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Q81WE4

- SYI1_BACAN

UniProt

Q81WE4 - SYI1_BACAN

Protein

Isoleucine--tRNA ligase 1

Gene

ileS1

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 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

    BioCyciBANT260799:GJAJ-3804-MONOMER.
    BANT261594:GJ7F-3922-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isoleucine--tRNA ligase 1UniRule annotation (EC:6.1.1.5UniRule annotation)
    Alternative name(s):
    Isoleucyl-tRNA synthetase 1UniRule annotation
    Short name:
    IleRS 1UniRule annotation
    Gene namesi
    Name:ileS1UniRule annotation
    Ordered Locus Names:BA_4034, GBAA_4034, BAS3746
    OrganismiBacillus anthracis
    Taxonomic identifieri1392 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000000427: Chromosome, UP000000594: Chromosome, UP000005639: 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 ligase 1PRO_0000098344Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    IntActiQ81WE4. 1 interaction.
    STRINGi198094.BA_4034.

    Structurei

    3D structure databases

    ProteinModelPortaliQ81WE4.
    SMRiQ81WE4. Positions 2-883.
    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.
    OMAiLGRRSCQ.
    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.

    Q81WE4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEYKNTLLMP KTEFPMRGNL PKREPAMQEK WAEMNIYETV QEHTKGRPLF    50
    VLHDGPPYAN GDIHMGHALN KVLKDFIVRY KSMTGFCAPY VPGWDTHGLP 100
    IEQALTNKGV KRKEMTVAEF RKLCAEYAYE QVERQREQFK RLGVRADWDN 150
    PYITLEPAYE AQQIKVFGDM AKKGYIYKGQ KPVYWSPTSE SALAEAEIEY 200
    QDKKSASIYV AFSVKDGKNV LEGDEKYIIW TTTPWTLPAN LGISVHPELE 250
    YAIVKVNDEK YIIASELFET VAKTLEWENA EVVKTVKGSE LEYTVAKHPF 300
    YDRDSLVMLG DHVTTDAGTG CVHTAPGHGE DDFIVGKKYG LEVLCPVDDK 350
    GVLTEEAPGF EGLFYDKANK PITEKLEEVG ALLKLTFITH SYPHDWRTKK 400
    PIIFRATAQW FASIEAFRKE LLEAVAETKW VPAWGETRLH NMVRDRGDWC 450
    ISRQRAWGVP IPVFYAENGD PIITDETINH VADLFREHGS NVWFEREAKD 500
    LLPEGFTHPG SPNGEFRKET DIMDVWFDSG SSHQAVLEER DDLQRPADLY 550
    LEGSDQYRGW FNSSLSTAVA VTGKAPYKGV LSHGFVLDGE GRKMSKSIGN 600
    IVVPKKIMDQ LGGDILRLWV SSVDYQSDVR ISDDILKQVA EVYRKIRNTF 650
    RFLLGNLDDF KPSENTVAVA ELREVDRYML VKLNDLITKV KEAYETYDFA 700
    AVYHAIHNFC TIDLSSFYLD FAKDILYIEG ANHEDRRAIQ TVLYDVLVAL 750
    TKLVTPILPH TADEVWPYIP GVTEESVQLT DMPEAVQLDD AEALKTKWDA 800
    FMTLRDDVLK ALEVARNEKV IGKSLNASIT LYPTAEMKAM LESINEDLKQ 850
    LFIVSEYKLG GMMEEAPADA PKYEHTAVVV AQATGETCER CWVVSETIGK 900
    DAEHETLCER CATVVKENYV K 921
    Length:921
    Mass (Da):104,611
    Last modified:June 1, 2003 - v1
    Checksum:i4B383BCCC606348B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP27760.1.
    AE017334 Genomic DNA. Translation: AAT33151.1.
    AE017225 Genomic DNA. Translation: AAT56048.1.
    RefSeqiNP_846274.1. NC_003997.3.
    YP_020676.1. NC_007530.2.
    YP_029997.1. NC_005945.1.

    Genome annotation databases

    EnsemblBacteriaiAAP27760; AAP27760; BA_4034.
    AAT33151; AAT33151; GBAA_4034.
    AAT56048; AAT56048; BAS3746.
    GeneIDi1086630.
    2818769.
    2848181.
    KEGGiban:BA_4034.
    bar:GBAA_4034.
    bat:BAS3746.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016879 Genomic DNA. Translation: AAP27760.1 .
    AE017334 Genomic DNA. Translation: AAT33151.1 .
    AE017225 Genomic DNA. Translation: AAT56048.1 .
    RefSeqi NP_846274.1. NC_003997.3.
    YP_020676.1. NC_007530.2.
    YP_029997.1. NC_005945.1.

    3D structure databases

    ProteinModelPortali Q81WE4.
    SMRi Q81WE4. Positions 2-883.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q81WE4. 1 interaction.
    STRINGi 198094.BA_4034.

    Protocols and materials databases

    DNASUi 1086630.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAP27760 ; AAP27760 ; BA_4034 .
    AAT33151 ; AAT33151 ; GBAA_4034 .
    AAT56048 ; AAT56048 ; BAS3746 .
    GeneIDi 1086630.
    2818769.
    2848181.
    KEGGi ban:BA_4034.
    bar:GBAA_4034.
    bat:BAS3746.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci BANT260799:GJAJ-3804-MONOMER.
    BANT261594:GJ7F-3922-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. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
      Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
      , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
      Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames / isolate Porton.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames ancestor.
    3. "Complete genome sequence of Bacillus anthracis Sterne."
      Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sterne.

    Entry informationi

    Entry nameiSYI1_BACAN
    AccessioniPrimary (citable) accession number: Q81WE4
    Secondary accession number(s): Q6HUJ1, Q6KNS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 88 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