CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003615
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine--tRNA ligase 
Protein Synonyms/Alias
 Tyrosyl-tRNA synthetase; TyrRS 
Gene Name
 tyrS 
Gene Synonyms/Alias
 b1637; JW1629 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
8MASSNLIKQLQERGLacetylation[1]
67RFQQAGHKPVALVGGacetylation[2]
85LIGDPSFKAAERKLNacetylation[1, 2]
103TVQEWVDKIRKQVAPacetylation[2]
144TFLRDIGKHFSVNQMacetylation[1, 2, 3]
154SVNQMINKEAVKQRLacetylation[2]
230LTVPLITKADGTKFGacetylation[2]
235ITKADGTKFGKTEGGacetylation[2]
238ADGTKFGKTEGGAVWacetylation[2]
249GAVWLDPKKTSPYKFacetylation[2]
250AVWLDPKKTSPYKFYacetylation[2]
255PKKTSPYKFYQFWINacetylation[2]
377PSRGQARKTIASNAIacetylation[2]
390AITINGEKQSDPEYFacetylation[2]
399SDPEYFFKEEDRLFGacetylation[2]
416TLLRRGKKNYCLICWacetylation[1]
Reference
 [1] 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]
 [2] 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]
 [3] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842
Functional Description
 Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). 
Sequence Annotation
 DOMAIN 357 414 S4 RNA-binding.
 MOTIF 42 51 "HIGH" region.
 MOTIF 235 239 "KMSKS" region.
 BINDING 37 37 Tyrosine.
 BINDING 175 175 Tyrosine.
 BINDING 179 179 Tyrosine.
 BINDING 198 198 Tyr-AMP intermediate adenyl group; via
 BINDING 200 200 Tyr-AMP intermediate adenyl group.
 BINDING 228 228 Tyr-AMP intermediate adenyl group; via
 BINDING 238 238 ATP (By similarity).
 MOD_RES 144 144 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 424 AA 
Protein Sequence
MASSNLIKQL QERGLVAQVT DEEALAERLA QGPIALYCGF DPTADSLHLG HLVPLLCLKR 60
FQQAGHKPVA LVGGATGLIG DPSFKAAERK LNTEETVQEW VDKIRKQVAP FLDFDCGENS 120
AIAANNYDWF GNMNVLTFLR DIGKHFSVNQ MINKEAVKQR LNREDQGISF TEFSYNLLQG 180
YDFACLNKQY GVVLQIGGSD QWGNITSGID LTRRLHQNQV FGLTVPLITK ADGTKFGKTE 240
GGAVWLDPKK TSPYKFYQFW INTADADVYR FLKFFTFMSI EEINALEEED KNSGKAPRAQ 300
YVLAEQVTRL VHGEEGLQAA KRITECLFSG SLSALSEADF EQLAQDGVPM VEMEKGADLM 360
QALVDSELQP SRGQARKTIA SNAITINGEK QSDPEYFFKE EDRLFGRFTL LRRGKKNYCL 420
ICWK 424 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0004831; F:tyrosine-tRNA ligase activity; IEA:HAMAP.
 GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:HAMAP. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002305; aa-tRNA-synth_Ic.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR002942; S4_RNA-bd.
 IPR002307; Tyr-tRNA-ligase.
 IPR024088; Tyr-tRNA-ligase_bac-type.
 IPR024107; Tyr-tRNA-ligase_bac_1. 
Pfam
 PF01479; S4
 PF00579; tRNA-synt_1b 
SMART
 SM00363; S4 
PROSITE
 PS00178; AA_TRNA_LIGASE_I
 PS50889; S4 
PRINTS
 PR01040; TRNASYNTHTYR.