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Q4FPA9 (SYI_PELUB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. 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:SAR11_0158
OrganismPelagibacter ubique (strain HTCC1062) [Complete proteome] [HAMAP]
Taxonomic identifier335992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSAR11 clusterCandidatus Pelagibacter

Protein attributes

Sequence length905 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

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
Nucleotide-binding
   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

extracellular space

Inferred from electronic annotation. Source: InterPro

   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 905905Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098435

Regions

Motif56 – 6611"HIGH" region HAMAP-Rule MF_02002
Motif604 – 6085"KMSKS" region HAMAP-Rule MF_02002

Sites

Binding site5631Aminoacyl-adenylate By similarity
Binding site6071ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4FPA9 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: B8CD6E7541EDEF57

FASTA905105,047
        10         20         30         40         50         60 
MSKENINLPK TAFSMKANLQ NKEPEILEYW KKIDLYKELR KSNKGKEKFI LHDGPPYANG 

        70         80         90        100        110        120 
NIHMGTALNK ILKDIIVKFH QMDGKDSVYV PGWDCHGLPI EWKIEEQYKK NKKNKNEVPI 

       130        140        150        160        170        180 
TEFRKECREF AEKWIEVHKT QFKRLGVVGD WENHYATMSF EAEAQIVREL GKFLKEGSLY 

       190        200        210        220        230        240 
RGFKPVLWST VEKTALADAE VEYQDHKSDT IYTAFPVKKT NIKELENTDV IIWTTTPWTI 

       250        260        270        280        290        300 
PANKALAYNE ALDYLIIELG DEGDFKNKKI VVAEALLESV IKDCEIKSYK EIKKFKGKDF 

       310        320        330        340        350        360 
KDTICSHPFL ELGYDYDIPM LEARFVTTEQ GTGIVHCAPS HGPDDFNLCL KYGIKAIETV 

       370        380        390        400        410        420 
DGDGKYTKNL PLFEGTHIFK ANPIVIEKLK EQKKLLSNGE LVHSYPHSWR SKAPLVHRAT 

       430        440        450        460        470        480 
PQWFISMESH GLRKKALKAL DDTKFYPDKG RERIKAMIET RPDWCVSRQR VWGVPLPIFV 

       490        500        510        520        530        540 
HKTTKEILVD DNVNENIASI YEKEGSDCWF SDSPQRFLGD KYKAEDYEKI SDIVEVWFDS 

       550        560        570        580        590        600 
GCTHAFVLEK REDLQWPASM YLEGSDQHRG WFHSSLLESC GTRGRAPYES ILSHGFVVDG 

       610        620        630        640        650        660 
KGLKMSKSVG NVIAPEDILK KYGADILRIW VASSNYAEDL RIDYSILEQH ADSYRKIRNT 

       670        680        690        700        710        720 
FRYLLGNLND DFQKIDLESL DIKQLPELER YMLHRVYELN NNFKNYFKSY DFHNLYKELL 

       730        740        750        760        770        780 
NFCTVDLSSF YFDIRKDALY CDSKNSDRRK SSIVVLNIIL ESLVKWFAPI LSFTTEEIFT 

       790        800        810        820        830        840 
LINKEQKSIH LEQFMKYPES FQDEELHKKW IELKKIRDIC NISIEAKRAS KEIGSSLEAS 

       850        860        870        880        890        900 
LIINLNKSLF EISKNVDFSE ICITSSALVH QSNTDEIIIK TIKAEGNKCP VCWKINKVKC 


ERHSD 

« Hide

References

[1]"Genome streamlining in a cosmopolitan oceanic bacterium."
Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D., Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M., Carrington J.C., Mathur E.J.
Science 309:1242-1245(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC1062.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000084 Genomic DNA. Translation: AAZ20980.1.
RefSeqYP_265583.1. NC_007205.1.

3D structure databases

ProteinModelPortalQ4FPA9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335992.SAR11_0158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ20980; AAZ20980; SAR11_0158.
GeneID3516865.
KEGGpub:SAR11_0158.
PATRIC31989773. VBICanPel5618_0157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0060.
HOGENOMHOG000246402.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.

Enzyme and pathway databases

BioCycCPEL335992:GH3Z-158-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.
[Graphical view]
PANTHERPTHR11946:SF9. PTHR11946:SF9. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 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_PELUB
AccessionPrimary (citable) accession number: Q4FPA9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: August 30, 2005
Last modified: May 14, 2014
This is version 68 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