CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024111
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Valine--tRNA ligase 
Protein Synonyms/Alias
 Protein G7a; Valyl-tRNA synthetase; ValRS 
Gene Name
 Vars 
Gene Synonyms/Alias
 Bat6; G7a; Vars2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1241VQEADEAKLQQTEAEacetylation[1]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
  
Sequence Annotation
 DOMAIN 89 219 GST C-terminal.
 MOTIF 343 353 "HIGH" region.
 MOTIF 861 865 "KMSKS" region.
 BINDING 864 864 ATP (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 644 644 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1263 AA 
Protein Sequence
MSILYVSPHP DAFPSLRALI AARYGEAGDG PGWGGPHPRI CLQPPPSSRT PFPPPRLPAL 60
EQGPGGLWVW GAPAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELIPA ACGATLPALG 120
LRGPGQDPQA ALGALGKALN PLEDWLRLHT YLAGDAPTLA DLAAVTALLL PFRYVLDPSA 180
RRIWGNVTRW FNTCVRQPEF RAVLGEVALY SGARSVTQQP GSEVIAPQKT PAQLKKEAKK 240
REKLEKFQQK QKTQQQPPHG EKKPKPEKKE KRDPGVITYD LPTPPGEKKD VSGAMPDSYS 300
PQYVEAAWYP WWERQGFFKP EYGRPSVSAP NPRGVFMMCI PPPNVTGSLH LGHALTNAIQ 360
DSLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLWKERG LNRHQLGREA FLEEVWKWKA 420
EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SATVTEAFVR LHEEGVIYRS TRLVNWSCTL 480
NSAISDIEVD KKELTGRTLL PVPGYKEKVE FGVLVSFAYK VQGSDSDEEV VVATTRIETM 540
LGDVAVAVHP KDPRYQHLKG KCVVHPFLSR SLPIVFDDFV DMEFGTGAVK ITPAHDQNDY 600
EVGQRHRLEA ISIMDSKGAL INVPPPFLGL PRFEARKAVL AALKERGLFR GVKDNPMVVP 660
LCNRSKDVVE PLLRPQWYVR CGEMAQAASA AVTRGDLRIL PEAHQRTWHS WMDNIRDWCI 720
SRQLWWGHRI PAYFITVHDP AVPPGEDPDG RYWVSGRTEA EAREKAAREF GVSPDKISLQ 780
QDEDVLDTWF SSGLFPFSIF GWPNQSEDLS VFYPGTLLET GHDILFFWVA RMVMLGLKLT 840
GKLPFREVYL HAIVRDAHGR KMSKSLGNVI DPLDVIHGVS LQGLYDQLLN SNLDPSEVEK 900
AKEGQKADFP AGIPECGTDA LRFGLCAYTS QGRDINLDVN RILGYRHFCN KLWNATKFAL 960
RGLGKGFVPS ATSKPEGHES LVDRWIRSRL TEAVRLSNEG FQAYDFPAIT TAQYSFWLYE 1020
LCDVYLECLK PVLNGVDQVA AECARQTLYT CLDVGLRLLS PFMPFVTEEL FQRLPRRTPK 1080
APASLCVTPY PEPSECSWKD PEAEAALELA LSITRAVRSL RADYNLTRTR PDCFLEVADE 1140
ATGALASAVS GYVQALASAG VVAVLALGAP APQGCAVAVA SDRCSIHLQL QGLVDPAREL 1200
GKLQAKRSEA QRQAQRLQER RAASSYSAKV PLEVQEADEA KLQQTEAELR KVDEAIALFQ 1260
KML 1263 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004832; F:valine-tRNA ligase activity; IEA:EC.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC.
 GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002300; aa-tRNA-synth_Ia.
 IPR010987; Glutathione-S-Trfase_C-like.
 IPR004045; Glutathione_S-Trfase_N.
 IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
 IPR004046; GST_C.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd.
 IPR013155; V/L/I-tRNA-synth_anticodon-bd.
 IPR009008; Val/Leu/Ile-tRNA-synth_edit.
 IPR002303; Valyl-tRNA_ligase. 
Pfam
 PF08264; Anticodon_1
 PF00043; GST_C
 PF02798; GST_N
 PF00133; tRNA-synt_1 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I
 PS50405; GST_CTER 
PRINTS
 PR00986; TRNASYNTHVAL.