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)

A0AKC5

- SYI_LISW6

UniProt

A0AKC5 - SYI_LISW6

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 61 (01 Oct 2014)
      Sequence version 1 (28 Nov 2006)
      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 sitei552 – 5521Aminoacyl-adenylateUniRule annotation
    Binding sitei596 – 5961ATPUniRule annotation
    Metal bindingi888 – 8881ZincUniRule annotation
    Metal bindingi891 – 8911ZincUniRule annotation
    Metal bindingi908 – 9081ZincUniRule annotation
    Metal bindingi911 – 9111ZincUniRule 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

    BioCyciLWEL386043:GI5X-2089-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:lwe2039
    OrganismiListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
    Taxonomic identifieri386043 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
    ProteomesiUP000000779: 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 – 921921Isoleucine--tRNA ligasePRO_1000022090Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi386043.lwe2039.

    Structurei

    3D structure databases

    ProteinModelPortaliA0AKC5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi57 – 6711"HIGH" regionAdd
    BLAST
    Motifi593 – 5975"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.
    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.

    A0AKC5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEYKDTLLMP KTDFPMRGNL PNKEPEWQAK WEEEKLYEKI QEKNTGRKAY    50
    ILHDGPPYAN GELHMGHALN KTIKDIIVRY KSMAGFSSPY VPGWDTHGLP 100
    IETAIAKKGV KRKEMSIAEF RKLCAEYAMT QVDGQRTGFK RLGINGDWEN 150
    PYITLLPEYE AEQIKVFGEM AKKGYIYKGK KPVYWSPSSE SALAEAEIEY 200
    QDKKSASIFV AFKVTDGKGV LDEGTNIVIW TTTPWTIPAN MGITVNPDLD 250
    YVVIESAGEK YVVAEALLPN LREKLGFEDA TVVKTVRGSE LDRIVTKHPF 300
    YDRDSLVMNG EHATAEAGTG AVHTAPGHGE DDFLIGKKYD LEILAPLDDR 350
    GVFTDEAPGF EGVFYDTANK MVTEKLEEVG ALLKMEFITH SYPHDWRTKK 400
    PVIFRATAQW FASIDAFRDD LLKAVKGVNW TPAWGETRLF NMVRDRGDWV 450
    ISRQRAWGVP LPIFYAENGE AIITDETINH ISELFREHGS NVWFERDVKD 500
    LLPDGFTHPG SPNGEFTKET DIMDVWFDSG SSHQAVLNAR PELTRPADLY 550
    MEGSDQYRGW FNSSLTTAVA ITGEAPYRNV LSHGFALDGE GRKMSKSLGN 600
    TLLPGKVIKQ LGADIVRLWV ASVDYQADVR VSDEILKQVS EVYRKIRNTM 650
    RFLLGNINDF NPTTNTVSYE NLREVDKYML IKLNDLVKNV KDSYEAFEFS 700
    TIYHQINNFC TVELSQFYMD FAKDVVYIEA ADSNDRRAMQ TVFYEAAVTL 750
    TKLLAPILPH TTEEVWNSLI GEGAESIHLQ DLPDVKVLAD SEEITAKWDA 800
    FMQIRDNVQK ALEFARNEKL IGKSMLAKVT LYVDGEAKTL FDSLEGDFAQ 850
    LFIVSDFELV EGLENAPESA FKSNQVAVQI TVAEGETCER CRVVKKDVGV 900
    DPKHPTLCGR CADIVVKHYE A 921
    Length:921
    Mass (Da):103,975
    Last modified:November 28, 2006 - v1
    Checksum:i4904C325059D8CF7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM263198 Genomic DNA. Translation: CAK21457.1.
    RefSeqiWP_011702803.1. NC_008555.1.
    YP_850236.1. NC_008555.1.

    Genome annotation databases

    EnsemblBacteriaiCAK21457; CAK21457; lwe2039.
    GeneIDi4465263.
    KEGGilwe:lwe2039.
    PATRICi20331285. VBILisWel39304_2049.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM263198 Genomic DNA. Translation: CAK21457.1 .
    RefSeqi WP_011702803.1. NC_008555.1.
    YP_850236.1. NC_008555.1.

    3D structure databases

    ProteinModelPortali A0AKC5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 386043.lwe2039.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAK21457 ; CAK21457 ; lwe2039 .
    GeneIDi 4465263.
    KEGGi lwe:lwe2039.
    PATRICi 20331285. VBILisWel39304_2049.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci LWEL386043:GI5X-2089-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. "Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
      Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.
      , Lampidis R., Kreft J., Goebel W., Chakraborty T.
      J. Bacteriol. 188:7405-7415(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35897 / DSM 20650 / SLCC5334.

    Entry informationi

    Entry nameiSYI_LISW6
    AccessioniPrimary (citable) accession number: A0AKC5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 61 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