ID D5DAJ0_PRIM3 Unreviewed; 328 AA. AC D5DAJ0; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 27-MAR-2024, entry version 77. 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:ADF37569.1}; GN OrderedLocusNames=BMD_0705 {ECO:0000313|EMBL:ADF37569.1}; OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia. OX NCBI_TaxID=592022 {ECO:0000313|EMBL:ADF37569.1, ECO:0000313|Proteomes:UP000002365}; RN [1] {ECO:0000313|EMBL:ADF37569.1, ECO:0000313|Proteomes:UP000002365} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 319 / IMG 1521 {ECO:0000313|Proteomes:UP000002365}; RX PubMed=21705586; DOI=10.1128/JB.00449-11; RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., RA Koenig S.S., Huot Creasy H., Rosovitz M.J., Riley D.R., Daugherty S., RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C., RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J., RA Bremer E., Jahn D., Ravel J., Vary P.S.; RT "Genome sequences of the biotechnologically important Bacillus megaterium RT strains QM B1551 and DSM319."; RL J. Bacteriol. 193:4199-4213(2011). 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; CP001982; ADF37569.1; -; Genomic_DNA. DR AlphaFoldDB; D5DAJ0; -. DR KEGG; bmd:BMD_0705; -. DR HOGENOM; CLU_029244_1_1_9; -. DR Proteomes; UP000002365; 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; IPR001412; aa-tRNA-synth_I_CS. 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. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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 10..18 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT MOTIF 192..196 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 9..11 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 17..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 132 FT /ligand="L-tryptophan" FT /ligand_id="ChEBI:CHEBI:57912" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 144..146 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 183 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" FT BINDING 192..196 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00140" SQ SEQUENCE 328 AA; 36501 MW; FD78423C2D9A2F69 CRC64; MKTIFSGIQP SGTITLGNYI GAMKQFVELQ HDYNCHFCIV DQHAITAPQD RLALRKNIRS LAALYVAVGI DPAKSTLFIQ SEVPAHTEAG WMLQCVAYIG ELERMTQFKD KSAGKEAVSA GLLTYPPLMA ADILLYNTDL VPVGEDQKQH LELTRDLAER FNKKYNDIFT IPEVRIPKVG ARVMSLQDPT KKMSKSDPNQ KAFITLLDDA KTIEKKIKSA VTDSEGIVRY DKENKPGISN LLSIYSILAN KSIEDIEAMY EGKGYGDFKA DTAKVVAEAL APIQERYYEL VDSSELDDIL DQGADKANAT ANKMLRKMRN AMGIGRKR //