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Q5N1G1 (SYI_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. 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:syc1669_d
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length954 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 – 954954Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098490

Regions

Motif60 – 7011"HIGH" region HAMAP-Rule MF_02002
Motif605 – 6095"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9231Zinc By similarity
Metal binding9261Zinc By similarity
Metal binding9431Zinc By similarity
Metal binding9461Zinc By similarity
Binding site5641Aminoacyl-adenylate By similarity
Binding site6081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5N1G1 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: DC282BC4C1431307

FASTA954107,414
        10         20         30         40         50         60 
MAEVSAYKDT LNLLQTPFNM RANAPVREPE IQQFWADRQI YETLSRQNPG APFVLHDGPP 

        70         80         90        100        110        120 
YANGALHMGH ALNKTLKDII NKYQLLQGRK VRYVPGWDCH GLPIELKVLQ ELSSEERRNL 

       130        140        150        160        170        180 
TPLTLRQKAK AYALAQVEQQ SQSFQRYGVW ADWDAPYLTL TPEYEAAQID VFGQMVLKGY 

       190        200        210        220        230        240 
IYRGLKPVHW SPSSRTALAE AELEYPDGHT SRSIYVAMPI VQLSEAAQPL LGNYANLALA 

       250        260        270        280        290        300 
IWTTTPWTIP ANLAVAVNGE LTYAVVQAGD CHLIVAAELA ESLSKTFATE LTVLATFPGS 

       310        320        330        340        350        360 
VLEHSRYRHP LYDRESPVVI GGDYITTESG TGLVHTAPGH GQDDFIVGNR YGLEVFCPVD 

       370        380        390        400        410        420 
DKGDFTAAVG DRLVGKNVLK DANAAVIEWL TEVGALLKEE SYAHRYPYDW RTKKPTIFRA 

       430        440        450        460        470        480 
TEQWFASVEG FREQALQAIA EVDWIPAQGE NRITSMVSER SDWCISRQRT WGVPIPVFYD 

       490        500        510        520        530        540 
EESGEALLNA ETIAHVRAIV AERGSDAWWE LDVADLLPEP YRSNGRRYRK GTDTMDVWFD 

       550        560        570        580        590        600 
SGSSWAAVAS QREGLHYPAD LYLEGSDQHR GWFQSSLLTS VACNGHAPYR RVLTHGFALD 

       610        620        630        640        650        660 
EKGRKMSKSL GNVVDPAIVI NGGKDQKQEP PYGADVLRLW VSSVDYSSDV PIGKNILKQM 

       670        680        690        700        710        720 
ADVYRKIRNT ARFLLGNLHD FDPAKDALPW EKLPELDRYL LHRLREVILE IQDAFESFQF 

       730        740        750        760        770        780 
FRFFQTVQNF CVVDLSNFYL DIGKDRLYIS APDSLRRRSC QTVLAICVEA LATAIAPVLS 

       790        800        810        820        830        840 
HMAEDIWQSL PYPARTKSVF QAGWVQLQDD WNQPELAAKW QQLRDLRSEV NKVLEQARRD 

       850        860        870        880        890        900 
QAIGSSLEAK LQLWVADSDW RAALADRNPA DSLSGTAVDD LRYLFLVSQV ELRDQPTGLT 

       910        920        930        940        950 
EAKYHAQTED WAIAVVDAEG QKCDRCWNYS TTVGQSSEHP DLCDRCVSAL QGTF 

« Hide

References

[1]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008231 Genomic DNA. Translation: BAD79859.1.
RefSeqYP_172379.1. NC_006576.1.

3D structure databases

ProteinModelPortalQ5N1G1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269084.syc1669_d.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD79859; BAD79859; syc1669_d.
GeneID3197837.
KEGGsyc:syc1669_d.
PATRIC32489338. VBISynElo117686_1910.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSELO269084:GCDQ-1714-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_SYNP6
AccessionPrimary (citable) accession number: Q5N1G1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 1, 2005
Last modified: April 16, 2014
This is version 71 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