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)

B8F5E2

- SYI_HAEPS

UniProt

B8F5E2 - SYI_HAEPS

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Haemophilus parasuis serovar 5 (strain SH0165)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 1 (03 Mar 2009)
      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 sitei562 – 5621Aminoacyl-adenylateUniRule annotation
    Binding sitei606 – 6061ATPUniRule annotation
    Metal bindingi901 – 9011ZincUniRule annotation
    Metal bindingi904 – 9041ZincUniRule annotation
    Metal bindingi921 – 9211ZincUniRule annotation
    Metal bindingi924 – 9241ZincUniRule 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

    BioCyciHPAR557723:GH24-916-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:HAPS_0916
    OrganismiHaemophilus parasuis serovar 5 (strain SH0165)
    Taxonomic identifieri557723 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000006743: 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 – 938938Isoleucine--tRNA ligasePRO_1000189168Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi557723.HAPS_0916.

    Structurei

    3D structure databases

    ProteinModelPortaliB8F5E2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi58 – 6811"HIGH" regionAdd
    BLAST
    Motifi603 – 6075"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.
    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.

    B8F5E2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDYKNTLNL PETGFPMRGD LAKREPAMLQ NWHDKKLYQK IREASKGKRS    50
    FILHDGPPYA NGNIHLGHAV NHILKDIINK SKTAMGFDTP YVPGWDCHGL 100
    PIELKVEGLV GKPNENISAS EFRQKCREYA KEQVDGQKAD FMRLGILGDW 150
    DNPYLTMNFD TEAHIIRTLG KVIANGHLYK GSKPVHWCLD CGSSLAEAEV 200
    EYEDKVSPSI YVRFSAVDPV AVEAKFNAQG KGSGQISAVI WTTTPWTLPS 250
    NRAIALNSEL EYQLVQFGDE RVILATELVE AVQKVTGVEQ VEVLGSAKGS 300
    DLELMRFNHP FYDFSVPFIL GDHVTTDGGT GLVHTAPDHG LDDYIVGQKY 350
    KLEMAGLVAN DGKFISTTPF FAGKGVFETN DLVLEKLKET GALLKLERIK 400
    HSYPHCWRHK TPIIFRATPQ WFIGMETQGL RKQALGEIKR VRWIPSWGEA 450
    RIDTMVANRP DWCISRQRTW GVPMTMFVHN ETEQLHPRTL EILEEVAKRV 500
    EQAGIQAWWD LDPKEVLGEE DAKIYRKVPD TLDVWFDSGS TYASVVQQRP 550
    EFNGNSADMY LEGSDQHRGW FMSSLMLSTA TDNKAPYNQV LTHGFTVDEK 600
    GRKMSKSLGN VIVPSEVWNK NGADILRLWV ASTDYTGEIA VSHNILNSAG 650
    DTYRRIRNTA RFLLANLNGF DPKRDLVKPE EMIALDRWAV SCALDAQNDI 700
    KEAYDNYQFH TVVQRLMRFC SIEMGSFYLD IIKDRQYTTK ADSLARRSCQ 750
    TALWHISEAL VRWIAPILSF TADEIWGYLP QVEGRSEFVF TEEFYTDLFG 800
    LSESDKLDDN YWQKLLKVRA EVNRVLEQAR NDKLIGAALE AKVTVYANDD 850
    IRPLLEQLGN ELGFVLITSQ AIVKPLAEAD VAEGELAGLA VKVERADGEK 900
    CPRCWHYATD IGANAEHAEI CGRCVENVVG EGETRNFA 938
    Length:938
    Mass (Da):105,815
    Last modified:March 3, 2009 - v1
    Checksum:iCAF030ADACA7BC38
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001321 Genomic DNA. Translation: ACL32544.1.
    RefSeqiYP_002475492.1. NC_011852.1.

    Genome annotation databases

    EnsemblBacteriaiACL32544; ACL32544; HAPS_0916.
    GeneIDi7277067.
    KEGGihap:HAPS_0916.
    PATRICi20194105. VBIHaePar127548_0914.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001321 Genomic DNA. Translation: ACL32544.1 .
    RefSeqi YP_002475492.1. NC_011852.1.

    3D structure databases

    ProteinModelPortali B8F5E2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 557723.HAPS_0916.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACL32544 ; ACL32544 ; HAPS_0916 .
    GeneIDi 7277067.
    KEGGi hap:HAPS_0916.
    PATRICi 20194105. VBIHaePar127548_0914.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci HPAR557723:GH24-916-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. "Complete genome sequence of Haemophilus parasuis SH0165."
      Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R., Jin M., Jin Q., Chen H.
      J. Bacteriol. 191:1359-1360(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: SH0165.

    Entry informationi

    Entry nameiSYI_HAEPS
    AccessioniPrimary (citable) accession number: B8F5E2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 41 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