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A1TYY9 (SYI_MARAV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:Maqu_0862
OrganismMarinobacter aquaeolei (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter hydrocarbonoclasticus (strain DSM 11845)) [Complete proteome] [HAMAP]
Taxonomic identifier351348 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeMarinobacter

Protein attributes

Sequence length939 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 – 939939Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022091

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9021Zinc By similarity
Metal binding9051Zinc By similarity
Metal binding9221Zinc By similarity
Metal binding9251Zinc By similarity
Binding site5641Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TYY9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: DA9F41B2A0343794

FASTA939105,741
        10         20         30         40         50         60 
MSDYKHTLNL PETAFPMRGN LAKREPDMLK HWQDLNVYGN LRKQRQGREK FILHDGPPYA 

        70         80         90        100        110        120 
NGSIHIGHAV NKILKDMIVK SRSFMGYDAP YVPGWDCHGL PIEHKVEQEI GKAGVKVDYK 

       130        140        150        160        170        180 
TFRQACRDYA TKQIEGQKTD FIRLGVMGEW DKPYLTMDPK VEAGIVRALG KIVAKGHLVR 

       190        200        210        220        230        240 
GFKPVYWSVV GQSALAEAEV EYQDKTSTQI DVRFTVVDRD AVLKTFGTSE GEGDVSLVIW 

       250        260        270        280        290        300 
TTTPWTIPAN QAVSIGADIE YALVQVDVGH GAERMILATD MVQGIMARWG VEDYKVLANA 

       310        320        330        340        350        360 
AGSALENQLL HHPVYDKQVP VLLGDHVSLD AGTGAVHTAP DHGMEDFVVG KEYGIGTLNL 

       370        380        390        400        410        420 
VKADGTYTDA AGEFAGVHVY KADEPVCAAL EREGKLVRSE KFRHSYPHCW RTKTPLIYRA 

       430        440        450        460        470        480 
TPQWFISMDK LNLRADALEA IKGVRWVPAW GQNRIEAMFE QSPDWCISRQ RTWGVPITLF 

       490        500        510        520        530        540 
IHKETQELHP NTQELIEKVA QAVETGGIDA WYDIDQNELL GADADQYEKV LDTLDVWFDS 

       550        560        570        580        590        600 
GVTHDSVLRV REELGQFPAD MYLEGSDQHR GWFQSSLKTS IAMNGVAPYK QVLTHGFTVD 

       610        620        630        640        650        660 
AKGYKMSKSL GNVIAPQEVM NELGADILRL WVSATDYSGE MSVSKDILRQ TADGYRRIRN 

       670        680        690        700        710        720 
TARFLLSNLT GFDPDQHMVA PEDMIALDRW MVDRALQLQN ELHEDYGNYA FLRIYQKVYN 

       730        740        750        760        770        780 
FCEATLGGFY LDIIKDRQYT TQADSLARRS CQTALYHVAE ALVRWIAPIL SFTADEIWQH 

       790        800        810        820        830        840 
LPGKRGDTVF YETWYEGLTA LPEGFELGRD YWREIYAVKE AVNKCLEEVR ARGEIKGSLS 

       850        860        870        880        890        900 
AEVTLYCEGS LAERLNYLGE ELRFVLITSE ATVKPVSEAA GVEQTNLEGL LVKVTPATHA 

       910        920        930 
KCERCWHHRE DVGQNEQYSD LCGRCVTNVE GPGETRAYA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Edwards K., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700491 / DSM 11845 / VT8.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000514 Genomic DNA. Translation: ABM17958.1.
RefSeqYP_958145.1. NC_008740.1.

3D structure databases

ProteinModelPortalA1TYY9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351348.Maqu_0862.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM17958; ABM17958; Maqu_0862.
GeneID4655096.
KEGGmaq:Maqu_0862.
PATRIC22456948. VBIMarAqu65105_1260.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKKRIELM.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycMHYD351348:GHYZ-876-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_MARAV
AccessionPrimary (citable) accession number: A1TYY9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 56 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