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P47587 (SYI_MYCGE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:MG345
OrganismMycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) [Complete proteome] [HAMAP]
Taxonomic identifier243273 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length895 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 – 895895Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098417

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif590 – 5945"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8691Zinc By similarity
Metal binding8721Zinc By similarity
Metal binding8881Zinc By similarity
Metal binding8911Zinc By similarity
Binding site5491Aminoacyl-adenylate By similarity
Binding site5931ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P47587 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 8C78DE6A05311B22

FASTA895104,396
        10         20         30         40         50         60 
MDLKKTLLMP KTSFAMQANL STSEKNFHDF WKDKKVFQKL KKQNKGKQIK ILHDGPPYAN 

        70         80         90        100        110        120 
GSIHVGHALN KILKDFILRS WLYEGYDVVF IPGWDCHGLP IEHAVSKKNP SSYSNLSTVE 

       130        140        150        160        170        180 
KRKLCHQFAL SQIAVQKEQF QRLGLLNDFQ NCYYTIDESF QFKELELFLQ AIKKGLIFQD 

       190        200        210        220        230        240 
LKPTYWSPIS RTSLAEAEIE YKEVNSIALY LTFKVSKSDF LDENANLLVW TTTPWTLPTN 

       250        260        270        280        290        300 
QAIAIHPDFD YLLFEYNQQK FVILEKLFEV FTNKLNWTNA IKLKKFKGSN LKNSSYSHCF 

       310        320        330        340        350        360 
YNKVLPVLMG IHVVDNEGTG IVHSSPAFGI DDFYLCQKNK IKEVLISIDE KGVFNNLLND 

       370        380        390        400        410        420 
KELENCFYLK ANDLIINRLK QNNSFIFSEV ISHREPHDWR SKTPVIYRAS KQLFIKTKSI 

       430        440        450        460        470        480 
KKQLKKQINQ VNFLNSKNQL RLKEMLLQRD EWCISRQRVW GLPIPIVYAN NKPLLDFSTI 

       490        500        510        520        530        540 
QYTIKQLKKH GIDSWFEKDV TCFLKPDKTK KWVKYHKEID TLDVWFDSGS SYNVLEINKY 

       550        560        570        580        590        600 
GSIADLYIEG SDQYRGWFNS SSNCGIIQND LIPFKSLVSH GFTLDENGNK MSKSLGNIVD 

       610        620        630        640        650        660 
PLKICDQYGA DILRLWVANT DWQIDNKIGV NILKQVAEQY RRIRNSLLRF ILGNINGFNF 

       670        680        690        700        710        720 
TSMDDYKFSL EDKIVIHKTN SLVEQIEKFL EKYNFLGCLK VINKFVLWLS SWYFEIIKDT 

       730        740        750        760        770        780 
LYCDAKNNPN RLAKQAVLNY IFTQLISFLN IFIPHTAEDA WKNYSFNKKP ISVNLFTKPT 

       790        800        810        820        830        840 
VFKVANSKNL GNIYKTFTSI KNAAFKEIEK LRKEGLISKN NQIELTVGIN KKIPKKLKDN 

       850        860        870        880        890 
LALWLNVNSV NLTNNENEIK VKKTKKTMCE RCWNFQTIIK QKLDHNLCSR CFKVC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L43967 Genomic DNA. Translation: AAC71570.1.
U02196 Genomic DNA. Translation: AAD12482.1.
U02254 Genomic DNA. Translation: AAD12519.1.
PIRB64238.
RefSeqNP_073015.2. NC_000908.2.

3D structure databases

ProteinModelPortalP47587.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243273.MG_345.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC71570; AAC71570; MG_345.
GeneID875496.
KEGGmge:MG_345.
PATRIC20010256. VBIMycGen98045_0405.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycMGEN243273:GH2R-395-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_MYCGE
AccessionPrimary (citable) accession number: P47587
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 99 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

Mycoplasma genitalium

Mycoplasma genitalium (strain G-37): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries