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Q6HER9 (SYI1_BACHK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. 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 1

EC=6.1.1.5
Alternative name(s):
Isoleucyl-tRNA synthetase 1
Short name=IleRS 1
Gene names
Name:ileS1
Ordered Locus Names:BT9727_3637
OrganismBacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]
Taxonomic identifier281309 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

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
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 1 HAMAP-Rule MF_02002
PRO_0000098352

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
Q6HER9 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: ABF082F44E94A891

FASTA921104,634
        10         20         30         40         50         60 
MEYKNTLLMP KTEFPMRGNL PKREPAMQEK WAEMNIYEKV QEHTKGRPLF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHMGHALN KVLKDFIVRY KSMTGFCAPY VPGWDTHGLP IEQALTNKGV KRKEMTVAEF 

       130        140        150        160        170        180 
RKLCAEYAYE QVERQREQFK RLGVRADWDN PYITLEPAYE AQQIKVFGDM AKKGYIYKGQ 

       190        200        210        220        230        240 
KPVYWSPTSE SALAEAEIEY QDKKSASIYV AFPVKDGKNV LEGDEKYIIW TTTPWTLPAN 

       250        260        270        280        290        300 
LGISVHPELE YAIVKVNDEK YIIASELFET VAKTLEWENA EVVKTVKGSE LEYTVAKHPF 

       310        320        330        340        350        360 
YDRDSLVMLG DHVTTDAGTG CVHTAPGHGE DDFVVGKKYG LEVLCPVDDK GVLTEEAPGF 

       370        380        390        400        410        420 
EGLFYDKANK PITEKLEEVG ALLKLTFITH SYPHDWRTKK PIIFRATAQW FASIEAFRKE 

       430        440        450        460        470        480 
LLEAVAETKW VPAWGETRLH NMVRDRGDWC ISRQRAWGVP IPVFYAENGD PIITDETINH 

       490        500        510        520        530        540 
VADLFREHGS NVWFEREAKD LLPEGFTHPG SPNGEFRKET DIMDVWFDSG SSHQAVLEER 

       550        560        570        580        590        600 
DDLQRPADLY LEGSDQYRGW FNSSLSTAVA VTGKAPYKGV LSHGFVLDGE GRKMSKSIGN 

       610        620        630        640        650        660 
IVVPKKIMDQ LGGDILRLWV SSVDYQSDVR ISDDILKQVA EVYRKIRNTF RFLLGNLDDF 

       670        680        690        700        710        720 
KPSENTVAVA ELREVDRYML VKLNDLITKV KEAYETYDFA AVYHAIHNFC TIDLSSFYLD 

       730        740        750        760        770        780 
FAKDILYIEG ANHEDRRAIQ TVLYDVLVAL TKLVTPILPH TADEVWPYIP GVTEESVQLT 

       790        800        810        820        830        840 
DMPEAVQLDD AEALKTKWDA FMTLRDDVLK ALEVARNEKV IGKSLNASIT LYPTAEMKAM 

       850        860        870        880        890        900 
LESINEDLKQ LFIVSEYKLG GMMEEAPADA PKYEHTAVVV AQATGETCER CWVVSETIGK 

       910        920 
DAEHETLCER CATVVKENYV K 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017355 Genomic DNA. Translation: AAT63892.1.
RefSeqYP_037957.1. NC_005957.1.

3D structure databases

ProteinModelPortalQ6HER9.
SMRQ6HER9. Positions 2-883.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281309.BT9727_3637.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT63892; AAT63892; BT9727_3637.
GeneID2857105.
KEGGbtk:BT9727_3637.
PATRIC18988298. VBIBacThu119411_3875.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycBTHU281309:GJID-3711-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 nameSYI1_BACHK
AccessionPrimary (citable) accession number: Q6HER9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 75 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