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A0B7P3 (SYI_METTP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 52. 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:Mthe_0929
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length1049 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 – 10491049Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000022157

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
A0B7P3 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: F491CBA9FA700B1E

FASTA1,049121,605
        10         20         30         40         50         60 
MIVEVPGQYN PKNVEDEVRE FWHREDTYHK VRRLRSGGRR FFFVDGPPYT TGRIHLGTAW 

        70         80         90        100        110        120 
NKVIKDSILR YMSMRGYDLK DRAGWDMHGL PIEVKVEEHL GFRSKRDIES YGVDRFIEQC 

       130        140        150        160        170        180 
KSFALRQKDE MTEQFKSLGV WLDWDNPYMT LKNEYIEAAW WTLKRAHERG LLERGLRVVN 

       190        200        210        220        230        240 
WCPRCQTAIA DSEVEYWDES DPSIYVKFPV EGEDNTYIVI WTTTPWTIPA NVAVAVHKDF 

       250        260        270        280        290        300 
MYSKVRAWRR DGTYEILIMA TDLIENVLKQ GRYVDYEILE SMRGEDLLSL TYKNPLQDLV 

       310        320        330        340        350        360 
PAQRDIVHRV HLADFVTAEN TGIVHIAPGH GLEDYELGLE KRLPIFCPVG EDGRYTSEAG 

       370        380        390        400        410        420 
KKYEGKYVRD ANPEVVEDLM ERGALLASGE LVHRYGHCWR CKTPIIFIAT RQWFIGISEL 

       430        440        450        460        470        480 
RDQMLKEIER VSWYPDWAGS ARFKDWISNA RDWCISRQRY WGIPLPIWIC RSCGAMDVIG 

       490        500        510        520        530        540 
TAAELEARAG RPVEDLHRPA VDDVRLRCSC GGAMERVPDV FDVWFDSAVA SWATLNFPRD 

       550        560        570        580        590        600 
EEEFRVWWPA DFITEGHDQT RGWFYSQLGA SMVAFGRAPY KSVLMHGFTL DEQGRKMSKS 

       610        620        630        640        650        660 
IGNVVHPEDV VERYGADTLR FYVLSSNAPW EDLHFSWEGA MNVNRMLNIL WNAYRFPLPY 

       670        680        690        700        710        720 
MVLDRFDISK ADTSKYDLRP EDRWIISRVN SLAKEIEENM SGYMLHRATR SLQEFVLEDL 

       730        740        750        760        770        780 
SRWYIQLVRP RTWIETEDPD KLAAYATLYN VMSTLVKLMA PFTPFLAESI YQNLVRGLDP 

       790        800        810        820        830        840 
SAPESVHMCD WPGYREDLID KGLEESMSYV REISEAAANA RQKGGRKLRW PVSRIIIASD 

       850        860        870        880        890        900 
EQLDLRDLLH VLRTQTNSKE VIILPPGEKP EMNLEISVVQ KKIGPVFKGE SRDVVEALTS 

       910        920        930        940        950        960 
MNPKEVKRII ESGEPLEWKG RSYMITEEMV EFREIPPANL IPAEFSKGTV YVDVSLTDEL 

       970        980        990       1000       1010       1020 
RAEGYAREII RRIQDMRKDL DLKVDEMIRV SVALNSNEVV DLVSGWRDYI SSEVRATLLR 

      1030       1040 
IGNDLDLEGE LTKDWEVDGV KIRVSVARA 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000477 Genomic DNA. Translation: ABK14717.1.
RefSeqYP_843357.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B7P3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349307.Mthe_0929.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK14717; ABK14717; Mthe_0929.
GeneID4463322.
KEGGmtp:Mthe_0929.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMAGARDWCI.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycMMET349307:GHKI-959-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_METTP
AccessionPrimary (citable) accession number: A0B7P3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 52 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