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Q8Y5N8 (SYI_LISMO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. 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:lmo2019
OrganismListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]
Taxonomic identifier169963 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length921 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
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 – 921921Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098411

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif593 – 5975"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8881Zinc By similarity
Metal binding8911Zinc By similarity
Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Binding site5521Aminoacyl-adenylate By similarity
Binding site5961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Y5N8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: A1FB8ED2EB475471

FASTA921103,851
        10         20         30         40         50         60 
MEYKDTLLMP KTDFPMRGNL PNKEPEWQAK WEEEKLYEKI QEKNAGRPTY ILHDGPPYAN 

        70         80         90        100        110        120 
GELHMGHALN KTIKDIIVRY KSMAGFSSPY VPGWDTHGLP IETAIAKKGV KRKEMSIAEF 

       130        140        150        160        170        180 
RKLCAEYAMK QVDGQRTGFK RLGINGDWEN PYITLLPEYE AEQIKVFGEM AKKGYIYKGK 

       190        200        210        220        230        240 
KPVYWSPSSE SALAEAEIEY QDKTSASIFV AFKVTDGKGV LDEGTNIVIW TTTPWTIPAN 

       250        260        270        280        290        300 
MGITVNPDLD YVVIESAGEK YVVAEALLPS LREKLGFEDA TVVKTVRGSE LDRVVTKHPF 

       310        320        330        340        350        360 
YDRDSLVMNG EHATAEAGTG AVHTAPGHGE DDFLIGKKYD LEILAPLDDR GVFTEEAPGF 

       370        380        390        400        410        420 
EGVFYDTANK MVTEKLEEVG ALLKMEFITH SYPHDWRTKK PVIFRATAQW FASIDAFRDD 

       430        440        450        460        470        480 
LLAAVKGVNW TPAWGETRLF NMVRDRGDWV ISRQRAWGVP LPIFYAENGE AIITDETINH 

       490        500        510        520        530        540 
ISELFREHGS NVWFERDVKD LLPAGFTHPG SPNGEFTKET DIMDVWFDSG SSHQAVLNAR 

       550        560        570        580        590        600 
PELSRPADLY MEGSDQYRGW FNSSLTTAVA ITGEAPYRNV LSHGFALDGE GRKMSKSLGN 

       610        620        630        640        650        660 
TLLPGKVIKQ LGADIVRLWV ASVDYQADVR VSDEILKQVS EVYRKIRNTM RFLLGNINDF 

       670        680        690        700        710        720 
NPTTNTVSYE NLREVDKYML IKLNDLVKNV KDSYEAFEFS TIYHQINNFC TVELSQFYMD 

       730        740        750        760        770        780 
FAKDVVYIEA ADSHDRRAMQ TVFYEAVVTL TKLLAPILPH TTEEVWNSLI GEGAESIHLQ 

       790        800        810        820        830        840 
DLPDVKVLAN SEEITAKWDA FMQIRDNVQK ALEFARNEKL IGKSMLAKVT LYVDGEAKTL 

       850        860        870        880        890        900 
FDSLEGDFAQ LFIVSDFELV EGLENAPESA FKSNQVAVQI TVAEGETCER CRVVKKDVGV 

       910        920 
NPKHPTLCGR CADIVVKHYE A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591981 Genomic DNA. Translation: CAD00097.1.
PIRAC1327.
RefSeqNP_465543.1. NC_003210.1.

3D structure databases

ProteinModelPortalQ8Y5N8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169963.lmo2019.

PTM databases

PhosSiteP11121157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD00097; CAD00097; CAD00097.
GeneID986874.
KEGGlmo:lmo2019.
PATRIC20313237. VBILisMon69206_2067.

Organism-specific databases

GenoListLMO2019.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.
PhylomeDBQ8Y5N8.

Enzyme and pathway databases

BioCycLMON169963:LMO2019-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.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. 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.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
PF06827. zf-FPG_IleRS. 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_LISMO
AccessionPrimary (citable) accession number: Q8Y5N8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 82 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