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B9DUU7 (B9DUU7_STRU0) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Isoleucine--tRNA ligase HAMAP-Rule MF_02002

EC=6.1.1.5 HAMAP-Rule MF_02002
Alternative name(s):
Isoleucyl-tRNA synthetase HAMAP-Rule MF_02002
Gene names
Name:ileS HAMAP-Rule MF_02002 EMBL CAR42801.1
Ordered Locus Names:SUB1284 EMBL CAR42801.1
OrganismStreptococcus uberis (strain ATCC BAA-854 / 0140J) [Complete proteome] [HAMAP] EMBL CAR42801.1
Taxonomic identifier218495 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length931 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 SAAS SAAS002301

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. HAMAP-Rule MF_02002

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif57 – 6711"HIGH" region By similarity HAMAP-Rule MF_02002
Motif595 – 5995"KMSKS" region By similarity HAMAP-Rule MF_02002

Sites

Binding site5541Aminoacyl-adenylate By similarity HAMAP-Rule MF_02002
Binding site5981ATP By similarity HAMAP-Rule MF_02002

Sequences

Sequence LengthMass (Da)Tools
B9DUU7 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 89969FB79AAD126D

FASTA931105,427
        10         20         30         40         50         60 
MKLKETLNLG KTAFPMRAGL PNKEPLWQAA WDEAQIYQKR QKLNEGKPSF HLHDGPPYAN 

        70         80         90        100        110        120 
GNIHVGHALN KISKDIIVRA KSMSGYNAPY VPGWDTHGLP IEQVLAKKGI KRKEMDLAEY 

       130        140        150        160        170        180 
LEMCRDYALS QVDKQRQDFK RLGVSADWDN PYVTLDPAYE ADQVRVFGAM ADKGYIYRGA 

       190        200        210        220        230        240 
KPVYWSWSSE SALAEAEIEY HDIDSTSLYY ANKVKDGKGI LDTDSYIVVW TTTPFTVTAS 

       250        260        270        280        290        300 
RGLTVGPDMD YVLVQPASTS KKYLVAEGLL DSLAPKFAWT DFEILSHHKG SELEYIVTEH 

       310        320        330        340        350        360 
PWDSDVDELV ILGDHVTLDS GTGIVHTAPG FGEDDYNVGT KYKLEVAVTV DERGMMMENA 

       370        380        390        400        410        420 
GPDFQGQFYD KVLPTVIEKL GDLLLAKEVI NHSYPFDWRT KKPIIWRAVP QWFASVSDFR 

       430        440        450        460        470        480 
QEILDEIEKT TFHPSWGKTR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTAIMTKEVT 

       490        500        510        520        530        540 
DHVANLFEKE GSIIWWKKEA KELLPEDFSH PGSPNGEFTK ETDIMDVWFD SGSSWNGVMN 

       550        560        570        580        590        600 
AREQLSYPAD LYLEGSDQYR GWFNSSLITS VAVNGHAPYK AVLSQGFVLD GKGEKMSKSK 

       610        620        630        640        650        660 
GNIISPNDVA KQYGAEILRL WVTSVDTDND VRVSMDILGQ VSETYRKIRN TLRFLIANTS 

       670        680        690        700        710        720 
DFNPNTNRVA YEELAPVDKY LTIKFNKLVE VFNNSYENYD FMAIYKAVVN FVTIDLSAFY 

       730        740        750        760        770        780 
LDFAKDVVYI EAANSLARRR MQTVFYDILV KITKLLTPIL PHTAEEIWSY LEFEEEEFVQ 

       790        800        810        820        830        840 
LTEMPVAEIF EGEEDILSAW DAFMTLRTQA QKALEEARNE KVIGKSLEAH LTIYASDEVK 

       850        860        870        880        890        900 
TLLTALDSDI ALLMIVSQLT IADFADAPTN AISFENVAFT VDHAVGEVCE RSRRVDPTTR 

       910        920        930 
MRSYGAFVCD ASAKIIEENF PEAVSQGFES N 

« Hide

References

[1]"Evidence for niche adaptation in the genome of the bovine pathogen Streptococcus uberis."
Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D., Parkhill J.
BMC Genomics 10:54-54(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-854 / 0140J.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM946015 Genomic DNA. Translation: CAR42801.1.
RefSeqYP_002562588.1. NC_012004.1.

3D structure databases

ProteinModelPortalB9DUU7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218495.SUB1284.

Proteomic databases

PRIDEB9DUU7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR42801; CAR42801; SUB1284.
GeneID7391876.
KEGGsub:SUB1284.
PATRIC19808276. VBIStrUbe20775_1254.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK13804.

Enzyme and pathway databases

BioCycSUBE218495:GJ7D-1318-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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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 nameB9DUU7_STRU0
AccessionPrimary (citable) accession number: B9DUU7
Entry history
Integrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: April 16, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)