A0A1L9P324 · A0A1L9P324_ASPVE

Function

function

May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins. May also function as a chaperone, playing a role in intracellular transport of proteins. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on proteins.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

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 ComponentP-body
Molecular FunctionmRNA binding
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Molecular Functionubiquitin-protein transferase activity
Biological Processdeadenylation-independent decapping of nuclear-transcribed mRNA
Biological ProcessP-body assembly
Biological Processprotein folding
Biological Processprotein peptidyl-prolyl isomerization
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Enhancer of mRNA-decapping protein 3
  • EC number
  • Alternative names
    • Cyclophilin-60
    • Cyclophilin-like protein Cyp-60
    • Peptidyl-prolyl cis-trans isomerase-like 2
    • RING-type E3 ubiquitin transferase isomerase-like 2

Gene names

    • ORF names
      ASPVEDRAFT_48211

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 583.65
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Nidulantes

Accessions

  • Primary accession
    A0A1L9P324

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region63-92Disordered
Compositional bias69-92Polar residues
Region164-205Disordered
Domain272-308DFDF
Region319-390Disordered
Compositional bias356-370Polar residues
Region403-427Disordered
Domain452-677YjeF N-terminal
Domain735-808U-box
Region918-956Disordered
Domain1014-1162PPIase cyclophilin-type
Compositional bias1176-1206Basic and acidic residues
Region1176-1223Disordered
Region1247-1272Disordered

Sequence similarities

Belongs to the EDC3 family.
Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,272
  • Mass (Da)
    138,759
  • Last updated
    2017-03-15 v1
  • Checksum
    217BB78E9B40BB30
MASEFIGYNVLVTLRAPPGATVQGVVADVIGQRLMLQNVSLSWIGYPVPAYSIEAPDIADLSLKPSDRPGAQAATTPQVTRNVAPPISRNQTQQQFVDPAILSFSKPSNEVHSSAQLQSNLIDGPAARQYPAPQSASHHISHATPATLNEPFSNLELNVSSIPTPQVEPEKELQGPSLHAAEEPPIHAASRHGTVRGRRGGKQKAQNVYNEHNGALNTNPKTKGWRQTAFVEPSSPSMMNSPQPYKERGALNNKRRKKKTKGYTEETNGWATEEATDIQELGEFDFASNLSKFDKRRVFEEIRNDDTTADEARLVSFNKRVPKPGTNGGRNLHWTENVLDDSPEEESDNGATDHEPSDAKLSSGTFSGRDVSRLSVRGRASRKGSGILGQPLIPAQINTVGRHQLSGSRTNSPLPTKSHVSASPITGPSVSNATLRLATTNRSCPTVSPLQILEVEQLAIGEVGLTEDMITENAGRSIAEAAVGLLNSDAAAPTILALVGNHRTGARAISSARHLRNRGHRVTVCMLGIEQEVELLESCRKQVEIFKKMGGRFLKWEELSPRLSTSEFEPDLILDALFGIHLTFNDLRTDDQATAFQMISWVNRSELDTLSVDVPSGISATTGEVTFVESGQLRVDSKSIVCLGAPKTGLVNALLAGEGSSWNLSVADIGIPQIAWRKFGTRRRHGIDFGNRWIVSLRFQPSITHSEWASDEAYSASAGAGVGRARLGADGASFRRLPFKFCSLSLQPFEHPVCTQSGTIFDLTNILPWIKKHGTNPVDGTPLKGSDLIKLTIAKNDADEYIDPVTYKVLTDNTHVVALRNTGNVYAWDTVERLNIKGKMWRDLMTDEEFSRKDIITLQDPQNIESRNLSSFNYIKEGETGLSDEQLREREDPARNVNANALGSSAKILKAREAVAKAREERAQRSGTTAASAALAKTGAPAKSLQKTASNQSGKPVPYNAAKYTTGLAAASFTSTGMTPHTSAELALLSDEDYMLKRGRVKQKGYARISTTSGDVNLELHTEYAPKAVWNFIKLAKKGYYKDVTFHRNIKGFMIQGGDPTGTGRGGESVWGKYFNDEFEGPLKHDSRGTLSMANKGKNTNSSQFFIAYRALPHLNLKHTIFGHVIDDPTPSSPTLNKLEAHPVNATTNKPTPDVRIIDVTIFVDPFEEFLKQKQIEQSAEKGEGKTAEDEEQNSRRAEDDQVTWTGKRVRGPGAAKDEGSAGVGKYLKAALTERAGQDEDEIVEFVDDEPAPEPARKKFKGGGFGDFSSWD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias69-92Polar residues
Compositional bias356-370Polar residues
Compositional bias1176-1206Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KV878125
EMBL· GenBank· DDBJ
OJI95925.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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