Reviewed, UniProtKB/Swiss-Prot Q3YT16 (SYV_EHRCJ)

Names and origin

Protein names

Recommended name:
    Valyl-tRNA synthetase
    EC=6.1.1.9
Alternative name(s):
    Valine--tRNA ligase
      Short name=ValRS

Gene names

Name:	valS
Ordered Locus Names:	Ecaj_0088

Organism

Ehrlichia canis (strain Jake) [Complete proteome] [HAMAP]

Taxonomic identifier

269484 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia

Protein attributes

Sequence length	802 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP MF_02005
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	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.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	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 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
Molecule processing
	Chain	1 – 802	802	Valyl-tRNA synthetase HAMAP MF_02005		PRO_0000224608
Regions
	Motif	45 – 55	11	"HIGH" region HAMAP MF_02005
	Motif	524 – 528	5	"KMSKS" region HAMAP MF_02005
Sites
	Binding site	527	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3YT16-1 [UniParc]. Last modified September 27, 2005. Version 1. Checksum: 4B1A79DFF931A674	FASTA	802	93,049
	10 20 30 40 50 60 MQSIFNNKYQ FKNIETKYNT LWDTTKLYKW KNSGTNQFVI DTPPPTISGQ LHIGHVFSYC 70 80 90 100 110 120 HTDFIARYQR MLGKDVFYPI GFDDNGLPTE RLVEKTKKIR ATDISRKEFK TICTQVSHEF 130 140 150 160 170 180 RIQFKQLFQS IGISYDWDLE YHTISKDIQK ISQTSFINLY NKGKLYRKLQ PIFWDCIDKT 190 200 210 220 230 240 AIARAEVEEN ELSSFMNTIA FSTEAGKAIN IATTRPELMP ACVAVFFNPS DIRYQDLLGQ 250 260 270 280 290 300 NAIVPIFGNK VKILSDDQVK IDKGTGLVMC CTFGDEMDVY WWNKHNLDTK IIISKSGTID 310 320 330 340 350 360 HLNTLQGQDV CKQLHGLSIT EARALIIEIL ERNNLLIQKQ EITHNVKCAE RSGAPIEILL 370 380 390 400 410 420 SHQWFIKVVD IKHELLKQVQ KINWHPQSMR KQIEIWIEGL NWDWCISRQR YFGVPFPVWY 430 440 450 460 470 480 SKDGKIILPD INKLPIDPTN DLPEGYQDTE IEVETDVMDT WATSSLSTQF HNISATPADL 490 500 510 520 530 540 RAQSHEIIRS WAFYTILQAY YHNNDIPWKN IMISGWCLAE DKTKMSKSKG NVLTPNKLLD 550 560 570 580 590 600 EYGADVVRYW TANSKLGADT TFSNEILKLG KRFTTKLWNA SKFVSMFIDQ YSEPDLQYIT 610 620 630 640 650 660 ETMDKWILSK LYKVIVKATE SFNSFEYCIA LDCIESFFWK DFCDNYLELS KKRAYGELIS 670 680 690 700 710 720 KQEHLSAVNT LSFVLRELLK MLAPFMPYVT EEIYRTLYSS NNSIHSHNTW PAADVNLYNE 730 740 750 760 770 780 SDELLGETFI EILNQVRKVK ASAQLSVKYK INKLIINKHF PVSLENDLKA VCNADCIVYD 790 800 NRQNDNKEQL LVSVEFENVQ IT

References

[1]

"The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies." Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P., Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M., Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C. J. Bacteriol. 188:4015-4023(2006) [PubMed: 16707693] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000107 Genomic DNA. Translation: AAZ68139.1.
RefSeq	YP_302737.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3618413.
GenomeReviews	Gene locus Ecaj_0088 in contig CP000107_GR.
KEGG	ecn:Ecaj_0088.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3YT16.
OMA	Q3YT16. SGWILDP.
Enzyme and pathway databases
BioCyc	ECAN269484:ECAJ_0088-MON.
Family and domain databases
HAMAP	MF_02005. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR014729. Rossmann-like_a/b/a_fold. IPR013155. V/L/I-tRNA-synth_anticodon-bd. IPR002303. Val-tRNA_synth_Ia. IPR019754. Val-tRNA_synth_Ia_N. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR11946:SF5. tRNA-synt_val. 1 hit.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. [Graphical view]
PRINTS	PR00986. TRNASYNTHVAL.
TIGRFAMs	TIGR00422. valS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYV_EHRCJ

Accession

Primary (citable) accession number: Q3YT16

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	September 27, 2005
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)