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)

P26499

- SYI_METTM

UniProt

P26499 - SYI_METTM

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 sitei594 – 5941ATPUniRule 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

    BioCyciMMAR79929:GH5J-1768-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:MTBMA_c17620
    OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
    Taxonomic identifieri79929 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
    ProteomesiUP000000345: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi589 – 5891G → D: Resistance to mupirocin (pseudomonic acid A).

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 10451044Isoleucine--tRNA ligasePRO_0000098579Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliP26499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi49 – 5911"HIGH" regionAdd
    BLAST
    Motifi591 – 5955"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

    HOGENOMiHOG000246403.
    KOiK01870.
    OMAiKPVHWCL.

    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.
    IPR023585. Ile-tRNA-ligase_type1.
    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]
    PANTHERiPTHR11946:SF9. PTHR11946:SF9. 1 hit.
    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.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P26499-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPIQEAEKSY KPHVIEEKVQ SFWEERDIYE RVKELREEGP RYSFLDGPPY     50
    CSGRIHLGTA WNKIMKDSYL RFKSMRGFNV RRQPGWDTHG LPIEHKVEGI 100
    LGVRSKKDIE DKIGIEEFVR KCREFAMENK AVMTSQFQRL GVWMDWDDPY 150
    VTFDPAYMES CWWTLKRAHE KDLLLRDLRV ITWCPRCETA LALAEIDYHE 200
    KEDPSIYVKF PVSGDTYILV WTTTPWTLPA NMAVAVHPDF DYAHTRLDGE 250
    TYIMAEALVE KVLGEEAEII KTVRGSELEG LTYRHPLDEE VPCHRDMEHR 300
    VILGDHVTLT EGTGCVHTAP GHGPEDFEIG KEYGLPVFCP VDEAGVFTED 350
    AGKYRGLFVK DADSDIIDDL RSKNLLLRAE TISHRYGFCW RCKTPIIYLA 400
    TEQWFLKITE IKDKMLSELD RVQWIPSWAG ESRFRNWIEN ARDWTISRQR 450
    YWGIPIPIWV CEDCDSIHVV GSIGELRELA VEGQLEGDFI HRPHVDRIIL 500
    ECGRCGGRMK RTPDVLDVWI DSGVAGWAAL HYPREKELFS EWFPYDFITE 550
    GHDQTRGWFY SQLGCGVIAL DETPYRRVLM HGFTLDEEGR KMSKSLGNVV 600
    EPEDVIEKYG ADVLRFYLLW ANKPWEDLKF VWDELKNVNK MFNILWNVYV 650
    FATTYMSLDR FQPGDHELED LHFRDEDRWI ISRVNSVALK VTEALDNLHF 700
    HRATREIHDF IVEDLSRWYI RLIRSRTWIE RDDPDKLAAY HSLYTALKTL 750
    IVTLSPIAPH VCEDIYQNLV RGAEPDSPES IHMLDWMVSE DAVDGKLEAE 800
    MDIVREIIEA CARARDTARY KLRWPVREIV VVSEDDKVLE AAESLKGVIA 850
    EQANAKSIRT STEFPDMRII AKPNPATLGP KLRQDMPPVM RKLEEADGAE 900
    VKAALESEGS FRVDLDGRII VLEPDDIIFE TELPENIVNA QFEGGSVFVD 950
    TELTPEIMSE AMARELVRRI QDMRKDLDLD VEARIEVSVK CSPEFRELTE 1000
    PQREFVENEV RASHLSFDYT ELEYTKEWKI SDENLIISIK PSDKV 1045
    Length:1,045
    Mass (Da):121,362
    Last modified:January 23, 2007 - v3
    Checksum:i5A935B0FE300077E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59245 Genomic DNA. Translation: AAA72950.1.
    CP001710 Genomic DNA. Translation: ADL59330.1.
    RefSeqiYP_003850643.1. NC_014408.1.

    Genome annotation databases

    EnsemblBacteriaiADL59330; ADL59330; MTBMA_c17620.
    GeneIDi9705473.
    KEGGimmg:MTBMA_c17620.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59245 Genomic DNA. Translation: AAA72950.1 .
    CP001710 Genomic DNA. Translation: ADL59330.1 .
    RefSeqi YP_003850643.1. NC_014408.1.

    3D structure databases

    ProteinModelPortali P26499.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADL59330 ; ADL59330 ; MTBMA_c17620 .
    GeneIDi 9705473.
    KEGGi mmg:MTBMA_c17620.

    Phylogenomic databases

    HOGENOMi HOG000246403.
    KOi K01870.
    OMAi KPVHWCL.

    Enzyme and pathway databases

    BioCyci MMAR79929:GH5J-1768-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 IPR001412. aa-tRNA-synth_I_CS.
    IPR002300. aa-tRNA-synth_Ia.
    IPR002301. Ile-tRNA-ligase.
    IPR023585. Ile-tRNA-ligase_type1.
    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 ]
    PANTHERi PTHR11946:SF9. PTHR11946:SF9. 1 hit.
    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.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isoleucyl-tRNA synthetase of Methanobacterium thermoautotrophicum Marburg. Cloning of the gene, nucleotide sequence, and localization of a base change conferring resistance to pseudomonic acid."
      Jenal U., Rechsteiner T., Tan P.-Y., Buehlmann E., Meile L., Leisinger T.
      J. Biol. Chem. 266:10570-10577(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.
    2. "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
      Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
      J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

    Entry informationi

    Entry nameiSYI_METTM
    AccessioniPrimary (citable) accession number: P26499
    Secondary accession number(s): D9PYN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 95 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing

    Documents

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

    External Data

    Dasty 3