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Q0APU9 (SYE2_MARMM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:Mmar10_1396
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP]
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis

Protein attributes

Sequence length479 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 – 479479Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367704

Regions

Motif18 – 2811"HIGH" region HAMAP-Rule MF_00022
Motif244 – 2485"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2471ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0APU9 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 09796695EE741EDB

FASTA47953,542
        10         20         30         40         50         60 
MNSQLQNNDK MIRTRFAPSP TGFLHIGGAR TALFNWLLAR RHGGAFLLRI EDTDRARSNP 

        70         80         90        100        110        120 
AAVEAILDGL SWMGLDWDGE PVSQFERADR HVEIAHELLA RGHAFKCYCT AEETQLLRDE 

       130        140        150        160        170        180 
AFAAGRALRS PWRDRDASEA RADTPFTIRF KAPDSDVVIE DAVQGQVRWA AKEFDDLILL 

       190        200        210        220        230        240 
RSDGTPTYNL AVVVDDHDME ITHIVRGDDH LVNAGRQSQI YDAMEWQRPV FAHVPLIHGQ 

       250        260        270        280        290        300 
DGKKLSKRHG ALGAEAYRDM GYLPEGLRNY LLRLGWSHGD QELFSDADAV AAFDLAGLNK 

       310        320        330        340        350        360 
APARMDLDKL NHINGYHLAQ ASDDRLCELV TPFLDSLENR IEDINLTTAR LKAAMPTLKT 

       370        380        390        400        410        420 
RAATLEELAD QSYFLLRQRP IQLEGKAAKP LKDDETRQRL YRLFTHLGDL KAWNEAALSD 

       430        440        450        460        470 
ALKQFAEAES VGFGKIGQPL RAALTGGAPA PDLALVMTFI GRDETLDRIK DQMTPATTE 

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000449 Genomic DNA. Translation: ABI65688.1.
RefSeqYP_756626.1. NC_008347.1.

3D structure databases

ProteinModelPortalQ0APU9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING394221.Mmar10_1396.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI65688; ABI65688; Mmar10_1396.
GeneID4284628.
KEGGmmr:Mmar10_1396.
PATRIC22450884. VBIMarMar77530_1432.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMADRERNNE.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycMMAR394221:GHNB-1423-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_MARMM
AccessionPrimary (citable) accession number: Q0APU9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 58 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