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ECOLI:SYI

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ileS (synonyms: ilvS)
Protein Name(s) Isoleucine--tRNA ligase

Isoleucyl-tRNA synthetase IleRS

External Links
UniProt P00956
EMBL U00096
AP009048
M10428
X00776
K01990
PIR B64723
RefSeq NP_414567.1
YP_488332.1
ProteinModelPortal P00956
SMR P00956
BioGrid 849163
DIP DIP-10017N
IntAct P00956
MINT MINT-1232480
STRING 511145.b0026
BindingDB P00956
ChEMBL CHEMBL3657
PaxDb P00956
PRIDE P00956
EnsemblBacteria AAC73137
BAB96595
GeneID 12932381
944761
KEGG ecj:Y75_p0026
eco:b0026
PATRIC 32115143
EchoBASE EB0487
EcoGene EG10492
eggNOG COG0060
HOGENOM HOG000246402
InParanoid P00956
KO K01870
OMA VLGDWDN
OrthoDB EOG644ZM1
PhylomeDB P00956
BioCyc EcoCyc:ILES-MONOMER
ECOL316407:JW0024-MONOMER
MetaCyc:ILES-MONOMER
PRO PR:P00956
Proteomes UP000000318
UP000000625
Genevestigator P00956
GO GO:0005737
GO:0002161
GO:0005524
GO:0004822
GO:0008270
GO:0006428
GO:0046677
Gene3D 1.10.730.10
3.40.50.620
3.90.740.10
HAMAP MF_02002
InterPro IPR001412
IPR002300
IPR002301
IPR023585
IPR013155
IPR014729
IPR009080
IPR009008
IPR010663
PANTHER PTHR11946:SF9
Pfam PF08264
PF00133
PF06827
PRINTS PR00984
SUPFAM SSF47323
SSF50677
TIGRFAMs TIGR00392
PROSITE PS00178

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0004822

isoleucine-tRNA ligase activity

PMID:4581276[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006428

isoleucyl-tRNA aminoacylation

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10492
PANTHER:PTN000235772

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10492
PANTHER:PTN000235772
UniProtKB:Q9NSE4

C

Seeded From UniProt

complete

enables

GO:0004822

isoleucine-tRNA ligase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10492
PANTHER:PTN000235772

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:8286369[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006428

isoleucyl-tRNA aminoacylation

PMID:764868[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004822

isoleucine-tRNA ligase activity

PMID:764868[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0106074

aminoacyl-tRNA metabolism involved in translational fidelity

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0002161

P

Seeded From UniProt

complete

enables

GO:0000049

tRNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR033708

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001412
InterPro:IPR002300
InterPro:IPR002301
InterPro:IPR009080

F

Seeded From UniProt

complete

enables

GO:0002161

aminoacyl-tRNA editing activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR009008

F

Seeded From UniProt

complete

enables

GO:0004812

aminoacyl-tRNA ligase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001412
InterPro:IPR002300
InterPro:IPR009080
InterPro:IPR013155

F

Seeded From UniProt

complete

enables

GO:0004822

isoleucine-tRNA ligase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002301
InterPro:IPR023585

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001412
InterPro:IPR002300
InterPro:IPR002301
InterPro:IPR009080

F

Seeded From UniProt

complete

involved_in

GO:0006418

tRNA aminoacylation for protein translation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001412
InterPro:IPR002300
InterPro:IPR009008
InterPro:IPR009080
InterPro:IPR013155

P

Seeded From UniProt

complete

involved_in

GO:0006428

isoleucyl-tRNA aminoacylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002301

P

Seeded From UniProt

complete

enables

GO:0004822

isoleucine-tRNA ligase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:6.1.1.5

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000090066

F

Seeded From UniProt

complete

involved_in

GO:0006428

isoleucyl-tRNA aminoacylation

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000090066

P

Seeded From UniProt

complete

enables

GO:0004822

isoleucine-tRNA ligase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000090066

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000090066

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000090066

F

Seeded From UniProt

complete

enables

GO:0016874

ligase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0436

F

Seeded From UniProt

complete

involved_in

GO:0006412

translation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0648

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0004812

aminoacyl-tRNA ligase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0030

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0046677

response to antibiotic

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0046

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Dureković, A et al. (1973) Isolation and properties of isoleucyl-tRNA synthetase from Escherichia coli MRE 600. Eur. J. Biochem. 36 528-33 PubMed GONUTS page
  2. 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. Xu, B et al. (1994) Probing the metal binding sites of Escherichia coli isoleucyl-tRNA synthetase. Biochemistry 33 398-402 PubMed GONUTS page
  4. 4.0 4.1 Fersht, AR & Kaethner, MM (1976) Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12. Biochemistry 15 818-23 PubMed GONUTS page
  5. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page