Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A3DMR5 (SYE_STAMF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:Smar_0824
OrganismStaphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP]
Taxonomic identifier399550 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeStaphylothermus

Protein attributes

Sequence length566 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

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 566566Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367805

Regions

Motif93 – 10311"HIGH" region HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
A3DMR5 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: 2684D577A98F429D

FASTA56665,806
        10         20         30         40         50         60 
MLNAYKHSGK AELKPVISKI IAEIPEIRRH VREVIDIVRE TINEVNQLPI EKQKEIIEKN 

        70         80         90        100        110        120 
WPELLEEKPR TEEKSLPPLP NAAKGRVVTR FAPNPDYTIH LGNARPALLS YWYAEMYEGK 

       130        140        150        160        170        180 
MILRFEDTDP RTKAPFPEAY DRIRNDLKWL GIKWNEEYIQ SLRLPILYNA LRELIKHGGA 

       190        200        210        220        230        240 
YVDKCSPKEF KKLRDSGKPC PHRELPPEKH LEELDRIFEG YYSEGEAVVR VKTDLSHPDP 

       250        260        270        280        290        300 
SVRDWVAARI IDTSKTPHPI VGDKYILWPT YNLAAAIDDH LMGVTHILRA KEHVSNTIKQ 

       310        320        330        340        350        360 
KFLYDHMGWK YPETIHFGRL SLEGVILSKS RMRKMIVEYN MEPYDDPRFG TLSGLRRRGI 

       370        380        390        400        410        420 
VRETLWRIIK DVGINVIDAR ISYVNLAAIN RSIIDPQAKR YMAIEEALPL KLIGFNNSIE 

       430        440        450        460        470        480 
AHVLRHPSTR ETYNYIIKPG DIVYISQKDF NIIQNKMFRL MGIGNFALTR PVFSKNYIGF 

       490        500        510        520        530        540 
EARLISLSAK EAKQYRAPII QWVKLEQSIR VKLIIPKETN LETRILLAEK ALTNEELGNI 

       550        560 
VQFYRIGFAR IDSKEPEEIK CIFAHE 

« Hide

References

[1]"The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota."
Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N.
BMC Genomics 10:145-145(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43588 / DSM 3639 / F1.
[2]"Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1."
Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., Kyrpides N.C.
Stand. Genomic Sci. 1:183-188(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43588 / DSM 3639 / F1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000575 Genomic DNA. Translation: ABN69925.1.
RefSeqYP_001040833.1. NC_009033.1.

3D structure databases

ProteinModelPortalA3DMR5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399550.Smar_0824.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN69925; ABN69925; Smar_0824.
GeneID4907409.
KEGGsmr:Smar_0824.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000073585.
KOK01885.
OMAMRFAPNP.
ProtClustDBPRK04156.

Enzyme and pathway databases

BioCycSMAR399550:GHK2-844-MONOMER.

Family and domain databases

Gene3D1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_A. Glu_tRNA_synth_A.
InterProIPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR022888. Glu_tRNA_synth_arc.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF50715. SSF50715. 1 hit.
TIGRFAMsTIGR00463. gltX_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYE_STAMF
AccessionPrimary (citable) accession number: A3DMR5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 20, 2007
Last modified: February 19, 2014
This is version 48 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