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Q72JR6

- SYI_THET2

UniProt

Q72JR6 - SYI_THET2

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 2 (20 Dec 2005)
      Previous versions | rss
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    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 2 zinc ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei57 – 571Aminoacyl-adenylateBy similarity
    Metal bindingi181 – 1811Zinc 1By similarity
    Metal bindingi184 – 1841Zinc 1By similarity
    Binding sitei319 – 3191ValineBy similarity
    Binding sitei328 – 3281ValineBy similarity
    Metal bindingi389 – 3891Zinc 1By similarity
    Metal bindingi392 – 3921Zinc 1By similarity
    Metal bindingi461 – 4611Zinc 2By similarity
    Metal bindingi464 – 4641Zinc 2By similarity
    Metal bindingi502 – 5021Zinc 2By similarity
    Metal bindingi504 – 5041Zinc 2By similarity
    Binding sitei550 – 5501Aminoacyl-adenylateBy similarity
    Binding sitei553 – 5531Aminoacyl-adenylateBy similarity
    Binding sitei554 – 5541Aminoacyl-adenylateBy similarity
    Binding sitei581 – 5811Aminoacyl-adenylateBy similarity
    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

    BioCyciTTHE262724:GCAT-716-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:TT_C0702
    OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
    Taxonomic identifieri262724 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000592: 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 – 10431043Isoleucine--tRNA ligasePRO_0000098566Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi262724.TTC0702.

    Structurei

    3D structure databases

    ProteinModelPortaliQ72JR6.
    SMRiQ72JR6. Positions 1-821.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi47 – 5711"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

    eggNOGiCOG0060.
    KOiK01870.
    OMAiKESHFDE.
    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. 1 hit.
    SSF50677. SSF50677. 1 hit.
    TIGRFAMsiTIGR00392. ileS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q72JR6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKEVGEPNF PKLEEEVLAF WKREKIFQKS VENRKGGPRY TVYEGPPTAN     50
    GLPHVGHAQA RSYKDLFPRY KTMRGYYAPR RAGWDTHGLP VELEVEKKLG 100
    LKSKREIEAY GIERFNQACR ESVFTYEKEW EAFTERIAYW VDLENAYATL 150
    EPTYIESIWW SLKNLFDRGL LYRDHKVVPY CPRCGTPLSS HEVALGYKEI 200
    QDPSVYVRFP LKEPKKLGLE KASLLIWTTT PWTLPGNVAA AVHPEYTYAA 250
    FQVGDEALIL EEGLGRKLLG EGTPVLKTFP GKALEGLPYT PPYPQALEKG 300
    YFVVLADYVS QEDGTGIVHQ APAFGAEDLE TARVYGLPLL KTVDEEGKLL 350
    VEPFKGLYFR EANRAILRDL RGRGLLFKEE SYLHSYPHCW RCSTPLMYYA 400
    TESWFIKNTL FKDELIRKNQ EIHWVPPHIK EGRYGEWLKN LVDWALSRNR 450
    YWGTPLPIWV CQACGKEEAI GSFQELRERA TQPLPEPFDP HRPYVDQVEL 500
    ACECGGTMRR VPYVIDVWYD SGAMPFASLH YPFEHQETFR ESFPADFIAE 550
    GIDQTRGWFN SLHQLGVMLF GSIAFKNVIC HGLILDEKGQ KMSKSKGNVV 600
    DPWDIIREFG ADALRWYIYV SAPPEADRRF GPNLVRETVR DYFLTLWNVY 650
    SFFVTYANLD RPDLKNPPPP EKRPEMDRWL LARMQDLIQR VTEALEAYDP 700
    TTSARALRDF VVEDLSQWYV RRNRRRFWKN EDALDREAAY ATLYEALVLV 750
    ATLAAPFTPF LAEVLWQNLV RSVRPEAKES VHLADWPEAD PALADEALVA 800
    QMRAVLKVVD LARAARAKSG VKTRTPLPLL LVTAPTALER EGLKRFAHEI 850
    AEELNVKEVR VLEPGEEILS YRVLPNLKLL GRKYGKLVPK IREALQRERE 900
    RAAALALKGE AIPLEVEGEA LTLLPEEVLL EAEAPKGYQA LEKDGYVAAL 950
    KVEVTEALRM EGLARDLIRL LQQARKDMGL KVSDRIRVGY EAEGPYLEAL 1000
    KRHGPWIAEE VLATAFGEGL FGGFEARVED EEGKAVFHLA RAE 1043
    Length:1,043
    Mass (Da):119,392
    Last modified:December 20, 2005 - v2
    Checksum:i47D67507C1C052F2
    GO

    Sequence cautioni

    The sequence AAS81050.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017221 Genomic DNA. Translation: AAS81050.1. Different initiation.
    RefSeqiYP_004677.2. NC_005835.1.

    Genome annotation databases

    EnsemblBacteriaiAAS81050; AAS81050; TT_C0702.
    GeneIDi2774814.
    KEGGitth:TTC0702.
    PATRICi23951809. VBITheThe54392_0699.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017221 Genomic DNA. Translation: AAS81050.1 . Different initiation.
    RefSeqi YP_004677.2. NC_005835.1.

    3D structure databases

    ProteinModelPortali Q72JR6.
    SMRi Q72JR6. Positions 1-821.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 262724.TTC0702.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS81050 ; AAS81050 ; TT_C0702 .
    GeneIDi 2774814.
    KEGGi tth:TTC0702.
    PATRICi 23951809. VBITheThe54392_0699.

    Phylogenomic databases

    eggNOGi COG0060.
    KOi K01870.
    OMAi KESHFDE.
    OrthoDBi EOG644ZM1.

    Enzyme and pathway databases

    BioCyci TTHE262724:GCAT-716-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.
    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.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB27 / ATCC BAA-163 / DSM 7039.

    Entry informationi

    Entry nameiSYI_THET2
    AccessioniPrimary (citable) accession number: Q72JR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 70 of the entry and version 2 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