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Q1JKZ4 (Q1JKZ4_STRPC) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 70. 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 ABF32425.1
Ordered Locus Names:MGAS9429_Spy1238 EMBL ABF32425.1
OrganismStreptococcus pyogenes serotype M12 (strain MGAS9429) [Complete proteome] [HAMAP] EMBL ABF32425.1
Taxonomic identifier370551 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length933 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
Q1JKZ4 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 22001A131679F834

FASTA933105,065
        10         20         30         40         50         60 
MKLKETLNLG KTAFPMRAGL PNKEPQWQAA WEQAELYKKR QELNAGKPAF HLHDGPPYAN 

        70         80         90        100        110        120 
GNIHVGHALN KISKDIIVRS KSMSGFQAPY VPGWDTHGLP IEQVLAKQGI KRKEMDLAEY 

       130        140        150        160        170        180 
LEMCRQYALS QVDKQRDDFK RLGVSADWEN PYVTLDPQFE ADQIRVFGAM AEKGYIYRGA 

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

       250        260        270        280        290        300 
RGLTVGPDMD YLVVKPAGSD RQYVVAEGLL DSLAGKFGWE SFETLASHKG ADLEYIVTEH 

       310        320        330        340        350        360 
PWDTDVEELV ILGDHVTLES GTGIVHTAPG FGEDDYNVGT KYKLEVAVTV DERGLMMENA 

       370        380        390        400        410        420 
GPDFHGQFYN KVTPIVIDKL GDLLLAQEVI NHSYPFDWRT KKPIIWRAVP QWFASVSDFR 

       430        440        450        460        470        480 
QDILDEIEKT TFHPSWGETR LYNMIRDRGD WVISRQRAWG VPLPIFYAED GTAIMTKEVT 

       490        500        510        520        530        540 
DHVADLFQEN GSIIWWQKEA KDLLPEGFTH PGSPNGEFTK ETDIMDVWFD SGSSWNGVMN 

       550        560        570        580        590        600 
ARENLSYPAD LYLEGSDQYR GWFNSSLITS VAVNGHAPYK AILSQGFVLD GKGEKMSKSK 

       610        620        630        640        650        660 
GNIISPNDVA KQYGADILRL WVASVDTDND IRVSMEILGQ VSETYRKIRN TLRFLIANTS 

       670        680        690        700        710        720 
DFNPATDTVA YADLGAVDKY MTIVFNQLVA TITDAYERYD FMAIYKAVVN FVTVDLSAFY 

       730        740        750        760        770        780 
LDFAKDVVYI EAANSLERRR MQTVFYDILV KITKLLTPIL PHTTEEIWSY LEYESEAFVQ 

       790        800        810        820        830        840 
LAEMPVAETF SAQEDILEAW SAFMTLRTQA QKALEEARNA KIIGKSLEAH LTIYASEEVK 

       850        860        870        880        890        900 
TLLTALDSDI ALLLIVSQLT IADLADAPAD AVAFEGVAFM VEHAIGEVCE RSRRIDPTTR 

       910        920        930 
MRSYNAFVCD HSAKIIEENF PEAVAEGFEE SGK 

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References

[1]"Molecular genetic anatomy of inter- and intraserotype variation in the human bacterial pathogen group A Streptococcus."
Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS9429 EMBL ABF32425.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000259 Genomic DNA. Translation: ABF32425.1.
RefSeqYP_596969.1. NC_008021.1.

3D structure databases

ProteinModelPortalQ1JKZ4.
SMRQ1JKZ4. Positions 1-918.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING370551.MGAS9429_Spy1238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF32425; ABF32425; MGAS9429_Spy1238.
GeneID4061215.
KEGGspk:MGAS9429_Spy1238.
PATRIC19753527. VBIStrPyo37061_1253.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSPYO370551:GHLY-1297-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 nameQ1JKZ4_STRPC
AccessionPrimary (citable) accession number: Q1JKZ4
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2006
Last sequence update: June 13, 2006
Last modified: April 16, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)