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Q0RF57 (SYE_FRAAA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:FRAAL5260
OrganismFrankia alni (strain ACN14a) [Complete proteome] [HAMAP]
Taxonomic identifier326424 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia

Protein attributes

Sequence length470 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-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001899

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1031Zinc By similarity
Metal binding1051Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0RF57 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: A3B2118E7A675150

FASTA47051,235
        10         20         30         40         50         60 
MGSGRVRVRF APSPTGIFHV GGARSALFNW LVALRAGGDF VLRVEDTDAS RNRPEWTDGI 

        70         80         90        100        110        120 
ISALDWLGIS PGRYEGPVLQ SSRADRHRAA AVRLREAGLA YFCDCTREAL AERTGNAQHG 

       130        140        150        160        170        180 
YDGFCRDRGL EPGPGRALRF RTPDDGVTTV HDLIRGTPEF PNDTIEDFVI ARADGSAVFL 

       190        200        210        220        230        240 
LANVVDDLEM GITHVIRGEE HLSNTPKQQL LWAALGAAEP PVWAHVPVIV NEKRQKLSKR 

       250        260        270        280        290        300 
RDKVALESYR DEGYLPGAMK NYLMLLGWAP SGDDEIVPWE TIESTFDLAD VKPSPAFFDE 

       310        320        330        340        350        360 
KKLRAFNGEY IRALSVEEFI AAVEPWLAPP AAPWAADAFD AGTFAAVAGL AQSRVSVLAE 

       370        380        390        400        410        420 
IVPMVDFLFL PAAPVDDAAW AKAMKGPAAQ LLADVHDVFG KIEWDAETLK ATLAELGERH 

       430        440        450        460        470 
GLKLAKAQAP VRVAVTGRTV GLPLFESLEV FGREATRRRI AAARDRLAAG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT573213 Genomic DNA. Translation: CAJ63893.1.
RefSeqYP_715425.1. NC_008278.1.

3D structure databases

ProteinModelPortalQ0RF57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING326424.FRAAL5260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4233601.
KEGGfal:FRAAL5260.
PATRIC21919740. VBIFraAln347_4821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAKRDANIM.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycFALN326424:GJ82-5177-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_FRAAA
AccessionPrimary (citable) accession number: Q0RF57
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries