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A7ZFB9 (SYE2_CAMC1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:Ccon26_16340
ORF Names:CCC13826_0242
OrganismCampylobacter concisus (strain 13826) [Complete proteome] [HAMAP]
Taxonomic identifier360104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length459 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 – 459459Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000330957

Regions

Motif8 – 1811"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZFB9 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 34A2FA57DC5B2E7C

FASTA45952,443
        10         20         30         40         50         60 
MIVTRFAPSP TGYLHIGGLR TALYNYLYAR ANNGKFLLRI EDTDLKRNSE EATQAIKEAF 

        70         80         90        100        110        120 
AWCKLDHDGE VTYQSKRFDL YKEYVKKLLD EGKAYKCYMS KEELEELRAS QEARKERPKY 

       130        140        150        160        170        180 
DNRYRDFTGT PPAGIEPVIR IKAPLSGEIV IHDGIKGEVK FKVEDILDDF IIARSDGTPT 

       190        200        210        220        230        240 
YNFTVVIDDA LMGVTDVIRG DDHLSNTPKQ IVLYEALGFK VPKFYHVAMI NGEDGKKLSK 

       250        260        270        280        290        300 
RHGATDVMEY KKMGYLPEAL LNFLVRLGWS HGDDEIFTIE DMLKYFNPND INKSSSTYNA 

       310        320        330        340        350        360 
QKLDWLNSHY IKTLPYERLA HDMLEFGVDF KALVKGELLL NSLRERSKTL IEMANSANAI 

       370        380        390        400        410        420 
INAPKSYDEK AWAKFINENS KEILAKFAQI LDRDLDAKGY EELTNKFLEQ NGLKLKDLAQ 

       430        440        450 
ALRIALTGSS VSPSIFEVLE VVGSNEIKNR IQNLLKEEK 

« Hide

References

[1]"Genome sequence of Campylobacter concisus 13826 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., On S., Nelson K.E.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13826.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000792 Genomic DNA. Translation: EAT98363.1.
RefSeqYP_001467477.1. NC_009802.1.

3D structure databases

ProteinModelPortalA7ZFB9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360104.CCC13826_0242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEAT98363; EAT98363; CCC13826_0242.
GeneID5597704.
KEGGcco:CCC13826_0242.
PATRIC20029525. VBICamCon95352_1688.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAIQECIND.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCCON360104:GHAC-1725-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 nameSYE2_CAMC1
AccessionPrimary (citable) accession number: A7ZFB9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 23, 2007
Last modified: February 19, 2014
This is version 47 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