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O66680 (SYLA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine--tRNA ligase subunit alpha
EC=6.1.1.4
Alternative name(s):
Leucyl-tRNA synthetase subunit alpha
Short name=LeuRS
Gene names
Name:leuS
Ordered Locus Names:aq_351
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu). HAMAP MF_00049_B

Subunit structure

Seems to consist of an alpha chain and a beta chain.

Subcellular location

Cytoplasm HAMAP MF_00049_B.

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 term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processleucyl-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

leucine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 634634Leucine--tRNA ligase subunit alpha HAMAP MF_00049_B
PRO_0000151962

Regions

Motif43 – 519"HIGH" region HAMAP MF_00049_B

Secondary structure

1 ................................ 634
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O66680 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 0119CA3F7A018766

FASTA63473,989
        10         20         30         40         50         60 
MMKEFNPREI EKKWQKRWEE AGVFKAQEGK PNKFYVLEMF PYPSGRIHMG HVRNYTIGDA 

        70         80         90        100        110        120 
IARYLKMRGK NILHPMGWDA FGLPAENAAI KHGIHPAKWT YENIDYMKKQ LKILGFSYDW 

       130        140        150        160        170        180 
DREIATCDPE YYKWNQWIFL KMLERGIAYR KTAKVNWCPH DQTVLANEQV IEGKCWRCGT 

       190        200        210        220        230        240 
PIVQKEVPSW FLRITAYADR LLEDLKKLEG KWPERVIAQQ RNWIGRSEGA LIRFYVEIEE 

       250        260        270        280        290        300 
PEKFLNCVPE ELKETLLKEK RIYIDVFTTR PDTVFGATFV VLAPEHPLVP VLACIGERLG 

       310        320        330        340        350        360 
NACYSDVENF VEKMKKMSTR ERTMEEDKEG VFLGVYATNP ANGEKIPVWS ANYVLYEYGT 

       370        380        390        400        410        420 
GAIMCVPAHD QRDWEFAKKY DLPIKVVVKP EGAWDFEKGA YEGKGTLVNS DGFDGLDSET 

       430        440        450        460        470        480 
AKRKITEWLQ DRGLGEKKVS YRLRDWNISR QRYWGTPIPV VYCEKCGMVP VPEDQLPVKL 

       490        500        510        520        530        540 
PLDVKFTGQG NPLETSEEFV NTTCPKCGGK ARRETDTMDT FFDSSWYFLR FCDPKNDREP 

       550        560        570        580        590        600 
FSREKVDYWM PVDVYIGGIE HAVLHLLYAR FFQKFLKDLG LVRDDEPFEK LITQGMVLKK 

       610        620        630 
WVSVKKLLDY LGLSEEDEVE ELKKRLEELG ARRA

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC06643.1.
PIRD70331.
RefSeqNP_213240.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O0AX-ray1.77A/B225-443[»]
3PZ0X-ray2.40A/B/C/D228-439[»]
3PZ5X-ray2.50A/B228-439[»]
ProteinModelPortalO66680.
SMRO66680. Positions 2-600.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193006.
GenomeReviewsGene locus aq_351 in contig AE000657_GR.
KEGGaae:aq_351.
NMPDRfig|224324.1.peg.255.
PATRIC20958296. VBIAquAeo85532_0284.

Phylogenomic databases

HOGENOMHBG693845.
OMAFRFNTAI.
PhylomeDBO66680.
ProtClustDBCLSK2299372.

Enzyme and pathway databases

BioCycAAEO224324:AQ_351-MONOMER.

Family and domain databases

HAMAPMF_00049_B. Leu_tRNA_synth_B. Divergent sequence.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002302. Leu-tRNA-synth_Ia_bac/mito.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
Gene3DG3DSA:3.90.740.10. G3DSA:3.90.740.10. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01869.
PfamPF00133. tRNA-synt_1. 3 hits.
[Graphical view]
PRINTSPR00985. TRNASYNTHLEU.
SUPFAMSSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMsTIGR00396. LeuS_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYLA_AQUAE
AccessionPrimary (citable) accession number: O66680
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 77 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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