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B7K5H5 (SYI_CYAP8) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:PCC8801_2707
OrganismCyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 / RF-1)) [Complete proteome] [HAMAP]
Taxonomic identifier41431 [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_1000189148

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
B7K5H5 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 56C3E3F7EB87F669

FASTA959109,180
        10         20         30         40         50         60 
MTEPKSYKDT VNLPQTDFSM RANAVQREPE IQQFWTENCI YEQLSQNNPE DLFILHDGPP 

        70         80         90        100        110        120 
YANGSLHMGH ALNKTLKDII NKYKLLRGHK VRYVPGWDCH GLPIELKVLQ SMKSEEREGL 

       130        140        150        160        170        180 
TPLKLRRKAR DFALKTQQEQ AEGFKRYGVW GDWENPYLTL TPEYEAAQIG VFGQMALKGY 

       190        200        210        220        230        240 
IYRGLKPVHW SPSSRTALAE AELEYPEGHT SQSIFAAFPI IKSSKDAQEI LDPFLSNLGV 

       250        260        270        280        290        300 
AIWTTTPWTL PGNLAVALNP ELTYAIVEQT SNLCNYQYII VAADLVERLS ATFSTELTVK 

       310        320        330        340        350        360 
ATLPGQILEH TIYRHPLYDR ESEIVIGGDY VTTESGTGLV HTAPGHGQED YIVGQRYGLQ 

       370        380        390        400        410        420 
VLSPVDDAGN FTEEAGQFSG LNVLKDANQA IINELKNKGS LLKEEPYLHK YPYDWRTKKP 

       430        440        450        460        470        480 
TIFRATEQWF ASVEGFREAA LEAIKSVNWI PPQGENRITP MVSDRSDWCI SRQRSWGVPI 

       490        500        510        520        530        540 
PVFYNEETNE PLLTEETINH VQAIIAKQGS DAWWELSIEE LLPEQYKKDA HKYRRGTDTM 

       550        560        570        580        590        600 
DVWFDSGSSW AAVAKQREEL KYPVDIYLEG SDQHRGWFQS SLLTSVAVNG IAPYKTVLTH 

       610        620        630        640        650        660 
GFVLDEKGHK MSKSLGNIVD PLVIINGGKN QKQEPPYGAD VLRLWVSSVD YSSDVPIGQT 

       670        680        690        700        710        720 
ILKQLSDVYR KIRNTARFLL GNLHDFDPEK DTVSYDQLPE LDQYMLHRIT EVFTEVTDAF 

       730        740        750        760        770        780 
EKFQFFRFFQ TVQNFCVVDL SNFYLDIAKD RLYISDTNSL RRRSCQTVLK VAVESLAKAI 

       790        800        810        820        830        840 
APVLCHMAED IWQFLPYKTP YQSVFASGWV EMQKQWERPE LTASWGKLRQ IRTEVNKVLE 

       850        860        870        880        890        900 
QARNEKAIGS SLDAKVLLYV SDQDFKKQLE SFNPNDSLKG NQVDELRYLV LASQVELVDS 

       910        920        930        940        950 
LEAIKKADYQ SESELVSVGV VKAEGQKCDR CWNYSTKVGE FSDDPTICER CNAALVGEF 

« 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 8801.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001287 Genomic DNA. Translation: ACK66708.1.
RefSeqYP_002372864.1. NC_011726.1.

3D structure databases

ProteinModelPortalB7K5H5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING41431.PCC8801_2707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK66708; ACK66708; PCC8801_2707.
GeneID7102093.
KEGGcyp:PCC8801_2707.
PATRIC21577729. VBICyaSp125535_2880.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCSP41431:GHLK-2738-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_CYAP8
AccessionPrimary (citable) accession number: B7K5H5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: April 16, 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