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Q7NF75 (SYI_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. 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:gll3651
OrganismGloeobacter violaceus (strain PCC 7421) [Reference proteome] [HAMAP]
Taxonomic identifier251221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter

Protein attributes

Sequence length983 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
Reference 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 – 983983Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_0000098392

Regions

Motif61 – 7111"HIGH" region HAMAP-Rule MF_02002
Motif649 – 6535"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding9521Zinc By similarity
Metal binding9551Zinc By similarity
Metal binding9721Zinc By similarity
Metal binding9751Zinc By similarity
Binding site6081Aminoacyl-adenylate By similarity
Binding site6521ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NF75 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 7F4A0F7C6DDD130C

FASTA983110,014
        10         20         30         40         50         60 
MTQTPVDYKQ TVRTPKTDFP MRANASTREV EIQRFWEEQG IYGRLAQENP GEIFILHDGP 

        70         80         90        100        110        120 
PYANGELHVG HALNKILKDI INRYQLLQGR RVRYVPGWDC HGLPIELKVL QDLSQAERSQ 

       130        140        150        160        170        180 
LTPLDVRTRA RDFAQRTVQS QCASYKRFGV WGDWDHPYLT LQPEYEAAQL GVFGKMALKG 

       190        200        210        220        230        240 
YIYRGLKPVH WSPSSQTALA EAELEYPTKD DGSPAHTSRS VYVKFPLISI AAPETATVMA 

       250        260        270        280        290        300 
AELLPRLSAF HDREEELIDA LLGERDDLPE IAVAIWTTTP WTLPGNLAVA LNGELDYALV 

       310        320        330        340        350        360 
ASDEHGLLIV AAELVERLAG TLATRFETIA TFRGRELEGS LLAHPLFRRT SPIVLGDHVT 

       370        380        390        400        410        420 
TESGTGAVHT APGHGSEDFE LAQRYNLGVL SPVDDYGRFT READSDRREN LPVFAGKAVL 

       430        440        450        460        470        480 
SDGNQAVIEA LSAAGALLKE EAYVHKYPYD WRTKKPTIFR ATTQWFASVS DFRPQALSAI 

       490        500        510        520        530        540 
AQTEWIPASG ENRITAMVAG RNDWCISRQR AWGLPIPAFY CENCANVLLT QESVEAVQAA 

       550        560        570        580        590        600 
VRVHGSDIWW QKEASELLPP GIACAHCGGT AFRKEKDIMD VWFDSGSSWA GVLGRRPELH 

       610        620        630        640        650        660 
YPADVYLEGS DQHRGWFQSS LLTCVATEGT APYKTVITHG FTLDEHGRKM SKSLGNVVDP 

       670        680        690        700        710        720 
KLVIDGGANQ KQHPAYGADV LRLWVASVDY TSDQLVGPSV LAQIAEVYRK IRNTARYLLG 

       730        740        750        760        770        780 
SLNDFVPERD LVAFDSLGEV DQYLLHRLSV VHLEVTQAFE SYQFSRFFQT IQNFCVADLS 

       790        800        810        820        830        840 
NFYLDISKDR LYISAEVSLR RRSCQTVLYR VLESLTRLIA PVLPHLAEDI WQHLPYPRSD 

       850        860        870        880        890        900 
ASVFEAGWPV DHSQWFQPLT VDRWPGLIVL RDRVNIALEA ARNAKRIGSS LEAKIRLHVE 

       910        920        930        940        950        960 
DPALTDELAR QKDELRYLFI VSQVELLDEL PAEVSVEEGA AVIVLDADGQ KCERCWNYSV 

       970        980 
HVGEDAEHPT LCERCVSALA GAF 

« Hide

References

[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000045 Genomic DNA. Translation: BAC91592.1.
RefSeqNP_926597.1. NC_005125.1.

3D structure databases

ProteinModelPortalQ7NF75.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING251221.gvip495.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC91592; BAC91592; BAC91592.
GeneID2602055.
KEGGgvi:gvip495.
PATRIC22046801. VBIGloVio86258_3686.

Phylogenomic databases

eggNOGCOG0060.
KOK01870.
OMAKPVHWCL.
OrthoDBEOG644ZM1.
PhylomeDBQ7NF75.

Enzyme and pathway databases

BioCycGVIO251221:GH9A-3700-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
3.40.50.620. 2 hits.
3.90.740.10. 2 hits.
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_GLOVI
AccessionPrimary (citable) accession number: Q7NF75
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 76 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