A0A427XSA2 · A0A427XSA2_9TREE

  • Protein
    Ubiquitin-activating enzyme E1-like
  • Gene
    UBA2
  • 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.

Pathway

Protein modification; protein sumoylation.

Features

Showing features for binding site, active site.

160750100150200250300350400450500550600
Type
IDPosition(s)Description
Binding site28-33ATP (UniProtKB | ChEBI)
Binding site52ATP (UniProtKB | ChEBI)
Binding site60-63ATP (UniProtKB | ChEBI)
Binding site76ATP (UniProtKB | ChEBI)
Binding site123-128ATP (UniProtKB | ChEBI)
Binding site164Zn2+ (UniProtKB | ChEBI)
Binding site167Zn2+ (UniProtKB | ChEBI)
Active site179Glycyl thioester intermediate
Binding site432Zn2+ (UniProtKB | ChEBI)
Binding site435Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentSUMO activating enzyme complex
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular FunctionSUMO activating enzyme activity
Biological Processprotein sumoylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ubiquitin-activating enzyme E1-like

Gene names

    • Name
      UBA2
    • ORF names
      EHS24_007898

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 27194
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Trichosporonales > Trichosporonaceae > Apiotrichum

Accessions

  • Primary accession
    A0A427XSA2

Proteomes

Subcellular Location

Interaction

Subunit

Heterodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain10-302THIF-type NAD/FAD binding fold
Domain303-386Ubiquitin-activating enzyme SCCH
Region547-607Disordered
Compositional bias564-580Basic and acidic residues
Compositional bias588-607Acidic residues

Sequence similarities

Belongs to the ubiquitin-activating E1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    607
  • Mass (Da)
    66,204
  • Last updated
    2019-05-08 v1
  • MD5 Checksum
    A8F414D1FC7184CD4E29C48E0AA0B0F1
MGRLSHAKALLGPQLFAKVRDTPVLIVGAGGIGSELLKNLVLVGFTNIELLDLDTIDLSNLNRQFLFRKPDIGKSKSLVAAATAHHFNPSSGIKINARHGNVKDSENDIAWISKFGFVMNALDNADARRHVNKLCAAADVPLIESGTAGYLGQVTPIIPGETECYDCNPKPPPKSFPVCTIRATPSEPIHCIVWAKSYLFGKLFGEDDEAGDEAELDKAKAEGENAAFREVRRLLSEENGPQRVFNKVFNEDINRLLAMEDMWKVAGRIKPVALDYDAIMDGTFVAPPPRTSAAQAAAAVNGTANGNAAASASTSTLKDQKELTLKENLELFIDSCARLAARSIAHPDVVLSFDKDDDDTLDFVVAIANLRATAYSIATRTRFQVKGFIVMQALSLLKRKSAEATKATDVYLRSIPHLPLAPSAPVPPNESCAVCRDTYIPFKADVSRCTLGEVLDAAKSWLQASLGENELECSVLEGARVLADPDFDDNHSRTLKDLDIERGKMITLMDEDDKYRPIHFCLLEPEANAETAFSFPETAPALALKPVQVKERSESPEVELVEAASRKRSEPDSGHDDLPSKKRKTETEEPEVVVDDGDDDDDIIIIE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias564-580Basic and acidic residues
Compositional bias588-607Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RSCE01000006
EMBL· GenBank· DDBJ
RSH81710.1
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.
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