Isoleucine--tRNA ligase - Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)

Contribute

Send feedback

Read comments (?) or add your own

Q6NGD7 (SYI_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	DIP1589

Organism

Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]

Taxonomic identifier

257309 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length	1052 AA.
Sequence status	Complete.
Protein existence	Inferred 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_02003
Catalytic activity	ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003
Cofactor	Zinc 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_02003
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	isoleucyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP regulation of translational fidelity Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP aminoacyl-tRNA editing activity Inferred from electronic annotation. Source: InterPro isoleucine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1052

1052

Isoleucine--tRNA ligase HAMAP-Rule MF_02003

PRO_0000098536

Regions

Motif

58 – 68

"HIGH" region HAMAP-Rule MF_02003

Motif

627 – 631

"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site

630

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6NGD7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 0E045969A137FBCD
Show »

FASTA

1,052

118,486

        10         20         30         40         50         60 
MSDAVGGVYP RVDMSGGTNV FPDMERQVLE YWKDDETFKA SLTNREENPE YVFYDGPPFA 

        70         80         90        100        110        120 
NGLPHYGHLL TGYVKDIVPR YQTMKGKLVN RVFGWDCHGL PAELEAEKQL GIKDKGEIEA 

       130        140        150        160        170        180 
MGLESFNNYC AKSVLEYTQE WKDYVTRQAR WVDFDNGYKT MDMDFMESVM WAFKTLYDKG 

       190        200        210        220        230        240 
LIYQGFRVLP YSWAEHTPLS NQETRLDDSY KMRQDPTLTV TFPITGVKDD SAADASLVGA 

       250        260        270        280        290        300 
YALAWTTTPW TLPSNLALAV NPQVNYVEVK VGDQGAEAIR GQRVLLAEAL VGAYAKELGE 

       310        320        330        340        350        360 
DHEVLTVRPG SELVGLTYQP IFSYFADHEN AFQILAAEYV TTEDGTGIVH QAPAFGEDDM 

       370        380        390        400        410        420 
NTCKEYGIEV VIPVDMDGKF TSLVPEYQGQ LVFDANKSII ADLKAAGRVV RHQTIEHSYP 

       430        440        450        460        470        480 
HSWRSGEPLI YMALPSWFVE VTKIRDRMVE LNKEIDWMPS HIRDGQFGKW LEGARDWNIS 

       490        500        510        520        530        540 
RNRYWGSPIP VWVSDDENYP RVDVYGSLEE LERDFGVRPE SLHRPHIDEL TRPNPDDPTG 

       550        560        570        580        590        600 
KSTMRRVPEV LDCWFESGSM PFAQKHYPFE NKDWFDTHSP ADFIVEYSGQ TRGWFYTLHV 

       610        620        630        640        650        660 
LATALFDRPA FKKVVAHGIV LGDDGTKMSK SRRNYPDVNE VFNRDGSDAM RWFLMSSPIL 

       670        680        690        700        710        720 
RGGNLIVTEQ GIREGVRQAL LPMWNAYSFL QLYSSKPAQW SVDSSDVLDR YILAKLHDVV 

       730        740        750        760        770        780 
AAVGDALDNT DIARACDEVR TFCDALTNWY VRRSRDRFWA GDTEHPEAFY TLYTVLETLT 

       790        800        810        820        830        840 
RVTAPLLPMV SEVIWRGLTG ERSVHLADFP QADQFPADDD LVRAMDEVRG VCSATSSVRK 

       850        860        870        880        890        900 
AHKLRNRLPL PKVTVALPES ARLADFADII RDEVNVKEVA LTSDVDSVGR FDVVVNAKVA 

       910        920        930        940        950        960 
GPRLCKDVQR AIKAVKSGNY ERRGDTVVAD GIELVAGEFT ERLVAADPDS TTQIDGVDGL 

       970        980        990       1000       1010       1020 
VVLDMTLTEE LEAEGWAADV IRGLQDARKA SGFEVSDRIE VKLVVPEEKK EWALRHTDMI 

      1030       1040       1050 
AGEVLATSFE VVTGEPAEHD IVAGVTATVQ KV

« Hide

References

[1]

"The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129."
Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S.

Parkhill J.
Nucleic Acids Res. 31:6516-6523(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248358 Genomic DNA. Translation: CAE50114.1.
RefSeq	NP_939931.1. NC_002935.2.
3D structure databases
ProteinModelPortal	Q6NGD7.
ModBase	Search...
Protein-protein interaction databases
STRING	257309.DIP1589.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE50114; CAE50114; DIP1589.
GeneID	2650778.
KEGG	cdi:DIP1589.
PATRIC	21484388. VBICorDip47633_1570.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0060.
HOGENOM	HOG000246403.
KO	K01870.
OMA	SRSRYWG.
ProtClustDB	PRK06039.
Family and domain databases
Gene3D	3.40.50.620. 2 hits. 3.90.740.10. 1 hit.
HAMAP	MF_02003. Ile_tRNA_synth_type2.
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR002300. aa-tRNA-synth_Ia. IPR002301. Ile-tRNA-ligase. IPR023586. Ile-tRNA-ligase_type2. 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]
Pfam	PF08264. Anticodon_1. 1 hit. PF00133. tRNA-synt_1. 1 hit. [Graphical view]
PRINTS	PR00984. TRNASYNTHILE.
SUPFAM	SSF47323. tRNAsyn_1a_bind. 2 hits. SSF50677. ValRS_IleRS_edit. 1 hit.
TIGRFAMs	TIGR00392. ileS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYI_CORDI

Accession

Primary (citable) accession number: Q6NGD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents