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Q8RDZ8 (SYE_FUSNN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. 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:FN1340
OrganismFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Taxonomic identifier190304 [NCBI]
Taxonomic lineageBacteriaFusobacteriaFusobacteralesFusobacteriaceaeFusobacterium

Protein attributes

Sequence length510 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm HAMAP MF_00022_B.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Sequence caution

The sequence AAL95536.1 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
Reference proteome
Gene Ontology (GO)
   Biological processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119565

Regions

Motif15 – 2511"HIGH" region HAMAP MF_00022_B
Motif256 – 2605"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2591ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8RDZ8 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: B2A87FEDC9BEDBBD

FASTA51058,753
        10         20         30         40         50         60 
MCVDCKKRVR TRVAPSPTGD PHVGTAYIAL FNIAFAHVND GDFILRIEDT DRNRYTEGSE 

        70         80         90        100        110        120 
QMIFDALKWL DLDYSEGPDV GGDYGPYRQS ERFDLYGKYA KELVEKGGAY YCFCDHERLE 

       130        140        150        160        170        180 
NLRERQKAMG LPPGYDGHCR SLSKEEIEEK LKAGVPYVIR LKMPYEGETV IHDRLRGDVV 

       190        200        210        220        230        240 
FENSKIDDQV LLKADGYPTY HLANIVDDHL MGITHVIRAE EWIPSTPKHI QLYKAFGWEA 

       250        260        270        280        290        300 
PEFIHMPLLR NDDRSKISKR KNPVSLIWYK EEGYLKEGLV NFLGLMGYSY GDGQEIFTLQ 

       310        320        330        340        350        360 
EFKDNFNIDK VTLGGPVFDL VKLGWVNNQH MKMKDLGELT RLTIPFFVNE GYLTNENVSE 

       370        380        390        400        410        420 
KEFETLKKVV GIEREGAKTL QELAKNSKFF FVDEFSLPEL REDMDKKERK SVERLLNSLK 

       430        440        450        460        470        480 
DEIGLKSIKL FIEKLEKWNG NEFTAEQAKD LLHSLLDDLQ EGPGKIFMPI RAVLTGESKG 

       490        500        510 
ADLYNILYVI GKERALKRIK NIVKKYNIGI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009951 Genomic DNA. Translation: AAL95536.1. Different initiation.
RefSeqNP_604237.1. NC_003454.1.

3D structure databases

ProteinModelPortalQ8RDZ8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID992212.
GenomeReviewsGene locus FN1340 in contig AE009951_GR.
KEGGfnu:FN1340.
NMPDRfig|190304.1.peg.1916.
PATRIC21952441. VBIFusNuc122357_1903.

Phylogenomic databases

HOGENOMHBG628189.
OMAWENVRVR.
PhylomeDBQ8RDZ8.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycFNUC190304:FN1340-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_FUSNN
AccessionPrimary (citable) accession number: Q8RDZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: January 25, 2012
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families