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Q9XDB4 (SYI_FERPD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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:Ferpe_1791
OrganismFervidobacterium pennivorans (strain DSM 9078 / Ven5) [Complete proteome] [HAMAP]
Taxonomic identifier771875 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeFervidobacterium

Protein attributes

Sequence length912 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.

Sequence caution

The sequence AAD30388.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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 – 912912Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098387

Regions

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

Sites

Metal binding8801Zinc By similarity
Metal binding8831Zinc By similarity
Metal binding9001Zinc By similarity
Metal binding9031Zinc By similarity
Binding site5491Aminoacyl-adenylate By similarity
Binding site5931ATP By similarity

Experimental info

Sequence conflict5251I → M in AAD30388. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9XDB4 [UniParc].

Last modified September 5, 2012. Version 3.
Checksum: A0C8FA7C5CE20B7E

FASTA912105,259
        10         20         30         40         50         60 
MDYKATLNLP QTNFQMKANL VNKEPEMLKF WEEKEIYKKT LETRANAPTY LLHDGPPYAN 

        70         80         90        100        110        120 
GDIHLGTAMN KILKDFVTRY KTMRGYRVPF VPGWDTHGLP IEHRVTTSLG EEAKKKSPAE 

       130        140        150        160        170        180 
IRKLCKEFAL KYVDIQREEF KRLGVKGDWE HPYITLDPDY EYHILDVFKT LVENGNVYRG 

       190        200        210        220        230        240 
NKPVYWCPTC RTALAEAEIE YHDHESPSIY VKFQMVDKPD TYIVIWTTTP WTIPANVAIA 

       250        260        270        280        290        300 
LHPDYTYVKI KVDEEYWIVA EGLLQKFAAD VGIDFEVVEK FVGKELEGKL TKHPLYDRTS 

       310        320        330        340        350        360 
VVVLADYVTL EDGTGCVHTA PGHGEEDYQT GLKYNLPVLS PVDDEGRFTK EAGKYEGLKI 

       370        380        390        400        410        420 
WDANKVIVED LKNNGSLIKA GKISHSYPHC WRCKGPVMFR ATPQWFISVD KNNLRGKVLE 

       430        440        450        460        470        480 
EIKKVKWYPA WGETRITAMV QERPDWTISR QRVWGVPIPA VKCKDCGEVT LEPKVIEHFA 

       490        500        510        520        530        540 
NIVKEKGTDA WFELDVNELI PADFKCPACG SKNFEKTHDT LDVWIDSGCS WEAVIRSKGE 

       550        560        570        580        590        600 
RFPVDLYLEG DDQHRGWFQS SIFLSTAKAG TAPFKAVVTH GFIKDEQGRK MSKSLGNVID 

       610        620        630        640        650        660 
PMEIVNKYGA DILRLWVAST DFFDNIRVGK NIIEQQVEVY RKLRNTLRYL LSNLYDFTEA 

       670        680        690        700        710        720 
DLLPYEKLLP LDKWALGRLQ KFIEQITQYY EGFEYSKVYN ATVKYCTTEL SAVYLDILKD 

       730        740        750        760        770        780 
RLYVEAKDSI YRRSAQTALH YILEALIKIL APIIPFTAEE AYQESHLKRY ESVHLEYWPE 

       790        800        810        820        830        840 
VRKEFIDEAL LEEFDHLLLI RDDVLKALEN ARASDIIGHS LDAHVIIEAK NEELKNLLRK 

       850        860        870        880        890        900 
YESLLEEFFI VSKVTLSENI SGLNGQFANV LVQRAEGQKC QRCWKYHPDT GKDLEHPETC 

       910 
PRCSAVLRGE RK 

« Hide

References

« Hide 'large scale' references
[1]"Pullulanase type I from fervidobacterium pennavorans ven5: cloning, sequencing, and expression of the gene and biochemical characterization of the recombinant enzyme."
Bertoldo C., Duffner F., Jorgensen P.L., Antranikian G.
Appl. Environ. Microbiol. 65:2084-2091(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 9078 / Ven5.
[2]"Complete sequence of Fervidobacterium pennivorans DSM 9078."
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Noll K.M., Woyke T.
Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9078 / Ven5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF096862 Genomic DNA. Translation: AAD30388.1. Different initiation.
CP003260 Genomic DNA. Translation: AFG35844.1.
RefSeqYP_005471963.1. NC_017095.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFG35844; AFG35844; Ferpe_1791.
GeneID12058543.
KEGGfpe:Ferpe_1791.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01870.

Enzyme and pathway databases

BioCycFPEN771875:GLDA-1791-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_FERPD
AccessionPrimary (citable) accession number: Q9XDB4
Secondary accession number(s): H9UEA1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 5, 2012
Last modified: April 16, 2014
This is version 85 of the entry and version 3 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