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B7KFT1 (SYI_CYAP7) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. 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:PCC7424_5054
OrganismCyanothece sp. (strain PCC 7424) (Synechococcus sp. (strain ATCC 29155)) [Complete proteome] [HAMAP]
Taxonomic identifier65393 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length959 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 – 959959Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189147

Regions

Motif60 – 7011"HIGH" region HAMAP-Rule MF_02002
Motif610 – 6145"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9281Zinc By similarity
Metal binding9311Zinc By similarity
Metal binding9481Zinc By similarity
Metal binding9511Zinc By similarity
Binding site5691Aminoacyl-adenylate By similarity
Binding site6131ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B7KFT1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 69BC3E8FB4EF089F

FASTA959109,390
        10         20         30         40         50         60 
MTEAKSYKDT VNLPQTKFDM RANAVKREPE LQKFWAENQI YETLSENNPG DIFILHDGPP 

        70         80         90        100        110        120 
YANGSLHMGH ALNKTLKDII NKYKLQRGYK ARYVPGWDCH GLPIELKVLQ SMKQKEREDL 

       130        140        150        160        170        180 
TPLKLRHKAR DFALSTQKEQ SESFQRFGVW GDWEHPYLTL TPDYEAAQIG VFGQMALKGY 

       190        200        210        220        230        240 
IYRGLKPVHW SPSSQTALAE AELEYPEGHT SRSVYAVFPI TKASDTAKKV LTPYLKDLGV 

       250        260        270        280        290        300 
AIWTTTPWTL PGNLAVALNP DLTYAVVESG KPVCKHQYFI VAADLVDKLS ATFETPLTVK 

       310        320        330        340        350        360 
ATLKGEDLEH TTYRHPLFDR ESEILIGGDY VTTESGTGLV HTAPGHGQED YIVGQRYGLP 

       370        380        390        400        410        420 
VLSPVDEKGN FTSEAGQFAG LNVLKDANEA IIKELEEKGA LLKEEPYQHK YPYDWRTKKP 

       430        440        450        460        470        480 
TIFRATEQWF ASVEGFRDTA LEAIKNVTWI PPQGENRITP MVADRSDWCI SRQRSWGVPI 

       490        500        510        520        530        540 
PVFYDEETNE PLLNEETINH VQAIFAEKGS DAWWELSVEE LLPQPYRNNG RKYRKGMDTM 

       550        560        570        580        590        600 
DVWFDSGSSW AAVAKQRPEL SYPVDIYLEG SDQHRGWFQS SLLTSVATNG IAPYKMVLTH 

       610        620        630        640        650        660 
GFVLDEQGRK MSKSIGNIVD PNMIINGGKD QKKEPAYGAD VLRLWVSSVD YSSDVPIGQN 

       670        680        690        700        710        720 
ILKQLVDVRN KIRNTARFLL GNLHDFDPEK DTVAYEDLPE LDRYMLHRIT EVFTEVTEAF 

       730        740        750        760        770        780 
ETFQFFRFFQ VVQNFCVVDL SNFYLDIAKD RLYISDPNNL RRRSCQTVLK VALENLAKSI 

       790        800        810        820        830        840 
APVLCHLAED IWQFLPYKTP YKSVFEAGWV ELESEWKRPE LTPKWSKFRQ IRDEVNKVME 

       850        860        870        880        890        900 
LARKDKMIGS SLDAKVLLYV SDKELREHLD SFNPSDSLSN NRVDELRYLF LASQVDLVDS 

       910        920        930        940        950 
PKTIGKANYK SESETLGVAI VKADGEKCDR CWNYSTHVGE FVDDPTLCER CNAALKGEF 

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001291 Genomic DNA. Translation: ACK73406.1.
RefSeqYP_002380274.1. NC_011729.1.

3D structure databases

ProteinModelPortalB7KFT1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING65393.PCC7424_5054.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK73406; ACK73406; PCC7424_5054.
GeneID7107200.
KEGGcyc:PCC7424_5054.
PATRIC21559142. VBICyaSp136448_5163.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCSP65393:GJP7-5109-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_CYAP7
AccessionPrimary (citable) accession number: B7KFT1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: April 16, 2014
This is version 40 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