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

A8GPA1 (SYI_RICAH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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:A1C_04840
OrganismRickettsia akari (strain Hartford) [Complete proteome] [HAMAP]
Taxonomic identifier293614 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length1103 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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_02003

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 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 – 11031103Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022158

Regions

Motif53 – 6311"HIGH" region HAMAP-Rule MF_02003
Motif628 – 6325"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6311ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8GPA1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 2D5D718E96221D88

FASTA1,103126,771
        10         20         30         40         50         60 
MANTKYYPEV SSNANFAAIE REILKFWQDN NIFQKSIDGR NGESEFIFYD GPPFANGLPH 

        70         80         90        100        110        120 
YGHLLTGFIK DVYARYQTVK GKKVERRFGW DCHGLPAEMQ SEKELGISGR LAITNFGIEK 

       130        140        150        160        170        180 
FNAHCRASVM EYASDWEEYV TRQARWVDFK NSYKTMDKNF MESVLWAFKE LYNKGLLCES 

       190        200        210        220        230        240 
MRVVPYSWAC ETPLSNFETR LDNSYRERSD KAVTVSFVLR DKLHEIPAFA GMISRESEMT 

       250        260        270        280        290        300 
VGGDYQEYRI LTWTTTPWTL PSNLAIAVGS DIDYALVPQE NICYIIAASS VSKYAKELGL 

       310        320        330        340        350        360 
SGEENFEIIK GSQLQGLRYK PLFDYFEHHP NSFKIFDVDF VVEGDGTGVV HMAPGFGEDD 

       370        380        390        400        410        420 
QILCESKGIS LVCPVDNSGK FTKEIPDLEG VQVFDANDKI IIKLKEQGNW LKTEQYIHNY 

       430        440        450        460        470        480 
PHCWRTDTPL IYKAVPSWYV KVTQFKDRMV ELNQQINWIP HHVKDNLFGK WLENARDWSI 

       490        500        510        520        530        540 
SRNRFWGTPL PVWKSDDPKY PRIDVYGSIE ELEKDFGVKV TDLHRPFIDK LTRPNPNDPT 

       550        560        570        580        590        600 
GKSTMRRIED VFDCWFESGS MPYGQAHYPF ENKEWFEDHF PADFIVEYSA QTRGWFYTLM 

       610        620        630        640        650        660 
VLSTALFDRP PFLNCICHGV ILDATGQKLS KRLNNYADPL ELFDQYGSDA LRVTMLSSNI 

       670        680        690        700        710        720 
VKGQELLIDK DGKMVFDTLR LFIKPIWSSY HFFTMYANAD SLKGEISFAS ENVLDVYILS 

       730        740        750        760        770        780 
KLKIAVSKIE ESLDNFDTQT AYHAVLEFFE VLNNWYIRRS RARFWKSEKD TDKQNAYNTL 

       790        800        810        820        830        840 
YSCLKTMAIA MSALVPMISE AIYKGLCHCE ETSTLSSRDL IAGSSKSINN LNPVVKPRDY 

       850        860        870        880        890        900 
TPSVHHNDQI SVHLCNYPTL SDFEINHELV ATMDNVLDIC SNSLFIRSTK NIRVRQPLAS 

       910        920        930        940        950        960 
ITIISKHNND LKAFENLIKD EINVKSVIYC DDLENYASKK LSINFPMLGK RLPAKMKEII 

       970        980        990       1000       1010       1020 
AASKKGDWKA IAGGLTICGE TLNNEEYKLI LEPYSHIKGA ASFENNSSLL ILDLELTAEL 

      1030       1040       1050       1060       1070       1080 
IEEGYARDIV RFIQQARKDA GFSITDRILI EIISEFDLSE IIYNYGDFIT EQTLGEFSKN 

      1090       1100 
FTPDYVSKVE LEDHPIQLKI KKS 

« Hide

References

[1]"Complete genome sequence of Rickettsia akari."
Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Dasch G., Eremeeva M.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hartford.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000847 Genomic DNA. Translation: ABV75226.1.
RefSeqYP_001493734.1. NC_009881.1.

3D structure databases

ProteinModelPortalA8GPA1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING293614.A1C_04840.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV75226; ABV75226; A1C_04840.
GeneID5645801.
KEGGrak:A1C_04840.
PATRIC17876936. VBIRicAka50705_1003.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycRAKA293614:GI4A-913-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 2 hits.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023586. Ile-tRNA-ligase_type2.
IPR014729. Rossmann-like_a/b/a_fold.
IPR022439. RPE4.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
TIGR03777. RPE4. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_RICAH
AccessionPrimary (citable) accession number: A8GPA1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 46 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