Q5P9M8 (SYV_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Valine--tRNA ligase
EC=6.1.1.9

Alternative name(s):
Valyl-tRNA synthetase
Short name=ValRS

Gene names

Name:	valS
Ordered Locus Names:	AM1170

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	823 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 MF_02005
Catalytic activity	ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP MF_02005
Subunit structure	Monomer By similarity. HAMAP MF_02005
Subcellular location	Cytoplasm By similarity HAMAP MF_02005.
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. HAMAP MF_02005
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: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW valine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 823	823	Valine--tRNA ligase HAMAP MF_02005		PRO_0000224606
Regions
	Motif	52 – 62	11	"HIGH" region HAMAP MF_02005
	Motif	549 – 553	5	"KMSKS" region HAMAP MF_02005
Sites
	Binding site	552	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P9M8 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: C8F916707C698F84	FASTA	823	94,004
	10 20 30 40 50 60 MNVRVRHFMQ SLDSRYQHKT VEEECNAAWD EHKIYKWKGN VAQSFVIDTP PPTVSGVLHM 70 80 90 100 110 120 GHVFSYCHTD FIARYQRMAG KDVFYPIGFD DNGLPTERLV EKIKKLRAVQ LERAEFTKMC 130 140 150 160 170 180 REVSHEFRTK FRNLFRRLGI SYDWALEYHT VSEEVQRLSQ ASFLDLYAKD KLYRKQQPIL 190 200 210 220 230 240 WDTVDCTAIA HAEVEELDLH SHLNTISFHT VGGEKIDIAT TRPELIPACV ALFFNPEDDR 250 260 270 280 290 300 YTHLHGQFAV VPVGGHKVKI LPDDKVRIDK GTGLVMCCTF GDETDVYWWR THNLDTKTIV 310 320 330 340 350 360 SRTGHIVDLA EDTPDAKIPA AQFDGMHVQK ARKAVCDALE GAGLLVSQEP IVHTVKCAER 370 380 390 400 410 420 SGAPIEILLS HQWFVRVMEH KHELLEQVQK VQWHPDSMRK RMEIWIENLN WDWCISRQRY 430 440 450 460 470 480 FGVPFPVWYS KREGEVGKVL LPDVRDLPVD PLRDLPSGYG RDEVEPDVDV MDTWATSSIS 490 500 510 520 530 540 PQFLTKSVGQ VLRNENLEPL FPTDLRAQSH EIIRSWAFYT MLKSYYHNGE IPWQNIMISG 550 560 570 580 590 600 WCLAEDKTKM SKSKGNAMDP ESTLDLYGAD SVRYWAAKSR LGADTVFSEE VLKTGRRLTT 610 620 630 640 650 660 KLWNASKFVA TFFLRDNPPA GTTAAPTDLW ILSKLHKAVA HNTENLKLFE YCAALNRTEE 670 680 690 700 710 720 FFWKDFCDNY LELVKHRAYN HGSAHGHASA VSTLHHTLKT LLLLFAPFLP YVTEAVYGTL 730 740 750 760 770 780 FSGCIHAQEW PNADEIPYNA SLEQHGDALI KIVEEVRKAK THAQVSVKYP VELITIGGLA 790 800 810 820 TDFPESMLED LKHMCCAEQI KLTAPDSTEL EVAVTLAPTV SSN

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: St. Maries.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000030 Genomic DNA. Translation: AAV87002.1.
RefSeq	YP_154257.1. NC_004842.2.
3D structure databases
ProteinModelPortal	Q5P9M8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5P9M8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3171649.
GenomeReviews	Gene locus AM1170 in contig CP000030_GR.
KEGG	ama:AM1170.
PATRIC	20948207. VBIAnaMar46146_1015.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0525.
HOGENOM	HBG577712.
OMA	WILDPDR.
ProtClustDB	PRK13208.
Enzyme and pathway databases
BioCyc	AMAR234826:AM1170-MONOMER.
Family and domain databases
HAMAP	MF_02005. Val_tRNA_synth_type2. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. 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_synthetase. IPR022874. Valyl-tRNA_synthetase_type_2. [Graphical view]
Gene3D	G3DSA:3.90.740.10. G3DSA:3.90.740.10. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KO	K01873.
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. [Graphical view]
PRINTS	PR00986. TRNASYNTHVAL.
SUPFAM	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

SYV_ANAMM

Accession

Primary (citable) accession number: Q5P9M8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program