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P57923

- SYL_PASMU

UniProt

P57923 - SYL_PASMU

Protein

Leucine--tRNA ligase

Gene

leuS

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (27 Apr 2001)
      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 sitei622 – 6221ATPUniRule 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

    BioCyciPMUL272843:GC8W-1264-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:PM1214
    OrganismiPasteurella multocida (strain Pm70)
    Taxonomic identifieri272843 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
    ProteomesiUP000000809: 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 – 860860Leucine--tRNA ligasePRO_0000152059Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272843.PM1214.

    Structurei

    3D structure databases

    ProteinModelPortaliP57923.
    SMRiP57923. Positions 228-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi42 – 5211"HIGH" regionAdd
    BLAST
    Motifi619 – 6235"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0495.
    HOGENOMiHOG000200747.
    KOiK01869.
    OMAiDKPKYYA.
    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.

    P57923-1 [UniParc]FASTAAdd to Basket

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    MQEQYRPDLI EAEVQQYWAE NKTFKAIKDT NKPKYYCLSM FPYPSGRLHM    50
    GHVRNYTIGD VVSRYQRMNG KNVLQPMGWD AFGLPAEGAA IKNKTAPAKW 100
    TYENIDYMKN QLKILGFGFD WDREVTTCKP DYYKWEQWFF TELYKKGLVY 150
    KKTSTVNWCP NDETVLANEQ VHEGCCWRCD TPVEQKEIPQ WFIKITDYAE 200
    QLLGGLDHLP LWPDQVKTMQ RNWIGRSEGV EITFQLANSE DNLTVYTTRP 250
    DTFFGVSYVA VAAAHPLAEK AAENNPELAQ FIQECKNTKV AEAELATMEK 300
    KGMATGVYAI HPLTGEKVPV WVANFVLMHY GTGAVMAVPG HDERDAEFAR 350
    KYGLPLLNVI KPINGEPLLE HELPYCEHGI LFNSGEFNGL DFDAAFNAIA 400
    DKLEALGKGK RQVNYRLRDW GVSRQRYWGA PIPMLTLENG EVVPAPLQDL 450
    PIELPEDVVM DGVKSPIKAD PEWAKTTYNG QPALKETDTF DTFMESSWYY 500
    ARYTSPKFAE AMLDADEANY WLPVDQYIGG IEHATMHLLY FRFFHKLLRD 550
    AGFVTSDEPA DKLLCQGMVL ADAFYYTSPT NERIWVSPTE VTLERDEKGR 600
    ILKAFDKEGR ELVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS 650
    PAEMTLEWQE SGVEGAKRFL GRLWNLVFEY NKHPAETTVE PTALSSAQKA 700
    LRRDVHKTIA KVSDDIGRRQ TFNTAIAAIM ELMNKLTKAP LVEVQDRAIM 750
    AEALSAVVRM LYPITPHICF QLWKDLGNTE AIDFAPWVEA DAAAMVDDEK 800
    LVVVQVNGKV RAKVTVPAEM SEDDIKQVAL ADSNVAKHLE GLNIVKTIYV 850
    PGKLFSFVAK 860
    Length:860
    Mass (Da):97,623
    Last modified:April 27, 2001 - v1
    Checksum:i30C4308EF6D99E5A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03298.1.
    RefSeqiNP_246151.1. NC_002663.1.
    WP_010907077.1. NC_002663.1.

    Genome annotation databases

    EnsemblBacteriaiAAK03298; AAK03298; PM1214.
    GeneIDi1244561.
    KEGGipmu:PM1214.
    PATRICi22871679. VBIPasMul88067_1224.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004439 Genomic DNA. Translation: AAK03298.1 .
    RefSeqi NP_246151.1. NC_002663.1.
    WP_010907077.1. NC_002663.1.

    3D structure databases

    ProteinModelPortali P57923.
    SMRi P57923. Positions 228-413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272843.PM1214.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK03298 ; AAK03298 ; PM1214 .
    GeneIDi 1244561.
    KEGGi pmu:PM1214.
    PATRICi 22871679. VBIPasMul88067_1224.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci PMUL272843:GC8W-1264-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Pm70.

    Entry informationi

    Entry nameiSYL_PASMU
    AccessioniPrimary (citable) accession number: P57923
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 88 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