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Reviewed, UniProtKB/Swiss-Prot Q7W8Z2 (SYI_BORPA)

Last modified February 9, 2010. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Isoleucyl-tRNA synthetase
    EC=6.1.1.5
Alternative name(s):
    Isoleucine--tRNA ligase
      Short name=IleRS
Gene names
Name: ileS
Ordered Locus Names: BPP1984
OrganismBordetella parapertussis [Complete proteome] [HAMAP]
Taxonomic identifier519 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

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Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

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) By similarity. HAMAP MF_02002

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_02002

Subunit structure

Monomer By similarity. HAMAP MF_02002

Subcellular location

Cytoplasm By similarity HAMAP MF_02002.

Domain

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)) By similarity. HAMAP MF_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processisoleucyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 953953Isoleucyl-tRNA synthetase HAMAP MF_02002
PRO_0000098358

Regions

Motif57 – 6711"HIGH" region HAMAP MF_02002
Motif623 – 6275"KMSKS" region HAMAP MF_02002

Sites

Metal binding9161Zinc By similarity
Metal binding9191Zinc By similarity
Metal binding9361Zinc By similarity
Metal binding9391Zinc By similarity
Binding site5821Aminoacyl-adenylate By similarity
Binding site6261ATP By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q7W8Z2-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 3E1887759A135559

FASTA953105,561
        10         20         30         40         50         60 
MDYKKSLNLP DTPFPMRGDL AKREPGWVAE WEETQVYQAI RAASRGRPRF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHIGHAVN KILKDIIVKS RNMAGYDAHY VPGWDCHGMP IEIQIEKKYG KHLPVTEVQS 

       130        140        150        160        170        180 
KARAYALEQI DRQRKDFKRL GVLGDWHNPY LTMNFSNEAD EIRVLGRILE KGYVFRGLKP 

       190        200        210        220        230        240 
VNWCFDCGSA LAEAEVEYAD RVDPAIDVAF PFTDRGALAR AFGLDEVDAG AIVIWTTTPW 

       250        260        270        280        290        300 
TIPSNQALNV HPEIDYALVR VTPTPVHGPL LLLAQERVEP SLKAWGLEGE IIATAKGEAL 

       310        320        330        340        350        360 
EGLRFRHPLA AAAQGYDRTS PIYLGDYVTL DTGTGVVHSA PAYGIEDFVS CKAHGLADSD 

       370        380        390        400        410        420 
ILGPVMGDGK FVDSLPLFGG LSIWDANPRI VEALKLAGSL MLVQKLSHSY MHCWRHKTPV 

       430        440        450        460        470        480 
IYRATSQWFA GMDVKPRDGG PSLRESALAG IDATAFYPAW GRARLHAMIA NRPDWTLSRQ 

       490        500        510        520        530        540 
RQWGVPMAFF VHKETGELHP RTVELLEQVA QRVEKGGIEA WQSLDPRELL GDEAELYEKN 

       550        560        570        580        590        600 
RDTLDVWFDS GSTHATVLGG KDGVLGSSHG AELAWPADLY LEGSDQHRGW FHSSLLTGCM 

       610        620        630        640        650        660 
LYGHPPYKGL LTHGFVVDGQ GRKMSKSVGN VIAPQKVSDS LGAEILRLWV ASTDYSGELS 

       670        680        690        700        710        720 
ISDEILKRVV ESYRRIRNTL RFLLANVADF DAVGQAVPYG ELFEIDRYAL AMTAQMQAEV 

       730        740        750        760        770        780 
QGHYERYDFH PAVSRLQTFC SEDLGAFYLD ILKDRLYTTA AGSAARRSAQ TALLDITQTL 

       790        800        810        820        830        840 
LKLMAPILSF TAEEAWKVLA GSALAKQADA PRVTIFTEVY HALPPFADGE ALTAKWTRLR 

       850        860        870        880        890        900 
AIRAEVQRKL EEVRSAGAIG SSLQAEVDLY ANAADHDILA SLGDDLRFVL IVSRATVHAD 

       910        920        930        940        950 
ADDLRIEIAA SGHKKCERCW HWRPDVGQDA DHPEICGRCV SNLFGAGEPR TRA

« Hide

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX640429 Genomic DNA. Translation: CAE37284.1.
RefSeqNP_884243.1.

3D structure databases

SMRQ7W8Z2. Positions 1-943.
ModBaseSearch...

Genome annotation databases

GeneID1664819.
KEGGbpa:BPP1984.
NMPDRfig|257311.1.peg.1877.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG577712.
OMAKQVLTHG.
PhylomeDBQ7W8Z2.

Enzyme and pathway databases

BioCycBPAR257311:BPP1984-MONOMER.
BRENDA6.1.1.5. 263123.

Family and domain databases

HAMAPMF_02002. Ile_tRNA_synth_type1.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR010663. DNA_glyclase/IsotRNA_synth_Znf.
IPR002301. Ile-tRNA-synt_Ia.
IPR015905. Ile-tRNA-synt_Ia_N.
IPR018353. Isoleucyl-tRNA_synthetase.
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_Ia_edit.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF9. Ile-tRNA-synt_Ia. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYI_BORPA
AccessionPrimary (citable) accession number: Q7W8Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents