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

B9EB60 (SYI_MACCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 42. 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:MCCL_0764
OrganismMacrococcus caseolyticus (strain JCSC5402) [Complete proteome] [HAMAP]
Taxonomic identifier458233 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesMacrococcus

Protein attributes

Sequence length914 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 – 914914Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000189180

Regions

Motif57 – 6711"HIGH" region HAMAP-Rule MF_02002
Motif595 – 5995"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8831Zinc By similarity
Metal binding8861Zinc By similarity
Metal binding9041Zinc By similarity
Metal binding9071Zinc By similarity
Binding site5541Aminoacyl-adenylate By similarity
Binding site5981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B9EB60 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 614783A59E2A6DAB

FASTA914104,435
        10         20         30         40         50         60 
MDYKDTLLMP KTDFPMRGGL PNKEPQIQAQ WDEKKLYEKI LKKNEGRTPY ILHDGPPYAN 

        70         80         90        100        110        120 
GQIHMGHALN KIIKDMIMRY KAMNGYYAPY VPGWDTHGLP IETALTKKGV DRKSMSEAEF 

       130        140        150        160        170        180 
RELCRAYALE QIELQKADFK RLGVNGDWEN PYITLQEKFE AEQIRLFGDM AAKGYIYKGK 

       190        200        210        220        230        240 
KPVYWSPSSE SSLAEAEIEY QDKVSPSIYV AFDVLDGKGL VDDDVKFVIW TTTPWTLPAN 

       250        260        270        280        290        300 
VAIALNKDLD YVQVRVNDTS YIVAQALLDN VCDAVGWDKE GVQIEKTFKG ADLEFVKARH 

       310        320        330        340        350        360 
PFIDRESLII LGDHVTTDAG TGCVHTAPGH GEDDFIVGQK YELDVISPVD GKGVYTSEAG 

       370        380        390        400        410        420 
EFEGMYYDKA NKVITEKLEA SGHLLKLDFF KHSYPHDWRT KKPVIFRATP QWFASINKVR 

       430        440        450        460        470        480 
QDILNAIEET EFKVEWGKTR IYNMIRDRGD WVISRQRVWG VPLPVFYAEN GDIIMDKAVI 

       490        500        510        520        530        540 
EHVATLVEKH GTNVWYEREA TDLLPEGYTH PGSPNGVFTK EKDIMDVWFD SGSSHRGVLE 

       550        560        570        580        590        600 
ARPELSFPAD LYFEGSDQYR GWFNSSITTA VATRGKSPYK KLLSHGFVMD GQGRKMSKSL 

       610        620        630        640        650        660 
GNTVLPEKVV KQMGADIIRL WVMSVDYLAD VRISDDILKQ VSEVYRKIRN TFKFLLGNVN 

       670        680        690        700        710        720 
DFNPATDAVP YAELVEIDQF MLNKLYTFVN NAHKHYDNND YLFMYQELQN FINVELSNFY 

       730        740        750        760        770        780 
LDYGKDILYI EAQDSHVRRS MQTVVYEVLT SLTKVLAPII PHTADEIWSH TPHVTEESVH 

       790        800        810        820        830        840 
LADMPEVQSV DTALIGKWNH FLEIRDDVLK AIEETRNDKV IGKSLEAAVY IQAKNEEDQA 

       850        860        870        880        890        900 
LLKSFDNLHQ LFITSYAEVV DEPQGTDYNL SNVLVKHAEG EKCERCWNYS TVLTEESHAH 

       910 
PHVCPRCLSV LESK 

« Hide

References

[1]"Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402, reflecting the ancestral genome of the human-pathogenic staphylococci."
Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.
J. Bacteriol. 191:1180-1190(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCSC5402.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009484 Genomic DNA. Translation: BAH17471.1.
RefSeqYP_002560167.1. NC_011999.1.

3D structure databases

ProteinModelPortalB9EB60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING458233.MCCL_0764.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH17471; BAH17471; MCCL_0764.
GeneID7389929.
KEGGmcl:MCCL_0764.
PATRIC22423841. VBIMacCas48391_0863.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMCAS458233:GI03-777-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_MACCJ
AccessionPrimary (citable) accession number: B9EB60
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: April 16, 2014
This is version 42 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