Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot O57963 (SYK_PYRHO)

Last modified November 24, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Hide | Top

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: PH0224
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Hide | Top

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit. HAMAP MF_00177

Subcellular location

Cytoplasm.

Sequence similarities

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

Hide | Top

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete 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

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 523523Lysyl-tRNA synthetase HAMAP MF_00177
PRO_0000152760

Regions

Motif30 – 389"HIGH" region HAMAP MF_00177
Motif279 – 2835"KMSKS" region HAMAP MF_00177

Sites

Metal binding951Zinc 1 HAMAP MF_00177
Metal binding991Zinc 1 HAMAP MF_00177
Metal binding1001Zinc 1 HAMAP MF_00177
Metal binding1061Zinc 1 HAMAP MF_00177
Metal binding1771Zinc 2 HAMAP MF_00177
Metal binding1801Zinc 2 HAMAP MF_00177
Metal binding1991Zinc 2 HAMAP MF_00177
Metal binding2031Zinc 2 HAMAP MF_00177

Secondary structure

1 .............................................................................. 523
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
O57963-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 0FA9AD39FE7FCD49

FASTA52361,579
        10         20         30         40         50         60 
MVHWADYIAD KIIRERGEKE KYVVESGITP SGYVHVGNFR ELFTAYIVGH ALRDKGYEVR 

        70         80         90        100        110        120 
HIHMWDDYDR FRKVPRNVPQ EWKDYLGMPI SEVPDPWGCH ESYAEHFMRK FEEEVEKLGI 

       130        140        150        160        170        180 
EVDFLYASEL YKRGEYSEEI RLAFEKRDKI MEILNKYREI AKQPPLPENW WPAMVYCPEH 

       190        200        210        220        230        240 
RREAEIIEWD GGWKVKYKCP EGHEGWVDIR SGNVKLRWRV DWPMRWSHFG VDFEPAGKDH 

       250        260        270        280        290        300 
LVAGSSYDTG KEIIKEVYGK EAPLSLMYEF VGIKGQKGKM SGSKGNVILL SDLYEVLEPG 

       310        320        330        340        350        360 
LVRFIYARHR PNKEIKIDLG LGILNLYDEF DKVERIYFGV EGGKGDDEEL RRTYELSMPK 

       370        380        390        400        410        420 
KPERLVAQAP FRFLAVLVQL PHLTEEDIIN VLIKQGHIPR DLSKEDVERV KLRINLARNW 

       430        440        450        460        470        480 
VKKYAPEDVK FSILEKPPEV EVSEDVREAM NEVAEWLENH EEFSVEEFNN ILFEVAKRRG 

       490        500        510        520 
ISSREWFSTL YRLFIGKERG PRLASFLASL DRSFVIKRLR LEG

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OT3.
[2]"Functional convergence of two lysyl-tRNA synthetases with unrelated topologies."
Terada T., Nureki O., Ishitani R., Ambrogelly A., Ibba M., Soell D., Yokoyama S.
Nat. Struct. Biol. 9:257-262(2002) [PubMed: 11887185] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Hide | Top

Cross-references

Sequence databases

BA000001 Genomic DNA. Translation: BAA29296.1.
PIRA71246.
RefSeqNP_142220.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1IRXX-ray2.60A/B1-523[»]
ModBaseSearch...

Genome annotation databases

GeneID1444114.
GenomeReviewsGene locus PH0224 in contig BA000001_GR.
KEGGpho:PH0224.
NMPDRfig|70601.1.peg.214.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO57963.
OMAAFSDDMD

Enzyme and pathway databases

BioCycPHOR70601:PH0224-MON.
BRENDA6.1.1.6. 74679.

Family and domain databases

HAMAPMF_00177.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR000924. Glu/Gln-tRNA-synth_Ic.
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.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF01921. tRNA-synt_1f. 1 hit.
[Graphical view]
TIGRFAMsTIGR00467. lysS_arch. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameSYK_PYRHO
AccessionPrimary (citable) accession number: O57963
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: November 24, 2009
This is version 71 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)

Hide | Top

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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