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Q98PQ2 (SYI_MYCPU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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:MYPU_6670
OrganismMycoplasma pulmonis (strain UAB CTIP) [Complete proteome] [HAMAP]
Taxonomic identifier272635 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length888 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 – 888888Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098425

Regions

Motif61 – 7111"HIGH" region HAMAP-Rule MF_02002
Motif592 – 5965"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8621Zinc By similarity
Metal binding8651Zinc By similarity
Metal binding8791Zinc By similarity
Metal binding8821Zinc By similarity
Binding site5511Aminoacyl-adenylate By similarity
Binding site5951ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q98PQ2 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: CCECB4F79293A390

FASTA888103,303
        10         20         30         40         50         60 
MNEKKDYKDT LNMPQTNFEM QAGLTRKEAQ FRQRWLDNKL YHKILAKNKN NKQFVVHDGP 

        70         80         90        100        110        120 
PYANGSIHIG HALNKILKDI VVRFKSLQGF YSPFVPGWDT HGLPIENKML SELKVNHKQI 

       130        140        150        160        170        180 
EVVKLRKEAA KYALNQMLIQ KEQFLKLQML SDFEEIYLTL DKNFEAKQLK LFKKMFFDGL 

       190        200        210        220        230        240 
IYKGLKPVYW SPSSMSALAE AEVEYYDHVS PSIYTCFTIT KGNEFVEVDD ELLIWTTTPW 

       250        260        270        280        290        300 
TLIANSGVAV GLDIEYSKVK FNKKNYIVAS DLLEKVMEIF GVQKYKVVDT FKGKNLLGVE 

       310        320        330        340        350        360 
YQRPIKTDLF GIVVAGYHVS IDAGTGLVHM APLFGEDDFI IGQENELDQI MHINDDGSIN 

       370        380        390        400        410        420 
SEGDEFQGLF YSSANIKIKE FLEKNDKVMF FEYFTHSYPH DWRTKKPIIF RGTPQWFVSI 

       430        440        450        460        470        480 
DKIKPAILKE IEKIEGRPSW AVKRLATMIE NRKTWTISRQ RSWGVPIPIF YNEKNEIVND 

       490        500        510        520        530        540 
EKVFDHVIEL VEKYGSDVWF EKSVDELLPS EYKNKNWTKE TNIMDVWFDS GSTSIGVEIE 

       550        560        570        580        590        600 
GVSVPFDLYL EGIDQYRGWF NSSIINSVAY WGQSPYRLLL SHGFVLDGKG KKMSKQLGNV 

       610        620        630        640        650        660 
VDPQEIIQKY GADILRLWVA NCEYAHDVSV SESIIKQTVE NYRKIRNTIK FLLGNLQDYD 

       670        680        690        700        710        720 
HSKFNLKLEG IHELINERLK KVKFDILQAY NDYDFNDVIK TLTNFLTDLS SFYLSISKDS 

       730        740        750        760        770        780 
LYADKINSKE RRMIQYNMYN ILEATLVVIA PIMPTTAEDA YDNFNKQDKQ ESVHLEKMFE 

       790        800        810        820        830        840 
ATIADDKLEK TWKEFFDLKD EVYKEIEVEI ANKKIKRTND AHVTINTKSN FLMSLDLKKL 

       850        860        870        880 
LMIGKISFGS SLRVETFDSH KCPRCWNHIE KTEVVEDLCQ RCYQTINS 

« Hide

References

[1]"The complete genome sequence of the murine respiratory pathogen Mycoplasma pulmonis."
Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F., Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.
Nucleic Acids Res. 29:2145-2153(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UAB CTIP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445565 Genomic DNA. Translation: CAC13840.1.
PIRC90595.
RefSeqNP_326498.1. NC_002771.1.

3D structure databases

ProteinModelPortalQ98PQ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272635.MYPU_6670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC13840; CAC13840; CAC13840.
GeneID911089.
KEGGmpu:MYPU_6670.
PATRIC20024280. VBIMycPul29704_0679.

Organism-specific databases

GenoListMYPU_6670.
CMRSearch...

Phylogenomic databases

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

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_MYCPU
AccessionPrimary (citable) accession number: Q98PQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2001
Last modified: April 16, 2014
This is version 76 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