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P67512

- SYL_STAAM

UniProt

P67512 - SYL_STAAM

Protein

Leucine--tRNA ligase

Gene

leuS

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    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 – 5791ATPUniRule annotation

    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

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSAUR158878:GJJ5-1777-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leucine--tRNA ligaseUniRule annotation (EC:6.1.1.4UniRule annotation)
    Alternative name(s):
    Leucyl-tRNA synthetaseUniRule annotation
    Short name:
    LeuRSUniRule annotation
    Gene namesi
    Name:leuSUniRule annotation
    Ordered Locus Names:SAV1760
    OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
    Taxonomic identifieri158878 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
    ProteomesiUP000002481: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 804804Leucine--tRNA ligasePRO_0000152083Add
    BLAST

    2D gel databases

    World-2DPAGE0002:P67512.

    Interactioni

    Protein-protein interaction databases

    STRINGi158878.SAV1760.

    Structurei

    3D structure databases

    ProteinModelPortaliP67512.
    SMRiP67512. Positions 3-802.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi40 – 5112"HIGH" regionAdd
    BLAST
    Motifi576 – 5805"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0495.
    KOiK01869.
    OMAiHISHELW.
    OrthoDBiEOG63Z74X.
    PhylomeDBiP67512.

    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.

    P67512-1 [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
    KFDLPIIEVI 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 WRLMVNEDGT LSSKIVTTNN 650
    KSLDKVYNQT VKKVTEDFET LGFNTAISQL MVFINECYKV DEVYKPYIEG 700
    FVKMLAPIAP HIGEELWSKL GHEESITYQP WPTYDEALLV DDEVEIVVQV 750
    NGKLRAKIKI AKDTSKEEMQ EIALSNDNVK ASIEGKDIMK VIAVPQKLVN 800
    IVAK 804
    Length:804
    Mass (Da):91,671
    Last modified:October 11, 2004 - v1
    Checksum:iD5E06EAF347D9E52
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB57922.1.
    RefSeqiNP_372284.1. NC_002758.2.

    Genome annotation databases

    EnsemblBacteriaiBAB57922; BAB57922; SAV1760.
    GeneIDi1121734.
    KEGGisav:SAV1760.
    PATRICi19564276. VBIStaAur52173_1816.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000017 Genomic DNA. Translation: BAB57922.1 .
    RefSeqi NP_372284.1. NC_002758.2.

    3D structure databases

    ProteinModelPortali P67512.
    SMRi P67512. Positions 3-802.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 158878.SAV1760.

    2D gel databases

    World-2DPAGE 0002:P67512.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAB57922 ; BAB57922 ; SAV1760 .
    GeneIDi 1121734.
    KEGGi sav:SAV1760.
    PATRICi 19564276. VBIStaAur52173_1816.

    Phylogenomic databases

    eggNOGi COG0495.
    KOi K01869.
    OMAi HISHELW.
    OrthoDBi EOG63Z74X.
    PhylomeDBi P67512.

    Enzyme and pathway databases

    BioCyci SAUR158878:GJJ5-1777-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Mu50 / ATCC 700699.

    Entry informationi

    Entry nameiSYL_STAAM
    AccessioniPrimary (citable) accession number: P67512
    Secondary accession number(s): Q99TA8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 73 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