H9E9D0 · H9E9D0_HEV

  • Protein
    Non-structural polyprotein pORF1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Methyltransferase: Displays a capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m7GTP or m7GDP. GDP is a better substrate than GTP. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m7GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure.
NTPase/helicase: Multi-functional protein that exhibits NTPase and RNA unwinding activities. Hydrolyzes all NTPs efficiently and unwinds RNA duplexes containing 5' overhangs. Possesses a sequence independent RNA-5'-triphosphatase (RTPase) activity suggestive of its role in forming viral cap structure. Participates also in viral genome replication, RNA translocation and genome packaging/unpackaging.
RNA-directed RNA polymerase: Plays an essential role in the virus replication. Binds to the 3'-end of the genomic RNA to initiate viral replication.
Y-domain: Indispensable for virus replication.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componenthost cell cytoplasm
Molecular FunctionATP binding
Molecular Functioncysteine-type peptidase activity
Molecular Functionhelicase activity
Molecular Functionmetal ion binding
Molecular FunctionmRNA methyltransferase activity
Molecular FunctionRNA binding
Molecular FunctionRNA-dependent RNA polymerase activity
Biological ProcessDNA-templated transcription
Biological ProcessmRNA modification
Biological Processproteolysis
Biological ProcessRNA processing
Biological Processviral protein processing
Biological Processviral RNA genome replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Non-structural polyprotein pORF1
  • EC number

Organism names

Accessions

  • Primary accession
    H9E9D0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

The protease domain interacts with host EIF2AK4 (via C-terminus); this interaction inhibits dimerization of EIF2AK4 and prevents EIF2AK4-mediated phosphorylation of host EIF2A.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain56-240Alphavirus-like MT
Region712-754Disordered
Compositional bias728-742Pro residues
Domain790-936Macro
Domain949-1231+RNA virus helicase C-terminal
Domain1469-1580RdRp catalytic

Sequence similarities

Belongs to the hepevirus non-structural polyprotein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,708
  • Mass (Da)
    187,196
  • Last updated
    2012-05-16 v1
  • Checksum
    720E069E8316A699
MEAHQFIKAPGITTAIEQAALAAANSALANAVVVRPFLSRLQTEILINLMQPRQLVFRPEVLWNHPIQRVIHNELEQYCRARAGRCLEVGAHPRSINDNPNVLHRCFLRPVGRDVQRWYSAPTRGPAANCRRSALRGLPPVDRTYCFDGFSRCAFAAETGVALYSLHDLWPADVAEAMARHGMTRLYAALHLPPEVLLPPGTYHTTSYLLIHDGDRAVVAYEGDTSAGYNHDVSILRAWIRTTKIVGDHPLVIERVRAIGCHFVLLLTAAPEPSPMPYVPYPRSTEVYVRSIFGPGGSPSLFPSACSTKSTFHAVPVHIWDRLMLFGATLDDQAFCCSRLMTYLRGISYKVTVGALVANEGWNASEDALTAVITAAYLTICHQRYLRTQAISKGMRRLEVEHAQKFITRLYSWLFEKSGRDYIPGRQLQFYAQCRRWLSAGFHLDPRVLVFDESVPCRCRTFLKKVAGKFCCFMRWLGQECTCFLEPAEGLVGDHGHDNEAYEGSEVDQAEPAHLDVSGTYAVHGHQLVALYRALNVPHDIAARASRLTATVELVAGPDRLECRTVLGNKTFRTTVVDGAHLEANGPEQYVLSFDASRQSMGAGSHNLTYELTPAGLQVRISSNGLDCTATFPPGGAPSAAPGEVAAFCGALYRYNRFTQRHSLTGGLWLHPEGLLGIFPPFSPGHIWESANPFCGEGTLYTRTWSTSGFSSDFSPPEAAAPASAAAPGLPHPTPPVGDIWALPPPSEESQVDAASVPLTLVPAGSPNPIVLPPPPLPSPVRKPFKPPSARTRRLLYTYPDGAKVYAGSLFESDCDWLVNASNLGHRPGGGLCHAFHQRFPEAFYSTEFIMREGLAAYTLTPRPIIHAVAPDYRVEQNPKRLEAAYRETCSRRGTAAYPLLGSGIYRVPVSLSFDAWERNHRPGDELYLTEPAAAWFEANKPAQPALTITEDTARTASLALEIDAATEVGRACAGCTISPGIVHYQFTAGVPGSGKSRSIQQGDVDVVVVPTRELRNSWRRRGFAAFTPHTAARVTNGRRVVIDEAPSLPPHLLLLHMQRASSVHLLGDPNQIPAIDFEHAGLVPAIRPELAPTSWWHVTHRCPADVCELIRGAYPKIQTTSRVLRSLFWNEPAIGQKLVFTQAAKAANPGAITVHEAQGATFTETTVIATADARGLIQSSRAHAIVALTRHTEKCVILDAPGLLREVGISDVIVNNFFLAGGEVGHHRPSVIPRGNPDQNLGTLQAFPPSCQISAYHQLAEELGHRPAPVAAVLPPCPELEQGLLYMPQELTVSDSVLVFELTDIVHCRMAAPSQRKAVLSTLVGRYGRRTKLYEAAHSDVRESLARFIPTIGPVQATTCELYELVEAMVEKGQDGSAVLELDLCNRDVSRITFFQKDCNKFTTGETIAHGKVGQGISAWSKTFCALFGPWFRAIEKEILALLPPNVFYGDAYEESVLAAAVSGAGSCMVFENDFSEFDSTQNNFSLGLECVVMEECGMPQWLIRLYHLVRSAWILQAPKESLKGFWKKHSGEPGTLLWNTVWNMAIIAHCYEFRDFRVAAFKGDDSVVLCSDYRQSRNAAALIAGCGLKLKVDYRPIGLYAGVVVAPGLGTLPDVVRFAGRLSEKNWGPGPERAEQLRLAVCDFLRGLTNVAQVCVDVVSRVYGVSPGLVHNLIGMLQTIADGKAHFTETIKPVLDLTNSIIQRVE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias728-742Pro residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JQ679014
EMBL· GenBank· DDBJ
AFD33686.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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