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B4F2T5 (SYI_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase
Short name=IleRS
Gene names
Name:ileS
Ordered Locus Names:PMI0015
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length936 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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-Rule MF_02002

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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-Rule MF_02002

Sequence similarities

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

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: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

aminoacyl-tRNA editing activity

Inferred from electronic annotation. Source: InterPro

isoleucine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 936936Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189187

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif601 – 6055"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8991Zinc By similarity
Metal binding9021Zinc By similarity
Metal binding9191Zinc By similarity
Metal binding9221Zinc By similarity
Binding site5601Aminoacyl-adenylate By similarity
Binding site6041ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B4F2T5 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: C93002D82AF46097

FASTA936105,191
        10         20         30         40         50         60 
MSDYKNTLNL PETGFPMRGD LAKREPEMLS RWYKEGLYQA IRQAKSGKKT FILHDGPPYA 

        70         80         90        100        110        120 
NGNIHIGHSV NKILKDIIIK SKGLSGFDSP YIPGWDCHGL PIELKVEQIV GKPGEKVSAA 

       130        140        150        160        170        180 
QFREECRKYA YEQIEAQKKD FIRLGVLGDW DKPYLTMDYK TEANTIRALA RIIANGHLLK 

       190        200        210        220        230        240 
GAKPVHWCTA CGSSLAEAEV EYYDKTSPSI DVRFRAVDSN AVAAKFGVVT DKPISLVIWT 

       250        260        270        280        290        300 
TTPWTLPANR AIALNGEFNY ALVSFDDECV ILAADLVEHV MKRIGVTDWA VLGECKGSDL 

       310        320        330        340        350        360 
ELLRFNHPFM GFDVPAILGD HVTLDAGTGA VHTAPGHGPD DFVIGQKYGL EVANPVGPNG 

       370        380        390        400        410        420 
CYLPNTYPTL DGVFVFKAND VIVELLKEKG ALLHHEAMQH SYPCCWRHKT PVIFRATPQW 

       430        440        450        460        470        480 
FIGMDKNGLR QQSLKEIKGV KWIPDWGQAR IESMVENRPD WCISRQRTWG TPMSLFVHKE 

       490        500        510        520        530        540 
TQEPHPRTLE LMEEVAKRVE VSGIQAWWDL DIRELLGDEA DDYMKTPDTL DVWFDSGSTH 

       550        560        570        580        590        600 
STVVDARPEF HGNSADLYLE GSDQHRGWFM SSLMISTAIK GKAPYREVLT HGFTVDGQGR 

       610        620        630        640        650        660 
KMSKSIGNTV SPQDVMNKLG ADILRLWVAS TDYTGEIAVS DEILKRSADT YRRIRNTARF 

       670        680        690        700        710        720 
FLANLNGFDP AKHQVKPEEM VILDRWAVGR AKAAQEDILK HYENYDFHNV IQRLMQFCSV 

       730        740        750        760        770        780 
EMGSFYLDII KDRQYTAKSD SVARRSCQTA LYHIIEALVR WMAPIMSFTA DEIWAQLPGE 

       790        800        810        820        830        840 
RAKFVFTQEW YTDLFGLEAS ETLNDEYWAE LLAVRSEVNK VLEQARTDKQ LRGSLEAAVT 

       850        860        870        880        890        900 
LYADKALAEK LNALGNELRF VLLTSQATVA DIHDAPENAL ASDMAGLKIV LSKAQGEKCP 

       910        920        930 
RCWHYATDIG QVAEHADLCG RCVTNVAGNG EERKFA 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942759 Genomic DNA. Translation: CAR40255.1.
RefSeqYP_002149802.1. NC_010554.1.

3D structure databases

ProteinModelPortalB4F2T5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING529507.PMI0015.

Proteomic databases

PRIDEB4F2T5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR40255; CAR40255; PMI0015.
GeneID6802405.
KEGGpmr:PMI0015.
PATRIC20514707. VBIProMir120933_0015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycPMIR529507:GJIW-15-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR001412. 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]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_PROMH
AccessionPrimary (citable) accession number: B4F2T5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries