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

Q3AEP2 (SYI_CARHZ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:CHY_0534
OrganismCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [Complete proteome] [HAMAP]
Taxonomic identifier246194 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCarboxydothermus

Protein attributes

Sequence length925 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 – 925925Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022056

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif597 – 6015"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8901Zinc By similarity
Metal binding8931Zinc By similarity
Metal binding9101Zinc By similarity
Metal binding9131Zinc By similarity
Binding site5561Aminoacyl-adenylate By similarity
Binding site6001ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3AEP2 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: D5D5B6E014DD26D7

FASTA925106,237
        10         20         30         40         50         60 
MDYGKTLNLP VTDFPMRGNL PEREPEILAY WQKIDLYRKV QQKNEGRPKF ILHDGPPYAN 

        70         80         90        100        110        120 
GDIHMGHVLN KVLKDMIVKF KSMDGYDAPY VPGWDTHGLP IEQRAIKDLG INRKEISPLE 

       130        140        150        160        170        180 
FRAKCREYAE KYARIQKEQF KRLGVRGDWE NPYLTLMPHY EAKQIEIFGE MAKKGYIYKG 

       190        200        210        220        230        240 
LKPVYWCPVC ETALAEAEIE YAEKKSPSIY VRFKVVEGKG KVPEDAYLVI WTTTPWTLPA 

       250        260        270        280        290        300 
NVAIAVHPEF TYALVKTEKG DYVVAEGLVQ QFFEATKLTG EIVARFKGEE LLGVVTRHPF 

       310        320        330        340        350        360 
IERESPVVLA DYVTLESGTG LVHTAPGHGT EDFETGKKYN LPVLSPVNHQ GVFTEGAGKY 

       370        380        390        400        410        420 
AGMKIDDGNK AITQDLEASG DLLAMSFIKH SYPHCWRCKN PVIFRATEQW FASIDGFREQ 

       430        440        450        460        470        480 
ALKEIEKVEW IPAWGKDRIY NMVRDRGDWC ISRQRTWGVP IPIFYCEACG KEIITDESIK 

       490        500        510        520        530        540 
AVSDLFRVEG SDAWWKYEAG EILPDGFRCP HCGGVKFRKE TDIMDVWFDS GSSHAAVLEQ 

       550        560        570        580        590        600 
PEYWPDLRWP ADLYLEGSDQ HRGWFNSSLS TAVATRGMAP YKAVLTHGFL VDEKGRKMSK 

       610        620        630        640        650        660 
SLGNVVDPLK VIKELGADIL RLWVASADYR SDLAISNNIL KQTAEGYRKI RNTIRFLLGN 

       670        680        690        700        710        720 
LYDYDHEKHR VPYERLLEID RWALAKLHRL IARVVRAYRD YEFHVVFHAV HNFCTVDMSA 

       730        740        750        760        770        780 
IYLDIIKDRL YVELPDSEKR RSAQTVLYEI LDSLLRLLTP ILAFTTEEAY RHFPAKGKKE 

       790        800        810        820        830        840 
SVQLLDMPKV EERYLDLTLE ETWDKILEVR AKVLKALEIA RQEKLIGHSL DAWVTLKASG 

       850        860        870        880        890        900 
ELYDFLVERV NMWPEIFIVS QVDIQNEEVT GENGELPLEV VVNKALGEKC QRCWMYSPEV 

       910        920 
GLDPEFPDTC PRCAGVLHEL KNRPL 

« Hide

References

[1]"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901."
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.
PLoS Genet. 1:563-574(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Z-2901 / DSM 6008.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000141 Genomic DNA. Translation: ABB14741.1.
RefSeqYP_359392.1. NC_007503.1.

3D structure databases

ProteinModelPortalQ3AEP2.
SMRQ3AEP2. Positions 1-920.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246194.CHY_0534.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB14741; ABB14741; CHY_0534.
GeneID3728472.
KEGGchy:CHY_0534.
PATRIC21274215. VBICarHyd26463_0495.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAERLMLHQ.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCHYD246194:GJCN-535-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_CARHZ
AccessionPrimary (citable) accession number: Q3AEP2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 65 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