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Q465G4 (SYI_METBF) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. 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:Mbar_A3613
OrganismMethanosarcina barkeri (strain Fusaro / DSM 804) [Complete proteome] [HAMAP]
Taxonomic identifier269797 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

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_1000022152

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
Q465G4 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 81BE7252A232D33A

FASTA1,058120,510
        10         20         30         40         50         60 
MIKEITAKYN AEQIEKKITQ LWKDSDAYRK TREHRKTGKR LFFVDGPPYT TGHIHLGTAW 

        70         80         90        100        110        120 
NKIIKDSILR YYSMNNRNIL ERPGWDMHGL PIEVKVEGVL GFKSKKDIES FGVENFIEKC 

       130        140        150        160        170        180 
KEFAINQKQE MTEQFQRLGV WMQWEAPYMT LKDDYIEAAW WTLKQASEKN LLDVGKRSVN 

       190        200        210        220        230        240 
WCPRCETAIA DSEVEYAERT DPSIYVKFKI KGEENTFIVI WTTTPWTIPA NVAVAVHPGF 

       250        260        270        280        290        300 
EYSKFRAIRQ DGSDEILIAA TDLIENVLRQ GRYVDYEVLE TMLGEDLTKL EYESPVGDLV 

       310        320        330        340        350        360 
PVQNEIKHGI YLADYVTAEN TGCVHIAPGH GMDDFNVGVK YNLPILCPVG PNGAYTEEAG 

       370        380        390        400        410        420 
EYAGKNVREA NPIVIEDLRK RNRLLAEGTV THRYGHCWRC KTPIIYLATE QWFLKVTDIK 

       430        440        450        460        470        480 
DKMLEAIDAV DWYPEWAGSA RFRTWVEGAR DWCISRQRYW GMPIPVWKCK KCGKLEVIGT 

       490        500        510        520        530        540 
KAELLEKSGA GSDVELHRPY VDKLTIPCEC GGEKKRVEDV FDVWFDSAVA SWATLKFPQT 

       550        560        570        580        590        600 
REQFDEWWPA DFITEGHDQT RGWFYSQLGA SMVGFGRAPY KSVLMHGFTL DAGGKKMSKS 

       610        620        630        640        650        660 
LGNVVSPIDV IDKYGADTLR AYVLSSSAPW DDLKFNQEEV ENVHRSINIL WNVFRFPLPY 

       670        680        690        700        710        720 
MALDNFDPLK VSLDSVKDAL REEDRWILSR IQSVVKAVDE AMSGYFLHKA VREILEFTLE 

       730        740        750        760        770        780 
DLSRWYIQLI RPRTWTEADD PDKLAAYRVL YEVYVTLTKL ISPFMPYLAE EMYQNLIRNV 

       790        800        810        820        830        840 
DPNALESVHM CDWPKVNEAY LDPELEAAMS TARSIVEAAS NARQKAGRKL RWPVSRIVVS 

       850        860        870        880        890        900 
PESEDAAKAV ERLRSVLMDQ TNSKAIVLTP VGESWDELGL EVIPDPSKIG PVFKKDAGKV 

       910        920        930        940        950        960 
IPALQKVDGF ALKKAFAEAG EFELSLADRT TVTVTPGMAN FKETLPEGTA SAESDAGLVY 

       970        980        990       1000       1010       1020 
VDANLTPELE AEGYAREVIR RLQDMRKELD LVVDENIRVS VRIEDERVLR LVETLKDLIA 

      1030       1040       1050 
EEVRAEILNL GSDIDVSGAL VKDWDVEGIA MKMGISKK 

« Hide

References

[1]"The Methanosarcina barkeri genome: comparative analysis with Methanosarcina acetivorans and Methanosarcina mazei reveals extensive rearrangement within methanosarcinal genomes."
Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.
J. Bacteriol. 188:7922-7931(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fusaro / DSM 804.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000099 Genomic DNA. Translation: AAZ72478.1.
RefSeqYP_307058.1. NC_007355.1.

3D structure databases

ProteinModelPortalQ465G4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269797.Mbar_A3613.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ72478; AAZ72478; Mbar_A3613.
GeneID3626315.
KEGGmba:Mbar_A3613.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAGARDWCI.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycMBAR269797:GHUW-3678-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_METBF
AccessionPrimary (citable) accession number: Q465G4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: April 16, 2014
This is version 70 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