CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011290
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Arginine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Arginyl-tRNA synthetase; ArgRS 
Gene Name
 YDR341C; D9651.10 
Gene Synonyms/Alias
  
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
156FSSPNIAKPFHAGHLacetylation[1]
194NYLGDWGKQFGLLAVubiquitination[2]
229DVYVRINKDIEEEGDacetylation[1]
229DVYVRINKDIEEEGDubiquitination[2]
299SGESQVSKESMLKAIubiquitination[2]
319KGLTHEDKGAVLIDLacetylation[1]
328AVLIDLTKFNKKLGKacetylation[1]
340LGKAIVQKSDGTTLYubiquitination[2]
361AAMDRYEKYHFDKMIacetylation[1]
474RINNYEFKWERMLSFacetylation[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
 Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis (By similarity). 
Sequence Annotation
 MOTIF 151 162 "HIGH" region.
 MOD_RES 15 15 Phosphoserine.  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 607 AA 
Protein Sequence
MASTANMISQ LKKLSIAEPA VAKDSHPDVN IVDLMRNYIS QELSKISGVD SSLIFPALEW 60
TNTMERGDLL IPIPRLRIKG ANPKDLAVQW AEKFPCGDFL EKVEANGPFI QFFFNPQFLA 120
KLVIPDILTR KEDYGSCKLV ENKKVIIEFS SPNIAKPFHA GHLRSTIIGG FLANLYEKLG 180
WEVIRMNYLG DWGKQFGLLA VGFERYGNEE ALVKDPIHHL FDVYVRINKD IEEEGDSIPL 240
EQSTNGKARE YFKRMEDGDE EALKIWKRFR EFSIEKYIDT YARLNIKYDV YSGESQVSKE 300
SMLKAIDLFK EKGLTHEDKG AVLIDLTKFN KKLGKAIVQK SDGTTLYLTR DVGAAMDRYE 360
KYHFDKMIYV IASQQDLHAA QFFEILKQMG FEWAKDLQHV NFGMVQGMST RKGTVVFLDN 420
ILEETKEKMH EVMKKNENKY AQIEHPEEVA DLVGISAVMI QDMQGKRINN YEFKWERMLS 480
FEGDTGPYLQ YAHSRLRSVE RNASGITQEK WINADFSLLK EPAAKLLIRL LGQYPDVLRN 540
AIKTHEPTTV VTYLFKLTHQ VSSCYDVLWV AGQTEELATA RLALYGAARQ VLYNGMRLLG 600
LTPVERM 607 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0004814; F:arginine-tRNA ligase activity; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006420; P:arginyl-tRNA aminoacylation; IDA:SGD. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR001278; Arg-tRNA-ligase_Ia.
 IPR015945; Arg-tRNA-synth_Ia_core.
 IPR005148; Arg-tRNA-synth_N.
 IPR008909; DALR_anticod-bd.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd. 
Pfam
 PF03485; Arg_tRNA_synt_N
 PF05746; DALR_1
 PF00750; tRNA-synt_1d 
SMART
 SM01016; Arg_tRNA_synt_N
 SM00836; DALR_1 
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR01038; TRNASYNTHARG.