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C3LLZ2

- C3LLZ2_VIBCM

UniProt

C3LLZ2 - C3LLZ2_VIBCM

Protein

Asparagine--tRNA ligase

Gene

asnS

Organism
Vibrio cholerae serotype O1 (strain M66-2)
Status
Unreviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn).UniRule annotationSAAS annotation

    GO - Molecular functioni

    1. asparagine-tRNA ligase activity Source: UniProtKB-EC
    2. ATP binding Source: UniProtKB-KW
    3. nucleic acid binding Source: InterPro

    GO - Biological processi

    1. asparaginyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetaseUniRule annotationSAAS annotationImported, Ligase

    Keywords - Biological processi

    Protein biosynthesisUniRule annotationSAAS annotation

    Keywords - Ligandi

    ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciVCHO579112:GJAW-1318-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Asparagine--tRNA ligaseUniRule annotation (EC:6.1.1.22UniRule annotation)
    Alternative name(s):
    Asparaginyl-tRNA synthetaseUniRule annotation
    Gene namesi
    Name:asnSUniRule annotationImported
    Ordered Locus Names:VCM66_1252Imported
    OrganismiVibrio cholerae serotype O1 (strain M66-2)Imported
    Taxonomic identifieri579112 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000001217: Chromosome I

    Subcellular locationi

    Cytoplasm UniRule annotationSAAS annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotationSAAS annotation

    PTM / Processingi

    Proteomic databases

    PRIDEiC3LLZ2.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi579112.VCM66_1252.

    Structurei

    3D structure databases

    ProteinModelPortaliC3LLZ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0017.
    HOGENOMiHOG000226033.
    KOiK01893.
    OMAiAIHRFFH.
    OrthoDBiEOG6ZSP6X.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    HAMAPiMF_00534. Asn_tRNA_synth.
    InterProiIPR004364. aa-tRNA-synt_II.
    IPR018150. aa-tRNA-synt_II-like.
    IPR006195. aa-tRNA-synth_II.
    IPR004522. Asn-tRNA-ligase.
    IPR002312. Asp/Asn-tRNA-synth_IIb.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view]
    PANTHERiPTHR22594. PTHR22594. 1 hit.
    PTHR22594:SF6. PTHR22594:SF6. 1 hit.
    PfamiPF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view]
    PRINTSiPR01042. TRNASYNTHASP.
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00457. asnS. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C3LLZ2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALGCLYIST ETVINMTYAP VNDVLSGKLA VDSEVTVRGW IRTRRDSKAG    50
    ISFLAIYDGS CFNPIQAVVP NNLNNYDNEV LKLTTGCSVE VTGKIVESPA 100
    SGQAFELAAS DVKVVGWVED ADTYPMAKTR HSIEYLREVA HLRPRTNVIG 150
    AVARVRNCLA QAIHRFYHEQ GYFWVSAPLI TASDAEGAGE MFRVSTLDME 200
    NLPRTDAGKV DYNQDFFGKE TFLTVSGQLN AEAYACAISK VYTFGPTFRA 250
    ENSNTSRHLA EFWMVEPEVA FADLNTVAKL AEDMLKYVFK AVLAERRDDL 300
    EFFNDRINNE VIARLEQFVE SDFAQVDYTD AIEILKNCGK TFEFPVEWGI 350
    DLASEHERFL AEEHFKAPVI VKNYPKDIKA FYMRMNEDGK TVAAMDVLAP 400
    GIGEIIGGSQ REERLDILDA RMREFGIDPE HMDWYRDLRR YGTVPHAGFG 450
    LGFERLVSYV TGMGNVRDVI PFPRTPRSAS F 481
    Length:481
    Mass (Da):54,065
    Last modified:June 16, 2009 - v1
    Checksum:iE473289C857E4C41
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001233 Genomic DNA. Translation: ACP05568.1.
    RefSeqiWP_001881065.1. NC_012578.1.
    YP_002810019.1. NC_012578.1.

    Genome annotation databases

    EnsemblBacteriaiACP05568; ACP05568; VCM66_1252.
    GeneIDi7772529.
    KEGGivcm:VCM66_1252.
    PATRICi20066285. VBIVibCho108967_1193.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001233 Genomic DNA. Translation: ACP05568.1 .
    RefSeqi WP_001881065.1. NC_012578.1.
    YP_002810019.1. NC_012578.1.

    3D structure databases

    ProteinModelPortali C3LLZ2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 579112.VCM66_1252.

    Proteomic databases

    PRIDEi C3LLZ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACP05568 ; ACP05568 ; VCM66_1252 .
    GeneIDi 7772529.
    KEGGi vcm:VCM66_1252.
    PATRICi 20066285. VBIVibCho108967_1193.

    Phylogenomic databases

    eggNOGi COG0017.
    HOGENOMi HOG000226033.
    KOi K01893.
    OMAi AIHRFFH.
    OrthoDBi EOG6ZSP6X.

    Enzyme and pathway databases

    BioCyci VCHO579112:GJAW-1318-MONOMER.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    HAMAPi MF_00534. Asn_tRNA_synth.
    InterProi IPR004364. aa-tRNA-synt_II.
    IPR018150. aa-tRNA-synt_II-like.
    IPR006195. aa-tRNA-synth_II.
    IPR004522. Asn-tRNA-ligase.
    IPR002312. Asp/Asn-tRNA-synth_IIb.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view ]
    PANTHERi PTHR22594. PTHR22594. 1 hit.
    PTHR22594:SF6. PTHR22594:SF6. 1 hit.
    Pfami PF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view ]
    PRINTSi PR01042. TRNASYNTHASP.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00457. asnS. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A recalibrated molecular clock and independent origins for the cholera pandemic clones."
      Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
      PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: M66-2Imported.

    Entry informationi

    Entry nameiC3LLZ2_VIBCM
    AccessioniPrimary (citable) accession number: C3LLZ2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 16, 2009
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 42 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3