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Q2NIP6 (SYE_AYWBP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:AYWB_580
OrganismAster yellows witches'-broom phytoplasma (strain AYWB) [Complete proteome] [HAMAP]
Taxonomic identifier322098 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeCandidatus PhytoplasmaCandidatus Phytoplasma asteris

Protein attributes

Sequence length449 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm HAMAP MF_00022_B.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000237339

Regions

Motif10 – 2011"HIGH" region HAMAP MF_00022_B
Motif214 – 2185"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2171ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2NIP6 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 9A3C1F148545480A

FASTA44952,265
        10         20         30         40         50         60 
MKKIKVRYAP SPTGFLHIGN ARTALFNYLF AKHNQGEFII RIEDTDFSRN VKGGEASQLK 

        70         80         90        100        110        120 
NLRWLGIDWS EGPDIQGPFG PYRQSERLAI YQKYAQKLLD QGLAYKEFQE NTTTFAIRFR 

       130        140        150        160        170        180 
VPTNQTFSFD DLIRGKLTFQ SQEIEDWVII KSNGYPSYNF AVVIDDHLMQ ISHIFRGEEH 

       190        200        210        220        230        240 
ITNTPKQIMI YQTFQWHLPQ FAHMTLILND NKKKLSKRDA NIMQFIEQYE KLGYLPQALF 

       250        260        270        280        290        300 
NFLSLLGFSP LSQTEILSPQ ELINLFDVAR LNKAPAMFDT VKLDYLNNQH LRKLTPEVIA 

       310        320        330        340        350        360 
SFIVQKKYLT LTTAPTNDKE WMTKFVSLFQ DRMNYIQQIA DFYQLFFQTK PSLSQEATIF 

       370        380        390        400        410        420 
LQTNPQTTLI LKTFYNVFDV IVFKKDVIFN AIKQVANQND FSKKTLFMAL RIGTTCKMHG 

       430        440 
PSIALLLELL GKKQVLKNLS YVLKQAQKF 

« Hide

References

[1]"Living with genome instability: the adaptation of phytoplasmas to diverse environments of their insect and plant hosts."
Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.
J. Bacteriol. 188:3682-3696(2006) [PubMed: 16672622] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AYWB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000061 Genomic DNA. Translation: ABC65697.1.
RefSeqYP_456776.1. NC_007716.1.

3D structure databases

ProteinModelPortalQ2NIP6.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2NIP6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3866073.
GenomeReviewsGene locus AYWB_580 in contig CP000061_GR.
KEGGayw:AYWB_580.
PATRIC21005226. VBIAstYel136969_0641.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAAHMTLIL.
PhylomeDBQ2NIP6.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycAYEL322098:AYWB_580-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_AYWBP
AccessionPrimary (citable) accession number: Q2NIP6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: February 7, 2006
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families