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Reviewed, UniProtKB/Swiss-Prot Q16AV0 (SYK_ROSDO)

Last modified March 2, 2010. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
Lysyl-tRNA synthetase

EC=6.1.1.6
Alternative name(s):
Lysine--tRNA ligase
Short name=LysRS
Gene names
Name:lysS
Ordered Locus Names:RD1_1246
OrganismRoseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) [Complete proteome] [HAMAP]
Taxonomic identifier375451 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRoseobacter

Protein attributes

Sequence length527 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP MF_00177

Subcellular location

Cytoplasm HAMAP MF_00177.

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 processlysyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

lysine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 527527Lysyl-tRNA synthetase HAMAP MF_00177
PRO_1000040354

Regions

Motif44 – 529"HIGH" region HAMAP MF_00177
Motif290 – 2945"KMSKS" region HAMAP MF_00177

Sites

Binding site2931ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q16AV0-1 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 23D33C5964D04CA1

FASTA52759,384
        10         20         30         40         50         60 
MSDTRTAAMT SKAWPFEEAR RVLKRYEKNP PEKGYVLFET GYGPSGLPHI GTFGEVARTS 

        70         80         90        100        110        120 
MVMRAFQEIS DIPTRLICFS DDLDGMRKVP GNVPNPDALT EHLQRPLTSV PDPFGTHASF 

       130        140        150        160        170        180 
GAHNNAMLRR FLDTFGFEYE FISATEFYNT GQFDEILLRA AAKYDEIMAV MLKSLREERR 

       190        200        210        220        230        240 
QTYSIFLPIH PESGRVMYVP MKEVNAQAGT ITFDSEDGEE MTLPVTGGAV KLQWKPDFGA 

       250        260        270        280        290        300 
RWAALGVDFE MYGKDHSTNT PIYDKICRIL GQRPPEHFTY ELFLDENGQK ISKSSGNGVS 

       310        320        330        340        350        360 
IDEWLTYAST ESLSYFMYQK PKTAKRMYFD VIPKAVDEYH QQLRAYAGQD TAQRLNNPVW 

       370        380        390        400        410        420 
HIHGGDVPAS NMLVPFSMLL NLASVSSAED KSQLWGFIQR YAPESNPENN PDMDAAADFA 

       430        440        450        460        470        480 
VRYFNDFVKP KKVYRAASDL EREALEDLRD QLKAYDGPVD DEALQSIVYA CGRERFDPLR 

       490        500        510        520 
GWFTALYEVL LGASQGPRFG GFIALYGVQE TVALIDAALA GELLSDD 

« Hide

References

[1]"The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism."
Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T., Touchman J.W.
J. Bacteriol. 189:683-690(2007) [PubMed: 17098896] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000362 Genomic DNA. Translation: ABG30893.1.
RefSeqYP_681579.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ16AV0.

Genome annotation databases

GeneID4197453.
GenomeReviewsGene locus RD1_1246 in contig CP000362_GR.
KEGGrde:RD1_1246.
NMPDRfig|375451.6.peg.1163.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1384.
HOGENOMHBG294650.
OMAAFSDDMD.
ProtClustDBPRK00750.

Enzyme and pathway databases

BioCycRDEN375451:RD1_1246-MONOMER.

Family and domain databases

HAMAPMF_00177. Lys_tRNA_synth_class1.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR002904. Lys-tRNA-synth_I.
IPR020754. Lys-tRNA-synth_Ic.
IPR020756. Lysyl-tRNA_synth_I_arc-type.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PfamPF01921. tRNA-synt_1f. 1 hit.
[Graphical view]
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00467. lysS_arch. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYK_ROSDO
AccessionPrimary (citable) accession number: Q16AV0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: March 2, 2010
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents