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C6DF04 (SYI_PECCP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PC1_3653
OrganismPectobacterium carotovorum subsp. carotovorum (strain PC1) [Complete proteome] [HAMAP]
Taxonomic identifier561230 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Pectobacterium ›

Protein attributes

Sequence length937 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.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 937937Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216242

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif602 – 6065"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9001Zinc By similarity
Metal binding9031Zinc By similarity
Metal binding9201Zinc By similarity
Metal binding9231Zinc By similarity
Binding site5611Aminoacyl-adenylate By similarity
Binding site6051ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C6DF04 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: AB25485AF292FC83

FASTA937104,502
        10         20         30         40         50         60 
MSDYKTTLNL PETGFPMRGD LAKREPDMLK RWYEQDLYGI IRNAKKGKKT FILHDGPPYA 

        70         80         90        100        110        120 
NGSIHIGHSV NKILKDIIVK SKGLSGYDSP YVPGWDCHGL PIELKVEQLI GKPGEKVSAA 

       130        140        150        160        170        180 
EFRAECRKYA AEQVAGQKAD FIRLGVLGDW DRPYLTMDFK TEANIIRALG RIIENGHLHK 

       190        200        210        220        230        240 
GAKPVHWCAD CGSALAEAEV EYYDKTSPSI DVAFNASDVA AVLAKFGVSS VDGPVSLVIW 

       250        260        270        280        290        300 
TTTPWTLPAN RAISLNAEFD YQLVQIDGQA LILAADLVES VMKRAGVTQW TVLGDCKGAD 

       310        320        330        340        350        360 
LELLRFKHPF LSFDVPAILG DHVTLDAGTG AVHTAGGHGP DDYVISQKYN LEIANPVGPN 

       370        380        390        400        410        420 
GCYLSGTYPE LDGKFVFKAN DLIVEILREK GMLLHVEKLQ HSYPCCWRHK SPIIFRATPQ 

       430        440        450        460        470        480 
WFVSMDQKGL RKQSLSEIKG VQWIPDWGQA RIEAMVANRP DWCISRQRTW GVPMSLFVHK 

       490        500        510        520        530        540 
ETEELHPRTA ELIEAVAKRV EADGIQAWWD LDPADVLGAD ADNYVKVPDT LDVWFDSGST 

       550        560        570        580        590        600 
HASVVDVRPE FGGHAADMYL EGSDQHRGWF MSSLMISTAI KGKAPYRQVL THGFTVDGQG 

       610        620        630        640        650        660 
RKMSKSIGNT VSPQDVMNKL GADILRLWIG STDYSGEIAV SDEILKRSAD AYRRIRNTAR 

       670        680        690        700        710        720 
FLLANLNGFD PQKDSVKPED MVVLDRWAVG CAKAAQEEIL EAYESYDFHR VVQRLMQFCS 

       730        740        750        760        770        780 
IEMGSFYLDI IKDRQYTAKS DSVARRSCQT ALYHISEALV RWMAPIMSFT ADEIWSYLPG 

       790        800        810        820        830        840 
KRAQYVFTEE WYDGLFGLDA SETMNDAFWA DILKVRSEVN KVIEQARNDK RIGGSLEASV 

       850        860        870        880        890        900 
TLYADANLAG KLNQLRQELH FALLTSKALV ERYENAPDSA QATELTGLKI ALSEAEGHKC 

       910        920        930 
PRCWHYETDI GSNADHPEVC GRCATNVGGN GEERKFV

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References

[1]"Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Balakrishnan V., Glasner J., Perna N.T.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001657 Genomic DNA. Translation: ACT14668.1.
RefSeqYP_003019204.1. NC_012917.1.

3D structure databases

ProteinModelPortalC6DF04.
ModBaseSearch...

Protein-protein interaction databases

STRING561230.PC1_3653.

Proteomic databases

PRIDEC6DF04.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT14668; ACT14668; PC1_3653.
GeneID8134633.
KEGGpct:PC1_3653.
PATRIC20492054. VBIPecCar70489_3677.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKQVLTHG.
ProtClustDBPRK05743.

Family and domain databases

Gene3D3.40.50.620. 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. tRNAsyn_1a_bind. 1 hit.
SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYI_PECCP
AccessionPrimary (citable) accession number: C6DF04
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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