Q10MU6 · Q10MU6_ORYSJ

Function

function

Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.

Catalytic activity

  • ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.
    EC:6.2.1.45 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for active site.

110641002003004005006007008009001,000
TypeIDPosition(s)Description
Active site640Glycyl thioester intermediate

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular FunctionATP binding
Molecular Functionubiquitin activating enzyme activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E1 ubiquitin-activating enzyme
  • EC number

Gene names

    • Ordered locus names
      LOC_Os03g18380

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa

Accessions

  • Primary accession
    Q10MU6

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-45Disordered
Domain937-1059Ubiquitin-activating enzyme E1 C-terminal

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,064
  • Mass (Da)
    117,453
  • Last updated
    2006-08-22 v1
  • Checksum
    906AEB0A4D40CCBE
MLPTKRANGAEAESSSDAPAKKARVGASASEAEAMVAGEAGGGGGGVSGNGSEVAEIDEDLHSRQLAVYGRETMRRLFASNVLVSGLNGLGAEIAKNLALAGVKSITLHDMGNVEMWDLSGNFFLSEDDIGKNRAVACTAKLQELNNAVLISTLTEDLTNEHLSKFQAVVFTDISLDKAFEFDDYCRNHQPSISFIKAEVCGLFGSVFCDFGPKFTVLDVDGEEPHTGIIASISNDNPAMISCVDDERLEFQDGDLVVFSEVQGMTELNDGKPRKIINARPYSFCIQEDTSKFGIYAKGGIVTQVKEPINLEFKSLRDSIREPGNFLLSDFSKFDRPPLLHFAFLALDKFRKEFGRFPGAGCDQDAQRFIEFVASVNEATIDYKMDELDGKLLRNFASGSRAVLNPMAAMFGGIVGQEVVKACSGKFHPQYQFFYFDSAESLPTYPLDSKDLKPLNSRYDAQISVFGSKLQKKMRDANVFVVGSGALGCEFLKNLALMGVSCGLKGKLTITDDDIIEKSNLSRQFLFRDWNIGQAKSTVAAAAASAINSSLHINALQNRACPETEHVFHDKFWEGLDVIINALDNVNARMYMDMRCLYFQKPLLESGTLGPKCNTQMVIPHLTENYGASRDPPEKQAPMCTVHSFPHNIDHCLTWARSEFEGLLEKTPNEVNSFISNPAQYAAAMRKAGDAQARELLERVCECLDKERCDGFEDCIAWARLKFEDYFANRVKQLTFTFPEDAVTSTGAFFWSAPKRFPRPLQFSTVNSSHIHFILAASILRAVSFGISIPDWAKNTSNLVDAVSKVVVPEFEPKSGVKIETDEKASNISSASVDDASVIEDLLTKLEASAKKLPPGFQMKAIQFEKDDDTNFHMDLIAGLANMRARNYGIQEVDKLKAKFIAGRIIPAIATSTAMATGLVCLELYKVLAGGHPVEDYRNSFANLAIPMFSMAEPLPPKVIKHQDMRWTIWDRWSIEGNITVAELLKWLSDKGLSAYSVSCGTSLLYNTMFPRHKDRVNKKLVDVAKEVAKVDVPAYRRHLDVVVACEDDDGNDVDIPLISIYFR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DP000009
EMBL· GenBank· DDBJ
ABF95428.1
EMBL· GenBank· DDBJ
Genomic DNA
AK120544
EMBL· GenBank· DDBJ
BAH00064.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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