CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013047
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable arginine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Arginyl-tRNA synthetase; ArgRS 
Gene Name
 Rars2 
Gene Synonyms/Alias
 Rarsl 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
111QVTEDGCKYGLKSELacetylation[1]
557GARLHLFKAVRSVLAacetylation[1, 2]
568SVLANGMKLLGITPVacetylation[1, 2, 3]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [3] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753] 
Functional Description
  
Sequence Annotation
 MOTIF 133 144 "HIGH" region.  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 578 AA 
Protein Sequence
MACGFRRSIA CQLSRVLALP PESLIKSISA VPVSKKEEVA DFQLSVDSLL EDNNHKSQVD 60
TQDQARRLAE KLKCDTVVTA ISAGPRTLNF KINRELLTKA VLQQVTEDGC KYGLKSELFS 120
DLPKKRIVVE FSSPNIAKKF HVGHLRSTII GNFIANLKEA LGHQVTRINY IGDWGMQFGL 180
LGTGFQLFGY EEKLQTNPLQ HLFDVYVQVN KEATDDKNVT KLAHEFFHRL EMGDTQALSL 240
WQRFRDLSIE EYTQIYKRLG IYFDEYSGES FYREKSQDVL KLLDSKGLLQ KTAEGNVVVD 300
LSGTGDLSSV CTVMRSDGTS LYATRDLAAA IHRMDKYNFD TMIYVADKGQ RRHFQQVFQM 360
LKIMGYDWAE RCQHVPFGIV KGMKTRRGGV TFLEDVLNEV QSRMLQNMAS IKTTKQLENP 420
QETAERVGLA AVIIQDFRGT LLSDYQFSWD RVFQSRGDTG VFLQYTHARL CSLEETFGCG 480
YLNDSNVACL QEPQSVSILQ HLLRFDEVLY LSSQDLQPKH IVSYLLTLSH LAAVAHKTLQ 540
VKDSPPDVAG ARLHLFKAVR SVLANGMKLL GITPVCRM 578 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0004814; F:arginine-tRNA ligase activity; IEA:EC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro. 
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
 PF05746; DALR_1
 PF00750; tRNA-synt_1d 
SMART
 SM00836; DALR_1 
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR01038; TRNASYNTHARG.