CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001850
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Methionine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Methionyl-tRNA synthetase; MetRS 
Gene Name
 MES1 
Gene Synonyms/Alias
 YGR264C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
9SFLISFDKSKKHPAHacetylation[1]
37EYASKNLKPEVDNDNacetylation[1]
253YGTATETKALEEGVTubiquitination[2]
270QLCDKYHKIHSDVYKacetylation[1]
293FGRTTTDKQTEIAQHubiquitination[2]
368ELINPRCKLDDASPEubiquitination[2]
411GNWSKNSKTITQSWLubiquitination[2]
419TITQSWLKDGLKPRCacetylation[1]
591NFVNRLIKFVNAKYNacetylation[1]
596LIKFVNAKYNGVVPKacetylation[1]
603KYNGVVPKFDPKKVSacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
  
Sequence Annotation
 MOTIF 205 215 "HIGH" region.
 MOTIF 408 412 "KMSKS" region.
 BINDING 411 411 ATP (By similarity).
 MOD_RES 2 2 N-acetylserine.  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 751 AA 
Protein Sequence
MSFLISFDKS KKHPAHLQLA NNLKIALALE YASKNLKPEV DNDNAAMELR NTKEPFLLFD 60
ANAILRYVMD DFEGQTSDKY QFALASLQNL LYHKELPQQH VEVLTNKAIE NYLVELKEPL 120
TTTDLILFAN VYALNSSLVH SKFPELPSKV HNAVALAKKH VPRDSSSFKN IGAVKIQADL 180
TVKPKDSEIL PKPNERNILI TSALPYVNNV PHLGNIIGSV LSADIFARYC KGRNYNALFI 240
CGTDEYGTAT ETKALEEGVT PRQLCDKYHK IHSDVYKWFQ IGFDYFGRTT TDKQTEIAQH 300
IFTKLNSNGY LEEQSMKQLY CPVHNSYLAD RYVEGECPKC HYDDARGDQC DKCGALLDPF 360
ELINPRCKLD DASPEPKYSD HIFLSLDKLE SQISEWVEKA SEEGNWSKNS KTITQSWLKD 420
GLKPRCITRD LVWGTPVPLE KYKDKVLYVW FDATIGYVSI TSNYTKEWKQ WWNNPEHVSL 480
YQFMGKDNVP FHTVVFPGSQ LGTEENWTML HHLNTTEYLQ YENGKFSKSR GVGVFGNNAQ 540
DSGISPSVWR YYLASVRPES SDSHFSWDDF VARNNSELLA NLGNFVNRLI KFVNAKYNGV 600
VPKFDPKKVS NYDGLVKDIN EILSNYVKEM ELGHERRGLE IAMSLSARGN QFLQENKLDN 660
TLFSQSPEKS DAVVAVGLNI IYAVSSIITP YMPEIGEKIN KMLNAPALKI DDRFHLAILE 720
GHNINKAEYL FQRIDEKKID EWRAKYGGQQ V 751 
Gene Ontology
 GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004825; F:methionine-tRNA ligase activity; IDA:SGD.
 GO:0006431; P:methionyl-tRNA aminoacylation; IDA:SGD. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR018285; Met-tRNA-synth_N.
 IPR023458; Met-tRNA_ligase_1.
 IPR014758; Met-tRNA_synth.
 IPR015413; Methionyl/Leucyl_tRNA_Synth.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd. 
Pfam
 PF09635; MetRS-N
 PF09334; tRNA-synt_1g 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR01041; TRNASYNTHMET.