CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001851
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methionine--tRNA ligase 
Protein Synonyms/Alias
 Methionyl-tRNA synthetase; MetRS 
Gene Name
 metG 
Gene Synonyms/Alias
 b2114; JW2101 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
121LKENGFIKNRTISQLacetylation[1]
133SQLYDPEKGMFLPDRacetylation[1]
143FLPDRFVKGTCPKCKacetylation[1]
283VSFDEYWKKDSTAELacetylation[1]
343KSRGTFIKASTWLNHacetylation[1]
363LRYYYTAKLSSRIDDacetylation[1]
389VNADIVNKVVNLASRacetylation[1]
403RNAGFINKRFDGVLAacetylation[1]
466QAPWVVAKQEGRDADacetylation[1]
493RVLMTYLKPVLPKLTacetylation[1]
498YLKPVLPKLTERAEAacetylation[1]
529GHKVNPFKALYNRIDacetylation[1]
548EALVEASKEEVKAAAacetylation[1]
597EFVEGSDKLLRLTLDacetylation[1]
609TLDLGGEKRNVFSGIacetylation[1]
659MAAGPGGKDIFLLSPacetylation[1]
671LSPDAGAKPGHQVK*acetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. 
Sequence Annotation
 DOMAIN 575 677 tRNA-binding.
 MOTIF 15 25 "HIGH" region.
 MOTIF 333 337 "KMSKS" region.
 METAL 146 146 Zinc.
 METAL 149 149 Zinc.
 METAL 159 159 Zinc.
 METAL 162 162 Zinc.
 BINDING 336 336 ATP.  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 677 AA 
Protein Sequence
MTQVAKKILV TCALPYANGS IHLGHMLEHI QADVWVRYQR MRGHEVNFIC ADDAHGTPIM 60
LKAQQLGITP EQMIGEMSQE HQTDFAGFNI SYDNYHSTHS EENRQLSELI YSRLKENGFI 120
KNRTISQLYD PEKGMFLPDR FVKGTCPKCK SPDQYGDNCE VCGATYSPTE LIEPKSVVSG 180
ATPVMRDSEH FFFDLPSFSE MLQAWTRSGA LQEQVANKMQ EWFESGLQQW DISRDAPYFG 240
FEIPNAPGKY FYVWLDAPIG YMGSFKNLCD KRGDSVSFDE YWKKDSTAEL YHFIGKDIVY 300
FHSLFWPAML EGSNFRKPSN LFVHGYVTVN GAKMSKSRGT FIKASTWLNH FDADSLRYYY 360
TAKLSSRIDD IDLNLEDFVQ RVNADIVNKV VNLASRNAGF INKRFDGVLA SELADPQLYK 420
TFTDAAEVIG EAWESREFGK AVREIMALAD LANRYVDEQA PWVVAKQEGR DADLQAICSM 480
GINLFRVLMT YLKPVLPKLT ERAEAFLNTE LTWDGIQQPL LGHKVNPFKA LYNRIDMRQV 540
EALVEASKEE VKAAAAPVTG PLADDPIQET ITFDDFAKVD LRVALIENAE FVEGSDKLLR 600
LTLDLGGEKR NVFSGIRSAY PDPQALIGRH TIMVANLAPR KMRFGISEGM VMAAGPGGKD 660
IFLLSPDAGA KPGHQVK 677 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004825; F:methionine-tRNA ligase activity; IEA:HAMAP.
 GO:0000049; F:tRNA binding; IEA:HAMAP.
 GO:0006431; P:methionyl-tRNA aminoacylation; IEA:HAMAP. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR004495; Met-tRNA-synth_Ia_bsu_C.
 IPR023458; Met-tRNA_ligase_1.
 IPR014758; Met-tRNA_synth.
 IPR015413; Methionyl/Leucyl_tRNA_Synth.
 IPR012340; NA-bd_OB-fold.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR002547; tRNA-bd_dom.
 IPR009080; tRNAsynth_1a_anticodon-bd. 
Pfam
 PF09334; tRNA-synt_1g
 PF01588; tRNA_bind 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I
 PS50886; TRBD 
PRINTS
 PR01041; TRNASYNTHMET.