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A1KS62 (SYI_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. 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:NMC0383
OrganismNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) [Complete proteome] [HAMAP]
Taxonomic identifier272831 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length929 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 – 929929Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022093

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8921Zinc By similarity
Metal binding8951Zinc By similarity
Metal binding9121Zinc By similarity
Metal binding9151Zinc By similarity
Binding site5631Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1KS62 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 0E17FA28C7261036

FASTA929104,241
        10         20         30         40         50         60 
MTDYSKTVNL LESPFPMRGN LAKREPAWLK SWYEQKRYQK LREIAKGRPK FILHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHAV NKILKDIIIR SKTQAGFDAP YVPGWDCHGL PIEVMVEKLH GKDMPKARFR 

       130        140        150        160        170        180 
ELCREYAAEQ VACQKKDFIR LGVLGDWDKP YLTMDFKTEA DTVRMLGEIY KSGYLYRGAK 

       190        200        210        220        230        240 
PVQFCLDCGS SLAEAEVEYK DKVSPAIDVG YPFKDTAALA AAFGLAGIEG KAFAVIWTTT 

       250        260        270        280        290        300 
PWTLPASQAV SAGADVVYQL IDTPKGKLVL AKDLAEDALK RYGFSDGIAI LAETTGDKLE 

       310        320        330        340        350        360 
NLHMNHPFLE RDIPMLNGDH VTTDAGTGLV HTAPAHGLED YAVCNKYGIE LYNPVNAEGK 

       370        380        390        400        410        420 
YISETPRVAG MSVWEANPVI LQWLEETGNL LASSKIEHSY AHCWRHKTPL IYRATGQWFV 

       430        440        450        460        470        480 
GMDKAGADGK TLRDKAIKAV DDTEFFPSWG RARLEAMIEG RPDWVVSRQR YWGTPMTFFV 

       490        500        510        520        530        540 
HKETGELHPN SAELLEKVAQ RIEEKGIEAW FSLDKGELLS AEDCEHYDKL SDTMDVWFDS 

       550        560        570        580        590        600 
GSTHYSVVKQ REELDWPADL YLEGSDQHRG WFQSSMLTGC ASSMGRAPYK QLLTHGFVVD 

       610        620        630        640        650        660 
QNGRKMSKSI GNVVAPQEVY NEFGADILRL WAASTDYSGE LAISKEILKR VTESYRRIRN 

       670        680        690        700        710        720 
TLSFLFANLS DFNPIEDAVQ QADMVEIDRY AVVLARQLQE RLAGDYYPRY TFHFAVKDIV 

       730        740        750        760        770        780 
SFCSEDLGAF YLDILKDRLY TTKADSRARR SAQTALYHIT RSLVLLIAPI LCFTGEEAWD 

       790        800        810        820        830        840 
IIGGGEEDSV LFHTWHEFPT INEKAEAELV KKWTAIREAR EAVTAAIEPL RADKTVGSSL 

       850        860        870        880        890        900 
QAEAEITAPE EMAGYLNALG EELRFALLVS KAEVKVGSEL AVAAKASDGE KCERCWHYTR 

       910        920 
DVGAVAGYET VCKRCAENVG REGETRHYA 

« Hide

References

[1]"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. expand/collapse author list , Barrell B.G., Saunders N.J., Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / DSM 15464 / FAM18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM421808 Genomic DNA. Translation: CAM09692.1.
RefSeqYP_974494.1. NC_008767.1.

3D structure databases

ProteinModelPortalA1KS62.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272831.NMC0383.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM09692; CAM09692; NMC0383.
GeneID4675586.
KEGGnmc:NMC0383.
PATRIC20350409. VBINeiMen17609_0462.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAVLGDWDN.
OrthoDBEOG644ZM1.
ProtClustDBPRK05743.

Enzyme and pathway databases

BioCycNMEN272831:GJDX-382-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_NEIMF
AccessionPrimary (citable) accession number: A1KS62
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: April 16, 2014
This is version 61 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