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Q3A1R3 (SYI_PELCD) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:Pcar_2455
OrganismPelobacter carbinolicus (strain DSM 2380 / Gra Bd 1) [Complete proteome] [HAMAP]
Taxonomic identifier338963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Protein attributes

Sequence length927 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 – 927927Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098436

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif602 – 6065"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8971Zinc By similarity
Metal binding9001Zinc By similarity
Metal binding9171Zinc By similarity
Metal binding9201Zinc By similarity
Binding site5611Aminoacyl-adenylate By similarity
Binding site6051ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3A1R3 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 835B83A6EE0B9CF5

FASTA927105,258
        10         20         30         40         50         60 
MDYKQTLNLP DTQFPMRGNL PKREPEILEK WQSMGLYEKM EEAGRTRPNF TLHDGPPYAN 

        70         80         90        100        110        120 
GHIHIGHALN KILKDIVLKS RRMKGFYAPY VPGWDCHGLP IELMVDKKLG KKKRDMTKVE 

       130        140        150        160        170        180 
IRKECRVYAD QWVKIQSEEF ERLGVMGEWD RPYLTMTHHY EAVTARELAR FVEKGGLFKG 

       190        200        210        220        230        240 
KKPIHWCSSC VTALAEAEVE YADHKSPSIY VKFPFDGELP AELNDLAGRK LSFVIWTTTP 

       250        260        270        280        290        300 
WTIPANLAVC LNPNLPYAVV ETGDELLVMA EGLVSGVMQE LGLENYRVLK TFEAPIFERK 

       310        320        330        340        350        360 
TCRHPFYDRP SLLILGDHVT LEAGTGCVHT APGHGQDDYV VGLAYGLDVY NPVDNYGRYY 

       370        380        390        400        410        420 
EDVEFFGGMK INQANGAVNA KLTEVGALLK ESEVSHSYPH CWRCKKPIIF RATEQWFISM 

       430        440        450        460        470        480 
EANGLREKAL GHINDVNWVP RWGRDRIYNM VENRPDWCIS RQRSWGVPIT IFYCAKCGEA 

       490        500        510        520        530        540 
LEDSKVMDYV ADLFEEGGSD LWFDKPAKEL MPAGTTCPGC GHDEFTKETD ILDVWFDSGV 

       550        560        570        580        590        600 
SHAAVLDNRD YLSWPADLYL EGSDQHRGWF HSSLLASVGT RELTPYKSVL THGFVVDGKG 

       610        620        630        640        650        660 
KKMSKSVGNV VAPEEVIKKY GAEILRLWVA AQDYRDDIRI SNEILQRLSD AYRRIRNTAR 

       670        680        690        700        710        720 
YILGNLSGFD PSRDMVADDQ LLELDRWALA KLEDLAGRVE KAYEDYEFHI IYHAVHNFCS 

       730        740        750        760        770        780 
VEMSSFYLDV LKDRLYVSGT DSIARRSAQT AMYRILDCIT RLIAPVLSFT AEEIWAFMPG 

       790        800        810        820        830        840 
ERSESVHLGE FVQFPTSFRD AALEERYDNL LEIRSDVSKA LELARNEKVI GHSLDARVLL 

       850        860        870        880        890        900 
SAPAGATLEL LEKYRDQLAS LFIVSQVELV DDLADGLTGE NLPDLKVKVE KALGEKCERC 

       910        920 
WNYATSVGDS AEHPALCHRC VAVLTDR 

« Hide

References

[1]"Complete sequence of Pelobacter carbinolicus DSM 2380."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2380 / Gra Bd 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000142 Genomic DNA. Translation: ABA89694.1.
RefSeqYP_006718218.1. NC_007498.2.

3D structure databases

ProteinModelPortalQ3A1R3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338963.Pcar_2455.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA89694; ABA89694; Pcar_2455.
GeneID3725157.
KEGGpca:Pcar_2455.
PATRIC22891226. VBIPelCar86875_2653.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPCAR338963:GKDU-2703-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_PELCD
AccessionPrimary (citable) accession number: Q3A1R3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 22, 2005
Last modified: April 16, 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