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Q898V2

- SYL_CLOTE

UniProt

Q898V2 - SYL_CLOTE

Protein

Leucine--tRNA ligase

Gene

leuS

Organism
Clostridium tetani (strain Massachusetts / E88)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (20 Jun 2003)
      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 sitei575 – 5751ATPUniRule 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

    BioCyciCTET212717:GJAM-296-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:CTC_00337
    OrganismiClostridium tetani (strain Massachusetts / E88)
    Taxonomic identifieri212717 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    ProteomesiUP000001412: 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 – 812812Leucine--tRNA ligasePRO_0000152004Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi212717.CTC00337.

    Structurei

    3D structure databases

    ProteinModelPortaliQ898V2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi40 – 5112"HIGH" regionAdd
    BLAST
    Motifi572 – 5765"KMSKS" region

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0495.
    KOiK01869.
    OMAiDKPKYYA.
    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.
    InterProiIPR002300. 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. 2 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.

    Sequencei

    Sequence statusi: Complete.

    Q898V2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNYGTNIDR KWQNKWEDSN LYHFDTNNLD KKLYVLEMFS YPSGSNLHAG    50
    HWFNYGPSDS WARFKRMQGF NVFQPMGFDS FGLPAENYAI KTGVHPKDST 100
    MKNIETMTKQ LKSMGAMFHW DNEVITSEPE YYKWTQWMFL QLYKNNLAYR 150
    KNAPVNWCPS CNTVLANEQV LDGACERCSS DVIKKDLTQW FFKITDYAEE 200
    LLEKLDDLDW PENTKSMQKH WIGKSIGAQL TFKIVDSDLS FDIFTTRADT 250
    LFGVTYAVLA PENPLVDKIT KEDHKAEIEA YKEQAKKQSE IERQSITREK 300
    TGVFTGSYAI NPINGKKVPV WVGDYVLSTY GTGAVMAVPA HDERDFEFAK 350
    KHNLPIEKVI EGGETLPYTE DGIMINSEEF NGLESSKGRS AVVEKLEKEN 400
    LGVKKINYRL RDWLVSRQRY WGAPIPIVYC DKCGTVAVPE EQLPVKLPYD 450
    VEFTPDGKSP LSKCDSFVNT TCPTCGGPAK REVDTLDTFV CSSWYFLRYA 500
    DNKNSEKAFD PKIINEILPV DKYVGGPEHA CMHLLYARFF TKALRDMGYL 550
    NFDEPFSSLT HQGLILGPDG LKMSKSKGNT ISPDDYIDEF GSDVFRMYLM 600
    FGFDYTEGGA WSDEGIKSVS RFVDRVERTL ASCRYYINNP SDDKITIDNN 650
    EKDLNFVRHN SIKSITEDAE KMQFNTCIAR LMEYTNALSK YINEDNKNSK 700
    FLKECVEDFI ILIAPFAPHF SEEQWELLGM TYSVFNEKWP QFDSKALVKD 750
    EIEIAVQVNG KIRDRITIAS GLDEESIKET ALNSEDVKKY TDGKNIVKII 800
    IIKGRLVNIV VK 812
    Length:812
    Mass (Da):93,037
    Last modified:June 20, 2003 - v1
    Checksum:i230DDDDC5F31CB2D
    GO

    Sequence cautioni

    The sequence AAO34977.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015927 Genomic DNA. Translation: AAO34977.1. Different initiation.
    RefSeqiNP_781040.1. NC_004557.1.

    Genome annotation databases

    EnsemblBacteriaiAAO34977; AAO34977; CTC_00337.
    GeneIDi1059914.
    KEGGictc:CTC00337.
    PATRICi19508494. VBICloTet101274_0304.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE015927 Genomic DNA. Translation: AAO34977.1 . Different initiation.
    RefSeqi NP_781040.1. NC_004557.1.

    3D structure databases

    ProteinModelPortali Q898V2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 212717.CTC00337.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO34977 ; AAO34977 ; CTC_00337 .
    GeneIDi 1059914.
    KEGGi ctc:CTC00337.
    PATRICi 19508494. VBICloTet101274_0304.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci CTET212717:GJAM-296-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 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. 2 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.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Massachusetts / E88.

    Entry informationi

    Entry nameiSYL_CLOTE
    AccessioniPrimary (citable) accession number: Q898V2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: June 20, 2003
    Last modified: October 1, 2014
    This is version 75 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