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B2FPR7

- SYL_STRMK

UniProt

B2FPR7 - SYL_STRMK

Protein

Leucine--tRNA ligase

Gene

leuS

Organism
Stenotrophomonas maltophilia (strain K279a)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 47 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      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 sitei641 – 6411ATPUniRule 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

    BioCyciSMAL522373:GJE8-3373-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:Smlt3485
    OrganismiStenotrophomonas maltophilia (strain K279a)
    Taxonomic identifieri522373 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group
    ProteomesiUP000008840: 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 – 880880Leucine--tRNA ligasePRO_1000091368Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi522373.Smlt3485.

    Structurei

    3D structure databases

    ProteinModelPortaliB2FPR7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi46 – 5611"HIGH" regionAdd
    BLAST
    Motifi638 – 6425"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0495.
    HOGENOMiHOG000200747.
    KOiK01869.
    OMAiMAFAGPP.
    OrthoDBiEOG63Z74X.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.40.50.620. 3 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.
    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]
    PANTHERiPTHR11946:SF7. PTHR11946:SF7. 1 hit.
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 3 hits.
    PF13603. tRNA-synt_1_2. 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.

    B2FPR7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSAETNAYD PQQVESAAQK YWDATRAFEV DETSDKPKYY CLSMLPYPSG    50
    ALHMGHVRNY TIGDVISRYK RMTGHNVLQP MGWDAFGLPA ENAAIKNKTA 100
    PAAWTYKNIE HMRGQFKAMG YAVDWSREFA TCRPDYYVHE QRMFTRLMRK 150
    GLAYRRNAVV NWDPVDQTVL ANEQVIDGRG WRSGALVEKR EIPQWFLRIT 200
    DYAQELLDGL DELDGWPDSV KTMQRNWIGR SEGLEIQFDV RDVDGTALDP 250
    LRVFTTRPDT VMGVTFVSIA AEHPLALHAA KNNPELAALL SEMKQGGVSE 300
    AELETQEKRG MDTGLRAIHP VTGEKVPVWV ANFVLMGYGT GAVMAVPGHD 350
    QRDNEVANKY GLPIKQVIAL KDPRNDDERT WDGARWQDWY SDKNRAFELV 400
    NSAEFDGLDF QGAFEALAER FERKAQGQRR VNYRLRDWGV SRQRYWGCPI 450
    PVIYCDKCGA VPVPEEQLPV VLPEDVAFSG TGSPIKTDPE WRKTTCPECG 500
    GAAERETDTF DTFMESSWYY ARYTSPGARD AVDKRGNYWL PVDQYIGGIE 550
    HAILHLMYFR FYHKLLRDAR MVDSNEPARN LLCQGMVIAE TYYRPNPDGS 600
    KDWINPADVE VQRDERGRIT GATLIADGQP VVVGGTEKMS KSKNNGVDPQ 650
    AMVDKYGADT VRLFSMFAAP PEQSLEWNEA GVDGMARFLR RLWAQVQKHA 700
    ADGAAPALDV AALDANQKAL RRKTHETIGK VGDDYGRRHS FNTAIAAVME 750
    LMNALAKFED GSEQGRAVRQ EALQAIVLLL NPITPHASHA LWQVLGHGET 800
    LLEDQPFPQA DAGALVRDAL TLAVQVNGKL RGTIEVAADA AREQVEALAL 850
    AEPNAAKFME GLTVRKIIIV PGKIVNIVAA 880
    Length:880
    Mass (Da):98,446
    Last modified:June 10, 2008 - v1
    Checksum:iF27102B3E388C6A6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM743169 Genomic DNA. Translation: CAQ46908.1.
    RefSeqiYP_001973197.1. NC_010943.1.

    Genome annotation databases

    EnsemblBacteriaiCAQ46908; CAQ46908; Smlt3485.
    GeneIDi6394000.
    KEGGisml:Smlt3485.
    PATRICi23702433. VBISteMal45202_3269.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM743169 Genomic DNA. Translation: CAQ46908.1 .
    RefSeqi YP_001973197.1. NC_010943.1.

    3D structure databases

    ProteinModelPortali B2FPR7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 522373.Smlt3485.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAQ46908 ; CAQ46908 ; Smlt3485 .
    GeneIDi 6394000.
    KEGGi sml:Smlt3485.
    PATRICi 23702433. VBISteMal45202_3269.

    Phylogenomic databases

    eggNOGi COG0495.
    HOGENOMi HOG000200747.
    KOi K01869.
    OMAi MAFAGPP.
    OrthoDBi EOG63Z74X.

    Enzyme and pathway databases

    BioCyci SMAL522373:GJE8-3373-MONOMER.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.40.50.620. 3 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.
    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 ]
    PANTHERi PTHR11946:SF7. PTHR11946:SF7. 1 hit.
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 3 hits.
    PF13603. tRNA-synt_1_2. 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. "The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
      Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A.
      , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
      Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K279a.

    Entry informationi

    Entry nameiSYL_STRMK
    AccessioniPrimary (citable) accession number: B2FPR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 47 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, Reference 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