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A9BI29 (SYI_PETMO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. 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:Pmob_1626
OrganismPetrotoga mobilis (strain DSM 10674 / SJ95) [Complete proteome] [HAMAP]
Taxonomic identifier403833 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaePetrotoga

Protein attributes

Sequence length919 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 – 919919Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000088551

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif593 – 5975"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8861Zinc By similarity
Metal binding8891Zinc By similarity
Metal binding9061Zinc By similarity
Metal binding9091Zinc By similarity
Binding site5521Aminoacyl-adenylate By similarity
Binding site5961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9BI29 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 712202C0E409C5DE

FASTA919106,486
        10         20         30         40         50         60 
MDYKDTINLP KTSFKMKANL KEKEPQILQK WEDINIAYYL RNIRIGGTKF VLHDGPPYAN 

        70         80         90        100        110        120 
GDIHMGTALN KVLKDIVLKY KTLRGYDAPY VPGWDTHGLP IEHNVTTKLG EKANALSKLE 

       130        140        150        160        170        180 
IRKLCEDYAM KYVDIQRESF KRLGVIGFWD KPYLTLKPEY EAKVLEILRS IVESGNIYRG 

       190        200        210        220        230        240 
TKPIYWCTEC QTALAEAEVE YHDHTSDSIY VKFPLVGENN TYVIIWTTTP WTLPANVAIA 

       250        260        270        280        290        300 
VHPNFDYAKV EIGNEYWIMA KELVDKTLKE AGIDDYKIID TFKGLTLEGE KARHPFVDRE 

       310        320        330        340        350        360 
SLLVLADYVT LDEGTGCVHT APGHGMEDYI TGTKYNLQVI SPVDSQGYFT DEAGKYKGMK 

       370        380        390        400        410        420 
IWEANKEIIK DLKENGFLVQ SGKITHSYPH CWRCKNPVIF RATPQWFIDL EKNNYREKVL 

       430        440        450        460        470        480 
EEIKKVNWIP KWGENRISSM VRERPDWVIS RQRAWGIPIP AIKCENCGET ILDTKIIDHV 

       490        500        510        520        530        540 
IEIIEKEGSN AWFEKEAKEL LPNDYRCPKC GGSEFKKEED ILDVWIDSGS SFEAVANSRE 

       550        560        570        580        590        600 
ELKKFPVDLY LEGSDQHRGW FQSSIFLSVA KHGIAPYESV LTHGFIKDEE GKKMSKSLGN 

       610        620        630        640        650        660 
VVNPKDIINK YGADILRLWV ASADYRMDIK ISYNILEQQV ETYRKLRNTI RFLLGNINDF 

       670        680        690        700        710        720 
DPDEDSVAYE EMLEIDQWAL MKLHNLIKNV TKAYDNYEFY KVHYLINNFC TIDMSSTYLD 

       730        740        750        760        770        780 
IIKDRIYVEG KKSKLRRSAQ TVLYETAIAL NKMISPILPF TAEEVYEHLN YSNKYETIFA 

       790        800        810        820        830        840 
ELWPEYKENY LSEELEEKWN KIFALREDVL KALEEKRKEK FLGNSLDAKI ILNLKDDTLK 

       850        860        870        880        890        900 
QILSQYDNNW IADLFIVSQF EFGNVDEGFE GRYATIKVTK AEGEKCERCW KVDPNTDNDP 

       910 
DFPGVCPRCA RVLKEEINA 

« Hide

References

[1]"Complete sequence of Petroga mobilis SJ95."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Noll K., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 10674 / SJ95.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000879 Genomic DNA. Translation: ABX32320.1.
RefSeqYP_001568643.1. NC_010003.1.

3D structure databases

ProteinModelPortalA9BI29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING403833.Pmob_1626.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX32320; ABX32320; Pmob_1626.
GeneID5756782.
KEGGpmo:Pmob_1626.
PATRIC22921064. VBIPetMob40494_1749.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMOB403833:GH51-1668-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_PETMO
AccessionPrimary (citable) accession number: A9BI29
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 48 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