CPLM-002439

Genbank Nucleotide ID

Protein Synonyms/Alias

Valyl-tRNA synthetase; ValRS

Escherichia coli (strain K12)

Position	Peptide	Type	References
3	*****MEKTYNPQDI	acetylation	[1]
20	PLYEHWEKQGYFKPN	acetylation	[1]
113	GREAFIDKIWEWKAE	acetylation	[1]
118	IDKIWEWKAESGGTI	acetylation	[1]
154	EGLSNAVKEVFVRLY	acetylation	[1]
162	EVFVRLYKEDLIYRG	acetylation	[1]
178	RLVNWDPKLRTAISD	acetylation	[1, 2]
214	GAKTADGKDYLVVAT	acetylation	[1]
243	NPEDPRYKDLIGKYV	acetylation	[1]
248	RYKDLIGKYVILPLV	acetylation	[1]
271	DEHADMEKGTGCVKI	acetylation	[1]
291	FNDYEVGKRHALPMI	acetylation	[1]
317	SAQVFDTKGNESDVY	acetylation	[1]
334	EIPAEFQKLERFAAR	acetylation	[1]
358	LGLLEEIKPHDLTVP	acetylation	[1]
391	VRADVLAKPAVEAVE	acetylation	[1]
554	IRDDEGQKMSKSKGN	acetylation	[1]
557	DEGQKMSKSKGNVID	acetylation	[1]
559	GQKMSKSKGNVIDPL	acetylation	[1]
593	MQPQLADKIRKRTEK	acetylation	[1]
600	KIRKRTEKQFPNGIE	acetylation	[1]
633	RDINWDMKRLEGYRN	acetylation	[1]
644	GYRNFCNKLWNASRF	acetylation	[1]
820	EMNIAPGKPLELLLR	acetylation	[1, 2]
861	TVLPADDKGPVSVTK	acetylation	[1]
898	RLAKEVAKIEGEISR	acetylation	[1]
909	EISRIENKLANEGFV	acetylation	[1, 2]
926	APEAVIAKEREKLEG	acetylation	[1]
930	VIAKEREKLEGYAEA	acetylation	[1]
940	GYAEAKAKLIEQQAV	acetylation	[1]

[1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
[2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]

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.

MOTIF 42 52 "HIGH" region.
MOTIF 554 558 "KMSKS" region.
BINDING 557 557 ATP (By similarity).

Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
GO:0005524; F:ATP binding; IEA:HAMAP.
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.

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.

PF08264; Anticodon_1
PF00133; tRNA-synt_1
PF10458; Val_tRNA-synt_C

PS00178; AA_TRNA_LIGASE_I

PR00986; TRNASYNTHVAL.