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Q66JG3 (SYEM_XENTR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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
OrganismXenopus tropicalis (Western clawed frog) (Silurana tropicalis) [Reference proteome]
Taxonomic identifier8364 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana

Protein attributes

Sequence length516 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 – 3939Mitochondrion Potential
Chain40 – 516477Probable glutamate--tRNA ligase, mitochondrial HAMAP-Rule MF_00022_B
PRO_0000254565

Regions

Nucleotide binding282 – 2865ATP By similarity
Region38 – 403Glutamate binding By similarity
Region226 – 2305Glutamate binding By similarity
Motif43 – 519"HIGH" region HAMAP-Rule MF_00022_B
Motif282 – 2865"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site481ATP By similarity
Binding site741Glutamate By similarity
Binding site2441Glutamate By similarity
Binding site2471ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66JG3 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: EB54FFDEBE953600

FASTA51658,607
        10         20         30         40         50         60 
MRPAFIRGKW LSRTLELATG LGRRTCSSRE SGREVRVRFA PSPTGFLHLG GLRTALYNYL 

        70         80         90        100        110        120 
FAKKHGGAFI LRLEDTDRSR LVPGAAESIE DMLEWAGIPP DESPRHGGPC GPYEQSKRLD 

       130        140        150        160        170        180 
LYHVAAQALL DSGAAYRCFC TPQRLELLKR EAMRNRQTPR YDNRCRHLTP KQVEEKLSRN 

       190        200        210        220        230        240 
SPFVIRFFLQ EGAQPFQDLV YGWTQHDVAS VEGDPVILKG DGFPTYHLAN VVDDHHMCVS 

       250        260        270        280        290        300 
HVLRGAEWLI STAKHLLLYQ ALGWQPPQFA HLPLLLNKDG SKLSKRQGDI FIQHYVHSGY 

       310        320        330        340        350        360 
LSDALLDLIT NCGSGFTENQ MGRTVDTLIQ QYELGKTSTH SALLDLDKLP EFNRIHLTRW 

       370        380        390        400        410        420 
IEGTETRVQL VGQLQVLLKD TYKDLELDEK HIERILLLRK GHLCRLTDLL SPEYSYLWVR 

       430        440        450        460        470        480 
PSVTREQLQC LTSEASKVKN LVVRLLQEND SGFTLETLNG ELRKQLKQVK DTKYSSAMKL 

       490        500        510 
LRVALSGQEH GPSVAEMLLS LGRQESIVRL QNALPD 

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC080925 mRNA. Translation: AAH80925.1.
RefSeqNP_001008042.1. NM_001008041.1.
UniGeneStr.26785.

3D structure databases

ProteinModelPortalQ66JG3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING8364.ENSXETP00000027183.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID493404.
KEGGxtr:493404.

Organism-specific databases

CTD124454.
XenbaseXB-GENE-970848. ears2.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
HOVERGENHBG056174.
InParanoidQ66JG3.
KOK01885.

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 nameSYEM_XENTR
AccessionPrimary (citable) accession number: Q66JG3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 69 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