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B3DYQ6 (SYI_METI4) 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:Minf_0370
OrganismMethylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain V4)) [Complete proteome] [HAMAP]
Taxonomic identifier481448 [NCBI]
Taxonomic lineageBacteriaVerrucomicrobiaunclassified VerrucomicrobiaMethylacidiphilalesMethylacidiphilaceaeMethylacidiphilum

Protein attributes

Sequence length907 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_02002

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02002

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_02002

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02002

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02002.

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_02002

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 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 – 907907Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216241

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif590 – 5945"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8671Zinc By similarity
Metal binding8701Zinc By similarity
Metal binding8891Zinc By similarity
Metal binding8921Zinc By similarity
Binding site5491Aminoacyl-adenylate By similarity
Binding site5931ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3DYQ6 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 74707C11A679ECDF

FASTA907103,868
        10         20         30         40         50         60 
MDYSLTVLLP KTDFPMKANL PQREPHWIEV WEKEKVYSTL LEKRKNCPQF ILHDGPPFAN 

        70         80         90        100        110        120 
GKAHMGSGLN KILKDIVLKS RNMLGFQCPY IPGWDCHGLP IEHKVMSEYP ALAADPLSIR 

       130        140        150        160        170        180 
NKCKEYARYW IEIQKEQFRR LGILGSWDNP YITMDPGYEA AELRLFAELV EKKWVYRGLR 

       190        200        210        220        230        240 
PVFWSVGCRT ALAEAEIEYQ KKEDIAIYVE FPVGEEELKK AGLPQGTSFL AWTTTPWTLP 

       250        260        270        280        290        300 
ANLALAVSPD LSYELRQVGG KKFIVAGKLA ESIPGFSHSV VLLSFPSGQN LEGLKYNHPL 

       310        320        330        340        350        360 
LPREGVVYTA DFVSGETGSG IVHIAPGHGM EDYQLGMVHG LEVYSPVDDQ GRFTKQCGIE 

       370        380        390        400        410        420 
KIVGLSVFEA NSILCAMLKE KGLLWAKYPY VHDYPFCWRS KTPIIFRSVP QWFIAIEAFK 

       430        440        450        460        470        480 
SLALKEIERV NWIPSRGENR IKGAVESRKD WCISRQRYWG VPIPAFYKKS GEAILDPSII 

       490        500        510        520        530        540 
RRFADKVEEE GTDLWFRLES KELCQLLGLA PSEDLVKGLD TLDVWIDSGS SHYSVLKPRG 

       550        560        570        580        590        600 
EDPADLYLEG SDQHRGWFQS SLLLSVASKG KAPYKSVLTH GFVVDLDGKK LSKSSGARDL 

       610        620        630        640        650        660 
SEQIQTYGAD LLRLWVASEE YAEDVPFSKE IFSRLSDSYR LIRNSLRILL GNLHDFNPQE 

       670        680        690        700        710        720 
QSLPDDRLRE IDRYFELCVN KLVKKTKAFY ENYEFSQVYQ ALTRFCSVEL SSFYIDILKD 

       730        740        750        760        770        780 
RLYCDGQNWL SRRSAQTVLY RTFECLVKLL APILPFTTEE AWRASGKTSS IHLELFPEER 

       790        800        810        820        830        840 
EIKEEEKLLK RWEKILQLRD LANRELEKAR KQKMIGKNLE AKLILFTDDF EAEDTALLTE 

       850        860        870        880        890        900 
VFLVSQLEII RSSKTEILVE KALGKKCPRC WKFSLFAQSN SDPQYPHVCP RCLKVLKGLP 


ESFLVSD 

« Hide

References

[1]"Complete genome sequence of the extremely acidophilic methanotroph isolate V4, Methylacidiphilum infernorum, a representative of the bacterial phylum Verrucomicrobia."
Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y., Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V., Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F. expand/collapse author list , Feng L., Wang L., Alam M.
Biol. Direct 3:26-26(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Isolate V4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000975 Genomic DNA. Translation: ACD82428.1.
RefSeqYP_001939026.1. NC_010794.1.

3D structure databases

ProteinModelPortalB3DYQ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING481448.Minf_0370.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD82428; ACD82428; Minf_0370.
GeneID6351287.
KEGGmin:Minf_0370.
PATRIC22489765. VBIMetInf111569_0389.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMATALWQIT.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycMINF481448:GJEI-377-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 1 hit.
HAMAPMF_02002. Ile_tRNA_synth_type1.
InterProIPR002300. aa-tRNA-synth_Ia.
IPR002301. Ile-tRNA-ligase.
IPR023585. Ile-tRNA-ligase_type1.
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.
ProtoNetSearch...

Entry information

Entry nameSYI_METI4
AccessionPrimary (citable) accession number: B3DYQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 22, 2008
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