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)

Q9ZCU4

- SYI_RICPR

UniProt

Q9ZCU4 - SYI_RICPR

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Rickettsia prowazekii (strain Madrid E)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      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

    Zinc.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei627 – 6271ATPUniRule 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

    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:RP617
    OrganismiRickettsia prowazekii (strain Madrid E)
    Taxonomic identifieri272947 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
    ProteomesiUP000002480: 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 – 10861086Isoleucine--tRNA ligasePRO_0000098560Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272947.RP617.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZCU4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi53 – 6311"HIGH" regionAdd
    BLAST
    Motifi624 – 6285"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 2 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0060.
    HOGENOMiHOG000246403.
    KOiK01870.
    OMAiRVEHMVE.
    OrthoDBiEOG644ZM1.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.40.50.620. 2 hits.
    3.90.740.10. 1 hit.
    HAMAPiMF_02003. Ile_tRNA_synth_type2.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023586. Ile-tRNA-ligase_type2.
    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]
    PfamiPF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    [Graphical view]
    PRINTSiPR00984. TRNASYNTHILE.
    SUPFAMiSSF47323. SSF47323. 2 hits.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00392. ileS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ZCU4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTNTKYYPDV SANVDFAAIE QEILKFWQNN NIFQKSIDYR NGESEFIFYD     50
    GPPFANGLPH YGHLLTGFIK DVYARYKTIK GKKVERRFGW DCHGLPAEMQ 100
    SEKELGISGR IAITNFGIEK FNNHCRASVM QYASEWEQYV TRQARWVAFK 150
    NAYKTMDKNF MESVLWAFKE LYNKDLLYES MRVMPYSWAC ETPLSNFETR 200
    LDNAYRERTD KAITVSFVLN EVTLINGIIS QKSDMKEGDN FKEYRILAWT 250
    TTPWTLPANL ALAVGSDIDY AFVDKNEVCY IIAASSVAKY AKELGLSGKE 300
    NFEIIKGLKL QGLSYKPLFN YFENHPNSFK IFASDFVVEG DGTGIVHMAP 350
    GFGEDDQILC ESKGIELVCP VDNSGKFTKE IPDLEGVQVF DANDKIIIKL 400
    KEQGNWIKTE QYIHNYPHCW RTDTPLIYKA VPSWYVRVTK FKDRMVELNQ 450
    QINWIPHNVK DNLFGKWLEN ARDWSISRNR FWGTPLPVWK SDDPKYPRID 500
    VYGSIEEIEK DFGVKINDLH RPFIDELTRT NPDDPTGKST MRRIDDVFDC 550
    WFESGSMPYG QVHYPFENKK WFVEHFPADF IVEYSSQTRG WFYTLMVLST 600
    ALFDRPPFLN CICHGVILDA TGQKLSKRLN NYADPLELFD KYGSDALRVT 650
    MLSSNVVKGQ ELLIDKDGKM VFDTLRLFIK PIWNAYHFFT IYANADSLKG 700
    TLNFASQNVL DVYILSKLKI AVNKIEESLD NFDTQTAYHA VSEFFEVLNN 750
    WYIRRSRARF WKNEKDTDKQ NAYNTLYSCL KIMTIAMSAL IPMISETIYQ 800
    GLHNTAITQL NCLLSEGKHI VQNPMSDTQD YNTSVHLCNY PTLSDFEINY 850
    ELVSTMDNVL DICSNSLFIR STENIRVRQP LACITIISKH NNNLKDFEDL 900
    IKDEINVKTV IYRDDLENYA RKKLSLNFAI LGKRLPHKMK AIIDAAKKGE 950
    WEATTLGLAI CGEILNSDEY TLILEPYSHI KGTANFDNNS SLLILNLELT 1000
    SELIEEGYAR DIVRFIQYAR KEADFSITDR ILIEIISEFD LSKIIDHYGD 1050
    FIKEQTLGEF AKNFTPDYVS KVALENNQIQ LKVKRL 1086
    Length:1,086
    Mass (Da):125,637
    Last modified:May 1, 1999 - v1
    Checksum:iDEC857A0D81E5963
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ235272 Genomic DNA. Translation: CAA15060.1.
    PIRiB71667.
    RefSeqiNP_220984.1. NC_000963.1.

    Genome annotation databases

    EnsemblBacteriaiCAA15060; CAA15060; CAA15060.
    GeneIDi883643.
    KEGGirpr:RP617.
    PATRICi17902053. VBIRicPro72556_0636.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ235272 Genomic DNA. Translation: CAA15060.1 .
    PIRi B71667.
    RefSeqi NP_220984.1. NC_000963.1.

    3D structure databases

    ProteinModelPortali Q9ZCU4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272947.RP617.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAA15060 ; CAA15060 ; CAA15060 .
    GeneIDi 883643.
    KEGGi rpr:RP617.
    PATRICi 17902053. VBIRicPro72556_0636.

    Phylogenomic databases

    eggNOGi COG0060.
    HOGENOMi HOG000246403.
    KOi K01870.
    OMAi RVEHMVE.
    OrthoDBi EOG644ZM1.

    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_02003. Ile_tRNA_synth_type2.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023586. Ile-tRNA-ligase_type2.
    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 ]
    Pfami PF08264. Anticodon_1. 1 hit.
    PF00133. tRNA-synt_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00984. TRNASYNTHILE.
    SUPFAMi SSF47323. SSF47323. 2 hits.
    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: Madrid E.

    Entry informationi

    Entry nameiSYI_RICPR
    AccessioniPrimary (citable) accession number: Q9ZCU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 85 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. Rickettsia prowazekii
      Rickettsia prowazekii (strain Madrid E): entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3