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B9L8Z9 (SYI_NAUPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:NAMH_0696
OrganismNautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH) [Complete proteome] [HAMAP]
Taxonomic identifier598659 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaNautilialesNautiliaceaeNautilia

Protein attributes

Sequence length911 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 – 911911Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189183

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8871Zinc By similarity
Metal binding8901Zinc By similarity
Metal binding9021Zinc By similarity
Metal binding9051Zinc By similarity
Binding site5641Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B9L8Z9 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 2061D723A2AA6983

FASTA911104,913
        10         20         30         40         50         60 
MDYKDTLLLP KTTFPMRGNL PQNEPKKYKK WFSEHVYERM KQNRVGNDKF NLHDGPPYAN 

        70         80         90        100        110        120 
GHIHIGHALN KILKDMIVKY YYFQGFDVRY TPGWDCHGLP IEQQVEKKIG REKKESLPKS 

       130        140        150        160        170        180 
KVRELCRQHA AKFIEIQKEE FQNLGVIGDW DNPYKTMDFE FEANIYKALA EIAKKGLLVE 

       190        200        210        220        230        240 
RSKPVFWCMH DKTALAEAEV EYEDKEDYSI YVAFPLSNEA KSKLGIDNAS IVIWTTTPWT 

       250        260        270        280        290        300 
LPANMGIALN PEEKYVLSED GKIVAKELYE NLKEAEVVSG EIVKEFDASE LENLKAINPL 

       310        320        330        340        350        360 
NGRESVIILG EHVTMDGGTG CVHTAPGHGE EDYRVWLKYG FSEILQPVDD EGKYSNLIVT 

       370        380        390        400        410        420 
EKLLPEEFKG MHIFEANPKI LDLLGDNLVK VSKFTHSYPH CWRCHNPVIF RATKQFFIAM 

       430        440        450        460        470        480 
DKEVNGDTLR HRALSEIEKV EFTPKTGKNR LSTMVANRPD WCISRQRDWG VPIAFFRNKD 

       490        500        510        520        530        540 
TGELIIDDEI IENVYEIFKV KGADAWYDLS IEELLPESKK EMASKLEKVN DILDVWFDSG 

       550        560        570        580        590        600 
STWFAVLKNG PYDAGEYPAN MYLEGSDQHR GWFQSSLLVS TSIEERAPYK SILTHGFTVD 

       610        620        630        640        650        660 
EKGEKMSKSK GNVVAPQEVS KKFGTEILRL WVATSDYSGD IKISDGILKQ VAEQYRKIRN 

       670        680        690        700        710        720 
TIRFLLANVN DLEEIKLTNP SMIDRWILAR SKEVFDEVVA LFGKYDFSKA FNILNNFIVT 

       730        740        750        760        770        780 
ELSAIYMDVC KDRLYCEPLN SEKRRNSQST MAVIVKELIS LLAPVLTYTM DEAVEHAPKV 

       790        800        810        820        830        840 
IKEDAKDVFD FVYTPLTAVE NPIDEEILEI RRRFFEIVDR LKKEKVIKDT LELAIETNYD 

       850        860        870        880        890        900 
KLLVDEMADF FVVSLISDNI EGETLDEFHI SDEQFVVKIK RSPLHKCPRC WRYLAEEEGA 

       910 
LCERCEKAIN G 

« Hide

References

[1]"Adaptations to submarine hydrothermal environments exemplified by the genome of Nautilia profundicola."
Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K., Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.
PLoS Genet. 5:E1000362-E1000362(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1463 / DSM 18972 / AmH.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001279 Genomic DNA. Translation: ACM92881.1.
RefSeqYP_002607107.1. NC_012115.1.

3D structure databases

ProteinModelPortalB9L8Z9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING598659.NAMH_0696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM92881; ACM92881; NAMH_0696.
GeneID7504838.
KEGGnam:NAMH_0696.
PATRIC22676107. VBINauPro131435_0667.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAERLMLHQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycNPRO598659:GH7N-694-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_NAUPA
AccessionPrimary (citable) accession number: B9L8Z9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 41 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