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Q21HK3 (SYI_SACD2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. 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:Sde_2566
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

Protein attributes

Sequence length932 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 – 932932Isoleucine--tRNA ligase HAMAP-Rule MF_02002
PRO_1000022114

Regions

Motif58 – 6811"HIGH" region HAMAP-Rule MF_02002
Motif600 – 6045"KMSKS" region HAMAP-Rule MF_02002

Sites

Metal binding8951Zinc By similarity
Metal binding8981Zinc By similarity
Metal binding9151Zinc By similarity
Metal binding9181Zinc By similarity
Binding site5591Aminoacyl-adenylate By similarity
Binding site6031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21HK3 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 96EA5D8EC7A224C6

FASTA932104,058
        10         20         30         40         50         60 
MTDYKATLNL PQTSFAMKAN LAQREPGMLK QWQQSKLYEQ IREARKGREQ FILHDGPPYA 

        70         80         90        100        110        120 
NGDIHIGHAV NKILKDIIIK AKTLSGFDAP YVPGWDCHGL PIEHNVEKKV GKAGVKIDHV 

       130        140        150        160        170        180 
AFRQKCRDYA RKQVEGQKKD FIRLGVLGEW DTPYLTMDFK TEADTVRALG KIVENGHLHK 

       190        200        210        220        230        240 
GFKPVYWSVV GASALAEAEV EYQDKTSFAI DVCFGVADVE DFAARVGSVA GTGNISVVIW 

       250        260        270        280        290        300 
TTTPWTLPAN QAVSVNGELD YVVVQHGEQR LVLAEALVES VAKRLGVEEL ATVATFKGAA 

       310        320        330        340        350        360 
IEGLKLNHPF YAKQVPVLLG DHVTTDAGTG CVHTAPDHGA DDFVVSNKYG IETLNYVDEN 

       370        380        390        400        410        420 
GIYRDNVEIF AGDHVYKVDE KVIGLLEENG RLLHQAKLVH SFPHCWRTKT PLIFRATPQW 

       430        440        450        460        470        480 
FVSMTKNNLL KDVKQAVEGV NWVPDWGRAR IDSMLDSSPD WCISRQRTWG VPITLFVHKE 

       490        500        510        520        530        540 
TQELHPNTAA LVEDVAKRIE EKGMDAWFEL DAVELLGDEA DQYQKVTDTL DVWFDSGVTH 

       550        560        570        580        590        600 
YSVVNARENL RYPADLYLEG SDQHRGWFQS SLKTSMAING SAPYKQVLTH GFTVDADGKK 

       610        620        630        640        650        660 
MSKSIGNTVS PQKVMNDLGA DVLRLWVAAT DFSGDMSVSD EILKRTADSY RRIRNTARFF 

       670        680        690        700        710        720 
LSNLTGFNPQ TDLLPAEEML SLDRWAVDRA AALQADILKS YDTYQLHQIY QKLHNFCVVE 

       730        740        750        760        770        780 
MGGFYLDIIK DRQYTTKETS HARRSAQSAL YHIVEAFVRW IAPICSFTAD EIWQAMPGEK 

       790        800        810        820        830        840 
TGTVFTAEWY NLPRLAEGAE LGNSYWQFIA KVKTAVNKTI EAKRSAGEVG GSLAAEVTLY 

       850        860        870        880        890        900 
CSESVAQKLT LLKDELRFVL ICSSVTVVAA SETEGEATEV EGLRVAVAKS SHEKCARCWH 

       910        920        930 
HREDVGQNTA HPEICGRCVE NIDGEGESRE FA 

« Hide

References

[1]"Complete genome sequence of the complex carbohydrate-degrading marine bacterium, Saccharophagus degradans strain 2-40 T."
Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., Richardson P.M., Borovok I., Hutcheson S.
PLoS Genet. 4:E1000087-E1000087(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2-40 / ATCC 43961 / DSM 17024.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000282 Genomic DNA. Translation: ABD81826.1.
RefSeqYP_528038.1. NC_007912.1.

3D structure databases

ProteinModelPortalQ21HK3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203122.Sde_2566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD81826; ABD81826; Sde_2566.
GeneID3968675.
KEGGsde:Sde_2566.
PATRIC23404196. VBISacDeg56404_2763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSDEG203122:GI2M-2611-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_SACD2
AccessionPrimary (citable) accession number: Q21HK3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: April 16, 2014
This is version 60 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