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

A9N3L6 (SYK_SALPB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:
Lysine--tRNA ligase

EC=6.1.1.6
Alternative name(s):
Lysyl-tRNA synthetase
Short name=LysRS
Gene names
Name:lysS
Ordered Locus Names:SPAB_03787
OrganismSalmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [Complete proteome] [HAMAP]
Taxonomic identifier1016998 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length505 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
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 – 505505Lysine--tRNA ligase HAMAP-Rule MF_00252
PRO_1000078508

Sites

Metal binding4151Magnesium 1 By similarity
Metal binding4221Magnesium 1 By similarity
Metal binding4221Magnesium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A9N3L6 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 48EBE562C708F96F

FASTA50557,575
        10         20         30         40         50         60 
MSEQNAQGAD EVVDLNNEMK ARREKLAALR EQGIPFPNDF RRDRTSDQLH AEFDAKEAEE 

        70         80         90        100        110        120 
LEALNIEVSV AGRMMTRRIM GKASFVTLQD VGGRIQLYVA RDDLPEGVYN EQFKKWDLGD 

       130        140        150        160        170        180 
ILGAKGKLFK TKTGELSIHC TELRLLTKAL RPLPDKFHGL QDQEARYRQR YLDLISNDES 

       190        200        210        220        230        240 
RNTFKTRSKI LAGIRQFMVA RGFMEVETPM MQVIPGGASA RPFITHHNAL DLDMYLRIAP 

       250        260        270        280        290        300 
ELYLKRLVVG GFERVFEINR NFRNEGISVR HNPEFTMMEL YMAYADYKDL IELTESLFRT 

       310        320        330        340        350        360 
LAQDVLGTTQ VPYGDEVFDF GKPFEKLTMR EAIKKYRPET DMADLDNFDS AKAIAESIGI 

       370        380        390        400        410        420 
HVEKSWGLGR IVTEIFDEVA EAHLIQPTFI TEYPAEVSPL ARRNDVNPEI TDRFEFFIGG 

       430        440        450        460        470        480 
REIGNGFSEL NDAEDQAQRF LDQVNAKAAG DDEAMFYDED YVTALEHGLP PTAGLGIGID 

       490        500 
RMVMLFTNSH TIRDVILFPA MRPVK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000886 Genomic DNA. Translation: ABX69119.1.
RefSeqYP_001589952.1. NC_010102.1.

3D structure databases

ProteinModelPortalA9N3L6.
SMRA9N3L6. Positions 12-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272994.SPAB_03787.

Proteomic databases

PRIDEA9N3L6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX69119; ABX69119; SPAB_03787.
PATRIC18534434. VBISalEnt120821_3056.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1190.
HOGENOMHOG000236578.
OMADLMDFTE.
OrthoDBEOG69PQ2M.
ProtClustDBPRK00484.

Enzyme and pathway databases

BioCycSENT28901:GH9O-3777-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_SALPB
AccessionPrimary (citable) accession number: A9N3L6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 44 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