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Q0TRN9 (SYE_CLOP1) 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

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Ordered Locus Names:CPF_1255
OrganismClostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195103 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length552 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 – 552552Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367650

Regions

Motif41 – 5111"HIGH" region HAMAP-Rule MF_00022
Motif293 – 2975"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0TRN9 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 47010E5CC99C8C52

FASTA55263,749
        10         20         30         40         50         60 
MSYENLANLI FPNIDKTPEY YFEKYPKRDL KEGAKVLRYA PSPTGFQHIG GVFASLINER 

        70         80         90        100        110        120 
LAHQSGGIFY LRIEDTDQKR EVEGAIDDTI KTMHNFGMDF DEGITGENSE KGAYAPYKQS 

       130        140        150        160        170        180 
QRADIYRAFV KDLLRKGLAY PCFMTSEELE ALREKQIAEK LTPGCYGEFA KYRDLSPEEA 

       190        200        210        220        230        240 
IKRIEAGESY VIRMKSPGNP EKRVVAHDMI KGEVSFPENL QDVVIIKGDG LPTYHFAHAI 

       250        260        270        280        290        300 
DDTLMRTTHV IRGEEWLSSL PIHLQMFEVL GVEAPKYAHI PTIMKMDGSS KRKLSKRKDP 

       310        320        330        340        350        360 
ESAVSYYSEK GYPSQSVIEY LLNIINSAFE EWRAENPDAD YHDYKVELDK MSKSGALFDL 

       370        380        390        400        410        420 
VKLNDVSKDV ICKMKPEVVY DLYTNWAKEY DKEMYDLVTS KEAMMKEVFN IDKEGPKPRK 

       430        440        450        460        470        480 
DFAKWDEVRE KIFYFFDELF DKETANDVEL PKTLELEEAK RIIEAYEKAY NFNTDKDTWF 

       490        500        510        520        530        540 
SDLKEVAVEL GYATDRKKYK KNPEEYKGMV SDVAGAVRAA LTHRANTPDL YTIMQIMGEE 

       550 
AVRERFKKFL SL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000246 Genomic DNA. Translation: ABG82688.1.
RefSeqYP_695701.1. NC_008261.1.

3D structure databases

ProteinModelPortalQ0TRN9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195103.CPF_1255.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG82688; ABG82688; CPF_1255.
GeneID4202557.
KEGGcpf:CPF_1255.
PATRIC19484782. VBICloPer106549_1211.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAEIFDMEY.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCPER195103:GHAW-1273-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_CLOP1
AccessionPrimary (citable) accession number: Q0TRN9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 5, 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