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Q11NV4 (SYI_CYTH3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. 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:CHU_3676
OrganismCytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469) [Complete proteome] [HAMAP]
Taxonomic identifier269798 [NCBI]
Taxonomic lineageBacteriaBacteroidetesCytophagiaCytophagalesCytophagaceaeCytophaga

Protein attributes

Sequence length1110 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
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 – 11101110Isoleucine--tRNA ligase HAMAP-Rule MF_02003
PRO_1000070895

Regions

Motif47 – 5711"HIGH" region HAMAP-Rule MF_02003
Motif658 – 6625"KMSKS" region HAMAP-Rule MF_02003

Sites

Binding site6611ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11NV4 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: BF665BCB606DE8B9

FASTA1,110126,860
        10         20         30         40         50         60 
MKYNEKKTEL SEVGKEVQQF WNDKKIFEKS VETREGNPTF TFYEGPPSAN GTPGIHHVMG 

        70         80         90        100        110        120 
RTVKDIFCRF KTMQGFQVKR KGGWDTHGLP VELQVEKELG ITKEDIGKKI TVEQYNQKCR 

       130        140        150        160        170        180 
EAVMKYKSQW DELTVKMGYW VDLEKPYITF ENNYIESVWY LLKEFHQKKL LYKGYTIQPY 

       190        200        210        220        230        240 
SPAAGTGLSS HELNQPGTYK DVRDTSAVAQ FKLKANPKFA DNTYFLAWTT TPWTLPSNSA 

       250        260        270        280        290        300 
LAVGENIEYV LVSTFNPYTF KPVQVILAKA LLGKYFSEKA KDLSLEAYKD GDKLIPFKIL 

       310        320        330        340        350        360 
QSYKGKDLVG IEYEQLMPYL QPETPAFRVI AGDFVSTEDG TGIVHIAPTF GADDARVAKL 

       370        380        390        400        410        420 
AGIPSIVTKD DRGNEYPLVD KRGRFTKEVT DFAGEYVKEA YLTDEEKEAE RVKQGRDKYL 

       430        440        450        460        470        480 
SVDERISIKL KEANRAFKVE KYEHSYPHCW RTDKPVLYYP LDSWFIKTTA KKERLVELNK 

       490        500        510        520        530        540 
TINWKPESTG VGRFGNWLEN LVDWNLSRSR YWGTPLPIWR SEDGSEEKCI GSIEELKTEI 

       550        560        570        580        590        600 
AKAQKAGIET ATDIKDLHRP YVDNIVLVSD SGKPMKRELD LIDVWFDSGA MPYAQWHYPF 

       610        620        630        640        650        660 
ENKELFNNNY PADFIAEGVD QTRGWFFTLH AISGMLYDKV AFKNVIANGL VLDKNGNKMS 

       670        680        690        700        710        720 
KRVGNVVNPF ETIDKYGPDA TRWYMITNAP PWDNLKFNLD GITEVQRRFF GTLQNTYSFF 

       730        740        750        760        770        780 
ALYANLDNFT FAEAEIPLAQ RTESDRWILS KLQSLVKDVA DAYSDYEPTK AGRAIQDFVV 

       790        800        810        820        830        840 
DDLSNWYVRL NRKRFWKGEY NADKTAAYQT LYTCLETVAK LGAPIAPFYM DKLFSDLNQV 

       850        860        870        880        890        900 
SKKNAVESVH LADFPKVNEA FLDVELEERM SLAQRISSLV HSIRKAQTIK VRQPLSRILI 

       910        920        930        940        950        960 
PILQPHLKAQ IQAVEDLIKN EVNIKAVEYI EDTSGVVIKT IKPNFKKLGK EYGAKLKEIG 

       970        980        990       1000       1010       1020 
NAIAELRAED ITAIERNVFE LKLADGTVIP ITSEDVEIRS QDIPGWSVAS EGGITVALDI 

      1030       1040       1050       1060       1070       1080 
TLSDDLRKEG IARDVVNRVQ NLRKDMGLEV QDKIRITIQK VDELINSALS ANQEYICTET 

      1090       1100       1110 
QAFSLELVEK LADGKEVEMD EQTLIMKIEK 

« Hide

References

[1]"Genome sequence of the cellulolytic gliding bacterium Cytophaga hutchinsonii."
Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B., McBride M.J.
Appl. Environ. Microbiol. 73:3536-3546(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33406 / NCIMB 9469.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000383 Genomic DNA. Translation: ABG60909.1.
RefSeqYP_680252.1. NC_008255.1.

3D structure databases

ProteinModelPortalQ11NV4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269798.CHU_3676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG60909; ABG60909; CHU_3676.
GeneID4184649.
KEGGchu:CHU_3676.
PATRIC21598233. VBICytHut34013_3661.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246403.
KOK01870.
OMADWNLSRS.
OrthoDBEOG644ZM1.
ProtClustDBPRK06039.

Enzyme and pathway databases

BioCycCHUT269798:GJ83-3669-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 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. 1 hit.
[Graphical view]
PRINTSPR00984. TRNASYNTHILE.
SUPFAMSSF47323. SSF47323. 2 hits.
SSF50677. SSF50677. 1 hit.
TIGRFAMsTIGR00392. ileS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYI_CYTH3
AccessionPrimary (citable) accession number: Q11NV4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 22, 2006
Last modified: April 16, 2014
This is version 58 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