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Q5PAL9

- SYI_ANAMM

UniProt

Q5PAL9 - SYI_ANAMM

Protein

Isoleucine--tRNA ligase

Gene

ileS

Organism
Anaplasma marginale (strain St. Maries)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (04 Jan 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

    Zinc.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei632 – 6321ATPUniRule 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

    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:AM684
    OrganismiAnaplasma marginale (strain St. Maries)
    Taxonomic identifieri234826 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma
    ProteomesiUP000006557: 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 – 11011101Isoleucine--tRNA ligasePRO_0000098514Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi234826.AM684.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5PAL9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi50 – 6011"HIGH" regionAdd
    BLAST
    Motifi629 – 6335"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.
    HOGENOMiHOG000246403.
    KOiK01870.
    OMAiENRDWFE.
    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.

    Q5PAL9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNYYPEVKGN PEFSAIEKEI LQYWNSEKIF EESVNTRSRD RSFVFYDGPP     50
    FANGLPHYGH LLTGFIKDAV ARYKTMRGFR VERKFGWDCH GLPAEMLAEK 100
    ELGVSGKVSI ESFGIDKFND YCRSSIMRFT QQWREYVERQ GRWVDFENGY 150
    RTMDKSFMES VMWAFHELWH KGLVYESVKV VPYSWACQTP LSNFETKMDN 200
    AYREKVSKSV TVRFKLSEQV GFVPQGVESC SILAWTTTPW TLVSNFALAI 250
    NTNMDYVGAV VGAEMLIFSA GYLDHFMRYC ERHSLECAKV VQIPAKELLA 300
    VKYMPPFPYF ADSKNAFMVL DAEFVAEGAG TGIVHLAPGF GEDDFLLCKQ 350
    HGIPNLGEES RGMLSVICPI DDAGRFTAAV GDFAGQHVFD VVDAVIRQLK 400
    EKGLWFATEQ CTHSYPHCWR TDTPLIYRAT SSWYVEVTKL KARMVELNKE 450
    VNWVPEHVQS GQFGKWLDGA KDWSVSRHRF WGAPVPVWRS DDPKYPRTDV 500
    YGSIKKVLPD VKALEEDFGP VEDLHRPYID NLVRPNPDDP TGKSMMRRVP 550
    DVLDCWFESG SMPYAQMHYP FENKEFFDSH FPADFITEYI AQTRGWFYTL 600
    FVLSTGLFDR HPFKNCICHG VVLDIKGQKL SKRLNNYPDP MEMFEKYGAD 650
    SVRFTMLSHA VSIGGDLLLD QDGDVVRDTL KSVVKPIWNS YSFFTVYANS 700
    DQMQGRILES LEGITNIMDQ YILYECACMV VKVLEAMESS SAGVRDPYNI 750
    RLACAAIVQF SDKLNNWYIR GCRGRFWMRD KTADKSDAYN TLYTVLYHLA 800
    RTIAPFLPFI AESIWLGLSF QREKSVHLAD FPDASSFSAV HQYKKNAEYM 850
    QLAMDVCSHV LSLRNAHNIR VRQPLRRMVV YPYNCESLLD MPQQYRDIIL 900
    NEVNVKSLQI ASTIGDMASF ELKLNFALLG QRVPEKVKQI ITLARAGVWE 950
    VQSDGSLLLG APGCEQCVIQ KDEFSLNLKV HSEYACQIIS GGVPVGVLHI 1000
    DHELTRELLL EGIARDVMRL IQQARKDCGL EMLDHAEVII NTDAAEIIEA 1050
    ISIWYDFIKQ QTFSHTLEHR PAQAVVEDCS KYTKISGKDF DIFLCKSALC 1100
    S 1101
    Length:1,101
    Mass (Da):125,904
    Last modified:January 4, 2005 - v1
    Checksum:i981A2927BF1933CD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000030 Genomic DNA. Translation: AAV86661.1.
    RefSeqiYP_153916.1. NC_004842.2.

    Genome annotation databases

    EnsemblBacteriaiAAV86661; AAV86661; AM684.
    GeneIDi3171286.
    KEGGiama:AM684.
    PATRICi20947361. VBIAnaMar46146_0597.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000030 Genomic DNA. Translation: AAV86661.1 .
    RefSeqi YP_153916.1. NC_004842.2.

    3D structure databases

    ProteinModelPortali Q5PAL9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 234826.AM684.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV86661 ; AAV86661 ; AM684 .
    GeneIDi 3171286.
    KEGGi ama:AM684.
    PATRICi 20947361. VBIAnaMar46146_0597.

    Phylogenomic databases

    eggNOGi COG0060.
    HOGENOMi HOG000246403.
    KOi K01870.
    OMAi ENRDWFE.
    OrthoDBi EOG644ZM1.

    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. "Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
      Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: St. Maries.

    Entry informationi

    Entry nameiSYI_ANAMM
    AccessioniPrimary (citable) accession number: Q5PAL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 68 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