A0A167EGQ2 · A0A167EGQ2_9PEZI

  • Protein
    Multifunctional fusion protein
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

pyridoxal 5'-phosphate (UniProtKB | Rhea| CHEBI:597326 )

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentribonucleoprotein complex
Cellular Componentribosome
Molecular Functionpyridoxal phosphate binding
Molecular Functionstructural constituent of ribosome
Molecular Functionthreonine deaminase activity
Biological Processisoleucine biosynthetic process
Biological Processtranslation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Threonine dehydratase
  • EC number
  • Alternative names
    • Threonine deaminase
  • Recommended name
    Ribosomal protein

Gene names

    • ORF names
      CI238_09360

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MAFF 238704
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Glomerellaceae > Colletotrichum > Colletotrichum spaethianum species complex

Accessions

  • Primary accession
    A0A167EGQ2

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-56Disordered
Compositional bias34-50Polar residues
Domain402-478ACT-like
Domain500-571ACT-like
Region617-692Disordered

Sequence similarities

Belongs to the bacterial ribosomal protein bL36 family.
Belongs to the serine/threonine dehydratase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    806
  • Mass (Da)
    88,782
  • Last updated
    2016-07-06 v1
  • Checksum
    A7F26792F1A31ED7
MSENAEPPVVAVMTNGTLNGVNGDHPPRPRTPQPQGMSLTEYSANPSTPPEERRSRIKGVVPDDFLLPDGHPDYLRLIAAATSRVYEACKITPLQPAVNLSNRLECNVLLKREDQQPVFSFKLRGAYNKMAHLDPAKSWKGVVCCSAGNHAQGVAYSARKLKIPATIIMPEATPSIKHLNVARLGGHVVLHGADFDAAKEECGRRALQDGLINIPPFDDPYVIAGQGTIGMELFGQINMSKLDAIFCCVGGGGLISGIGVYVKRMAPHVKIIGVETYDANALVQSLAKGERVVLDNVGLFADGAAVKTVGEETFRLCKDVVDEVIQVTTDEVCAAIKDMYDDTRAGLEPAGALSIAGLKKYVAQNPSDRRRSMVAVTSGANMNFDRLRFVAERATLGEGKEALLAVSIPEKPGAFANLITSIMPHSVTEFSYRYATDEVANVLIGISLTAPASQRTQELQMLLERIQSHDMSVTDLSGDELAKSHIRYLVGGRSNVPNERLYMFNFPERPGALEKFLMTLRPKFNISLFNYRNYGGDTGKILAGILCPDNEVEELEKFLTEIGYPWEDCSQSAVFKTFLRRPWRWVQSRVLVTFVRYRSIAIRSIVLISARTRIPRDSDKTSKMLPPKPSGPLQHQRRRHREAPRLTTSPSSPAPDRSRRKFARRIELPSTPFTSDTRKPYLEPRKRAGKKKMASLAASLRSLTLTTARATIPRVGTTVTATRALSTAILTKKPAQKTESVLAAFGQKAAAVGNAVVQQTRGMKVHSSVKKRCEHCKIVRRKAGKRHNGYLYVICKANPRHKQRQS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias34-50Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LFIW01000726
EMBL· GenBank· DDBJ
KZL85115.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp