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A5IY09 (SYI_MYCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. 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:MAG2200
OrganismMycoplasma agalactiae (strain PG2) [Complete proteome] [HAMAP]
Taxonomic identifier347257 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length892 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 – 892892Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189181

Regions

Motif60 – 7011"HIGH" region HAMAP-Rule MF_02002
Motif593 – 5975"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8621Zinc By similarity
Metal binding8651Zinc By similarity
Metal binding8791Zinc By similarity
Metal binding8821Zinc By similarity
Binding site5521Aminoacyl-adenylate By similarity
Binding site5961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IY09 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 84FAA196980A3941

FASTA892102,793
        10         20         30         40         50         60 
MSEIDYKETL NMPKTDFEMR ANLTTKEPLF REKWEKDNLY ARVLEKNKNN TPFVLHDGPP 

        70         80         90        100        110        120 
YANGSIHIGH ALNKILKDII VRYKSMCGFY SPYVPGWDTH GLPIELKMLT DAKINYKVIS 

       130        140        150        160        170        180 
PIELRKRASE YADIQIENQI SQFKSLQLLT DFKKIYKTKE PKFEAAQLKL FKKMVLDGLV 

       190        200        210        220        230        240 
YKGLKPVYWS PSSQTALAEA EVEYHDVDSP SIYVALEIID QNGSQKVKNG DKLVIWTTTP 

       250        260        270        280        290        300 
WTLLANAAVA IGENFVYCRV EHNNQGYIVA KELANKFIEI SKLDNAQISV DFNANELIGI 

       310        320        330        340        350        360 
KYKSVLNDLV CPVVIGHHVS LESGTGLVHI APLFGEDDFQ IGTANSLEMI MHVEDDGVLN 

       370        380        390        400        410        420 
DAAGKYKGIF YEKANAQIFD KLTSKSALLA KGTIRHSYPH DWRTHKPILF RGTPQWFVSI 

       430        440        450        460        470        480 
DKIRQQLLNE LESINTYPEW AKKRLVNMIS ERKDWTISRQ RTWGVPIIIF YDKDGKPVIN 

       490        500        510        520        530        540 
SAIFDYVIDL VEKYGTDIWW EKEADELLPE EFRSNGYTKE MDIMDVWFDS GTTSLAVEID 

       550        560        570        580        590        600 
EKLKPPYDLY LEGSDQYRGW FNSSLINSVA YTHKSPYKQI VSHGFVLDSK GEKMSKSKGN 

       610        620        630        640        650        660 
VVDPLKVIKK YGADILRLWV ANAEYTNDVN ISDEIINQNS EIYRKIRNTI KFLLGNLNGY 

       670        680        690        700        710        720 
EYDESVKRTG VHQYIYNELE SIKEKVYKAY DEYNFSSVIK TINKYVVELS SFYLNITKDI 

       730        740        750        760        770        780 
LYVHEFDSNE RMMTLANFYD ITNFLIKAIA PIIPTTAEDA YMHFYKKNKL ESIHLENFDI 

       790        800        810        820        830        840 
VKPYDSNVLK EWEEFFSLKD EVNLLLENAI KSGLIKRTNE AKVTIKNPSE VIKGYDLKQL 

       850        860        870        880        890 
LMVGAIEFGN VSKVESFMSE KCNRCWNHFS PAQIKDNLCP LCYKIVQKVN GK 

« Hide

References

[1]"Being pathogenic, plastic, and sexual while living with a nearly minimal bacterial genome."
Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V., Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A., Blanchard A., Citti C.
PLoS Genet. 3:744-758(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PG2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU179680 Genomic DNA. Translation: CAL58918.1.
RefSeqYP_001256362.1. NC_009497.1.

3D structure databases

ProteinModelPortalA5IY09.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347257.MAG_2200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL58918; CAL58918; MAG2200.
GeneID5183418.
KEGGmaa:MAG_2200.
PATRIC32271886. VBIMycAga119067_0236.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycMAGA347257:GC07-237-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_MYCAP
AccessionPrimary (citable) accession number: A5IY09
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 26, 2007
Last modified: April 16, 2014
This is version 54 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