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A0RM82 (SYE1_CAMFF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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 1

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 1
Short name=GluRS 1
Gene names
Name:gltX1
Ordered Locus Names:CFF8240_0105
OrganismCampylobacter fetus subsp. fetus (strain 82-40) [Complete proteome] [HAMAP]
Taxonomic identifier360106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length429 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 – 429429Glutamate--tRNA ligase 1 HAMAP-Rule MF_00022
PRO_0000367635

Regions

Motif6 – 1611"HIGH" region HAMAP-Rule MF_00022
Motif235 – 2395"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2381ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0RM82 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: C07E8FD0E9F1103A

FASTA42949,119
        10         20         30         40         50         60 
MYRFAPSPTG DMHIGNLRAA IFNYICSLQD NSGFILRIED TDNARNIDGK DKEIFDILTK 

        70         80         90        100        110        120 
FNIKWDTLYY QSKNLKFHQE FAAKLLAEKK AFLCFCDETT LESKKEAAKT AGKPYRYDGT 

       130        140        150        160        170        180 
CENLSDDDVL SNPRPAAVRL KIKNEPQSFY DAIKGEVKFE PQNIDSFVLL RADKTPTYNF 

       190        200        210        220        230        240 
ACAIDDMLEG VTFVIRGEDH VSNTPKQNLI REALGYTGKI GYAHLPIILN KEGKKMSKRE 

       250        260        270        280        290        300 
NSSSVKWLLN RGYMPEAIAN YLILLGNKTP CEIFTLEESL QWFSIKNISK SPAKFDEEKL 

       310        320        330        340        350        360 
AQINREHIKK ASDERLKELG LSKPHLARFY TQECSLISEI KDKIDQIYSK KDISDEWKQN 

       370        380        390        400        410        420 
ANLIKDAVLN SNIPNNFDEL KNEIIQITNL KGKSLFMPFR LLLTGSEHGP ELKELYALIK 


DDIKEIIAK 

« Hide

References

[1]"Sequence of Campylobacter fetus subsp. fetus 82-40."
Fouts D.E., Nelson K.E.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 82-40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000487 Genomic DNA. Translation: ABK82769.1.
RefSeqYP_891315.1. NC_008599.1.

3D structure databases

ProteinModelPortalA0RM82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360106.CFF8240_0105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK82769; ABK82769; CFF8240_0105.
GeneID4539322.
KEGGcff:CFF8240_0105.
PATRIC20034742. VBICamFet25865_0108.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAIHGPELS.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12410.

Enzyme and pathway databases

BioCycCFET360106:GHTH-105-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 nameSYE1_CAMFF
AccessionPrimary (citable) accession number: A0RM82
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 50 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