Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

A9NG38

- SYI_ACHLI

UniProt

A9NG38 - SYI_ACHLI

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Acholeplasma laidlawii (strain PG-8A)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).UniRule annotation

    Catalytic activityi

    ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei543 – 5431Aminoacyl-adenylateUniRule annotation
    Binding sitei587 – 5871ATPUniRule annotation
    Metal bindingi869 – 8691ZincUniRule annotation
    Metal bindingi872 – 8721ZincUniRule annotation
    Metal bindingi885 – 8851ZincUniRule annotation
    Metal bindingi888 – 8881ZincUniRule annotation

    GO - Molecular functioni

    1. aminoacyl-tRNA editing activity Source: InterPro
    2. ATP binding Source: UniProtKB-HAMAP
    3. isoleucine-tRNA ligase activity Source: UniProtKB-HAMAP
    4. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. isoleucyl-tRNA aminoacylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciALAI441768:GI40-702-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoleucine--tRNA ligaseUniRule annotation (EC:6.1.1.5UniRule annotation)
    Alternative name(s):
    Isoleucyl-tRNA synthetaseUniRule annotation
    Short name:
    IleRSUniRule annotation
    Gene namesi
    Name:ileSUniRule annotation
    Ordered Locus Names:ACL_0702
    OrganismiAcholeplasma laidlawii (strain PG-8A)
    Taxonomic identifieri441768 [NCBI]
    Taxonomic lineageiBacteriaTenericutesMollicutesAcholeplasmatalesAcholeplasmataceaeAcholeplasma
    ProteomesiUP000008558: 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 – 896896Isoleucine--tRNA ligasePRO_1000216231Add
    BLAST

    Proteomic databases

    PRIDEiA9NG38.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi441768.ACL_0702.

    Structurei

    3D structure databases

    ProteinModelPortaliA9NG38.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi57 – 6711"HIGH" regionAdd
    BLAST
    Motifi584 – 5885"KMSKS" region

    Domaini

    IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).UniRule annotation

    Sequence similaritiesi

    Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0060.
    HOGENOMiHOG000246402.
    KOiK01870.
    OMAiKPVHWCL.
    OrthoDBiEOG644ZM1.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPiMF_02002. Ile_tRNA_synth_type1.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    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:SF9. PTHR11946:SF9. 1 hit.
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    [Graphical view]
    PRINTSiPR00984. TRNASYNTHILE.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00392. ileS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A9NG38-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNYKDTLLMP KTDFEMRGNL GKREPEIQKH WESIDLYNKV LEKNKDNTPF    50
    VLHDGPPYAN NNIHIGHAFQ KTLKDFVLRY QTMSGRYTPY IPGWDTHGLP 100
    IENEVTKSGV DRKQLTRAEF RKICREYAIK QVEVQRAQFK RLGILGDWDN 150
    PYLTLDKSYI ADQVRVFSQM VDKGIIYKGL KPIYWSPSSE SAFAEAEIEY 200
    MDKQSKSIYV GFDMMGDKFP NTKLLIWTTT PWTLPANLAV SVHPNFDYVW 250
    FNNDGKNYIA LKELLPKLVE KLGFSHAKVL KEFKGSTLEF MNYKHPLYDR 300
    VSPIILGEHV TAEDGTGLVH TAPGHGEDDY FVGKKYNLDL LSPVDEKGHM 350
    TEEAGPYAGM FYEKANAQIV EDLRENGHLL YDETITHSYP HDWRTKKPVI 400
    FRSTPQWFAS IDMLKGDLLE AIKGVKWHTS WGEVRLTNMI KDRNDWVISR 450
    QRVWGVPIPI FYDNENNPLL DRKLIDHVAS LFEVHGSDIW YEWDVEKLLP 500
    SDYEGPRDLT KELDIMDVWF DSGTSYNILK RRGLPFPADM YLEGSDQYRG 550
    WFNSSLTTAI AVDGVSPYKE IVSHGFVLDG KGRKMSKSLG NVIDPLTVMN 600
    DQGADVLRLW VASVDYEADV RISNDLMKQV SESYRKFRNT FRFMLGVLDG 650
    FNPEVNYIGW SMRGQLNRVM TDKYYVLATK VNESYAKYNF VEVTRLIIPF 700
    VVNDLSAFYL DYTKDSLYCD AEDDFERRAI QSTIYDILLG LLRLLTPIMP 750
    HTTSEAYDSL KYKEYDNIYL EKMPIGGKLK EPKLQENYDI FDELRNHVLK 800
    HLELAREAKV IGKSLDAHLD LSVDQTTYDA LEYLDLLNKL DKILIVSSVH 850
    ITKADQLDIK VSKADGHVCA RCWNIVKEVN QNDVCVRCES VLEGLK 896
    Length:896
    Mass (Da):103,532
    Last modified:February 5, 2008 - v1
    Checksum:i9BBDA617784DDC24
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000896 Genomic DNA. Translation: ABX81318.1.
    RefSeqiYP_001620694.1. NC_010163.1.

    Genome annotation databases

    EnsemblBacteriaiABX81318; ABX81318; ACL_0702.
    GeneIDi5803218.
    KEGGiacl:ACL_0702.
    PATRICi20638124. VBIAchLai134690_0682.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000896 Genomic DNA. Translation: ABX81318.1 .
    RefSeqi YP_001620694.1. NC_010163.1.

    3D structure databases

    ProteinModelPortali A9NG38.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 441768.ACL_0702.

    Proteomic databases

    PRIDEi A9NG38.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABX81318 ; ABX81318 ; ACL_0702 .
    GeneIDi 5803218.
    KEGGi acl:ACL_0702.
    PATRICi 20638124. VBIAchLai134690_0682.

    Phylogenomic databases

    eggNOGi COG0060.
    HOGENOMi HOG000246402.
    KOi K01870.
    OMAi KPVHWCL.
    OrthoDBi EOG644ZM1.

    Enzyme and pathway databases

    BioCyci ALAI441768:GI40-702-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_02002. Ile_tRNA_synth_type1.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    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:SF9. PTHR11946:SF9. 1 hit.
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00984. TRNASYNTHILE.
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsi TIGR00392. ileS. 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: PG-8A.

    Entry informationi

    Entry nameiSYI_ACHLI
    AccessioniPrimary (citable) accession number: A9NG38
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 57 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