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O58792 (SYI_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. 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:PH1065
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length1066 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 – 10661066Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098590

Regions

Motif49 – 5911"HIGH" region HAMAP-Rule MF_02003
Motif625 – 6295"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6281ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O58792 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 4C9444C82BB14018

FASTA1,066125,941
        10         20         30         40         50         60 
MIKEPEFRDY TPGKLEEKIE EFWKENNIYQ KIKELRKNGP KYYFLDGPPY VSGAIHLGTA 

        70         80         90        100        110        120 
WNKIIKDMII RFRTMQGYNV WRQPGFDMHG LPIEVKVEQA LGLKTKKEIE EKIGVENFIK 

       130        140        150        160        170        180 
KCKEFALNNL KIMTEQFKML GIWMDWDDPY MTIKNEYIES AWFTLKKAWE KGLLEKDKRV 

       190        200        210        220        230        240 
LHWCPRCETA LAEHEVRGEY KLRKDPSIYV KFPIEGKENE YLLIWTTTPW TLPANLAVSA 

       250        260        270        280        290        300 
HPEYDYVKVK VEFNGKEEYW ILAKALVDKV LGEIGVKGEV IEEFKGRELE GLRYIHVLMD 

       310        320        330        340        350        360 
EYPRQKEFRE KYEWAHRIIL ADFVTLEEGT GLVHTAPGHG EEDFEVGKKY GLPIYSPVDD 

       370        380        390        400        410        420 
QGRYVEGKWK GIYVKEADPQ IIEHLKEKGY LVKAGEIEHK YPHCWRCKTP LIFRATDQWF 

       430        440        450        460        470        480 
LKVSKVKDRI IKENDEKVTW YPDWVKIRFD NGVRDSGDWV ISRQRYWGIP LPIWQSEDGE 

       490        500        510        520        530        540 
IYVVGSWREL VELAVAIEVN GERIDLPESY EEKLKVIEEK LGPEDLHRPY VDAFIIKVNG 

       550        560        570        580        590        600 
KEMRRVKDVV DVWFDSGIAS WASLGYPRNK ELFEKLWPAD FIVEGEDQVT KWFYSQQAAS 

       610        620        630        640        650        660 
VIAFDTVPYR RVAMHGYVLD EKGDKMSKSL GNIIRPEEVV EKAGRDTFRF YMLWATNPWE 

       670        680        690        700        710        720 
NLKFSWKGVE QVRRMLNILW NVYVLSATYM SLDNFDPRNV KVEELAFREE DKWILSRVNS 

       730        740        750        760        770        780 
LIREVENGIE TFYLTKATRA LYNFVVEDLS RWYVRLIRKR LWVEGDDPDK LAAYYTLWKV 

       790        800        810        820        830        840 
FDVLLRLMAP FTPYITEEIY QNLMRPFIGI ESVHMLDWPK VDESAVDEDL EKEMEFIRRI 

       850        860        870        880        890        900 
VEAGSAARQK ARIKLRYPVR KIIIETQDET VKKAVERLNY ILRDQLNAKE VVIGKVEREL 

       910        920        930        940        950        960 
TVKPNFAKVG PEFKGDSRLV AKWINEHGLE LYEKGEVDVE IEGKKFHLTR EHIIVEEKLP 

       970        980        990       1000       1010       1020 
DFLVAEDFEG GRVYVDKTLT RELLAEGLAR EFVRRIQEMR KRLDLDVNDR IVVTIETTDD 

      1030       1040       1050       1060 
NRELLQENLD YIMRETRAIE VRFEEAKGYV VEWPEVQAKI GIEKVE 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA30164.1.
PIRF71100.
RefSeqNP_142976.1. NC_000961.1.

3D structure databases

ProteinModelPortalO58792.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING70601.PH1065.

Proteomic databases

PRIDEO58792.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA30164; BAA30164; BAA30164.
GeneID1443389.
KEGGpho:PH1065.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAPSWYIRT.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-1060-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. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_PYRHO
AccessionPrimary (citable) accession number: O58792
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 90 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