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A6UVK2 (SYI_META3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:Maeo_0945
OrganismMethanococcus aeolicus (strain Nankai-3 / ATCC BAA-1280) [Complete proteome] [HAMAP]
Taxonomic identifier419665 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length1040 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 – 10401040Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022150

Regions

Motif47 – 5711"HIGH" region HAMAP-Rule MF_02003
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A6UVK2 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 21BA4C114FCB46B2

FASTA1,040121,325
        10         20         30         40         50         60 
MKEIKGKVDF REMDKEIKEF WENNEIYQKV KKLNENYPDY YFVDGPPYCS GSIHLGTAWN 

        70         80         90        100        110        120 
KTIKDTVLRF KRMQNYNVLD KAGWDMHGLP IEVKVEHEFN LQSKKDIETK VGTDVFIEKC 

       130        140        150        160        170        180 
KEFALNNKEV MENQFKNLGI WLDWENAYLP IKNDYIEAGW WSLKRAHEKE LLSKDLRVGY 

       190        200        210        220        230        240 
WCPRCETSLA EHEVRGEYQD VLDPSVYVKF KVADDNSYPN TYFVIWTTTP WTLISNLLIA 

       250        260        270        280        290        300 
VNPEFDYGFV EVIFDNERKE TWVIAEALVE AVIKLAKKQN NIKSYNIVKK VKGKELEGIK 

       310        320        330        340        350        360 
YVPALLEENE RQKEFFQLEK VHTIVLGEHV SLDGGTGLVH TAPGFGEEDF EVGKKYNSPI 

       370        380        390        400        410        420 
YSPIDDEGKY VEGKWKGVFV KDADEDIIAT LTDKNLIVNA GKKKHTYPHC WRCKTPLLFR 

       430        440        450        460        470        480 
STEQWFLNIS KIKNNIVEHA KNTDWVPNWV ETRYINGVKF VGDWNISRQR YWGIPLPIWI 

       490        500        510        520        530        540 
CENKDCGKYK IIGSVEELKQ EMINDIPIND DLHKPTVDKI IMKCDCGCEM KRTPDVLDVW 

       550        560        570        580        590        600 
YDSGLAPYAS INAKELKKAD FIVEGNDQVT KWFYSQHALS EIVFDDIPYK KCMMHGFTLD 

       610        620        630        640        650        660 
ETGEKMSKSI GNVVNPDDVV EEFGADLLRF YLLSANKAWE DLRFSIGEMN DVKSVFNTLW 

       670        680        690        700        710        720 
NSYSFAVNYM VLDDFSPNEE YFNYLRDEDK WIISKINSLT KEAIEVLEIP HLHEYTWKVR 

       730        740        750        760        770        780 
DFILNDLSRW YIKLIRNRTW MEKEDPDKLS AYQTLYYVLM KLVVILAPVA PHISEKIYQN 

       790        800        810        820        830        840 
LKIEGMPQSI FMTKIVVEEE YINKEVEEGI ETAREIVDAI LKGRDKVKYT LRYPISKIIL 

       850        860        870        880        890        900 
PNELGDIVNK YHYIIKEQGN VKNIEVKEFE GNISLKPNFR TLGASFKSDV PAVVKILNSQ 

       910        920        930        940        950        960 
NPKELKDKLA EGEITIDGFT IKPEHVEFKI DIPDNIVGME LRKGSVYIDI ELTEEIIKDG 

       970        980        990       1000       1010       1020 
LKREVIRRIQ SMRKDMDLDI EEKIKITMEG IEFNEDALKD IEKEVRGTFE PTIECDNIQE 

      1030       1040 
WNIKTPNGEV YNLKIGVKKN 

« Hide

References

[1]"Complete sequence of Methanococcus aeolicus Nankai-3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A. expand/collapse author list , Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nankai-3 / ATCC BAA-1280.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000743 Genomic DNA. Translation: ABR56524.1.
RefSeqYP_001325136.1. NC_009635.1.

3D structure databases

ProteinModelPortalA6UVK2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING419665.Maeo_0945.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR56524; ABR56524; Maeo_0945.
GeneID5327661.
KEGGmae:Maeo_0945.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARYVEGKW.

Enzyme and pathway databases

BioCycMAEO419665:GHVZ-957-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_META3
AccessionPrimary (citable) accession number: A6UVK2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 47 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