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Q5PAG8 (SYE2_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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:AM775
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length466 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.

Sequence caution

The sequence AAV86712.1 differs from that shown. Reason: Erroneous initiation.

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 – 466466Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000119493

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif236 – 2405"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2391ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PAG8 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 779D34443F542391

FASTA46652,783
        10         20         30         40         50         60 
MRVITRFAPS PTGSLHLGGA RTALFNWLFA RRHGGQFLLR MEDTDQERSS ETVAQSIIED 

        70         80         90        100        110        120 
MAWLGLHHDQ DVVIQSARRE RHTQVAEELL ARGKAYYCYC SEDDIAAEKL RHENEGKHYR 

       130        140        150        160        170        180 
HHCPSRDANH AQSGTAGVLR LKSPENREIK FTDGVYGEIS VSSEQIDDMV ILRSNGHPTY 

       190        200        210        220        230        240 
LLAVVVDDHD MCITHIIRGS DHITNTIKQM LLAEAMGWDN PQFCHIPLIH DEGGAKLSKR 

       250        260        270        280        290        300 
NRAPGVHEYR ELGFLPEAVC NYLLRMGWSH KDEEIITMQS ATQLFSIEKI GTSHSCLDSK 

       310        320        330        340        350        360 
KLLFLNHHYM NQKTELEILG LLLPFLEQEL GHTVAETKLA RLSLGVKKLM ERAKTLADLA 

       370        380        390        400        410        420 
RDSVFYVQNI PISVDDDAKQ VILKSSELLA KLVGAMSQIE PKTWTKDFLS SYIKEWTKSN 

       430        440        450        460 
DVVISDVYHL LRAAIAGRLS TPSISEVMEI LGQEECISRL RFFLNS 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86712.1. Different initiation.
RefSeqYP_153967.1. NC_004842.2.

3D structure databases

ProteinModelPortalQ5PAG8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234826.AM775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV86712; AAV86712; AM775.
GeneID3171550.
KEGGama:AM775.
PATRIC20947507. VBIAnaMar46146_0669.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

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_ANAMM
AccessionPrimary (citable) accession number: Q5PAG8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: February 19, 2014
This is version 66 of the entry and version 2 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