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B6IST4 (SYE2_RHOCS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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:RC1_1191
OrganismRhodospirillum centenum (strain ATCC 51521 / SW) [Complete proteome] [HAMAP]
Taxonomic identifier414684 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length468 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 – 468468Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367750

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif238 – 2425"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2411ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B6IST4 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 36817233D98A55D0

FASTA46852,030
        10         20         30         40         50         60 
MTIVTRFAPS PTGFLHIGGA RTALFNWLYA RGHGGKFLLR IEDTDRARST QAAVDAILDG 

        70         80         90        100        110        120 
LDWLGLEWDG DPISQFERKD RHAEVAHEML RRGMAYRCYA SPEELEAMKE EQRRQGLPMR 

       130        140        150        160        170        180 
YDGRWRDRDP SEAPAGVNPV IRLKAPQEGE TVVRDHVQGE VRVQNAQLDD MILLRSDGTP 

       190        200        210        220        230        240 
TYLLAVVVDD YDMGVTHVVR GDDHLTNTFR QLQIYAAMGW TPPEYAHVPL IHGPDGAKLS 

       250        260        270        280        290        300 
KRHGALGVDA YRDMGYLPET MRNYLLRLGW SHGDDEIIST DQAKAWFNLD DIGRSPSRLD 

       310        320        330        340        350        360 
FAKLDNLNGH YIRQSDDARL VSLVVPMVEK RLGRPLTGSE HARLLAAMPG FKPRVKTLVE 

       370        380        390        400        410        420 
LADGCLFLFA LRPLAMDDKA AALLTPEAKA QLGELHALFS GLGDWTGGAL EQAVRDFAER 

       430        440        450        460 
TGLKLGKVAQ PLRAALTGST VSPPIFEVAE VLGRTETLER IDDARKAG 

« Hide

References

[1]"Genome sequence of Rhodospirillum centenum."
Touchman J.W., Bauer C., Blankenship R.E.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51521 / SW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000613 Genomic DNA. Translation: ACI98605.1.
RefSeqYP_002297418.1. NC_011420.2.

3D structure databases

ProteinModelPortalB6IST4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING414684.RC1_1191.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI98605; ACI98605; RC1_1191.
GeneID7005961.
KEGGrce:RC1_1191.
PATRIC23317592. VBIRhoCen1465_1147.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAHCLRASI.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycRCEN414684:GHCM-1173-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_RHOCS
AccessionPrimary (citable) accession number: B6IST4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 35 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