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Q5ZJ66 (SYEM_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 68. 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:
Probable glutamate--tRNA ligase, mitochondrial

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:EARS2
ORF Names:RCJMB04_20f12
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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_B

Catalytic activity

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

Subcellular location

Mitochondrion matrix By similarity HAMAP-Rule MF_00022_B.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
RNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrial matrix

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: UniProtKB-EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2020Mitochondrion Potential
Chain21 – 502482Probable glutamate--tRNA ligase, mitochondrial HAMAP-Rule MF_00022_B
PRO_0000254563

Regions

Nucleotide binding263 – 2675ATP By similarity
Region19 – 213Glutamate binding By similarity
Region207 – 2115Glutamate binding By similarity
Motif24 – 329"HIGH" region HAMAP-Rule MF_00022_B
Motif263 – 2675"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site291ATP By similarity
Binding site551Glutamate By similarity
Binding site2251Glutamate By similarity
Binding site2281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5ZJ66 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 1E84C3BB0E744570

FASTA50256,954
        10         20         30         40         50         60 
MAGMLREVCG AAASGLRVRF GPSPTGFLHL GGLRTALYNY VFAKQQRGTF VLRVEDTDQG 

        70         80         90        100        110        120 
RVVAGAAESI EDMLHWAGIP PDESPRRGGP FGPYQQSLRL DLYRAASEAL LDRGAAYRCF 

       130        140        150        160        170        180 
CTPQRLELLR KEALRNQQTP RYDNRCRHLT PKEVAEKLAQ GLDWVVRFRL ERGVEPFQDL 

       190        200        210        220        230        240 
VYGWNKHEVA EVEGDPVILK ADGFPTYHLA NVVDDHHMGI SHVLRGTEWL TSTSKHLLLY 

       250        260        270        280        290        300 
KAFGWDPPQF GHLPLLLNKD GSKLSKRQGD IFLERFAQEG YLPEALLDMI TNCGSGFAEK 

       310        320        330        340        350        360 
QMGRTLEELI SQFEIGRITT HSALLDLEKL PEFNRMHLTR HIENEGLRQK LIQELQLLVE 

       370        380        390        400        410        420 
DVYGDQEVDK EVLEKEYVEQ VLLLRKGHIS HLKDLVSDNY SYLWVRPSVS REQLQMISAE 

       430        440        450        460        470        480 
VDEIGKLVLG LMTKPAAVWT IEELNKDLRS LQKQTRETKY SSMMKLLRLA LSGQQHGPSV 

       490        500 
AEMMVTLGPR EVCGRISKVL SS 

« Hide

References

[1]"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis."
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.
Genome Biol. 6:R6.1-R6.9(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: CB.
Tissue: Bursa of Fabricius.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ720568 mRNA. Translation: CAG32227.1.
RefSeqNP_001026638.1. NM_001031467.1.
UniGeneGga.22559.

3D structure databases

ProteinModelPortalQ5ZJ66.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000009866.

Proteomic databases

PaxDbQ5ZJ66.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID427672.
KEGGgga:427672.

Organism-specific databases

CTD124454.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
HOVERGENHBG056174.
InParanoidQ5ZJ66.
KOK01885.
PhylomeDBQ5ZJ66.

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...

Other

NextBio20828882.
PROQ5ZJ66.

Entry information

Entry nameSYEM_CHICK
AccessionPrimary (citable) accession number: Q5ZJ66
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 23, 2004
Last modified: April 16, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries