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)

B8FT35

- SYI_DESHD

UniProt

B8FT35 - SYI_DESHD

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Desulfitobacterium hafniense (strain DCB-2 / DSM 10664)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 42 (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 sitei553 – 5531Aminoacyl-adenylateUniRule annotation
    Binding sitei597 – 5971ATPUniRule annotation
    Metal bindingi892 – 8921ZincUniRule annotation
    Metal bindingi895 – 8951ZincUniRule annotation
    Metal bindingi912 – 9121ZincUniRule annotation
    Metal bindingi915 – 9151ZincUniRule 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

    BioCyciDHAF272564:GCV8-4117-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:Dhaf_4041
    OrganismiDesulfitobacterium hafniense (strain DCB-2 / DSM 10664)
    Taxonomic identifieri272564 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium
    ProteomesiUP000007726: 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 – 922922Isoleucine--tRNA ligasePRO_1000189151Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi272564.Dhaf_4041.

    Structurei

    3D structure databases

    ProteinModelPortaliB8FT35.
    SMRiB8FT35. Positions 1-922.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi57 – 6711"HIGH" regionAdd
    BLAST
    Motifi594 – 5985"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.

    B8FT35-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDYRNTLNLP ETDFPMRGNL PQREPEILQK WEEEDIYATV QKARAGRPKF    50
    VLHDGPPYAN GDIHLGHALN KVIKDIIVKY KTMAGFDAPY VPGWDTHGLP 100
    IEQQVIKKLG VNRHAVSVVE FRRMCKEYAK KYISIQKEQF KRLGVRGDWQ 150
    NPYLTLEKEY EAAQIGVFGK MARKKYIYKG LKPVYWCPSC ETALAEAEIE 200
    YAEKTSHAIY VKFPVKEGKG VLTDENTFVI IWTTTPWTLP ANLAITLHEE 250
    FSYVQVQVEK EHWLVAEGML ESLRSLWNLE LPVEKRFVGK ELEGVICKHP 300
    FIERDSVLIL GEHVTLEAGT GCVHTAPGHG EEDFNVGKKY GLPVLCPVDH 350
    QGKFTAEGGA YAGMKVDKAN PVIIEDLKNL HALVHEDKIK HSYAHCWRCN 400
    NPIIYRATEQ WFASIDGFRK AALEEIDKVQ WIPSWGKDRI YNMIADRGDW 450
    CISRQRTWGV PIPIFYCEDC GKEIISDETI AKVQEIFREE GSDAWFLRPA 500
    AELLPEGFTC ACGGKSFRKE TDIMDVWFDS GTSHTSVLME RKELAWPADL 550
    YMEGSDQHRG WFNSSLSTSV AAYGKAPYKA VLTHGFLVDE KGRKMSKSLG 600
    NGVDPLQVTK EMGADILRLW VCAADYKNDV AVSPRIMKQM SEAYRKIRNT 650
    LRFLLSNLND FDPAKDRVAY KDLPEIDRWA LLQLGKVTQR VLQGYEKYEF 700
    HWVYHSVHNF CAVELSAIYL DIVKDRLYVE GKNSTLRRAS QTVLYDVLNA 750
    LVRLMAPVLT YTADEIWPYV PGVPAGSHVQ TEEMPEALPQ WLDEALEKKW 800
    DTLLAVRSEV TKALEKARQD KLINHPLTAQ VDLYPNAELE GFLRGIPNLS 850
    EIFIVSAVQL HSAGEEKPEG LSMAEDLAGF GIAVNSAAGE KCERCWIYDT 900
    GVGENQEHPT LCPRCASVVS HL 922
    Length:922
    Mass (Da):104,696
    Last modified:March 3, 2009 - v1
    Checksum:iB643CE2C0E98E9F2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001336 Genomic DNA. Translation: ACL22051.1.
    RefSeqiWP_015944977.1. NC_011830.1.
    YP_002460487.1. NC_011830.1.

    Genome annotation databases

    EnsemblBacteriaiACL22051; ACL22051; Dhaf_4041.
    GeneIDi7261061.
    KEGGidhd:Dhaf_4041.
    PATRICi21666091. VBIDesHaf15223_4202.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001336 Genomic DNA. Translation: ACL22051.1 .
    RefSeqi WP_015944977.1. NC_011830.1.
    YP_002460487.1. NC_011830.1.

    3D structure databases

    ProteinModelPortali B8FT35.
    SMRi B8FT35. Positions 1-922.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272564.Dhaf_4041.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACL22051 ; ACL22051 ; Dhaf_4041 .
    GeneIDi 7261061.
    KEGGi dhd:Dhaf_4041.
    PATRICi 21666091. VBIDesHaf15223_4202.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci DHAF272564:GCV8-4117-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. "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive anaerobe capable of dehalogenation and metal reduction."
      Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L., Tiedje J.M.
      BMC Microbiol. 12:21-21(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DCB-2 / DSM 10664.

    Entry informationi

    Entry nameiSYI_DESHD
    AccessioniPrimary (citable) accession number: B8FT35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 42 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

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3