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Q12ZD1 (SYI_METBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:Mbur_0185
OrganismMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M) [Complete proteome] [HAMAP]
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length1058 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 – 10581058Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022153

Regions

Motif48 – 5811"HIGH" region HAMAP-Rule MF_02003
Motif596 – 6005"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site5991ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12ZD1 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 33EE2B998BACB728

FASTA1,058120,483
        10         20         30         40         50         60 
MIKEVTDQYN AKEIETKVHE FWEANNAYRS VREHRKGAKK FYFVDGPPYT TGHIHLGTAW 

        70         80         90        100        110        120 
NKIIKDSILR YMSMNDHDIL DRAGWDMHGL PIEVKVEGAL GFESKKDIET YGVGNFIEKC 

       130        140        150        160        170        180 
KEFALRQKDD MTEQFQTLGV WLDWEDPYMT LKDEYIEAAW WTLKQAQDKN LLETGKRVVN 

       190        200        210        220        230        240 
WCPRCETAIA DAEVEYEDRE DPSTYIKFKL KDEDNTFVVI WTTTPWTIPS NIAVAVHPEF 

       250        260        270        280        290        300 
EYSKVKAISE NSATEILIIA SELVENVLRI GRYLDYEILS TMSGKDLEGT VYEHPLADLV 

       310        320        330        340        350        360 
PLQAEIEHRI CNADYVTADS TGCVHIAPGH GVDDFEVGVK NEFPIFCPVG PNGSYTHEAG 

       370        380        390        400        410        420 
KYCGMNILDA NRVVMDDLLE RGLLMAERMI SHRYGHCWRC KTAIIYLATE QWFLKIGELK 

       430        440        450        460        470        480 
EDMLEEIKKV NWTPEWAGSA RFKDWIEGAR DWCISRQRYW GIPIPVWKCS SCNSLTVVGT 

       490        500        510        520        530        540 
RKELIERSGA DPHIELHRPY VDKVTIPCEC GGTMKRVEDV FDVWFDSAVA SWATLRFPHQ 

       550        560        570        580        590        600 
KEKFNEWWPA DFITEGHDQT RGWFYSQLGA SMVAFGKAPY KNVLMHGFTL DGSGKKMSKS 

       610        620        630        640        650        660 
IGNVIQPAEV IDKFGADTLR SYVLSASAPW EDLKFNWDEL ATVHRTNNIL WNVYRFPLPY 

       670        680        690        700        710        720 
MALDDFDPQK VSYESVEAYL RSEDKWILSR MQTVIAEVNK AMDARLLHKA MRSINEFVLE 

       730        740        750        760        770        780 
DLSRWYIQLI RPRTWVEADN PDKLAVYRVL YDVFVTTAKL IAPFMPHLAE EMYQNLVRNI 

       790        800        810        820        830        840 
DENAPVTIHL CDWPVVNEAL VDTSLEAQMK VARSIVEASS NARQKVGRKL RWPVSRIVVS 

       850        860        870        880        890        900 
PTDENTIAAV EGLRSVLMDQ TNAKDIETTK VGESWNELGV ESTPNPGAIG PVFKGNAGNI 

       910        920        930        940        950        960 
SAAIGAMDAY DLKKGLAGGE MEISLADGTN VTITEKMVNF SETVPEDVGS AEFNCGVVFV 

       970        980        990       1000       1010       1020 
DAKLTHEIES EGYSREVIRR IQDMRKELDL DVDDSIRGHI QISDERVLDL VLDFENYIAK 

      1030       1040       1050 
EVRANVLVIG LDVETTGELA KEWNVEGIPM TIAISKEE 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242 / NBRC 107633 / OCM 468 / ACE-M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE51195.1.
RefSeqYP_564945.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12ZD1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259564.Mbur_0185.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE51195; ABE51195; Mbur_0185.
GeneID3997152.
KEGGmbu:Mbur_0185.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAKPVHWCL.

Enzyme and pathway databases

BioCycMBUR259564:GHBZ-195-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_METBU
AccessionPrimary (citable) accession number: Q12ZD1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 56 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