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Q8PVP6 (SYK2_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. 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 2

EC=6.1.1.6
Alternative name(s):
Lysyl-tRNA synthetase 2
Short name=LysRS 2
Gene names
Name:lysS2
Ordered Locus Names:MM_1916
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length511 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_00252

Cofactor

Binds 3 magnesium ions per subunit By similarity. HAMAP MF_00252

Subunit structure

Homodimer By similarity. HAMAP MF_00252

Subcellular location

Cytoplasm HAMAP 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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

lysine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Lysine--tRNA ligase 2 HAMAP MF_00252
PRO_0000152712

Sites

Metal binding4211Magnesium 1 By similarity
Metal binding4281Magnesium 1 By similarity
Metal binding4281Magnesium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8PVP6 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 6DF668BA4E971849

FASTA51158,795
        10         20         30         40         50         60 
MTMEINNTDP FEKMPLPDDS GLSGSGAFDD SKLAKLNGVI SQGLNPYPYK FEKDEDICEI 

        70         80         90        100        110        120 
LEKFEDFEKN EGLTVRTAGR LYNIRKHGKM IFADLGDQAG RVQVLVRKGN LPDEEFEIFK 

       130        140        150        160        170        180 
NLVDSGDIIG VQGDLFRTKR GENSISVSEF SLLSKSLCAL PEKFHGLKDV ETRYRKRYLD 

       190        200        210        220        230        240 
LIVNAEKREI FVMRSKLISE IRRFLTDREF LEFETPILQT VYGGANARPF TTFHNCLGQN 

       250        260        270        280        290        300 
LFLRIAPELY LKRLVVGGYE KVFEICKNFR NEDIDTTHNP EFTMIEVYEA YRDYNDMMDL 

       310        320        330        340        350        360 
TESLVSELVF KLTGSYEVQM GEKTINLRSP WKRISMEDAL KEYAGLDIFA HSIEDLKKIA 

       370        380        390        400        410        420 
IENRIEDYEK AKSHGEFLAL LFEGLVEDKL IDPTFIYDFP VENSPLAKNH REKAGFVERF 

       430        440        450        460        470        480 
ELFLNGWELA NGYSELNDPL EQEKRFEEQD KKRKLGDLEA QTVDYDFINA LGYGLPPTGG 

       490        500        510 
MGLGIDRLTM ILSGLESIKE VILFPQMKRE D 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM31612.1.
RefSeqNP_633940.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PVP6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1480258.
GenomeReviewsGene locus MM_1916 in contig AE008384_GR.
KEGGmma:MM_1916.
NMPDRfig|192952.1.peg.1916.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG631383.
OMAMEINNTD.
PhylomeDBQ8PVP6.
ProtClustDBPRK00484.

Enzyme and pathway databases

BioCycMMAZ192952:MM1916-MONOMER.

Family and domain databases

HAMAPMF_00252. Lys_tRNA_synth_class2.
[Tree]
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR002313. Lys-tRNA-synth_II.
IPR018149. Lys-tRNA-synth_II_C.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK04567.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF4. tRNA-synt_lys_2. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR00982. TRNASYNTHLYS.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMsTIGR00499. LysS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYK2_METMA
AccessionPrimary (citable) accession number: Q8PVP6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 65 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