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Q0SU18 (SYE_CLOPS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:CPR_1067
OrganismClostridium perfringens (strain SM101 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier289380 [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 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 By similarity HAMAP MF_00022_B.

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: 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 – 552552Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000367651

Regions

Motif41 – 5111"HIGH" region HAMAP MF_00022_B
Motif293 – 2975"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0SU18 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: A8EA61A0C59C4F58

FASTA55263,760
        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 
IKRIEAGENY 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 AL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000312 Genomic DNA. Translation: ABG86873.1.
RefSeqYP_698389.1. NC_008262.1.

3D structure databases

ProteinModelPortalQ0SU18.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0SU18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4204243.
GenomeReviewsGene locus CPR_1067 in contig CP000312_GR.
KEGGcpr:CPR_1067.
PATRIC19490425. VBICloPer122123_1043.
TIGRCPR_1067.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADKETAND.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCPER289380:CPR_1067-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.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_CLOPS
AccessionPrimary (citable) accession number: Q0SU18
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 5, 2006
Last modified: January 25, 2012
This is version 45 of the entry and version 1 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