A0A9N8VT78 · A0A9N8VT78_9GLOM

  • Protein
    E3 ubiquitin-protein ligase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.

Caution

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

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)

Pathway

Protein modification; protein ubiquitination.

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
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processprotein ubiquitination
Biological Processubiquitin-dependent protein catabolic process via the N-end rule pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase
  • EC number

Gene names

    • ORF names
      ALEPTO_LOCUS1756

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • FL130A
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Glomeromycotina > Glomeromycetes > Archaeosporales > Ambisporaceae > Ambispora

Accessions

  • Primary accession
    A0A9N8VT78

Proteomes

Family & Domains

Features

Showing features for compositional bias, region, domain, zinc finger.

TypeIDPosition(s)Description
Compositional bias1-32Polar residues
Region1-46Disordered
Domain74-114RING-type
Region392-431Disordered
Region489-537Disordered
Region636-694Disordered
Compositional bias711-751Polar residues
Region711-786Disordered
Compositional bias758-778Polar residues
Domain878-950UBR-type
Zinc finger878-950UBR-type
Region2315-2355Disordered

Sequence similarities

Belongs to the UBR1 family.
Belongs to the ZNF598/HEL2 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,925
  • Mass (Da)
    333,695
  • Last updated
    2023-09-13 v1
  • Checksum
    729B200832F65DA8
MQEQQPQGQSQELQTQQFQNAENASINVGRESSHRPSNRRGFRGGRGAAARLRASLAAEADNDASTSNADTNICFICAEKIQYYAVSSCNHRTCHICCLRLRALYKTQDCTFCKTEQRHVIFTTDPEKQYQDYKTGEIPYTDKKLNISCETEQMLDDSIFLLKYNCPDPACVITCEAGWPALRRHCKQVHNKLLCTLCTQFKKVFAHEQSLFTKNQLDRHFRQGDQYGKSGFKGHPQCEFCQTSFYGDDELYEHCRDRHQQCEICKKRGIRHEYYVDYDALAEHFRQQHYLCNDPECLAQKVIVFETDIDLKAHEVEIHGSNFAGQRAKHEARRIEVNISYSDSRLRTRRRSIERELPATSSSASLSSSYNNQFQSQLHSIRQLRLESEANRARNLQLSPSREISSTEDVEQTNETQSSTSLSSLRSLGETRVVETKNKNDFPALNQSTAQTAIAKGSAQQAELIQTKTDSTNQANKHSLYLLNNTSNKQQENSAAGTSSSAQLLSPLPQSPSINNEKKTDQITSLKGKNPEQPASSNSINQIMSVSKAPANPPTIDDSKLSRFKSLTSAYKKTLIDAKDFINDIWPLFNKSSEIVGKVVSGLADLLDSESSKKDLLSAWEDRKATLTIHFPTLGSATEGSKQQNIQAKKPESETKKARVLVIKSSTHPPNSPVWDRNLNSAPKPKISHGKHNTSFPTLAAATVVGNSGINSSTNNAWKGNRPQFIRPESSKASASESASSSEQSIGFRRGKPITNGSEDFPSLNKTKSSTSERQAGDSARDSSAEHRFHHTPIIFDPNFNSSLSQYLQSCPQLFGYRLTEVAQQKILARLFSEFWSRDKNYAKLFFPNGFGEGSEAYKLIHTQSDLEVEYSPAQRGKACGHIFKKGEGVYRCRNCSLDATCVFCSRCYHATNHEGHDISFSINNGHGGCCDCGDPEAWKVPIRCTYHSPDPSVVESLESEKKRFEENLPQDLIISIHNTVSTVFEFILDTLSTSPKEKTPPRSVDEVKQEALTTTYAIDKDANEDTEQEKLFAVLLWNDEHHSFHEVIDQVTAAIECSNVEARRITERVDFYGRDIVEISENIQRLLEIARQISSIGLAVTIRSARDTFREEMCGLLIDWLKDLATGQIGTHPTILRDIICKELTKEWKKDHSTYYPHNALRLKNQPVKPIQPYMIKAQPLMGVQDNIEYMIEDDVMERSEEDESGQIDQDQLSDYNQSGGDYEMIAADELLDETEPMDEDDPIMIKQKQKADDFLKVLRLDVLLTLDHRLWKDARSGLRDLYISTLIINSEYKKILGIRFVRNYMKLVDAFLTQDREPEHSIILFTVQLFTVPTIATILVKNYNFLSTIFTILRNFFIANQIDGLGNIESNAKLNCESDSFKNRRYFHIFCDLRYIIGMESVRKIVSRNSDNLQEYLDLIGLFQGMNPNIRATQQHVEYESDSWMNAFNVTLQLAKSCRQFSSCYISDTQLLTEAIRKVLWKIYLWSSRRDIKSENEEEKMDVTSDNAQEIETSVNRIRGHTQQTHDIWSSVLNYPDNRKLELRQQEFHEISFPSNPYIPTFKVVKFNVASQPVSFHHPLHWFLGELLEHIELLNDEALVQHGWDSFQDMMMSFDVENDEGIDKAKEKILEIFDYPLRVLVLLVQIRSGLWVRNGFGIRGQCLHYREVSLRENTYDEDIFLIQTAFILNEPNLILATILDRFDMVDWFCGKTSHQVYDNLQMIFMAEELLTLLIVCASERGIAAGLTNEQKIRREIIHSLCLSPLAYSELIKRIPERLHEEISFDEILGQLATYRNPDSLTDHGTYELRDEFYDEVDPYFVHYSRNNREETEEALKNRLKKKWEASSIRSSASLIIPKLIPITNGPFVRLGNFLQARLMNQIIFYALWHVKNDKIKSDTLIDEALHLVMLALIDENNDIARESKRKGKQKAASSLSSQNRINLDDKISDFMHYAVSDYFPVEIDSAYHPEGINLLTLLLQLSIDSISKEFLPKFEFIINNFETNGSEDAKLIIRAHREKQRAELQAREGKEKGLSDFERKKLAAKERQAKIMEQFAKAQKSFIEKHEDLYEEDEEMDEDWEVAAEEGHLGDKEKQNTETIWSYPTGTCILCQEETNLSALYGMLGLIQPSNMLRITPFHNKDYVMEVLDLPESLDRKYERNQPFGVASKAFSMHEDLQYETRLQNDLIKGFPSKSCKKGLYASTCGHLMHVKCFETYFASIEQRHQSQLARNHPEEATRKEFMCPLCRSLGNALLPIVWKGKRETYPGILESKVDFEKWLNEGVGDVIDDLSRIPEINATPLIPGIDRIRSNPSAAELTSGGRSTDEFREMGNNVNLPDNSQNTQRRRNSSSAGRIREVITQFVTDMWRAPPALPAVSDVNNAQEINNAHMDPSTLSPAAVPEEYDHESMRRIYVRLYDVVLLAYQRLPNESSFIVNDNTMKGIDILWNLYSYTISCVEINQRGIDSLSSEGLPATTLLDGINTKTLTLLKIISETIPTYSDVTLKGASSKSKLKRITTRRLSQLFYGCLESQGQQTPMTTTTGLGGKDKSIVNSHDYPLLLEDSFIFLSELCVTSPDYGIQSEVHNLMHLMYYAELVRIVIAVSDAVINEQAKAWCEDARLKRKYFTQTQQQSSSKNKQEASNLLRDFIVWTLEQVGNNKIDISNFLGGMDELVLEKMIHSFCLPYLRKCVILMHTKFGVVFPKAGLEISEAVDEFTRLSQLLRLPSIKAMCATMLNPTEEESTLVVIVSGWCKHLKQRRIEVNRVKSTPLTSQTISFGKSLRKVCRKCKTVPNDPALCLLCGTFLCFQSYCCSERDSGECNLHARSCGGDVGIYFLVKKWVILLLHLNNGCFMNPPYLDKHGEVDLGLKRGRPQFLNLKRYDEFRNLWLTHEIPIRVARKIEQSFDLGGWSTFDLGGWTTM

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-32Polar residues
Compositional bias711-751Polar residues
Compositional bias758-778Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAJVPS010000211
EMBL· GenBank· DDBJ
CAG8465516.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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