A0A5P1ETI6 · A0A5P1ETI6_ASPOF

Function

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Features

Showing features for active site, binding site.

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Type
IDPosition(s)Description
Active site118Proton donor
Active site258
Active site351Proton donor
Active site372
Binding site462Ca2+ (UniProtKB | ChEBI)

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
Cellular Componentendoplasmic reticulum quality control compartment
Cellular Componentmembrane
Molecular Functioncalcium ion binding
Molecular Functionmannosyl-oligosaccharide 1,2-alpha-mannosidase activity
Biological Processcarbohydrate metabolic process
Biological Processendoplasmic reticulum mannose trimming
Biological Processmannose trimming involved in glycoprotein ERAD pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    alpha-1,2-Mannosidase
  • EC number

Gene names

    • ORF names
      A4U43_C06F19470

Organism names

  • Taxonomic identifier
  • Strain
    • cv. DH0086
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Asparagales > Asparagaceae > Asparagoideae > Asparagus

Accessions

  • Primary accession
    A0A5P1ETI6

Proteomes

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-25
ChainPRO_502441768726-631alpha-1,2-Mannosidase

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias582-604Polar residues
Region582-631Disordered
Compositional bias605-631Basic and acidic residues

Sequence similarities

Belongs to the glycosyl hydrolase 47 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    631
  • Mass (Da)
    70,476
  • Last updated
    2020-02-26 v1
  • Checksum
    66570B7D5E7E5D3D
MRGILLVKVGCLILFSALSPTNSLADGVTPSEAKQLRDEVREMFYHAFEGYMQHAFPLDELRPLTCKGEDTLGGYALTLIDALDTLALLGDREGFGAAVEWVGKNVRFDIDKTVSLFETTIRILGGLLSAHLIASDYATGMKLPSYDDELLHLAEDLAQRLLPAFDTPTGIPYGSVNLMHGVDENESKITSTAGGGTLTLEFGVLSRLTNNPIFEEVTKNAVRGIWARRSNINLVGAHINIFTGEWTQKDAGIGTSIDSFYEYLLKAYLLFGDEEYLFMFREAYKAAMHYLHTDPWYVEVNMYSAVTVWPLFNSLQAFWPGLQVLAGDIDPAVRTHAAFFSVWKKYGFTPEGFNLATFNVQHGQRSYPLRPELIESTYWLFKATRDPRYLDAGRDMLASLQYGARCPCGYCHIADVESHKQDDHMESFFLAETVKYLWLLFDLAVGPDNLVENGPYKYIFSTEGHVLPATPEISLVSDHCSYLGAFCKSDRWKKDGHTKILFDHHETNDSQLHADRGASISSQKARDTFTASSFIKGFCPGLTHGQKFGISYVEEKHETNEHESTSPQSQKHSIILISNPTTIHSINADESDGSNNIEETNEESRALVPNTDEKDAEALSQEGIQQDKDSS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias582-604Polar residues
Compositional bias605-631Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM007386
EMBL· GenBank· DDBJ
ONK67370.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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