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B0JSP4 (SYI_MICAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:MAE_11160
OrganismMicrocystis aeruginosa (strain NIES-843) [Complete proteome] [HAMAP]
Taxonomic identifier449447 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesMicrocystis

Protein attributes

Sequence length952 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 952952Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000088549

Regions

Motif60 – 7011"HIGH" region HAMAP-Rule MF_02002
Motif603 – 6075"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9211Zinc By similarity
Metal binding9241Zinc By similarity
Metal binding9411Zinc By similarity
Metal binding9441Zinc By similarity
Binding site5621Aminoacyl-adenylate By similarity
Binding site6061ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0JSP4 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: EF727BAFF613E084

FASTA952107,865
        10         20         30         40         50         60 
MSNAKSYKDT VNLPQTDFDM RANASKREPE IQKFWQDEQI YEKLAQNNPK ELFILHDGPP 

        70         80         90        100        110        120 
YANGSLHIGH ALNKILKDII NKYKLLQGYK VRYVPGWDCH GLPIELKVLQ SLKSSEKEGL 

       130        140        150        160        170        180 
TPVKLRQKAH DFALQTQKEQ CEGFKRYGVW GDWENPYLTL QPEYEAAQIA VFGKMALKGY 

       190        200        210        220        230        240 
IYRGLKPVHW SPSSQTALAE AELEYPEGHT SRSVYVAFPI TSVSTPVLRP FLPNLSVAIW 

       250        260        270        280        290        300 
TTTPWTLPGN LAVALNPELN YSVVETSESN YLIVATDLVE KLADTFNRTL TIKATVKGLE 

       310        320        330        340        350        360 
LEHTKYRHPL FDRESAILIG GDYVTTDSGT GLVHTAPGHG QEDYIVGQRY GLPILSPVDD 

       370        380        390        400        410        420 
KGNFTAEAGQ FAGLNVLKDA NEAIILALTE KGALLKEEAY QHKYPYDWRT KKPTIFRATE 

       430        440        450        460        470        480 
QWFASVEGFR ELALEAIDSV RWIPATGKNR ITSMVSERSD WCISRQRSWG VPIPVFYDEE 

       490        500        510        520        530        540 
TNEPLLTEET INHVQAIFGV KGSNAWWELS VEELLPPSYR NNGRSYRKGM DTMDVWFDSG 

       550        560        570        580        590        600 
SSWNAVANAR PELSYPADMY LEGSDQHRGW FQSSLLTSVA ANGIAPYKTV LTHGFVLDEQ 

       610        620        630        640        650        660 
GRKMSKSLGN VIDPNVIING GKDQKKEPAY GVDVIRLWVS SVDYTNDVNI GQNILKQLVD 

       670        680        690        700        710        720 
IRNKIRNTAR FLLGSLNDFD PVKDAVAYED LPEIDRYMLH RISEVFTEVT AAFESFQFFR 

       730        740        750        760        770        780 
FFQTVQNFCV VDLSNFYIDI AKDRLYISDP NSFRRRSCQT VYAIALENLA KAIAPVLSHL 

       790        800        810        820        830        840 
AEDIWQFLPY KTPYLSVFES GWLNIDPAWN NRELADKWAK FRQLRTEVNK VMETARNDKA 

       850        860        870        880        890        900 
IGASLEAKVL LYVPDESLQQ ELELFNNCDS LTGNKVDELR YLFLSSQVEL VSDISAIQTA 

       910        920        930        940        950 
EYKGESDFVS VGIVKAEGEK CDRCWNYSTQ VGKFADDPTI CERCNAALKG EF 

« Hide

References

[1]"Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843."
Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M. expand/collapse author list , Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.
DNA Res. 14:247-256(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NIES-843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009552 Genomic DNA. Translation: BAG00938.1.
RefSeqYP_001656130.1. NC_010296.1.

3D structure databases

ProteinModelPortalB0JSP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING449447.MAE_11160.

Proteomic databases

PaxDbB0JSP4.
PRIDEB0JSP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG00938; BAG00938; MAE_11160.
GeneID5861914.
KEGGmar:MAE_11160.
PATRIC22627365. VBIMicAer59304_1022.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMAER449447:GHO8-1118-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 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_MICAN
AccessionPrimary (citable) accession number: B0JSP4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: February 19, 2014
This is version 43 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