ID A0A4D6P5L7_SALET Unreviewed; 677 AA. AC A0A4D6P5L7; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 02-JUN-2021, entry version 5. DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00098}; DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_00098}; DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00098}; DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_00098}; GN Name=metG {ECO:0000256|HAMAP-Rule:MF_00098, GN ECO:0000313|EMBL:QCF21272.1}; GN ORFNames=SEEB0189_08655 {ECO:0000313|EMBL:QCF21272.1}; OS Salmonella enterica subsp. enterica serovar Bareilly str. CFSAN000189. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=1173427 {ECO:0000313|EMBL:QCF21272.1}; RN [1] {ECO:0000313|EMBL:QCF21272.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CFSAN000189 {ECO:0000313|EMBL:QCF21272.1}; RA Hoffmann M., Sanchez M., Timme R.; RT "Whole genome sequencing of cultured pathogen."; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. 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_00098}. 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; CC Evidence={ECO:0000256|ARBA:ARBA00001234, ECO:0000256|HAMAP- CC Rule:MF_00098}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00098}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00098}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_00098}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00098}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|RuleBase:RU363039}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC MetG type 1 subfamily. {ECO:0000256|ARBA:ARBA00008258, CC ECO:0000256|HAMAP-Rule:MF_00098}. 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; CP039502; QCF21272.1; -; Genomic_DNA. DR RefSeq; WP_000195334.1; NZ_CP045753.1. DR SMR; A0A4D6P5L7; -. DR KEGG; seeb:SEEB0189_008740; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; 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 CDD; cd02800; tRNA_bind_EcMetRS_like; 1. DR Gene3D; 2.20.28.20; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR041872; Anticodon_Met. DR InterPro; IPR004495; Met-tRNA-synth_bsu_C. DR InterPro; IPR023458; Met-tRNA_ligase_1. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR033911; MetRS_core. DR InterPro; IPR029038; MetRS_Zn. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR Pfam; PF09334; tRNA-synt_1g; 1. DR Pfam; PF01588; tRNA_bind; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF57770; SSF57770; 1. DR TIGRFAMs; TIGR00398; metG; 1. DR TIGRFAMs; TIGR00399; metG_C_term; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00098}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00098}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00098}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00098}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00098}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00098}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00098}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00098}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00098}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00098}. FT DOMAIN 575..677 FT /note="TRNA-binding" FT /evidence="ECO:0000259|PROSITE:PS50886" FT MOTIF 15..25 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT MOTIF 333..337 FT /note="'KMSKS' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT METAL 146 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT METAL 149 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT METAL 159 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT METAL 162 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" FT BINDING 336 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00098" SQ SEQUENCE 677 AA; 76244 MW; 3591C811C8CEFEDB CRC64; MTQVAKKILV TCALPYANGS IHLGHMLEHI QADVWVRYQR MRGHEVNFIC ADDAHGTPIM LKAQQLGITP EQMIGEMSQE HQTDFAGFNI SYDNYHSTHS DENRELSELI YTRLKENGFI KNRTISQLYD PEKGMFLPDR FVKGTCPKCK SADQYGDNCE VCGATYSPTE LIEPKSVVSG ATPVMRDSEH FFFDLPSFSE MLQAWTRSGA LQEQVANKMQ EWFESGLQQW DISRDAPYFG FEIPNAPGKY FYVWLDAPIG YMGSFKNLCD KRGDTTSFDE YWKKDSDAEL YHFIGKDIVY FHSLFWPAML EGSHFRKPTN LFVHGYVTVN GAKMSKSRGT FIKASTWLKH FDADSLRYYY TAKLSSRIDD IDLNLEDFVQ RVNADIVNKV VNLASRNAGF INKRFDGVLA AELADPQLYK TFTDAAAVIG EAWESREFGK AIREIMALAD VANRYVDEQA PWVVAKQEGR DADLQAICSM GINLFRVLMT YLKPVLPTLS ERVEAFLNSE LNWDAIEQPL LGHKVNTFKA LYNRIDMKQV EALVEASKEE VKAAAAPVTG PLADFPIQET ITFDDFAKID LRVALIENAE FVDGSDKLLR LTLDLGGEKR NVFSGIRSAY PDPQALIGRQ TVMVANLAPR KMRFGVSEGM VMAAGPGGKD IFLLSPDDGA KPGQQVK //