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Q7NS57 (SYI_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. 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:CV_3569
OrganismChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757) [Complete proteome] [HAMAP]
Taxonomic identifier243365 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium

Protein attributes

Sequence length925 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 – 925925Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098375

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif601 – 6055"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8881Zinc By similarity
Metal binding8911Zinc By similarity
Metal binding9081Zinc By similarity
Metal binding9111Zinc By similarity
Binding site5601Aminoacyl-adenylate By similarity
Binding site6041ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NS57 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: E26FBAADD12CB49A

FASTA925103,787
        10         20         30         40         50         60 
MSIDYRKTVN LLDTPFAMRG DLAKREPAWV KRWQEEKRYE KLRKLAAGRP KFILHDGPPY 

        70         80         90        100        110        120 
ANNDIHLGHA VNKVLKDIIV RSKTLAGFDA PYVPGWDCHG LPIELMVEKL HGKDIPAAKF 

       130        140        150        160        170        180 
RELCREYAKE QVARQKKGFI RLGVLGDWDN PYLTMDFKTE ADIVRTLGKI HENGYLTKGE 

       190        200        210        220        230        240 
KPVHWCIECG SSLAEAEVEY EDKVSPAIDV GFKVVDTDKA SAAFGADAAG AMAVIWTTTP 

       250        260        270        280        290        300 
WTLPANQAVA AGANLDYQLV DTPKGKLILG KDLVESAMKR YGVETYRVLG EAKGQALELL 

       310        320        330        340        350        360 
QLQHPFYGRQ VPVILGDHVT TDAGTGLVHT APAHGLEDFQ AGLQYKLPIA NPVADDGRYK 

       370        380        390        400        410        420 
STTELFAGML VWDANPRVIE TLESHGSLVH KSKLEHSYPH CWRHKTPIIF RATPQWFISM 

       430        440        450        460        470        480 
DRKANGGETL REVSQRAVDA TEFFPSWGRA RLDAMIKNSP DWCVSRQRNW GVPMTFFIHK 

       490        500        510        520        530        540 
ESGELHPRSA QLLEEVALRI EQQGIEAWFS LDAKELLGEE AEQYRKLTDT LDVWFDSGAT 

       550        560        570        580        590        600 
HFAVLKQRPE LAWPADLYLE GSDQHRGWFQ SSLKTGCATI GRAPYKQLLT HGFTVDDKGY 

       610        620        630        640        650        660 
KMSKSKGNGI APEEICGTLG ADILRLWVAS ADYSGDMSLS QEILKRTTES YRRLRNTIRF 

       670        680        690        700        710        720 
LLSNLSDFDP LEHVVPLANM VEMDQYALLR AREVQEKVVG ELYSRYAFHH VVQEVVGYCS 

       730        740        750        760        770        780 
EDLGAFYLDV IKDRLYTTKA DSHARRSAQT ALYHITRSLL LMVAPILCFT ADEAWNVLVD 

       790        800        810        820        830        840 
SEEESTLYHI WHEFPAQTVE REAALSSKWQ AIRELRAAVN KEIEALRSAD KLGSSLQAEV 

       850        860        870        880        890        900 
EIDAPAELAR HLASLGEELK FVLIVSKADV REAGEVAIRV SPSAHGKCDR CWHYRADVGS 

       910        920 
HAGHGAVCGR CVDNLDGQGE PRRYA 

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016825 Genomic DNA. Translation: AAQ61231.1.
RefSeqNP_903239.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NS57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243365.CV_3569.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ61231; AAQ61231; CV_3569.
GeneID2549895.
KEGGcvi:CV_3569.
PATRIC21441957. VBIChrVio67196_3494.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAERLMLHQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCVIO243365:GHUD-3664-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_CHRVO
AccessionPrimary (citable) accession number: Q7NS57
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 78 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