Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7UNZ2 (SYI_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:RB7259
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length1213 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_02003

Catalytic activity

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile). HAMAP-Rule MF_02003

Cofactor

Zinc By similarity. HAMAP-Rule MF_02003

Subunit structure

Monomer By similarity. HAMAP-Rule MF_02003

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_02003.

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 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 – 12131213Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_0000098557

Regions

Motif100 – 11011"HIGH" region HAMAP-Rule MF_02003
Motif742 – 7465"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site7451ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UNZ2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 353E3470B13258B3

FASTA1,213137,200
        10         20         30         40         50         60 
MPRQAPTRPR SPKKPRESDG GGGNVLQRIK LCVVLTFPSH SSGYHVSANS TAAFRAPAAS 

        70         80         90        100        110        120 
PHFPTLEEQV LAFWDQHSIY EQSLARRANA PTFVFYEGPP TANGMPHPGH CLTRAIKDVF 

       130        140        150        160        170        180 
PRYKTMRGYR CERKAGWDTH GLPVEVEVGK ELGIHSKEEI EAYGVEPFIQ KCQSSVWRYM 

       190        200        210        220        230        240 
QEWQTLTRRL GFWVNLEEAY VTYHQSYVES VWWSLKNLFD RGLLYQGHKI VWWWAQGGTA 

       250        260        270        280        290        300 
LSAGEVGQGY REVADPSVYV LFPLVDQPER SLVVWTTTPW TLPSNMYAAV KPELEYAVVK 

       310        320        330        340        350        360 
DSETGQELVL AAALVDSLAG KLKRELTVVD TISGESLVGQ RYQPPFEDYQ TRLNDPTGEL 

       370        380        390        400        410        420 
VTGGKESLYW RVVAADFVTT DSGSGLVHLA PAFGEIDHEV LVTERTRFVD GQRPELLCAV 

       430        440        450        460        470        480 
GPDGKFTDEF ASMKGVWVKE ADKTLTRTLR ESGRLLHLEQ YLHDYPFCWR ADDDPLIQYP 

       490        500        510        520        530        540 
RESWFIRTTK FRDLMLKNNS KIGWQPEHIR DGRFGNFLES NVDWALSRER YWGTPLPIWV 

       550        560        570        580        590        600 
CQSTGRMEAI ESYEELLAKP GVDGTQVWDN AKAANPELPD DLRVHKPYID SVTYDSPFES 

       610        620        630        640        650        660 
GARMQRVSEV IDCWYDSGAM PFAQWGWPHQ NDAQFQEQFP ADFISEAIDQ TRGWFYSQLA 

       670        680        690        700        710        720 
ISTMLFGEGA SIREAGTKAN ELAPSRDSES DYPHPFRNCI VLGLMLSQWY ESAGKEGQPK 

       730        740        750        760        770        780 
TVLLSESEAE QADGKFTKKT GKMSKSLRNY RSPSEIFDKY GADAMRWYFF ANQAPWNSII 

       790        800        810        820        830        840 
YADQAIRDSI PEFLLRLWNT YSFFSIYAEI DGFDPTSATD VDEQLSPESL ASAPTYRPIS 

       850        860        870        880        890        900 
ERSEIDRWIH SELHRTLATV IDRMDAFDNY NACQAITNLL DGLSNWYVRR SRDRFWAPDS 

       910        920        930        940        950        960 
DSPDKHDAYW TLYEVMLELT KVIAPFVPFL ADTLWQELTA PFGDKALKSV HLCDFPKPDA 

       970        980        990       1000       1010       1020 
SRVDQKLSDS MRLLREIASM GRSARADAKL KVRLPLAKVE VILTDDSAID WLQSHDALVR 

      1030       1040       1050       1060       1070       1080 
EELNVKAVDY TTDGGDYVQY TIVPNFKRLG PKVGKNIPVV KKMLGEADGN QLLTQLQTAG 

      1090       1100       1110       1120       1130       1140 
FVELELASGP LKLDGEDIEV RLQAREGWAA AQGSGCVVVL NTEVTPELRR EGLAKDLIRG 

      1150       1160       1170       1180       1190       1200 
IQSQRKELDC QYTDRIRVAV ETSDAELQSA IEEHRTMICG ETLADDLVIG TLPNAQQVAI 

      1210 
EGGELYVAKV SDK 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294145 Genomic DNA. Translation: CAD75273.1.
RefSeqNP_867726.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UNZ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB7259.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD75273; CAD75273; RB7259.
GeneID1791528.
KEGGrba:RB7259.
PATRIC23248485. VBIRhoBal59814_3516.

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMARVEHMVE.
OrthoDBEOG644ZM1.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 3 hits.
3.90.740.10. 1 hit.
HAMAPMF_02003. Ile_tRNA_synth_type2.
InterProIPR002300. 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]
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 2 hits.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_RHOBA
AccessionPrimary (citable) accession number: Q7UNZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 69 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