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Q4R4F1 (SYEM_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:
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:QtsA-10185
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length506 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
   PTMAcetylation
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 – 4141Mitochondrion Potential
Chain42 – 506465Probable glutamate--tRNA ligase, mitochondrial HAMAP-Rule MF_00022_B
PRO_0000254561

Regions

Nucleotide binding284 – 2885ATP By similarity
Region40 – 423Glutamate binding By similarity
Region228 – 2325Glutamate binding By similarity
Motif45 – 539"HIGH" region HAMAP-Rule MF_00022_B
Motif284 – 2885"KMSKS" region HAMAP-Rule MF_00022_B

Sites

Binding site501ATP By similarity
Binding site761Glutamate By similarity
Binding site2461Glutamate By similarity
Binding site2491ATP By similarity

Amino acid modifications

Modified residue2561N6-succinyllysine By similarity
Modified residue4861N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4R4F1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 314400085FF645F6

FASTA50656,865
        10         20         30         40         50         60 
MAALLRRLLQ RGRPLAASGR RVGRREARLG TGPGVAVRVR FAPSPTGFLH LGGLRTALYN 

        70         80         90        100        110        120 
YIFAKKYQGS FILRLEDTDQ TRFVPGAAEN IENMLEWAGI PPDESPRRGG PAGPYQQSQR 

       130        140        150        160        170        180 
LELYAQATEA LLKTGAAYPC FCSPQRLELL KKEALRNHQM PRYDNRCRNM SQEQVAQKLA 

       190        200        210        220        230        240 
KDPKPAIRFR LEQAAPAFED LVYGWNRHDV ASVEGDPVIM KSDGFPTYHL ACVVDDHHMG 

       250        260        270        280        290        300 
ISHVLRGSEW LISTAKHLLL YQALGWHPPH FAHLPLLLNR DGSKLSKRQG DIFLEHFAAE 

       310        320        330        340        350        360 
GFLPDSLLDI ITNCGSGFAE NQMGRTLPEL ITQFNLTRVT CHSALLDLEK LPEFNRLHLQ 

       370        380        390        400        410        420 
RLVNNESQRC QLVEKLQALV EEAFGSQLQN RDVLNPIYME RILLLRQGHI CRLQDLVSPV 

       430        440        450        460        470        480 
YSYLWTRPSV GRAQLDAISE EVDVIAKRVL GLLERSGMSL TQDMLSGELK KLSEGLEGTK 

       490        500 
HSNVMKLLRV ALSGQQALSS MFKVQG 

« Hide

References

[1]"DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."
International consortium for macaque cDNA sequencing and analysis
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB178963 mRNA. Translation: BAE02014.1.
RefSeqNP_001270434.1. NM_001283505.1.
UniGeneMfa.3351.

3D structure databases

ProteinModelPortalQ4R4F1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101926460.
KEGGmcf:101926460.

Organism-specific databases

CTD124454.

Phylogenomic databases

HOVERGENHBG056174.
KOK01885.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
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_MACFA
AccessionPrimary (citable) accession number: Q4R4F1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: July 19, 2005
Last modified: April 16, 2014
This is version 47 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