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A2SPV6 (SYI_METLZ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:Mlab_0186
OrganismMethanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z) [Complete proteome] [HAMAP]
Taxonomic identifier410358 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanocorpusculaceaeMethanocorpusculum

Protein attributes

Sequence length1066 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 – 10661066Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022155

Regions

Motif47 – 5711"HIGH" region HAMAP-Rule MF_02003
Motif594 – 5985"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5971ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SPV6 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 7362A12BEBD8228A

FASTA1,066121,910
        10         20         30         40         50         60 
MKEISESYVP AVVENEVREY WKANNTYRET RKLHESGKPW LFVDGPPYTT GYIHLGTAWN 

        70         80         90        100        110        120 
KILKDAILRY HSMTGQHIIE RAGYDMHGLP IEVKVEEKLG FKNKADIEKY GVAKFIEECR 

       130        140        150        160        170        180 
EFALTHKDLM SEQFKDLGTW MDFDDPYQTV DKGYIEAAWY TLKRCEEEKM LERGSRVVNW 

       190        200        210        220        230        240 
CPRCGTAIAD AEVEYWDETD PSIFVKFPIQ GTENEYLVIW TTTPWTLPAN VAVAVGEEFV 

       250        260        270        280        290        300 
YAKCRAVKDG KSEDLWIAKE LAEQILKYGK YQDYSIIETK TGAELAGTKY ISPLASAVPM 

       310        320        330        340        350        360 
QAQIEHRVVI ADYVAMENTG MVHIAPGHGW DDYLVGLKEN LPAVCPVDGN GNFTDEAGIF 

       370        380        390        400        410        420 
AGKYVKAPET NQEVIDVLGD AMLAVRKITH RYGHCWRCKT PIIYRATSQW FLKVKDIREK 

       430        440        450        460        470        480 
MLEEIADEVT WYPEWAGSAR FHDWVEEARD WCISRQRYWG IPIPVWVCPV CNKYHVVGRY 

       490        500        510        520        530        540 
EELEQLSGQK MTDPHRPYVD DITIPCECGG TMKRIPDIFD VWYDSGIASW ATLRFPEKPE 

       550        560        570        580        590        600 
DFGKYWPADF ILEGHDQTRG WFYSQLALST IAFGKAPYKS VLMHGFALDA EGKKMSKSLG 

       610        620        630        640        650        660 
NVIAPEDVAK QFGVDVMRQY ILSANAPWDD MRFSLEGVKT NHRMFNVLWN VYKFPLPYMA 

       670        680        690        700        710        720 
LDGYKPAAKD GVWDPSAVED HISEFCREDR WLISRVNSLA EQVTKEMEVC NLHRATRPIS 

       730        740        750        760        770        780 
TFILDELSRW YVQLVRPRMW LEEESVSKMQ AYDTMYYVMR RLVTIFAPFA PHITECMYQN 

       790        800        810        820        830        840 
LRCEGDLPSV HMVDWFSGND ALRDPVLEEE MEIVQEFDEA VANARQNGKR KGRWPVGTVV 

       850        860        870        880        890        900 
VATDSEKVAG AVSAMNDMCC DRANARTVTV VKGVWDKLDW TAVPVMKVIG KQFGRDGPKV 

       910        920        930        940        950        960 
KAFIEEANGT KLKALLTADG KVSMEKDGFT AELTEEHMTF EEKMPENIFS SPMENGTIYV 

       970        980        990       1000       1010       1020 
DVTLTPELEA EGYSREVIRR IQEMRKQAGL AVDAKIKAEV VIDDARVMPL VDSKHDVIET 

      1030       1040       1050       1060 
EVRANCLKIR VPDGETCSCR VADEAILAMD WEIDDLKVRI SISKAE 

« Hide

References

[1]"Complete genome sequence of Methanocorpusculum labreanum type strain Z."
Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L., Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:197-203(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43576 / DSM 4855 / Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000559 Genomic DNA. Translation: ABN06362.1.
RefSeqYP_001029629.1. NC_008942.1.

3D structure databases

ProteinModelPortalA2SPV6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING410358.Mlab_0186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN06362; ABN06362; Mlab_0186.
GeneID4795794.
KEGGmla:Mlab_0186.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAKWIISEI.

Enzyme and pathway databases

BioCycMLAB410358:GH7C-189-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
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.
IPR023585. Ile-tRNA-ligase_type1.
IPR023586. Ile-tRNA-ligase_type2.
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_METLZ
AccessionPrimary (citable) accession number: A2SPV6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: May 14, 2014
This is version 53 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