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Q7VEZ0 (SYI_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. 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:Mb1563
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length1041 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 – 10411041Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098547

Regions

Motif53 – 6311"HIGH" region HAMAP-Rule MF_02003
Motif619 – 6235"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6221ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VEZ0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 4513382E3248D3AB

FASTA1,041117,314
        10         20         30         40         50         60 
MTDNAYPKLA GGAPDLPALE LEVLDYWSRD DTFRASIARR DGAPEYVFYD GPPFANGLPH 

        70         80         90        100        110        120 
YGHLLTGYVK DIVPRYRTMR GYKVERRFGW DTHGLPAELE VERQLGITDK SQIEAMGIAA 

       130        140        150        160        170        180 
FNDACRASVL RYTDEWQAYV TRQARWVDFD NDYKTLDLAY MESVIWAFKQ LWDKGLAYEG 

       190        200        210        220        230        240 
YRVLPYCWRD ETPLSNHELR MDDDVYQSRQ DPAVTVGFKV VGGQPDNGLD GAYLLVWTTT 

       250        260        270        280        290        300 
PWTLPSNLAV AVSPDITYVQ VQAGDRRFVL AEARLAAYAR ELGEEPVVLG TYRGAELLGT 

       310        320        330        340        350        360 
RYLPPFAYFM DWPNAFQVLA GDFVTTDDGT GIVHMAPAYG EDDMVVAEAV GIAPVTPVDS 

       370        380        390        400        410        420 
KGRFDVTVAD YQGQHVFDAN AQIVRDLKTQ SGPAAVNGPV LIRHETYEHP YPHCWRCRNP 

       430        440        450        460        470        480 
LIYRSVSSWF VRVTDFRDRM VELNQQITWY PEHVKDGQFG KWLQGARDWS ISRNRYWGTP 

       490        500        510        520        530        540 
IPVWKSDDPA YPRIDVYGSL DELERDFGVR PANLHRPYID ELTRPNPDDP TGRSTMRRIP 

       550        560        570        580        590        600 
DVLDVWFDSG SMPYAQVHYP FENLDWFQGH YPGDFIVEYI GQTRGWFYTL HVLATALFDR 

       610        620        630        640        650        660 
PAFKTCVAHG IVLGFDGQKM SKSLRNYPDV TEVFDRDGSD AMRWFLMASP ILRGGNLIVT 

       670        680        690        700        710        720 
EQGIRDGVRQ VLLPLWNTYS FLALYAPKVG TWRVDSVHVL DRYILAKLAV LRDDLSESME 

       730        740        750        760        770        780 
VYDIPGACEH LRQFTEALTN WYVRRSRSRF WAEDADAIDT LHTVLEVTTR LAAPLLPLIT 

       790        800        810        820        830        840 
EIIWRGLTRE RSVHLTDWPA PDLLPSDADL VAAMDQVRDV CSAASSLRKA KKLRVRLPLP 

       850        860        870        880        890        900 
KLIVAVENPQ LLRPFVDLIG DELNVKQVEL TDAIDTYGRF ELTVNARVAG PRLGKDVQAA 

       910        920        930        940        950        960 
IKAVKAGDGV INPDGTLLAG PAVLTADEYN SRLVAADPES TAALPDGAGL VVLDGTVTAE 

       970        980        990       1000       1010       1020 
LEAEGWAKDR IRELQELRKS TGLDVSDRIR VVMSVPAERE DWARTHRDLI AGEILATDFE 

      1030       1040 
FADLADGVAI GDGVRVSIEK T 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248333 Genomic DNA. Translation: CDO42811.1.
RefSeqNP_855215.1. NC_002945.3.

3D structure databases

ProteinModelPortalQ7VEZ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb1563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD96230; CAD96230; Mb1563.
GeneID1092424.
KEGGmbo:Mb1563.
PATRIC18005125. VBIMycBov88188_1709.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAENRDWFE.
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. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_MYCBO
AccessionPrimary (citable) accession number: Q7VEZ0
Secondary accession number(s): X2BI93
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 67 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