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Q1MPH2 (SYI_LAWIP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:LI1051
OrganismLawsonia intracellularis (strain PHE/MN1-00) [Complete proteome] [HAMAP]
Taxonomic identifier363253 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeLawsonia

Protein attributes

Sequence length937 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 – 937937Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000070889

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif607 – 6115"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9061Zinc By similarity
Metal binding9091Zinc By similarity
Metal binding9251Zinc By similarity
Metal binding9281Zinc By similarity
Binding site5661Aminoacyl-adenylate By similarity
Binding site6101ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1MPH2 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 5CCC1C52FF4081CF

FASTA937107,965
        10         20         30         40         50         60 
MTDYKETLNL PNTTFPMKAN LVQREPEIIL WWEENAVYEK MLEASGAKGI FILHDGPPYA 

        70         80         90        100        110        120 
NGHIHLGTAL NKILKDIVIK SRNMQGYRSC YVPGWDCHGL PIELKVEQEL GKKKQEMPLS 

       130        140        150        160        170        180 
LIRNRCREYA EKFLDIQREE FKRLGVFGSW DHPYQTMDPI YESVITLELA RFVEKGSVIR 

       190        200        210        220        230        240 
SKKPIYWCYS CETALAEAEV EYADHTSSAI FVRFPIHDKR LHTIFPQADL TTTSIVIWTT 

       250        260        270        280        290        300 
TPWTLPSNMA IALNADFDYA LLQYKNEYII IASELVDICL KQFNWEDAKV IKVVQGKDLE 

       310        320        330        340        350        360 
GMKARHPLYD QESMIVLGDH VTLEAGTGCV HTAPGHGPED YEVALRYNLD VYSPLDDQGR 

       370        380        390        400        410        420 
YLDTVKFFAG LRVDQANPVV IQKLEEFHRI IQKNTIQHSY PHCWRCKSPV IFRATTQWFI 

       430        440        450        460        470        480 
SMEKNNLREQ SLKAIKKNIE WIPSWGEDRI YNMIASRPDW CISRQRIWGV PIVALICESC 

       490        500        510        520        530        540 
GEVWNDPSWM KKIAEFFAIH PRGCDYWYEA KLEDIVPVGL KCPHCEGEQW KRESDILDVW 

       550        560        570        580        590        600 
FDSGSSFAAV LEERPNLGFP ADLYLEGSDQ HRGWFHSSLL ISIGTRGVPP YHAVLTHGYV 

       610        620        630        640        650        660 
VDGDGRKMSK SMGNVTSPQE IISKFGVEIL RLWVSSVDYR EDVRISNEIL QRLVDAYRRI 

       670        680        690        700        710        720 
RNTCRYLLGN INDLTLDELV PVKEMESLDQ YILDVVATAY TEIQKSYISY DFHTVFHKLH 

       730        740        750        760        770        780 
NLCTTDLSAF YLDILKDRLY TSGVRSHKRK SAQTALFYIL HMLLRSMAPI LSFTAEEVYK 

       790        800        810        820        830        840 
YIPDTLKDDN VISVFMLPFF ETSSFLLDDR VRSYWETLLL IRAEVNQAIE PMRKKGEIGH 

       850        860        870        880        890        900 
SLDTHITLYV APELHTLLLE LNTDLCSLFI VSQLDIMPLS EASVDAAVSK IDGLAVAVNR 

       910        920        930 
AQGNKCQRCW MYKELGSNHQ YPTLCPRCTE VVENMKI 

« Hide

References

[1]"The complete genome sequence of Lawsonia intracellularis: the causative agent of proliferative enteropathy."
Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., Peterson A., May B., Singh S., Gebhart C., Kapur V.
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PHE/MN1-00.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180252 Genomic DNA. Translation: CAJ55105.1.
RefSeqYP_595426.1. NC_008011.1.

3D structure databases

ProteinModelPortalQ1MPH2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING363253.LI1051.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4059667.
KEGGlip:LI1051.
PATRIC22305659. VBILawInt40445_1144.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycLINT363253:GH6E-1093-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_LAWIP
AccessionPrimary (citable) accession number: Q1MPH2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 30, 2006
Last modified: May 14, 2014
This is version 62 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