CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011200
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Valine--tRNA ligase 
Protein Synonyms/Alias
 Valyl-tRNA synthetase; ValRS 
Gene Name
 Vars 
Gene Synonyms/Alias
 Vars2 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
398VVEKKLWKERGLNRHacetylation[1]
432DRIYHQLKKLGSSLDacetylation[1]
645KAVLAALKEQGLFRGacetylation[1]
975FVPSPTSKPEGHESLacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
  
Sequence Annotation
 DOMAIN 89 219 GST C-terminal.
 MOTIF 344 354 "HIGH" region.
 MOTIF 862 866 "KMSKS" region.
 BINDING 865 865 ATP (By similarity).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 645 645 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
 1264 AA 
Protein Sequence
MSILYVSPHP DAFPSLRALI AARYGEAGDG PGWGGPHPRI CLQPPPSSRT PFPPPRLPAL 60
EQGPGGLWVW GAPAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELTPA ACGATLPALG 120
LRGPGQDPQA ALGALGKALN PLEEWLRLHT YLAGDAPTLA DLAAVTALLL PFRYVLDPSA 180
RRIWGNVTRW FNTCVRQPEF RAVLGEVVLY SGARSVTQQP GSEITAPQKT AAQLKKEAKK 240
REKLEKFQQK QKTQQQQPAH GEKKPKPEKK EKRDPGVITY DLPTPPGEKK DVSGTMPDSY 300
SPQYVEAAWY PWWERQGFFK PEYGRPSVSA PNPRGVFMMC IPPPNVTGSL HLGHALTNAI 360
QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWKER GLNRHQLGRE AFLQEVWKWK 420
AEKGDRIYHQ LKKLGSSLDW DRACFTMDPK LSATVTEAFV RLHEEGVIYR STRLVNWSCT 480
LNSAISDIEV DKKELTGRTL LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET 540
MLGDVAVAVH PKDPRYQHLK GKSVVHPFLS RSLPIVFDDF VDMEFGTGAV KITPAHDQND 600
YEVGQRHRLE AISIMDSKGA LVNVPPPFLG LPRFEARKAV LAALKEQGLF RGIKDNPMVV 660
PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI LPEAHQRTWH SWMDNIRDWC 720
ISRQLWWGHR IPAYFITVHD PAVPPGEDPD GRYWVSGRTE AEAREKAARE FGVSPDKISL 780
QQDEDVLDTW FSSGLFPFSI FGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL 840
TEKLPFREVY LHAIVRDAHG RKMSKSLGNV IDPLDVIHGV SLQGLHDQLL NSNLDPSEVE 900
KAKEGQRADF PAGIPECGTD ALRFGLCAYT SQGRDINLDV NRILGYRHFC NKLWNATKFA 960
LRGLGKGFVP SPTSKPEGHE SLVDRWIRSR LAEAVRLSNE GFQAYDFPAV TTAQYSFWLY 1020
ELCDVYLECL KPVLNGVDQV AADCARQTLY TCLDVGLRLL SPFMPFVTEE LFQRLPRRTP 1080
NAPASLCVTP YPEPSECSWK DPEAEAALEL ALSITRAVRS LRADYNLTRT RPDCFLEVAD 1140
EATGALASAV SAYVQTLASA GVVAVLALGA PAPQGCAVAV ASDRCSIHLQ LQGLVDPARE 1200
LGKLQAKRSE AQRQAQRLQE RRAASGYSAK VPLEVQEADE VKLQQTEAEL RKVDEAIALF 1260
QKML 1264 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004832; F:valine-tRNA ligase activity; IDA:RGD.
 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.