Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6MT28 (SYI_MYCMS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:MSC_0585
OrganismMycoplasma mycoides subsp. mycoides SC (strain PG1) [Reference proteome] [HAMAP]
Taxonomic identifier272632 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length915 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
Reference 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 – 915915Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098422

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif595 – 5995"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8831Zinc By similarity
Metal binding8861Zinc By similarity
Metal binding8991Zinc By similarity
Metal binding9021Zinc By similarity
Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MT28 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 55288E92EC9CE1BB

FASTA915106,344
        10         20         30         40         50         60 
MSNKYKDTLL IGKTDFDMRA NLNQKEPKFE QFWQENQIYN KKLKLNENKK VFVLHDGPPY 

        70         80         90        100        110        120 
ANGDLHIGHA LNKTLKDFII RFKNTTGYYA PFIMGWDTHG LPIESAVTKM GVDRKSMSSV 

       130        140        150        160        170        180 
AFRELCYKYA LEQVSNQANQ FNRLGMFTDY DTKYVTLTHD FEMSELRLFE KMYQKGLIYK 

       190        200        210        220        230        240 
DLKPIYWSPS SESALADSEI IYKDISSPSI YVGCDVINSD EFKNTQLIIW TTTPWTLPSN 

       250        260        270        280        290        300 
QLIAIGSKIK YSLIQVENSD KQFILASDLI NQVSQNIGWE NVKVIKEIDA NKLVGLNYVH 

       310        320        330        340        350        360 
PLYDTKISKV VLGHHVTSES GSGLVHIASG FGEDDFLIAK QNNIKPFAPI DNQGKFTTQI 

       370        380        390        400        410        420 
SDLDPQLVGM FYDDTNKIIT KRLEENKKLL KLKFLTHSYP HDWRTKKPVI YRCTLQWFVN 

       430        440        450        460        470        480 
LAPVKNDILK NVDQINTHPK WAKKRLYQVL DERTDWTISR QRLWGVPIIA FYDQNDDLVL 

       490        500        510        520        530        540 
NEQILNYAIN KIEEVGTNAW FSLDADEFLP EQYKNKSLKK EKDILDVWFD SGSSAIALSQ 

       550        560        570        580        590        600 
KYPNLKLPYD MYLEGNDQYR GWFNASMINS TIYSNTSPYK QLVSHGMTTD EKGNKMSKSL 

       610        620        630        640        650        660 
GNGVDPIAFA NDLGADILRL WVASTDFTDD QKIGKEIIKQ ISESYRKIRN TIRFILANLN 

       670        680        690        700        710        720 
DFNVKTDYQT KLSEVDMYSL FNLTSFKNKV IQAYQELNFS LVYTLVMNYV TKNLSAFYLD 

       730        740        750        760        770        780 
FIKDILYINS KNDLRRRQVQ TVLYEQLYCL IDVLRPILVH TIEEVYQNLN DNNKVESVHL 

       790        800        810        820        830        840 
LDNKEQNFVY DKEFINKWDQ VMILRDDVNK ALEISRENKI INKGFEAVVN IKLDKEYDDL 

       850        860        870        880        890        900 
KNIKDLSQIF IVNSINFVDN IDNSFIKTNI SSIKVEQKQG LKCQRCWQIF DNLIDDEICN 

       910 
HCNNVVKSLL ETKCE 

« Hide

References

[1]"The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP)."
Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J., Johansson K.-E., Pettersson B., Uhlen M.
Genome Res. 14:221-227(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PG1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX293980 Genomic DNA. Translation: CAE77208.1.
RefSeqNP_975566.1. NC_005364.2.

3D structure databases

ProteinModelPortalQ6MT28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272632.MSC_0585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE77208; CAE77208; MSC_0585.
GeneID2745219.
KEGGmmy:MSC_0585.
PATRIC20017969. VBIMycMyc4973_0630.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycMMYC272632:GI1G-570-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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
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_MYCMS
AccessionPrimary (citable) accession number: Q6MT28
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 73 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