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Q6MKX0 (SYI_BDEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:Bd2257
OrganismBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) [Complete proteome] [HAMAP]
Taxonomic identifier264462 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaBdellovibrionalesBdellovibrionaceaeBdellovibrio

Protein attributes

Sequence length1056 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 – 10561056Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098523

Regions

Motif56 – 6611"HIGH" region HAMAP-Rule MF_02003
Motif603 – 6075"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6061ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MKX0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 2B200E2A1FCA95CA

FASTA1,056119,738
        10         20         30         40         50         60 
MTNANTRSTP YSAVKPDVNL AKQEETILDF WDQEKIFAQS LNPEGKKTYS FYDGPPFATG 

        70         80         90        100        110        120 
LPHYGHLLAG VLKDVVPRYW TMKGYTVPRR FGWDCHGLPV EYEINKTHKI ESRKDVFKMG 

       130        140        150        160        170        180 
VANYNDACRS IVKRYSTEWK TTVRRVGRWV DMENPYFTMD VSFMQSVWWV FQQLFNKGLI 

       190        200        210        220        230        240 
YEGYKVVPYS VGISTSLSNF EANQNYKMVQ DPAITVMFKL VNQPDTAIMA WTTTPWTLPS 

       250        260        270        280        290        300 
NLALAVGNDI EYVKVQEKAT GRKLIMAQAL LSSVFKKADE EVEVLQMMKG TELVGLTYEP 

       310        320        330        340        350        360 
LFPYFGDRAD KGAFRIISSD HVTTESGTGV VHMAPAFGEE DYYACAKAGI PMVNPVDDDG 

       370        380        390        400        410        420 
MFTMEVPDYA GKRVKEADKD IIADLKKRGN LFKQDTIQHS YPFCYRSDTP LIYRAVSSWF 

       430        440        450        460        470        480 
VAVEKIKEEL IANNKQTSWV PDHLRDGRFG NWLEGARDWA ISRNRFWGTP LPIWRNAEGE 

       490        500        510        520        530        540 
VMCIGSRAEL EKLSGQKVDD LHIEFVDKIT IPSPTGKSPL KRVDGVLDCW FESGSMPYAQ 

       550        560        570        580        590        600 
WGYPETSVED FKKAFPADFI AEGLDQTRGW FYTLSIIGTA LFNQAPFKNV VVNGLVLAED 

       610        620        630        640        650        660 
GRKMSKSLKN YPDPMEVLNQ HGADALRLYL IDSPVVKAQE LKFSEKGVYD IVRKILLRWW 

       670        680        690        700        710        720 
NSYSFFANYA NIDGFVPKGD AKKSPNILDQ WVLSRLNGLI ANTHKEMDAY RLYNVVPHLL 

       730        740        750        760        770        780 
QFIEDLTNTY IRFNRSLFWQ DGMPETKRYA YETLHEVLVT LSRLMAPFAP FMSEVTYKNL 

       790        800        810        820        830        840 
AQVLKDKKDS VHLESFPTAD LSMLRPELEE AVKAMDTLVT LGRNHREKIG VKAKIPLNEI 

       850        860        870        880        890        900 
KIIHRSAELL ETLKKFEPFF VDELNFRKVV YNPNEDQFVQ VTAKANFPVL GKRLGPKMKA 

       910        920        930        940        950        960 
VGAGIMSMSL ENILKLEGGG VVVIEGEEIS LSDVEIRRAP KGDNANLSVH QIVSIEVDPT 

       970        980        990       1000       1010       1020 
VTPEQEREGL AREIMRKIQV ARKTADFQMD DKITLEIACD GALLDALNAH KDMITGETLT 

      1030       1040       1050 
KNLNILALTA EPNGKHTETS DIDGQVIKIG VTNLPR 

« Hide

References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / DSM 50701 / NCIB 9529 / HD100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842652 Genomic DNA. Translation: CAE80087.1.
RefSeqNP_969094.1. NC_005363.1.

3D structure databases

ProteinModelPortalQ6MKX0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264462.Bd2257.

Proteomic databases

PRIDEQ6MKX0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE80087; CAE80087; Bd2257.
GeneID2733851.
KEGGbba:Bd2257.
PATRIC21079000. VBIBdeBac73187_2065.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. 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]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_BDEBA
AccessionPrimary (citable) accession number: Q6MKX0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 68 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