CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013886
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Valine--tRNA ligase 
Protein Synonyms/Alias
 Valyl-tRNA synthetase; ValRS 
Gene Name
 valS 
Gene Synonyms/Alias
 TTHA1169 
Created Date
 July 27, 2013 
Organism
 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) 
NCBI Taxa ID
 300852 
Lysine Modification
Position
Peptide
Type
References
118LERVWQWKEESGGTIacetylation[1]
Reference
 [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus.
 Okanishi H, Kim K, Masui R, Kuramitsu S.
 J Proteome Res. 2013 Aug 1;. [PMID: 23901841] 
Functional Description
 Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a "posttransfer" editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner (By similarity). 
Sequence Annotation
 MOTIF 44 53 "HIGH" region.
 MOTIF 528 532 "KMSKS" region.
 METAL 176 176 Zinc 1 (By similarity).
 METAL 179 179 Zinc 1 (By similarity).
 METAL 344 344 Zinc 1 (By similarity).
 METAL 347 347 Zinc 1 (By similarity).
 METAL 417 417 Zinc 2 (By similarity).
 METAL 420 420 Zinc 2 (By similarity).
 METAL 438 438 Zinc 2 (By similarity).
 METAL 441 441 Zinc 2 (By similarity).
 BINDING 531 531 ATP (By similarity).  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 862 AA 
Protein Sequence
MDLPKAYDPK SVEPKWAEKW AKNPFVANPK SGKPPFVIFM PPPNVTGSLH MGHALDNSLQ 60
DALIRYKRMR GFEAVWLPGT DHAGIATQVV VERLLLKEGK TRHDLGREKF LERVWQWKEE 120
SGGTILKQLK RLGASADWSR EAFTMDEKRS RAVRYAFSRY YHEGLAYRAP RLVNWCPRCE 180
TTLSDLEVET EPTPGKLYTL RYEVEGGGFI EIATVRPETV FADQAIAVHP EDERYRHLLG 240
KRARIPLTEV WIPILADPAV EKDFGTGALK VTPAHDPLDY EIGERHGLKP VSVINLEGRM 300
EGERVPEALR GLDRFEARRK AVELFREAGH LVKEEDYTIA LATCSRCGTP IEYAIFPQWW 360
LRMRPLAEEV LKGLRRGDIA FVPERWKKVN MDWLENVKDW NISRQLWWGH QIPAWYCEDC 420
QAVNVPRPER YLEDPTSCEA CGSPRLKRDE DVFDTWFSSA LWPLSTLGWP EETEDLKAFY 480
PGDVLVTGYD ILFLWVSRME VSGYHFMGER PFKTVLLHGL VLDEKGQKMS KSKGNVIDPL 540
EMVERYGADA LRFALIYLAT GGQDIRLDLR WLEMARNFAN KLYNAARFVL LSREGFQAKE 600
DTPTLADRFM RSRLSRGVEE ITALYEALDL AQAAREVYEL VWSEFCDWYL EAAKPALKAG 660
NAHTLRTLEE VLAVLLKLLH PMMPFLTSEL YQALTGKEEL ALEAWPEPGG RDEEAERAFE 720
ALKQAVTAVR ALKAEAGLPP AQEVRVYLEG ETAPVEENLE VFRFLSRADL LPERPAKALV 780
KAMPRVTARM PLEGLLDVEE WRRRQEKRLK ELLALAERSQ RKLASPGFRE KAPKEVVEAE 840
EARLKENLEQ AERIREALSQ IG 862 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004832; F:valine-tRNA ligase activity; IEA:HAMAP.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC.
 GO:0006438; P:valyl-tRNA aminoacylation; IEA:HAMAP. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002300; aa-tRNA-synth_Ia.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR010978; tRNA-bd_arm.
 IPR009080; tRNAsynth_1a_anticodon-bd.
 IPR013155; V/L/I-tRNA-synth_anticodon-bd.
 IPR019499; Val-tRNA_synth_tRNA-bd.
 IPR009008; Val/Leu/Ile-tRNA-synth_edit.
 IPR002303; Valyl-tRNA_ligase. 
Pfam
 PF08264; Anticodon_1
 PF00133; tRNA-synt_1
 PF10458; Val_tRNA-synt_C 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00986; TRNASYNTHVAL.