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Q2YTH9

- SYL_STAAB

UniProt

Q2YTH9 - SYL_STAAB

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Protein

Leucine--tRNA ligase

Gene
leuS, SAB1618c
Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei579 – 5791ATP By similarity

GO - Molecular functioni

  1. aminoacyl-tRNA editing activity Source: InterPro
  2. ATP binding Source: UniProtKB-HAMAP
  3. leucine-tRNA ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. leucyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSAUR273036:GJVS-1640-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine--tRNA ligase (EC:6.1.1.4)
Alternative name(s):
Leucyl-tRNA synthetase
Short name:
LeuRS
Gene namesi
Name:leuS
Ordered Locus Names:SAB1618c
OrganismiStaphylococcus aureus (strain bovine RF122 / ET3-1)
Taxonomic identifieri273036 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001927: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 804804Leucine--tRNA ligaseUniRule annotationPRO_1000009439Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi273036.SAB1618c.

Structurei

3D structure databases

ProteinModelPortaliQ2YTH9.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi40 – 5112"HIGH" regionUniRule annotationAdd
BLAST
Motifi576 – 5805"KMSKS" regionUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0495.
HOGENOMiHOG000200748.
KOiK01869.
OMAiNENGVEG.
OrthoDBiEOG63Z74X.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPiMF_00049_B. Leu_tRNA_synth_B.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002302. Leu-tRNA-ligase.
IPR025709. Leu_tRNA-synth_edit.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF13603. tRNA-synt_1_2. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSiPR00985. TRNASYNTHLEU.
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsiTIGR00396. leuS_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2YTH9-1 [UniParc]FASTAAdd to Basket

« Hide

MNYNHNQIEK KWQDYWDENK TFKTNDNLGQ KKFYALDMFP YPSGAGLHVG    50
HPEGYTATDI ISRYKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNDPREFT 100
KKNIQTFKRQ IKELGFSYDW DREVNTTDPE YYKWTQWIFI QLYNKGLAYV 150
DEVAVNWCPA LGTVLSNEEV IDGVSERGGH PVYRKPMKQW VLKITEYADQ 200
LLADLDDLDW PESLKDMQRN WIGRSEGAKV SFDVDNTEGK VEVFTTRPDT 250
IYGASFLVLS PEHALVNSIT TDEYKEKVKA YQTEASKKSD LERTDLAKDK 300
SGVFTGAYAI NPLSGEKVQI WIADYVLSTY GTGAIMAVPA HDDRDYEFAK 350
KFDLLIIEVI EGGNVEEAAY TGEGKHINSG ELDGLENEAA ITKAIQLLEQ 400
KGAGEKKVNY KLRDWLFSRQ RYWGEPIPVI HWEDGTMTTV PEEELPLLLP 450
ETDEIKPSGT GESPLANIDS FVNVVDEKTG MKGRRETNTM PQWAGSCWYY 500
LRYIDPKNEN MLADPEKLKH WLPVDLYIGG VEHAVLHLLY ARFWHKVLYD 550
LGIVPTKEPF QKLFNQGMIL GEGNEKMSKS KGNVINPDDI VQSHGADTLR 600
LYEMFMGPLD AAIAWSEKGL DGSRRFLDRV WRLIVNEDGT LSSKIVTTNN 650
KSLDKVYNQT VKKVTDDFET LGFNTAISQL MVFINECYKV DEVYKPYIEG 700
FVKMLAPIAP HIGEELWSKL GHEESITYQP WPTYDEALLV DDEVEIVVQV 750
NGKLRAKIKI AKDTSKEEMQ EIALSNDNVK ASIEGKDIMK VIAVPQKLVN 800
IVAK 804
Length:804
Mass (Da):91,655
Last modified:December 20, 2005 - v1
Checksum:iDD957BB01CC274B3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ938182 Genomic DNA. Translation: CAI81307.1.
RefSeqiYP_417087.1. NC_007622.1.

Genome annotation databases

EnsemblBacteriaiCAI81307; CAI81307; SAB1618c.
GeneIDi3794808.
KEGGisab:SAB1618c.
PATRICi19524137. VBIStaAur92441_1717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ938182 Genomic DNA. Translation: CAI81307.1 .
RefSeqi YP_417087.1. NC_007622.1.

3D structure databases

ProteinModelPortali Q2YTH9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273036.SAB1618c.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAI81307 ; CAI81307 ; SAB1618c .
GeneIDi 3794808.
KEGGi sab:SAB1618c.
PATRICi 19524137. VBIStaAur92441_1717.

Phylogenomic databases

eggNOGi COG0495.
HOGENOMi HOG000200748.
KOi K01869.
OMAi NENGVEG.
OrthoDBi EOG63Z74X.

Enzyme and pathway databases

BioCyci SAUR273036:GJVS-1640-MONOMER.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPi MF_00049_B. Leu_tRNA_synth_B.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002302. Leu-tRNA-ligase.
IPR025709. Leu_tRNA-synth_edit.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view ]
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF13603. tRNA-synt_1_2. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
[Graphical view ]
PRINTSi PR00985. TRNASYNTHLEU.
SUPFAMi SSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsi TIGR00396. leuS_bact. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular correlates of host specialization in Staphylococcus aureus."
    Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.
    PLoS ONE 2:E1120-E1120(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: bovine RF122 / ET3-1.

Entry informationi

Entry nameiSYL_STAAB
AccessioniPrimary (citable) accession number: Q2YTH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 20, 2005
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi