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)

Q3Z7P5

- SYI_DEHM1

UniProt

Q3Z7P5 - SYI_DEHM1

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195) (Dehalococcoides ethenogenes (strain 195))
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (27 Sep 2005)
      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 sitei631 – 6311ATPUniRule 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

    BioCyciDETH243164:GJNF-1039-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:DET1038
    OrganismiDehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195) (Dehalococcoides ethenogenes (strain 195))
    Taxonomic identifieri243164 [NCBI]
    Taxonomic lineageiBacteriaChloroflexiDehalococcoidiaDehalococcoidalesDehalococcoidaceaeDehalococcoides
    ProteomesiUP000008289: 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 – 10141014Isoleucine--tRNA ligasePRO_0000098540Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi243164.DET1038.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3Z7P5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi48 – 5811"HIGH" regionAdd
    BLAST
    Motifi628 – 6325"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.
    InterProiIPR002300. 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. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00392. ileS. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q3Z7P5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKAVNPRQN FPQMEEDILK LWQDKGVFKK SIENRRDGKR FTLYEGPPTA     50
    NGRPGIHHVL SRVFKDVIPR YKVMKGYYAP RIGGWDTHGL PVELEVEKEL 100
    GFTSKNDIEK YGIAEFNARC RSSVFKYVSE WNKLTERIAY WVDLDNAYIT 150
    MDNNYIESGW WALKQMWDKG LVYQGHRVTP HCPRCGTSLS SHEVAQGYKD 200
    NTEDPSVFVK FEIAKESLAK AGLAKKWAYP ADKPLYLLAW TTTPWTLPAN 250
    TALAVSAADQ YAILDMTDYY MILAKPRLSA LKLAENPVAG ECLGSDLSGL 300
    FYKPLFDPRE FGIPVRNMQD NSETGVSEEL LYPVITTSYV SMDDGTGIVH 350
    TAPAYGELDY ESGVKYGLKF VHHVDLQGRI TGSYPFAGKF VKEADKDISR 400
    NLKERGLMFR NERMHHTYPF CWRCDSPLIY YAKQSWYIRT TAVRDELIKG 450
    NQQINWYPEH IKDGRFGDWL ENNIDWAFSR ERYWGTPVPI WRCEKCGRTE 500
    CVGGIDELKA KPNFKGMQEK LDIHRPYVDE WTYDCDKCGG NMKRVTEVMD 550
    CWYDSGAMPV AQYHYPFEPE SRSIAKDGRF PADYICEAVD QTRGWFYSLH 600
    AISTLIFNRP CYQNVICLGH ILDERGEKMS KSRNNVIQPA TVLDKYGADA 650
    VRWYFYTAAP PGNARRFSEK LVGEVTRQFL LMLWNVYSFF VTYANIDSFT 700
    PSEKYLEGEV PELDRWILSE LNQLVLDVDK GLDNYDPTQA GRRIEDFVGY 750
    LSNWYVRRSR RRFWKSENDA DKLSAYQALY TCLVTLSRLL APFTPFVAEE 800
    LYQNLVLSAD PSALESVHLT DFPVADTALI DEQLDNEIRL VMKVSSMGRS 850
    ARSKAALKVR QPLAEVRVVL ASAGERTGLM RLAEQVLEEL NVKALAVEEP 900
    GTVIPEKNYA ASTEGAYTVA VYTGLSPELL AEGTAREIVH RLQTMRKSAG 950
    FEIADYINTH YQADEYLDSV IRMHSEYIKK ETLSNQLIKG NAPEGAYAES 1000
    LDIDGHSLSL WVAR 1014
    Length:1,014
    Mass (Da):116,015
    Last modified:September 27, 2005 - v1
    Checksum:iDBA88E1091CC8AE2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000027 Genomic DNA. Translation: AAW39707.1.
    RefSeqiWP_010936733.1. NC_002936.3.
    YP_181754.1. NC_002936.3.

    Genome annotation databases

    EnsemblBacteriaiAAW39707; AAW39707; DET1038.
    GeneIDi3229669.
    KEGGidet:DET1038.
    PATRICi21609123. VBIDehEth89364_0979.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000027 Genomic DNA. Translation: AAW39707.1 .
    RefSeqi WP_010936733.1. NC_002936.3.
    YP_181754.1. NC_002936.3.

    3D structure databases

    ProteinModelPortali Q3Z7P5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243164.DET1038.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW39707 ; AAW39707 ; DET1038 .
    GeneIDi 3229669.
    KEGGi det:DET1038.
    PATRICi 21609123. VBIDehEth89364_0979.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci DETH243164:GJNF-1039-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_02003. Ile_tRNA_synth_type2.
    InterProi 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. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsi TIGR00392. ileS. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-2266 / KCTC 15142 / 195.

    Entry informationi

    Entry nameiSYI_DEHM1
    AccessioniPrimary (citable) accession number: Q3Z7P5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 64 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