Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8TN62 (SYI_METAC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. 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:MA_2431
OrganismMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) [Reference proteome] [HAMAP]
Taxonomic identifier188937 [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
Reference 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_0000098583

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
Q8TN62 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 3940FED68C23AEA3

FASTA1,058120,217
        10         20         30         40         50         60 
MIKEITAKYN AEQIEKKVTQ FWEDSDAYRK TRERRKTGKR LFFVDGPPYT TGHIHLGTAW 

        70         80         90        100        110        120 
NKIIKDTILR YYSMNNRYIL ERPGWDMHGL PIEVRVEGVL GFKSKKDIES FGVENFIEKC 

       130        140        150        160        170        180 
KEFAITQKQA MTEQFQRLGV WMQWPEPYMT LKDDYIEAAW WTLKQAHEKD LLEVGKRSVN 

       190        200        210        220        230        240 
WCPRCETAIA DSEVEYSERT DPSIYVKFKV KGEENTFIVI WTTTPWTIPA NVAVAVHPAY 

       250        260        270        280        290        300 
EYSKFRAIRQ DGSEEILIAA TELIKNVLKQ GRYADFKVLE TMLGEELTKL EYESPVGDLV 

       310        320        330        340        350        360 
PIQNEIKHGV YLADFVTVEN TGCVHIAPGH GMDDFNLGVK HKLPILCPVG SNGAYTEEAG 

       370        380        390        400        410        420 
EYAGKNVREA NPIVIEDLKA RNRLLAEGTV THRYGHCWRC KTPIIYLATE QWFLKITEIK 

       430        440        450        460        470        480 
EKMLEEIDAV DWYPDWAGSA RFRTWVEGAR DWCISRQRYW GIPLPVWKCK KCGKLEVIGT 

       490        500        510        520        530        540 
KAELLEKAGL SGDIELHRPY VDRVTVPCEC GGEKKRVEDV FDVWFDSAVA SWATLKFPQT 

       550        560        570        580        590        600 
HDQFDEWWPA DFVTEGHDQT RGWFYSQLGA SMVGFGRAPY KSVLMHGFTL DAGGKKMSKS 

       610        620        630        640        650        660 
LGNVVSPLDI IDRLGADTLR AYVLSSSAPW EDLKYNLEEV ETVHRSINIL WNVFRFPLPY 

       670        680        690        700        710        720 
MALDNFDPMQ VSLDSVKDAL REEDRWILSR AQSVIKAVNE AMSGYLLHKA VREILEFALE 

       730        740        750        760        770        780 
DLSRWYIQLI RPRTWTEADD PDKLAAYCVL YEVYVTITKL ISPFMPYLAE EMYQNLIRNV 

       790        800        810        820        830        840 
DPNAPESVHM CDWPKVNDTY LDPELEVAMD TVRSIVEAAS NARQKAGRKL RWPVSRIIVS 

       850        860        870        880        890        900 
PESEAAAKAV NRLGSVLMDQ TNSKAIVLTG VGKSWDELGL EVIPDPGKIG PVFKKDAGRV 

       910        920        930        940        950        960 
IPALQKVEGF TLKKAFAETG EFELTLADGT TVPVTSGMAN FKETLPEGTA SAESDAGLVY 

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

      1030       1040       1050 
EEVRADVFDL GSSIEVSGTL VKDWDVEGTA MKMGIAKK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010299 Genomic DNA. Translation: AAM05817.1.
RefSeqNP_617337.1. NC_003552.1.

3D structure databases

ProteinModelPortalQ8TN62.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING188937.MA2431.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM05817; AAM05817; MA_2431.
GeneID1474320.
KEGGmac:MA2431.

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAGARDWCI.
PhylomeDBQ8TN62.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycMACE188937:GI2O-2453-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_METAC
AccessionPrimary (citable) accession number: Q8TN62
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 73 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