.1.1.2 {ECO:0000256|HAMAP-Rule:MF_00140}; DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00140}; DE Short=TrpRS {ECO:0000256|HAMAP-Rule:MF_00140}; GN Name=trpS {ECO:0000256|HAMAP-Rule:MF_00140, GN ECO:0000313|EMBL:ACP53587.1}; GN OrderedLocusNames=RAF_ORF0697 {ECO:0000313|EMBL:ACP53587.1}; OS Rickettsia africae (strain ESF-5). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=347255 {ECO:0000313|EMBL:ACP53587.1, ECO:0000313|Proteomes:UP000002305}; RN [1] {ECO:0000313|EMBL:ACP53587.1, ECO:0000313|Proteomes:UP000002305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ESF-5 {ECO:0000313|EMBL:ACP53587.1, RC ECO:0000313|Proteomes:UP000002305}; RX PubMed=19379498; DOI=10.1186/1471-2164-10-166; RA Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B., RA Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.; RT "Analysis of the Rickettsia africae genome reveals that virulence RT acquisition in Rickettsia species may be explained by genome reduction."; RL BMC Genomics 10:166-166(2009). CC -!- FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). CC {ECO:0000256|HAMAP-Rule:MF_00140}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + H(+) + L- CC tryptophanyl-tRNA(Trp); Xref=Rhea:RHEA:24080, Rhea:RHEA-COMP:9671, CC Rhea:RHEA-COMP:9705, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57912, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78535, ChEBI:CHEBI:456215; EC=6.1.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00000107, ECO:0000256|HAMAP- CC Rule:MF_00140}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00140}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00140, CC ECO:0000256|RuleBase:RU363036}. 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; CP001612; ACP53587.1; -; Genomic_DNA. DR RefSeq; WP_012719785.1; NC_012633.1. DR AlphaFoldDB; C3PNS7; -. DR KEGG; raf:RAF_ORF0697; -. DR HOGENOM; CLU_029244_1_4_5; -. DR Proteomes; UP000002305; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00806; TrpRS_core; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 1.10.240.10; Tyrosyl-Transfer RNA Synthetase; 1. DR HAMAP; MF_00140_B; Trp_tRNA_synth_B; 1. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002306; Trp-tRNA-ligase. DR InterPro; IPR024109; Trp-tRNA-ligase_bac-type. DR NCBIfam; TIGR00233; trpS; 1. DR PANTHER; PTHR43766; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43766:SF1; TRYPTOPHAN--TRNA LIGASE, MITOCHONDRIAL; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01039; TRNASYNTHTRP. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00140}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00140}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00140}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00140}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00140}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00140}. FT MOTIF 11..19 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT MOTIF 195..199 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 10..12 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 18..19 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 134 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 146..148 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 186 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 195..199 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" SQ SEQUENCE 330 AA; 37503 MW; 964BF64DDE81E6AA CRC64; MKKTVLSGVQ ATGSLHLGNY LGAIKNWVKM QEEYNCFFFL ADLHAITVDI KPSELNNSIM EVLAVYLAAG LNPDKVTIFA QSMVKEHTEL AWLLNCVTPL GWLKRMTQFK DKAGSDQEKA CLGLFSYPVL MAADILIYKA DIVPVGEDQK QHLELTRDIA GVINRKFNKE ILKVPEVLIS ETGTRIMSLR DGLKKMSKSD ISDFSRINLK DNNDLIHQKI KKAKTDHLSF VSYDQETRPE ISNLLDIYSS LSEESLEKII GNYQNQGFAK FKEDLAEIII TNLQPIRNKY LELMNDKEYL LKILHKGAEK ARIRASETVN EVKEQFGFVI //