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)

Q88V89

- SYI_LACPL

UniProt

Q88V89 - SYI_LACPL

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 sitei556 – 5561Aminoacyl-adenylateUniRule annotation
    Binding sitei600 – 6001ATPUniRule annotation
    Metal bindingi891 – 8911ZincUniRule annotation
    Metal bindingi894 – 8941ZincUniRule annotation
    Metal bindingi911 – 9111ZincUniRule annotation
    Metal bindingi914 – 9141ZincUniRule 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

    BioCyciLPLA220668-WGS:GSPK-1868-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:lp_2187
    OrganismiLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
    Taxonomic identifieri220668 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
    ProteomesiUP000000432: 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 – 932932Isoleucine--tRNA ligasePRO_0000098403Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi220668.lp_2187.

    Structurei

    3D structure databases

    ProteinModelPortaliQ88V89.
    SMRiQ88V89. Positions 1-920.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi57 – 6711"HIGH" regionAdd
    BLAST
    Motifi597 – 6015"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.
    OMAiERLMLHQ.

    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.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view]
    PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 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.

    Q88V89-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRVKETLNLG KTKFKMRGNL PVKEVERQNV WAENKVYEQR QKLNEGKPSF    50
    ILHDGPPYAN GDIHMGHALN KITKDFIVRY KSMNGFRAPY VPGWDTHGLP 100
    IEQKLKQAGY DRKKMTDNEF RELCRKYALE QVDRQRDEFK RLGVAGEWDN 150
    PYLTLKPEFE AAQVRVFGAF AKRHLIYRGQ KPVFWSWSSE SALAEAEVEY 200
    HDVTSPSAFY GEHVIDGKGV LDDDTYMVVW TTTPWTIPAS EGITIDASFD 250
    YVVVQPAGEN RKFVLAAELL DENAERFGWE DVQVLKTVKG AELENILCEH 300
    PFDNSRHLVT MLGDFVTLDS GTGLVHTAPG YGEDDYRIGK QYDLPIFAPV 350
    DDKGFLTAEA GDDFAGVFYD DANKIALDKL KAAGLLLKYM PYEHSYPFDW 400
    RTKKPIIFRA TPQWFASVGD MRDEILKSMD DVEFFPEWGK KRLYNMIRDR 450
    GDWVISRQRV WGVPLPIFYA EDGTAIMDEV TINHVADLFG KYGSNVWFER 500
    DAKDLLPDGY TNEHSPNGTF TKETDIMDVW FDSGSSHQGV LAERSYLDYP 550
    ADLYLEGSDQ YRGWFNSSLI TSVAVSGHAP YKQVLSQGFT LDNQGRKMSK 600
    SLGNTIAPAD VIKQMGAEIV RMWVASVDTS SDVRVSMESF KQVADSYKKF 650
    RNTVRFMLGN TADFDPKANR VAYEDLASVD QYMETRLNEF VAETKDHYDH 700
    YDFLDIYKKL INFLTVDLSN FYLDIAKDIM YIDAEDSHSR RSMQTVFYDV 750
    LVALTKLFTP MLPHTTEEIW PFLKEPEEFA QLAEMPAVQN YANSDELMAQ 800
    WTRFMDLRSN VLKALEEARD AKLIGKSLEA HLDLYVDDDT QAFLDHLNTN 850
    VRQMLMVSAL DLHALSDAPE DAETFGDTLA IKVGHADGDV CDRCRMVKTD 900
    VGSDEAYPML CARCAAIVRE NYPESVTTGL EA 932
    Length:932
    Mass (Da):106,318
    Last modified:June 1, 2003 - v1
    Checksum:i559234B1D9AD149E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL935263 Genomic DNA. Translation: CCC79407.1.
    RefSeqiWP_011101679.1. NC_004567.2.
    YP_004889921.1. NC_004567.2.

    Genome annotation databases

    EnsemblBacteriaiCCC79407; CCC79407; lp_2187.
    GeneIDi1063600.
    KEGGilpl:lp_2187.
    PATRICi22250415. VBILacPla27411_1848.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL935263 Genomic DNA. Translation: CCC79407.1 .
    RefSeqi WP_011101679.1. NC_004567.2.
    YP_004889921.1. NC_004567.2.

    3D structure databases

    ProteinModelPortali Q88V89.
    SMRi Q88V89. Positions 1-920.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 220668.lp_2187.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCC79407 ; CCC79407 ; lp_2187 .
    GeneIDi 1063600.
    KEGGi lpl:lp_2187.
    PATRICi 22250415. VBILacPla27411_1848.

    Phylogenomic databases

    eggNOGi COG0060.
    HOGENOMi HOG000246402.
    KOi K01870.
    OMAi ERLMLHQ.

    Enzyme and pathway databases

    BioCyci LPLA220668-WGS:GSPK-1868-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.
    IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
    [Graphical view ]
    PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    PF06827. zf-FPG_IleRS. 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: ATCC BAA-793 / NCIMB 8826 / WCFS1.

    Entry informationi

    Entry nameiSYI_LACPL
    AccessioniPrimary (citable) accession number: Q88V89
    Secondary accession number(s): F9UQB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 78 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