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Q83E97 (SYK_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Lysine--tRNA ligase

EC=6.1.1.6
Alternative name(s):
Lysyl-tRNA synthetase
Short name=LysRS
Gene names
Name:lysS
Ordered Locus Names:CBU_0430
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP-Rule MF_00252

Cofactor

Binds 3 magnesium ions per subunit By similarity. HAMAP-Rule MF_00252

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00252

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00252.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlysyl-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

lysine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 498498Lysine--tRNA ligase HAMAP-Rule MF_00252
PRO_0000152620

Sites

Metal binding4091Magnesium 1 By similarity
Metal binding4161Magnesium 1 By similarity
Metal binding4161Magnesium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83E97 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8092BC68989DAC00

FASTA49857,739
        10         20         30         40         50         60 
MELKDQIKEE NEQIAQRKLK LKKRREEGQA YPNDFKRDSL AADLHAVYDQ FDSGALTAKA 

        70         80         90        100        110        120 
IRVKMAGRMM TRRIMGKASF AHIQDMKGRM QIYVTRDSLP QGVYSDFKSW DLGDIVGIEG 

       130        140        150        160        170        180 
ELFKTKTEEL SVKVDQIRLL TKALRPMPDK FHGLHDQEQR FRQRYLDLIV NESSRHLFQT 

       190        200        210        220        230        240 
RSQVIAQIRR FLDDRGYIEV ETPMMHPLPG GAAARPFETH HNAMNMDLFL RIAPELYLKR 

       250        260        270        280        290        300 
LVVGGFEKVY EINRNFRNEG ISTRHNPEFT MLEFYQAYAT YEDMMMLTES MIRHLAEKIF 

       310        320        330        340        350        360 
GVMEIKYQGV RIDLNKPFPR LSLRDAILQF NPGITPDQID HLETARELAH KYEIATPAHY 

       370        380        390        400        410        420 
GLGKIQTELF EKLVEEKLQQ PIFITHFPKE VSPLSRANEE NDFITDRFEF YVGGREIANG 

       430        440        450        460        470        480 
FSELNDPEDQ AARFREQLKA RNAGDLEAMS FDEDYITALE YGLPPTAGEG IGIDRLVMLF 

       490 
TDNASIRDVI LFPLLRSK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO89981.1.
RefSeqNP_819467.1. NC_002971.3.

3D structure databases

ProteinModelPortalQ83E97.
SMRQ83E97. Positions 7-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_0430.

Proteomic databases

PRIDEQ83E97.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO89981; AAO89981; CBU_0430.
GeneID1208314.
KEGGcbu:CBU_0430.
PATRIC17929547. VBICoxBur82552_0419.

Phylogenomic databases

eggNOGCOG1190.
HOGENOMHOG000236578.
KOK04567.
OMADLMDFTE.
OrthoDBEOG69PQ2M.
ProtClustDBPRK00484.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-428-MONOMER.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_00252. Lys_tRNA_synth_class2.
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR002313. Lys-tRNA-ligase_II.
IPR018149. Lys-tRNA-synth_II_C.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF4. PTHR22594:SF4. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSPR00982. TRNASYNTHLYS.
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00499. lysS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYK_COXBU
AccessionPrimary (citable) accession number: Q83E97
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 74 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

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries