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C5BQX2 (SYI_TERTT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:TERTU_1040
OrganismTeredinibacter turnerae (strain ATCC 39867 / T7901) [Complete proteome] [HAMAP]
Taxonomic identifier377629 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadales genera incertae sedisTeredinibacter

Protein attributes

Sequence length934 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 – 934934Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000216247

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif600 – 6045"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8971Zinc By similarity
Metal binding9001Zinc By similarity
Metal binding9171Zinc By similarity
Metal binding9201Zinc By similarity
Binding site5591Aminoacyl-adenylate By similarity
Binding site6031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
C5BQX2 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 4329BDB88BC66E91

FASTA934104,465
        10         20         30         40         50         60 
MTDYKSTLNL PQTSFAMKAN LAQREPQTLK RWQKENLYQQ IRQARAGREK FILHDGPPYA 

        70         80         90        100        110        120 
NGEIHIGHAV NKILKDIIVK AKTLSGFDAP YIPGWDCHGL PIEHNVEKKV GKAGVKVDFA 

       130        140        150        160        170        180 
TFRKKCREYA AKQVAGQKEG FVRLGVLADW DKPYLTMDYK TEADIVRALG KIVANGHLVR 

       190        200        210        220        230        240 
GFKPVYWSVV GGSALAEAEV EYQEKTSFSI DVKYAVKDEA DFTQRVAELG GEGPVSVVIW 

       250        260        270        280        290        300 
TTTPWTLPSS QAVSLNADLE YVVVQQPGAR LLVAEALLES VGKRAGIDTA TIVGRCHGRD 

       310        320        330        340        350        360 
LENLVLQHPF YTREVPVILG DHVTTDAGTG CVHTAPDHGM EDFEVGSRYG IGTLNYVDEN 

       370        380        390        400        410        420 
GLYRESVEIF AGDHVYKVDE KIIELLESRD ALLHQEKFTH SYPHCWRTKT PLIFRATPQW 

       430        440        450        460        470        480 
FISMTKNGLL DTVKTAVDGV EWIPDWGEAR MRSMLEASPD WCISRQRTWG VPIALFVHKE 

       490        500        510        520        530        540 
TQDLHPDTPA LVEKVAALIE TDGMDAWFNL NPEEILGEDA ANYSKVTDTL DVWFDSGVTH 

       550        560        570        580        590        600 
YSVIQQREEL QYPADLYLEG SDQHRGWFQS SLKTAIAING TAPYKQVLTH GFTVDANGKK 

       610        620        630        640        650        660 
MSKSIGNTVS PQKVMNELGA DVLRLWVAAT DFSGDMSVSD EILMRTADSY RRIRNTMRYF 

       670        680        690        700        710        720 
MSNLNGFDPA INSVAFDDMV ALDRWAVDRA AKLQRDIVAC YDSYQFHTIY QKIHNFCIVD 

       730        740        750        760        770        780 
MGGFYLDIIK DRVYTMQEDS RARRSAQTAQ YLIVQALVRW IAPILSFTAD EIWQALPGEK 

       790        800        810        820        830        840 
TGPVFVAEWL ELPELSEDDA LNNSYWQTAA KVKTAVNKVL ESKRSSGVIG GSLGAEVTLY 

       850        860        870        880        890        900 
ASDELHAKLN SLGEELRFVL LVSAVNLKKL DEAPEDADQV DVVGLKVAVT KSEAAKCARC 

       910        920        930 
WHQRDDVGSH SEHPELCGRC VSNVEGNGEV RHYA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001614 Genomic DNA. Translation: ACR11703.1.
RefSeqYP_003072635.1. NC_012997.1.

3D structure databases

ProteinModelPortalC5BQX2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING377629.TERTU_1040.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR11703; ACR11703; TERTU_1040.
GeneID8211008.
KEGGttu:TERTU_1040.
PATRIC23869259. VBITerTur118718_0982.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycTTUR377629:GHSU-945-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_TERTT
AccessionPrimary (citable) accession number: C5BQX2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 39 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