Valine--tRNA ligase - Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)

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P47576 (SYV_MYCGE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	MG334

Organism

Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) [Complete proteome] [HAMAP]

Taxonomic identifier

243273 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma ›

Protein attributes

Sequence length	837 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
Catalytic activity	ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val). HAMAP-Rule MF_02004
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. HAMAP-Rule MF_02004 The C-terminal coiled-coil domain is crucial for aminoacylation activity By similarity. HAMAP-Rule MF_02004
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase 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

Molecule processing

Chain

1 – 837

837

Valine--tRNA ligase HAMAP-Rule MF_02004

PRO_0000106230

Regions

Coiled coil

767 – 837

Potential

Motif

46 – 56

"HIGH" region HAMAP-Rule MF_02004

Motif

514 – 518

"KMSKS" region HAMAP-Rule MF_02004

Sites

Binding site

517

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P47576 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 7F2FD1FE95D3D8C5
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FASTA

837

97,464

        10         20         30         40         50         60 
MKDKFSFQKN YDFNLVSDGL YEIWNNAGFF KPKDKNNSFT AILPPPNLTG TLHIGHAFEV 

        70         80         90        100        110        120 
SITDQIMRFK KMQGFSINWI PGFDHAGIAT QTKYEKIALK ENQKYFDADD DKKSEMIMNW 

       130        140        150        160        170        180 
ALNQSEIIKN QLKSLGVCLN WSETKFTLSE QANKIVNNCF KNLYENGFIY QAYTLVNWDT 

       190        200        210        220        230        240 
KLNTAISNIE VINKPVNQHL HYVVYKLAND SKQELIVATT RPETIFADVC LLVNPKDKRY 

       250        260        270        280        290        300 
TNFWNKLVVN PLTGKQIPVV TDSYVDIKFG TGILKCTPAH DFNDYEINTK YKFDFLSCID 

       310        320        330        340        350        360 
SNGILNQNAS KFQGLSVLQA RNKIVKWLEK NKLLVKSIPL TSNVGFSERS GTVVEPMLSK 

       370        380        390        400        410        420 
QWFVDLPKLK DHLYLKKYPD FIPKRFNKQV SNWLNKLKPW CISRQLIWGH KIPVWFENNT 

       430        440        450        460        470        480 
GEIVVGEKPS KNLQNYTRSK DVLDTWFSSS LWPLICLNWE QDDSFHETEL LVTGYDILFF 

       490        500        510        520        530        540 
WVLRMLFNSF FETKKLPFKT VLIHGLVRDE QNRKMSKSLN NGIDPVDLIR NYGADAVRLF 

       550        560        570        580        590        600 
LCSNHTPGDD LIFSEQKIKS AWNFLNKLWN VTKFVIQLEN DQEISYDLDK LSLSETWILA 

       610        620        630        640        650        660 
KLDKVIQKIT KLLDKFQLAL ANQILVKFVW DDFCNTFIEA IKKEPNQLKP QLFYTAKSVL 

       670        680        690        700        710        720 
SNIAILLSIT VPFLSERIYQ QFNNKSVMQA TWPLATKIKI PKLFDLVLAA INDLRNYRKQ 

       730        740        750        760        770        780 
YMLNSQQKLV VILSGKNAVD VKQYFNFSWI ELKIETNKKV SFKYQIVDDT TQRLKSLQKQ 

       790        800        810        820        830 
QAFFESEVKR SQAIVKNKSF LEKAPKEKVK SEFLKLEEYQ KKLTETNQLI AKLTKAH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The minimal gene complement of Mycoplasma genitalium." Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., Nguyen D.T., Utterback T.R., Saudek D.M. Venter J.C. Science 270:397-403(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33530 / G-37 / NCTC 10195.
[2]	"A survey of the Mycoplasma genitalium genome by using random sequencing." Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III J. Bacteriol. 175:7918-7930(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 801-837. Strain: ATCC 33530 / G-37 / NCTC 10195.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L43967 Genomic DNA. Translation: AAC71557.1. U02249 Genomic DNA. Translation: AAD12537.1.
PIR	I64236.
RefSeq	NP_073002.1. NC_000908.2.
3D structure databases
ProteinModelPortal	P47576.
ModBase	Search...
Protein-protein interaction databases
STRING	243273.MG_334.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC71557; AAC71557; MG_334.
GeneID	875510.
KEGG	mge:MG_334.
PATRIC	20010224. VBIMycGen98045_0389.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0525.
KO	K01873.
OMA	CETAISQ.
ProtClustDB	PRK05729.
Enzyme and pathway databases
BioCyc	MGEN243273:GH2R-384-MONOMER.
Family and domain databases
Gene3D	3.40.50.620. 2 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

SYV_MYCGE

Accession

Primary (citable) accession number: P47576

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Mycoplasma genitalium

Mycoplasma genitalium (strain G-37): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents