ID A9WP14_RENSM Unreviewed; 529 AA. AC A9WP14; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01228}; DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_01228}; DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228}; DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_01228}; GN Name=metG {ECO:0000256|HAMAP-Rule:MF_01228}; GN OrderedLocusNames=RSal33209_1051 {ECO:0000313|EMBL:ABY22789.1}; OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / OS NBRC 15589 / NCIMB 2235). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Renibacterium. OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY22789.1, ECO:0000313|Proteomes:UP000002007}; RN [1] {ECO:0000313|Proteomes:UP000002007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235 RC {ECO:0000313|Proteomes:UP000002007}; RX PubMed=18723615; DOI=10.1128/JB.00721-08; RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.; RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests RT reductive evolution away from an environmental Arthrobacter ancestor."; RL J. Bacteriol. 190:6970-6982(2008). CC -!- FUNCTION: Is required not only for elongation of protein synthesis but CC also for the initiation of all mRNA translation through initiator CC tRNA(fMet) aminoacylation. {ECO:0000256|ARBA:ARBA00003314, CC ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L- CC methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667, CC Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530, CC ChEBI:CHEBI:456215; EC=6.1.1.10; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01228}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC MetG type 2B subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}. 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; CP000910; ABY22789.1; -; Genomic_DNA. DR RefSeq; WP_012244480.1; NC_010168.1. DR AlphaFoldDB; A9WP14; -. DR SMR; A9WP14; -. DR STRING; 288705.RSal33209_1051; -. DR KEGG; rsa:RSal33209_1051; -. DR eggNOG; COG0143; Bacteria. DR HOGENOM; CLU_009710_9_4_11; -. DR Proteomes; UP000002007; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07957; Anticodon_Ia_Met; 1. DR CDD; cd00814; MetRS_core; 1. DR Gene3D; 2.170.220.10; -; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_01228; Met_tRNA_synth_type2; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR041872; Anticodon_Met. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR023457; Met-tRNA_synth_2. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR033911; MetRS_core. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR NCBIfam; TIGR00398; metG; 1. DR PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 1. DR Pfam; PF19303; Anticodon_3; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. 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_01228}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01228}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01228}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01228}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01228}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_01228}; Reference proteome {ECO:0000313|Proteomes:UP000002007}. FT DOMAIN 10..368 FT /note="Methionyl/Leucyl tRNA synthetase" FT /evidence="ECO:0000259|Pfam:PF09334" FT DOMAIN 380..516 FT /note="Methionyl-tRNA synthetase anticodon-binding" FT /evidence="ECO:0000259|Pfam:PF19303" FT MOTIF 305..309 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228" SQ SEQUENCE 529 AA; 59191 MW; 30D9647955EA8BA4 CRC64; MTESSNKRPY YLTTAITYPN GVPHIGHAYE YVSADALARF KRLDGFDVFY MSGTDEHGIK VQQAAEKEGV TPLELVDRNS AAIRAVHDLV ESSYDRFIRT TEPEHYLASQ ELWRRMEANG DIYLDKYTGW YSVRDEAYYT DEQTELRADG IRYAIETETE VTWTEEESYF FRLSNYQEKL LALYEAQPEF AAPQYRFNEV ISFVKSGLQD LSISRTSFNW GVPVPGNDKH VMYVWVDALT NYLTGAGFPD ESSSQWKYWP ADVHIIGKDI SRFHAIFWPG FLMSAGLPLP KRVMIHGFLF NNGVKMSKSF GNVVAPADWV AAYGVDAVRF FFLREVSYGQ DGNYSHEAII SRKNSDLANN LGNLAQRSLS MVAKNCDGVV PTPGEFSSAD QAILAKAQAL LAANRASYEV QEFHRALEAI WAVLGDTNAY FADQAPWVLR KTDPERMATV LYVTLEVLRI VALLIQPVMP GSAAKLLDVL GVSAAEGARD FTAVETPLVA GTALPAPSPI FPRYEEPAEA SAHGKPQTH //