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B0TZQ5 (SYI_FRAP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:Fphi_0396
OrganismFrancisella philomiragia subsp. philomiragia (strain ATCC 25017) [Complete proteome] [HAMAP]
Taxonomic identifier484022 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length935 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 – 935935Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000088546

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif599 – 6035"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8971Zinc By similarity
Metal binding9001Zinc By similarity
Metal binding9171Zinc By similarity
Metal binding9201Zinc By similarity
Binding site5581Aminoacyl-adenylate By similarity
Binding site6021ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0TZQ5 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: C82D382AC612D76C

FASTA935107,504
        10         20         30         40         50         60 
MSDYKDTLNL PKTSFSMKGN LANKEPMILN KWEKQGIYKK IREHFAGREK FVLHDGPPYA 

        70         80         90        100        110        120 
NGSIHVGHAV NKILKDIIVK SKTLSGYDAP YIPTWDCHGL PIELQVEKKH GKAGQKISED 

       130        140        150        160        170        180 
AFRKECRKYA KQQVEIQKKD FKRLGVLGQW DQPYLTMDFS YEANMIRTLA KIIENKHLTK 

       190        200        210        220        230        240 
GFKPVHWCTD CGSALAEAEV EYKDKISPAI DVKFKIKDKE KLAKAFGLES LNHDAFAIIW 

       250        260        270        280        290        300 
TTTPWTLPAN QAIAVNNQLN YSLVKIEDFY IILAENLVEQ TLKRYAIENA QVIANTSGYK 

       310        320        330        340        350        360 
LIGIIAEHPF YSRHVPILHG DHVTDDSGTG MVHTAPTHGV EDFTLGKEHD LSMEIFVKGN 

       370        380        390        400        410        420 
GCYSENTKLF AGEFVFKAND RVIELLGEKK RLMNFDKLKH SYPHCWRHKT PLIFRATPQW 

       430        440        450        460        470        480 
FISMEKEGLR EKAIEAIKET SWAPSWGQAR IEGMIKDRPD WCISRQRTWG VPLPLFIHKE 

       490        500        510        520        530        540 
TEELHPNTIE ILHKVAQKIE KGGIEAWFNA DDNEFIAETD KYKRVKDTLD VWFDSGSSSM 

       550        560        570        580        590        600 
CILDIDKSLS YPADLYLEGS DQHRGWFQTS LLVAMSAKGN QPYKEVFTHG FVVDEHGRKM 

       610        620        630        640        650        660 
SKSLGNVTSP QDIYNTLGAD ILRLWTASTD YKSEMAVSDQ ILKRTADTYR RLRNTARFLL 

       670        680        690        700        710        720 
SNLEGFNPET DIIEFDKLVK LDQWAIAKTK EFQDKIIEAY DKYQTHTVAQ LIHHFCSIEM 

       730        740        750        760        770        780 
GSFYLDIIKD RQYTAKADGH PRKSAQTAIY HIVHALVRWM APILSYTADE IWEATPKTTD 

       790        800        810        820        830        840 
LPIQLCEWYT DLKSFNDQDE LNLEFWAKIQ EIRSEVNRIL EIKRNEEVIK ASLEAEIIIY 

       850        860        870        880        890        900 
ADNDNYKLLE KLGNELRFLL ISSKASLRAI EEKTNNSIES NITGLNIEVN KIEEPKCERC 

       910        920        930 
WHRSATVGQN EEYQDICSRC VENITTEAGE SREFA 

« Hide

References

[1]"Complete sequence of chromosome of Francisella philomiragia subsp. philomiragia ATCC 25017."
US DOE Joint Genome Institute
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Richardson P.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000937 Genomic DNA. Translation: ABZ86614.1.
RefSeqYP_001677115.1. NC_010336.1.

3D structure databases

ProteinModelPortalB0TZQ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING484022.Fphi_0396.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ86614; ABZ86614; Fphi_0396.
GeneID5907234.
KEGGfph:Fphi_0396.
PATRIC17937619. VBIFraPhi43880_0412.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycFPHI484022:GHVB-403-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_FRAP2
AccessionPrimary (citable) accession number: B0TZQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 46 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