CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005018
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartate--tRNA ligase 
Protein Synonyms/Alias
 Aspartyl-tRNA synthetase; AspRS 
Gene Name
 aspS 
Gene Synonyms/Alias
 tls; b1866; JW1855 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
58PDRADALKLASELRNacetylation[1]
81TVRARDEKNINRDMAacetylation[1]
184LVPSRVHKGKFYALPacetylation[1]
186PSRVHKGKFYALPQSacetylation[1]
283ERRYGSDKPDLRNPMacetylation[1, 2]
315AGPANDPKGRVAALRacetylation[1]
332GGASLTRKQIDEYGNacetylation[1]
342DEYGNFVKIYGAKGLacetylation[1]
347FVKIYGAKGLAYIKVacetylation[1]
353AKGLAYIKVNERAKGacetylation[1, 2]
359IKVNERAKGLEGINSacetylation[1]
370GINSPVAKFLNAEIIacetylation[3]
399IFFGADNKKIVADAMacetylation[1]
415ALRLKVGKDLGLTDEacetylation[1]
513NEEEQREKFGFLLDAacetylation[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]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [3] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508] 
Functional Description
  
Sequence Annotation
  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 590 AA 
Protein Sequence
MRTEYCGQLR LSHVGQQVTL CGWVNRRRDL GSLIFIDMRD REGIVQVFFD PDRADALKLA 60
SELRNEFCIQ VTGTVRARDE KNINRDMATG EIEVLASSLT IINRADVLPL DSNHVNTEEA 120
RLKYRYLDLR RPEMAQRLKT RAKITSLVRR FMDDHGFLDI ETPMLTKATP EGARDYLVPS 180
RVHKGKFYAL PQSPQLFKQL LMMSGFDRYY QIVKCFRDED LRADRQPEFT QIDVETSFMT 240
APQVREVMEA LVRHLWLEVK GVDLGDFPVM TFAEAERRYG SDKPDLRNPM ELTDVADLLK 300
SVEFAVFAGP ANDPKGRVAA LRVPGGASLT RKQIDEYGNF VKIYGAKGLA YIKVNERAKG 360
LEGINSPVAK FLNAEIIEDI LDRTAAQDGD MIFFGADNKK IVADAMGALR LKVGKDLGLT 420
DESKWAPLWV IDFPMFEDDG EGGLTAMHHP FTSPKDMTAA ELKAAPENAV ANAYDMVING 480
YEVGGGSVRI HNGDMQQTVF GILGINEEEQ REKFGFLLDA LKYGTPPHAG LAFGLDRLTM 540
LLTGTDNIRD VIAFPKTTAA ACLMTEAPSF ANPTALAELS IQVVKKAENN 590 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0004815; F:aspartate-tRNA ligase activity; IDA:EcoCyc.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006422; P:aspartyl-tRNA aminoacylation; IDA:EcoCyc. 
Interpro
 IPR004364; aa-tRNA-synt_II.
 IPR018150; aa-tRNA-synt_II-like.
 IPR006195; aa-tRNA-synth_II.
 IPR004524; Asp-tRNA-ligase_IIb_bac/mt.
 IPR002312; Asp/Asn-tRNA-synth_IIb.
 IPR004115; GAD_dom.
 IPR012340; NA-bd_OB-fold.
 IPR004365; NA-bd_OB_tRNA-helicase. 
Pfam
 PF02938; GAD
 PF00152; tRNA-synt_2
 PF01336; tRNA_anti 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR01042; TRNASYNTHASP.