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A5GUL0 (SYE_SYNR3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:SynRCC307_1666
OrganismSynechococcus sp. (strain RCC307) [Complete proteome] [HAMAP]
Taxonomic identifier316278 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length475 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

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
Nucleotide-binding
   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

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001980

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif247 – 2515"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2501ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GUL0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: EB5C3AD058364FEA

FASTA47552,732
        10         20         30         40         50         60 
MVRVRLAPSP TGTLHIGTAR TAVFNWLYAR RHGGEFVLRI EDTDKERSKS EYTSNILDGL 

        70         80         90        100        110        120 
KWLGIDWDAE PVIQSERVEQ HRQAIQQLLD AGLAYRCYAS EEELNAMREA QMANKKAPRY 

       130        140        150        160        170        180 
DNRHRNLSHE QEADYQAEGR QATVRFRIDD SRNIQWNDLV RGAMSWSGAD LGGDMVIARR 

       190        200        210        220        230        240 
APADQIGDPL YNLVVVVDDA AMAITHVIRG EDHIANTAKQ LLLYEALGLP LPEFAHTPLI 

       250        260        270        280        290        300 
LNQEGRKLSK RDGVTSVSDF RGMGYTASAL ANYMTLLGWS PPEGMGERFS LAEAAKVFDF 

       310        320        330        340        350        360 
QRVNKAGARF DWDKLNWLNG QVLHELGAAE LNRKLTPLWQ EAGFETSGRS QAWLEQLCEL 

       370        380        390        400        410        420 
LGPSLTLLAD GVEQARPFFE TPSLKEDAQQ QLQQPGAKEA LKALLSSLSD EPLQAEQAKA 

       430        440        450        460        470 
LISDACKAAD VKKGVLMKSL RGALMGQLQG PDLMESWLLL NAAGQDRGRI SSALG 

« Hide

References

[1]Genoscope
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCC307.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT978603 Genomic DNA. Translation: CAK28569.1.
RefSeqYP_001227922.1. NC_009482.1.

3D structure databases

ProteinModelPortalA5GUL0.
SMRA5GUL0. Positions 2-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316278.SynRCC307_1666.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK28569; CAK28569; SynRCC307_1666.
GeneID5158060.
KEGGsyr:SynRCC307_1666.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

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_SYNR3
AccessionPrimary (citable) accession number: A5GUL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 49 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