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Q9PQ79 (SYI_UREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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:UU410
OrganismUreaplasma parvum serovar 3 (strain ATCC 700970) [Complete proteome] [HAMAP]
Taxonomic identifier273119 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeUreaplasma

Protein attributes

Sequence length900 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

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
Nucleotide-binding
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 900900Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098496

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif593 – 5975"KMSKS" region HAMAP-Rule MF_02002

Sites

Binding site5521Aminoacyl-adenylate By similarity
Binding site5961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PQ79 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: FA478902AE347D87

FASTA900105,806
        10         20         30         40         50         60 
MKDYKSTLNM PTTGFEMRAN LNVKEPKIQQ FWVEHQIYEK LLTKNKDKKP FILHDGPPYA 

        70         80         90        100        110        120 
NGNIHIGHAL NKILKDFVVS YHNMNNYYSP YIPGWDTHGL PIEVALSKKI KLSNLSVNER 

       130        140        150        160        170        180 
REQCKKYALE QVNNQIQQFL RLGMISDFKQ RYLTLDHNYE IDQLKLFTYM LKKGFIYQDF 

       190        200        210        220        230        240 
KPVFWSWSSQ TALAESEIEY ADRQSSAIYV KMKVVDHNDL FTDKPTSLVI WTTTPWTLPA 

       250        260        270        280        290        300 
NLAIAIHPEL VYSLIEYKNE NYIIAKPLVE TFVKKVGFED YKWIKDFKAN TLEKIKYISP 

       310        320        330        340        350        360 
ISKKHAFVIM DEYVSANDGT GLVHNAPAFG LEDYYACKKY GIETVVMIDQ FGKYNALVND 

       370        380        390        400        410        420 
LELENMFYED ANQVILNRLM NEHLLIHHEV ITHSVAHDWR TKKPVMYRAT KQWFVSIEKI 

       430        440        450        460        470        480 
LPNILQTLNN DVKSTSFRGI ERMHEMIVNR KEWCISRQRV WGVPIPMIFD ENHNAIMDHE 

       490        500        510        520        530        540 
LVENIINVLN EKGVNAWFDL DVNAFLTPKY LSMKNKTFYK EKDIMDVWFD SGSSYNILGH 

       550        560        570        580        590        600 
YNLNYPADVY LEGYDQYRGW FNSSLITGTI LNNRAPYKYL VAHGMVLDGE GYKMSKSKGN 

       610        620        630        640        650        660 
VVDPLDVCKI YGADVLRLWI ANSDYQNDTR ISEEILKQNA EIYRRIRNTL FKYSLSILND 

       670        680        690        700        710        720 
FEPSVDFSFN VRQEEQFVLN EFNELHIKVI KAYENFDYQT VVKLFNKFIL DLSSWYFENI 

       730        740        750        760        770        780 
KDDMYCLAIN DPIRKQIQSA VYWILKNSLI DLTPIIPHTT EEAYSFLKDA NKKESIRLED 

       790        800        810        820        830        840 
FYDQSQFQFK KGIAHVKAFF SIKDQIFNEL ENARKNNILK KNNEAFVTIA KNLILDDYLI 

       850        860        870        880        890        900 
NNPKLLAKWF GVAKIEFANN TNVANANFKK CLRCWNHFPD EEMYNDELSM NCYKVINKIK 

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References

[1]"The complete sequence of the mucosal pathogen Ureaplasma urealyticum."
Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., Cassell G.H.
Nature 407:757-762(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700970.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF222894 Genomic DNA. Translation: AAF30821.1.
RefSeqNP_078246.1. NC_002162.1.

3D structure databases

ProteinModelPortalQ9PQ79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273119.UU410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF30821; AAF30821; UU410.
GeneID876236.
KEGGuur:UU410.
PATRIC20534400. VBIUrePar45146_0426.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK13804.

Enzyme and pathway databases

BioCycUPAR273119:GHVP-428-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_UREPA
AccessionPrimary (citable) accession number: Q9PQ79
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 80 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