A0A7J7FM02 · A0A7J7FM02_DICBM

Function

Caution

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

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Can bind about 5 Ca2+ ions per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Features

Showing features for binding site, active site.

158850100150200250300350400450500550
TypeIDPosition(s)Description
Binding site87Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site166Ca2+ 2 (UniProtKB | ChEBI)
Binding site176Zn2+ 1 (UniProtKB | ChEBI)
Binding site178Zn2+ 1 (UniProtKB | ChEBI)
Binding site183Ca2+ 3 (UniProtKB | ChEBI)
Binding site184Ca2+ 3 (UniProtKB | ChEBI)
Binding site191Zn2+ 1 (UniProtKB | ChEBI)
Binding site203Ca2+ 2 (UniProtKB | ChEBI)
Binding site205Zn2+ 1 (UniProtKB | ChEBI)
Binding site207Ca2+ 3 (UniProtKB | ChEBI)
Binding site208Ca2+ 1 (UniProtKB | ChEBI)
Binding site210Ca2+ 3 (UniProtKB | ChEBI)
Binding site210Ca2+ 1 (UniProtKB | ChEBI)
Binding site259Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site260
Binding site263Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site269Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site277Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site348Ca2+ 4 (UniProtKB | ChEBI)
Binding site350Ca2+ 5 (UniProtKB | ChEBI)
Binding site399Ca2+ 5 (UniProtKB | ChEBI)
Binding site491Ca2+ 4 (UniProtKB | ChEBI)
Binding site493Ca2+ 5 (UniProtKB | ChEBI)

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 Componentextracellular matrix
Cellular Componentextracellular space
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcollagen catabolic process
Biological Processextracellular matrix organization
Biological Processproteolysis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Peptidase metallopeptidase domain-containing protein

Gene names

    • ORF names
      HPG69_009574

Organism names

Accessions

  • Primary accession
    A0A7J7FM02

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_502945349219-588Peptidase metallopeptidase domain-containing protein

Keywords

Family & Domains

Features

Showing features for motif, domain, region, compositional bias, repeat.

TypeIDPosition(s)Description
Motif85-92Cysteine switch
Domain108-307Peptidase metallopeptidase
Region304-342Disordered
Compositional bias313-338Pro residues
Repeat340-389Hemopexin
Repeat393-438Hemopexin
Repeat439-487Hemopexin
Repeat488-534Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    588
  • Mass (Da)
    64,445
  • Last updated
    2021-04-07 v1
  • Checksum
    5A3C88A47CEE17F0
MLRLLALLLPLLPPPARASEPAAQDVSLGVDWLTRYGYLPPPHPAQAQLQSPAKLRDAIKVMQRFAGLPETGLLDRGTVAAMHKPRCSLPDVLGVAGLVKRRRRYALSGSMWKKRTLTWRVQSFPQSSALSQETVRTLMHHALTAWGVESGLRFREVGSQGPSEPDILIDFARAYHQDSYPFDGQGGTLAHAFFPGEHSISGDTHFDDEETWTFGSKAGPTPSCLAAPFLVWGWGTQLQPTLAPFPDGEGTDLFAVAVHEFGHALGLGHSSAPDSIMRPFYQGPVGNPAEYRLSQDDREGLQQLYGKAPQPPYDTPTRKPLAPPPPPPALPPDSPSLPGPDRCEGNFDAIANIRGETFFFKGPWFWRLQPSGQLVSPRPARLHRFWEGLPAQVQVIQAAYARHPDGRILLFSGPQFWVFQDRQLEGAARPLSDLGLPPGEAVDAVFSWPLNGKTYLIRGRRYWRYDEAAARPDPGYPRDLSLWEGAPLAPDDVTVSNTGDTYFFKGAHYWRFPKGSVQAEPDSPQPMGPKWLDCPAPSAGPRAPRTPKATLKPGPCDCQCEINQATGRGSVSLLLPLLSLLVGGVTSR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias313-338Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACDTQ010000128
EMBL· GenBank· DDBJ
KAF5929092.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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