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Q72W44

- LFTR_LEPIC

UniProt

Q72W44 - LFTR_LEPIC

Protein

Leucyl/phenylalanyl-tRNA--protein transferase

Gene

aat

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.UniRule annotation

    Catalytic activityi

    L-leucyl-tRNA(Leu) + [protein] = tRNA(Leu) + L-leucyl-[protein].UniRule annotation
    L-phenylalanyl-tRNA(Phe) + [protein] = tRNA + L-phenylalanyl-[protein].UniRule annotation

    GO - Molecular functioni

    1. leucyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciLINT267671:GHQI-96-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leucyl/phenylalanyl-tRNA--protein transferaseUniRule annotation (EC:2.3.2.6UniRule annotation)
    Alternative name(s):
    L/F-transferaseUniRule annotation
    LeucyltransferaseUniRule annotation
    PhenyalanyltransferaseUniRule annotation
    Gene namesi
    Name:aatUniRule annotation
    Ordered Locus Names:LIC_10096
    OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
    Taxonomic identifieri267671 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
    ProteomesiUP000007037: Chromosome I

    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 – 219219Leucyl/phenylalanyl-tRNA--protein transferasePRO_0000207226Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi267671.LIC10096.

    Structurei

    3D structure databases

    ProteinModelPortaliQ72W44.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L/F-transferase family.UniRule annotation

    Phylogenomic databases

    KOiK00684.
    OMAiERFRYPR.
    OrthoDBiEOG6WX4R3.

    Family and domain databases

    HAMAPiMF_00688. Leu_Phe_trans.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR004616. Leu/Phe-tRNA_Trfase.
    [Graphical view]
    PfamiPF03588. Leu_Phe_trans. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    TIGRFAMsiTIGR00667. aat. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q72W44-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKDFSDFFRN PHIWDREIVA VGGDLSPERL LYAYKNGIFP WSDQPILWYC    50
    LDPRSIFDLN KLHISKRLKR KINQKRYTIT FNRAFEQVMR CCAYRPGEDT 100
    WITDLFIKSY TEFHKLGYAH SLEVWDENGK LGGGVYGIAI GNFFAGESMF 150
    SFIPDFGKIG LFHLFETLKK DHFTLFDTQQ LNLVTLSLGA YQIPKKEYLK 200
    RLESAVASGK KWNPSHFVL 219
    Length:219
    Mass (Da):25,596
    Last modified:July 5, 2004 - v1
    Checksum:iE461CFFE1B4FB575
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016823 Genomic DNA. Translation: AAS68730.1.
    RefSeqiYP_000093.1. NC_005823.1.

    Genome annotation databases

    EnsemblBacteriaiAAS68730; AAS68730; LIC_10096.
    GeneIDi2772131.
    KEGGilic:LIC10096.
    PATRICi22371856. VBILepInt6257_0107.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016823 Genomic DNA. Translation: AAS68730.1 .
    RefSeqi YP_000093.1. NC_005823.1.

    3D structure databases

    ProteinModelPortali Q72W44.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 267671.LIC10096.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS68730 ; AAS68730 ; LIC_10096 .
    GeneIDi 2772131.
    KEGGi lic:LIC10096.
    PATRICi 22371856. VBILepInt6257_0107.

    Phylogenomic databases

    KOi K00684.
    OMAi ERFRYPR.
    OrthoDBi EOG6WX4R3.

    Enzyme and pathway databases

    BioCyci LINT267671:GHQI-96-MONOMER.

    Family and domain databases

    HAMAPi MF_00688. Leu_Phe_trans.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR004616. Leu/Phe-tRNA_Trfase.
    [Graphical view ]
    Pfami PF03588. Leu_Phe_trans. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    TIGRFAMsi TIGR00667. aat. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis."
      Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S.
      , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.
      J. Bacteriol. 186:2164-2172(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Fiocruz L1-130.

    Entry informationi

    Entry nameiLFTR_LEPIC
    AccessioniPrimary (citable) accession number: Q72W44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 58 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3