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Q8ER41 (SYI1_OCEIH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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:OB1484
OrganismOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831) [Complete proteome] [HAMAP]
Taxonomic identifier221109 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeOceanobacillus

Protein attributes

Sequence length918 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 – 918918Isoleucine--tRNA ligase 1 HAMAP-Rule MF_02002
PRO_0000098432

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif594 – 5985"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8851Zinc By similarity
Metal binding8881Zinc By similarity
Metal binding9051Zinc By similarity
Metal binding9081Zinc By similarity
Binding site5531Aminoacyl-adenylate By similarity
Binding site5971ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ER41 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: CDCAD9A3F063C7B7

FASTA918104,887
        10         20         30         40         50         60 
MDYKQTLLMP KTAFPMRGNL PNKEPERQKK WEETNQYAKT LERTKGRPLF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHIGHALN KVLKDFIVRY KSMTGYHAPY IPGWDTHGLP IETALTKKKK IKRKEMDIAA 

       130        140        150        160        170        180 
FRKLCEEYAL GQINNQREQF KQLGVRGDWD NPYITLTKDY EASQIKVFGD MARKGYIYKG 

       190        200        210        220        230        240 
LKPVYWSPSS ESALAEAEIE YQDKRSPSIY VAFEVKGGQA LLSGGEKFII WTTTPWTLPA 

       250        260        270        280        290        300 
NLGISLHADL TYIVVQVGEE KYIIAEALFD DVSESLGWEN PQVLQSFKGK EAEGIEAQHP 

       310        320        330        340        350        360 
FYDRTSLVML GEHVTTDAGT GCVHTAPGHG EDDFYVSRSY GIDAFCPVDE KGVFTQEAPG 

       370        380        390        400        410        420 
FEGLFYDEAN KIITEKLDAS GALLKLEFIT HSYPHDWRTK KPTIFRATSQ WFASIKDFRV 

       430        440        450        460        470        480 
DILEEIKQVN WYPHWGETRL YNMVRDREDW CISRQRAWGV PIPVFYGEDG TPIITDETIN 

       490        500        510        520        530        540 
HVSELFREHG SNIWFEKEAK ELLPEGFTSE HSPNGNFAKE TDIMDVWFDS GSSHEGVLLN 

       550        560        570        580        590        600 
RQNHQRPANV YLEGSDQYRG WFNSSLSTSV AVTGKAPYKA VISHGFVLDG NGRKMSKSLG 

       610        620        630        640        650        660 
NVIVPSKVQK QLGSDILRLW VSSVDYQADV RISDDILKQT SESYRKIRNT FRFLLANLAD 

       670        680        690        700        710        720 
FNPNTDRVKE ENMEEVDRYM VHRLQNVLAE AHKNYNQYEF APVFQQIHHF CSVDLSSFYL 

       730        740        750        760        770        780 
DFAKDILYIE AKDHPRRRSI QTGYYEVLTS LVKLIAPIIP HTAEEVWEYI PEPEAESVHL 

       790        800        810        820        830        840 
TDIPEARDVA INEQTVDKWN HFMKIRDDVL KALEEARSEK VIGKSLEAKI SIAAKDEGTK 

       850        860        870        880        890        900 
KVLDEMEHLH QYFIVSEAVI VDTLTDAKEG NVVNVQVEVH PGETCDRCWV SSETVGENKN 

       910 
HPSLCSRCAD VVTKHYAD 

« Hide

References

[1]"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
Takami H., Takaki Y., Uchiyama I.
Nucleic Acids Res. 30:3927-3935(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000028 Genomic DNA. Translation: BAC13440.1.
RefSeqNP_692405.1. NC_004193.1.

3D structure databases

ProteinModelPortalQ8ER41.
SMRQ8ER41. Positions 2-866.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING221109.OB1484.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC13440; BAC13440; BAC13440.
GeneID1017739.
KEGGoih:OB1484.
PATRIC22793988. VBIOceIhe82024_1510.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycOIHE221109:GI2A-1562-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_OCEIH
AccessionPrimary (citable) accession number: Q8ER41
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 80 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