A0A0K0MBN4 · A0A0K0MBN4_9CALI

Function

function

3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. May cleave polyadenylate-binding protein thereby inhibiting cellular translation.

Catalytic activity

Features

Showing features for active site.

116992004006008001,0001,2001,4001,600
TypeIDPosition(s)Description
Active site1038For 3CLpro activity
Active site1062For 3CLpro activity
Active site1147For 3CLpro activity

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functioncysteine-type endopeptidase activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Molecular FunctionRNA-dependent RNA polymerase activity
Biological ProcessDNA-templated transcription
Biological Processproteolysis
Biological ProcessRNA-protein covalent cross-linking
Biological Processviral RNA genome replication

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Genome polyprotein

Organism names

Accessions

  • Primary accession
    A0A0K0MBN4

Proteomes

Subcellular Location

Host cell

PTM/Processing

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro is first autocatalytically cleaved, then processes the whole polyprotein.

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-78Disordered
Compositional bias10-31Polar residues
Compositional bias53-76Pro residues
Region95-118Disordered
Compositional bias97-113Polar residues
Domain465-632SF3 helicase
Region843-862Disordered
Compositional bias847-862Basic and acidic residues
Region874-895Disordered
Domain1009-1189Peptidase C37
Domain1425-1546RdRp catalytic

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,699
  • Mass (Da)
    188,801
  • Last updated
    2015-11-11 v1
  • Checksum
    0ED02054D76A624B
MKMASTDASAAAVAISNNDTAKSSSDGVLSSMAVTFKRALGARPKQPPPREKPQRPPRPPTPELVKNIPPPPPNGEDEIVVSYSVKDGVSGLPDLSTVRQPEESNTAFSVPPLNQRENRDAKEPLTGTILEMWDGEIYHYGLYVERGLVLGVHKPPAAISLARVELAPLSLYWRPVYTPQYLISPDTLRKLSGETFPYTAFDNNCYAFCCWVLDLNDSWLSRRMIQRTTGFFRPYQDWNRKPLPTMDDSKIKKVANIFLCALSSLFTRPIKDIIGKIRPLNILNILASCDWTFAGVVESLILLAELFGVFWTPPDVSAMIAPLLGDYELQGSEDLAVELVPVVMGGIGLVLGFTKEKIGKMLSSAASTLRACKDLGAYGLEILKLVMKWFFPKKEEANELAIVRSIEDAVLDLEAIENNHMTTLLKDKDSLATYMRTLDLEEEKARKLSTKSASPDIVGTINALLARIAAARSLVHRAKEELSSRPRPVVLMISGRPGIGKTHLAREVAKRIAASLTGDQRVGLIPRNGVDHWDAYKGERVVLWDDYGMSNPIHDALRLQELADTCPLTLNCDRIENKGKVFDSDVIIITTNLANPAPLDYVNFEACSRRIDFLVYAEAPEVEKAKRDFPGQPDMWKNAFSSDFSHIKLALAPQGGFDKNGNTPHGKGVMKTLTTGSLIARASGLLHERLDEFELQGPALTTFNFDRNKVLAFRQLAAENKYGLMDTMRVGKQLKDVRTMPELKQALKNVSIKKCQIVYSGCTYILESDGKGNVKVDRIQSAAVQTNNELAGALHHLRCARIRYYVKCVQEALYSIIQIAGAAFVTTRIAKRMNIQDLWSKPQVENTEETTSKDGCPKPKDDEEFVISSDDIKAEGKKGKNKTGRGKKHTAFSSKGLSDEEYDEYKRIREERNGKYSIEEYLQDRDKYYEEVAIARATEEDFCEEEEAKIRQRIFRPTRKQRKEERASLGLVTGSEIRKRNPDDFKPKGKLWADDDRSVDYNEKLSFEAPPSIWSRIVNFGSGWGFWVSPSLFITSTHVIPQGAKEFFGVPIKQIQVHKSGEFCRLRFPKPIRTDVTGMILEEGAPEGTVVTLLIKRSTGELMPLAARMGTHATMKIQGRTVGGQMGMLLTGSNAKSMDLGTTPGDCGCPYIYKRGNDYVVIGVHTAAARGGNTVICATQGSEGEATLEGGDNKGTYCGAPILGPGSAPTLSTKTKFWRSSTASLPPGTYEPAYLGGKDPRVKGGPSLQQVMREQLKPFTEPRGKPPKPSVLEAAKKTIINVLEQTIDPPEKWSFAQACASLDKTTSSGHPHHMRKNDCWNGESFTGKLADQASKANLMFEEGKNMTPVYTAALKDELVKTDKIYGKIKKRLLWGSDLATMIRCARAFGGLMDELKAHCVTLPIRVGMNMNEDGPIIFERHSRYTYHYDADYSRWDSTQQRAVLAAALEIMVKFSPEPHLAQVVAEDLLSPSVVDVGDFTISINEGLPSGVPCTSQWNSIAHWLLTLCALSEVTNLSPDTIQANSLFSFYGDDEIVSTDIKLDPEKLTAKLREYGLRPTRPDKTEGPLVISEDLNGLTFLRRTVTRDPAGWFGKLEQSSILRQMYWTRGPNHGDPSETMIPHSQRPIQLMSLLGEAALHGPAFYSKISKLVIAELKEGGMDFYVPRQEPMFRWMRFSDLSTWEGDRNLAPSFVNEDGVE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias10-31Polar residues
Compositional bias53-76Pro residues
Compositional bias97-113Polar residues
Compositional bias847-862Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KM258131
EMBL· GenBank· DDBJ
AJZ77035.1
EMBL· GenBank· DDBJ
Genomic RNA

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