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P43824 (SYI_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:HI_0962
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length941 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.

Sequence caution

The sequence L42023 differs from that shown. Reason: Erroneous termination at position 30. Translated as Leu.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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 – 941941Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098395

Regions

Motif59 – 6911"HIGH" region HAMAP-Rule MF_02002
Motif603 – 6075"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9041Zinc By similarity
Metal binding9071Zinc By similarity
Metal binding9241Zinc By similarity
Metal binding9271Zinc By similarity
Binding site5621Aminoacyl-adenylate By similarity
Binding site6061ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P43824 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: 35B9C66B921B1DAF

FASTA941106,529
        10         20         30         40         50         60 
MTVDYKNTLN LPETSFPMRG DLAKREPDKL KNWYEKNLYQ KIRKASKGKK SFILHDGPPY 

        70         80         90        100        110        120 
ANGNIHIGHA VNKILKDIII KSKTALGFDS PYIPGWDCHG LPIELKVEGL VGKPNEKISA 

       130        140        150        160        170        180 
AEFRQKCREY AAEQVEGQKK DFIRLGVLGD WDNPYLTMNF DTEANIIRTL GKVIENGHLY 

       190        200        210        220        230        240 
KGSKPVHWCL DCGSSLAEAE VEYEDKVSPS IYVRFPAESA DEIEAKFSAQ GRGQGKLSAI 

       250        260        270        280        290        300 
IWTTTPWTMP SNRAIAVNAD LEYNLVQLGD ERVILAAELV ESVAKAVGIE HIEILGSVKG 

       310        320        330        340        350        360 
DDLELSRFHH PFYDFTVPVI LGDHVTTDGG TGLVHTAPDH GLDDFIVGKQ YDLPMAGLVS 

       370        380        390        400        410        420 
NDGKFISTTE FFAGKGVFEA NPLVIEKLQE VGNLLKVEKI KHSYPHCWRH KTPIIFRATP 

       430        440        450        460        470        480 
QWFIGMETQG LRQQALGEIK QVRWIPDWGQ ARIEKMVENR PDWCISRQRT WGVPMTLFVH 

       490        500        510        520        530        540 
KETEELHPRT LDLLEEVAKR VERAGIQAWW DLDEKELLGA DAETYRKVPD TLDVWFDSGS 

       550        560        570        580        590        600 
TYSSVVANRL EFNGQDIDMY LEGSDQHRGW FMSSLMLSTA TDSKAPYKQV LTHGFTVDGQ 

       610        620        630        640        650        660 
GRKMSKSIGN IVTPQEVMDK FGGDILRLWV ASTDYTGEMT VSDEILKRAA DSYRRIRNTA 

       670        680        690        700        710        720 
RFLLANLNGF DPKRDLVKPE KMISLDRWAV ACALDAQNEI KDAYDNYQFH TVVQRLMRFC 

       730        740        750        760        770        780 
SVEMGSFYLD IIKDRQYTTK ADSLARRSCQ TALWHIAEAL VRWMAPILSF TADEIWQHLP 

       790        800        810        820        830        840 
QTESARAEFV FTEEFYQGLF GLGEDEKLDD AYWQQLIKVR SEVNRVLEIS RNNKEIGGGL 

       850        860        870        880        890        900 
EAEVTVYAND EYRALLAQLG NELRFVLITS KVDVKSLSEK PADLADSELE GIAVSVTRSN 

       910        920        930        940 
AEKCPRCWHY SDEIGVSPEH PTLCARCVEN VVGNGEVRYF A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. No translation available.
PIRS78633.

3D structure databases

ProteinModelPortalP43824.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

OMAVLGDWDN.

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_HAEIN
AccessionPrimary (citable) accession number: P43824
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 9, 2007
Last modified: April 16, 2014
This is version 103 of the entry and version 2 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries