C8U0M1 (C8U0M1_ECO10) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Valine--tRNA ligase HAMAP-Rule MF_02004
EC=6.1.1.9 HAMAP-Rule MF_02004

Alternative name(s):
Valyl-tRNA synthetase HAMAP-Rule MF_02004

Gene names

Name:	valS HAMAP-Rule MF_02004 EMBL BAI33733.1
Ordered Locus Names:	ECO103_5054 EMBL BAI33733.1

Organism

Escherichia coli O103:H2 (strain 12009 / EHEC) [Complete proteome] [HAMAP] EMBL BAI33733.1

Taxonomic identifier

585395 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli › Escherichia coli O103:H2

Protein attributes

Sequence length	951 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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. HAMAP-Rule MF_02004 SAAS SAAS019499
Catalytic activity	ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP-Rule MF_02004 SAAS SAAS019499
Subunit structure	Monomer By similarity. HAMAP-Rule MF_02004 SAAS SAAS019499
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_02004 SAAS SAAS019499.
Domain	The C-terminal coiled-coil domain is crucial for aminoacylation activity By similarity. HAMAP-Rule MF_02004 ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site By similarity. HAMAP-Rule MF_02004
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. HAMAP-Rule MF_02004

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP-Rule MF_02004 SAAS SAAS019499
Cellular component	Cytoplasm HAMAP-Rule MF_02004 SAAS SAAS019499
Domain	Coiled coil HAMAP-Rule MF_02004 SAAS SAAS019499
Ligand	ATP-binding HAMAP-Rule MF_02004 SAAS SAAS019499 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase HAMAP-Rule MF_02004 SAAS SAAS019499 EMBL BAI33733.1 Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	regulation of translational fidelity Inferred from electronic annotation. Source: GOC valyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activity Inferred from electronic annotation. Source: InterPro valine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Coiled coil	880 – 944	65	By similarity HAMAP-Rule MF_02004
	Motif	42 – 52	11	"HIGH" region By similarity HAMAP-Rule MF_02004
	Motif	554 – 558	5	"KMSKS" region By similarity HAMAP-Rule MF_02004
Sites
	Binding site	557	1	ATP By similarity HAMAP-Rule MF_02004

Sequences

	Sequence		Length	Mass (Da)
	C8U0M1 [UniParc]. Last modified November 3, 2009. Version 1. Checksum: A276D542D6A1C82B	FASTA	951	108,164
	10 20 30 40 50 60 MEKTYNPQDI EQPLYEHWEK QGYFKPNGDE SQESFCIMIP PPNVTGSLHM GHAFQQTIMD 70 80 90 100 110 120 TMIRYQRMQG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TRHDYGREAF IDKIWEWKAE 130 140 150 160 170 180 SGGTITRQMR RLGNSVDWER ERFTMDEGLS NAVKEVFVRL YKEDLIYRGK RLVNWDPKLR 190 200 210 220 230 240 TAISDLEVEN RESKGSMWHI RYPLADGAKT ADGKDYLVVA TTRPETLLGD TGVAVNPEDP 250 260 270 280 290 300 RYKDLIGKYV ILPLVNRRIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRHALPMINI 310 320 330 340 350 360 LTFDGDIRES AQVFDTKGNE SDVYSSEIPA EFQKLERFAA RKAVVAAVDA LGLLEEIKPH 370 380 390 400 410 420 DLTVPYGDRG GVVIEPMLTD QWYVRADVLA KPAVEAVENG DIQFVPKQYE NMYFSWMRDI 430 440 450 460 470 480 QDWCISRQLW WGHRIPAWYD EAGNVYVGRN EDEVRKENNL GADVALRQDE DVLDTWFSSA 490 500 510 520 530 540 LWTFSTLGWP ENTDALRQFH PTSVMVSGFD IIFFWIARMI MMTMHFIKDE NGKPQVPFHT 550 560 570 580 590 600 VYMTGLIRDD EGQKMSKSKG NVIDPLDMVD GISLPELLEK RTGNMMQPQL ADKIRKRTEK 610 620 630 640 650 660 QFPNGIEPHG TDALRFTLAA LASTGRDINW DMKRLEGYRN FCNKLWNASR FVLMNTEGQD 670 680 690 700 710 720 CGFNGGEMTL SLADRWILAE FNQTIKAYRE ALDSFRFDIA AGILYEFTWN QFCDWYLELT 730 740 750 760 770 780 KPVMNGGTEA ELRGTRHTLV TVLEGLLRLA HPIIPFITET IWQRVKVLCG ITADTIMLQP 790 800 810 820 830 840 FPQYDASQVD EAALADTEWL KQAIVAVRNI RAEMNIAPGK PLELLLRGCS ADAERRVNEN 850 860 870 880 890 900 RGFLQTLARL ESITVLPADD KGPVSVTKII DGAELLIPMA GLINKEDELA RLAKEVAKIE 910 920 930 940 950 GEISRIENKL ANEGFVARAP EAVIAKEREK LEGYAEAKAK LIEQQAVIAA L

References

[1]

"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli." Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T. Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12009 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP010958 Genomic DNA. Translation: BAI33733.1.
RefSeq	YP_003224867.1. NC_013353.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	585395.ECO103_5054.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAI33733; BAI33733; ECO103_5054.
GeneID	8478259.
KEGG	eoh:ECO103_5054.
PATRIC	32102397. VBIEscCol146794_5312.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0525.
HOGENOM	HOG000020094.
KO	K01873.
OMA	IMDALIR.
ProtClustDB	PRK05729.
Enzyme and pathway databases
BioCyc	ECOL585395:GJA9-5242-MONOMER.
Family and domain databases
Gene3D	1.10.287.380. 1 hit. 3.40.50.620. 3 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02004. Val_tRNA_synth_type1.
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. [Graphical view]
PANTHER	PTHR11946:SF5. PTHR11946:SF5. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. PF10458. Val_tRNA-synt_C. 1 hit. [Graphical view]
PRINTS	PR00986. TRNASYNTHVAL.
SUPFAM	SSF46589. tRNA_binding_arm. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit. SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMs	TIGR00422. valS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C8U0M1_ECO10

Accession

Primary (citable) accession number: C8U0M1

Entry history

Integrated into UniProtKB/TrEMBL:	November 3, 2009
Last sequence update:	November 3, 2009
Last modified:	May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)