A0A240FW11 · A0A240FW11_9ALPC

Function

function

Forms a primer, NSP9-pU, which is utilized by the polymerase for the initiation of RNA chains. Interacts with ribosome signal recognition particle RNA (SRP). Together with NSP8, suppress protein integration into the cell membrane, thereby disrupting host immune defenses.
RNA-directed RNA polymerase that catalyzes the transcription of viral genomic and subgenomic RNAs. Acts in complex with nsp7 and nsp8 to transcribe both the minus and positive strands of genomic RNA. The kinase-like NiRAN domain of NSP12 attaches one or more nucleotides to the amino terminus of NSP9, forming a covalent RNA-protein intermediate that serves as transcription/replication primer. Subgenomic RNAs (sgRNAs) are formed by discontinuous transcription: The polymerase has the ability to pause at transcription-regulating sequences (TRS) and jump to the leader TRS, resulting in a major deletion. This creates a series of subgenomic RNAs that are replicated, transcribed and translated. In addition, Nsp12 is a subunit of the viral RNA capping enzyme that catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. Subsequently, the NiRAN domain transfers RNA to GDP, and forms the core cap structure GpppA-RNA.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site5261
Active site5263
Active site5362
Active site5438
Active site5443
Binding site5501-5507S-adenosyl-L-methionine (UniProtKB | ChEBI)
Active site5916
Active site5931
Active site5972

GO annotations

AspectTerm
Cellular Componenthost cell endoplasmic reticulum-Golgi intermediate compartment
Cellular Componenthost cell membrane
Cellular Componenthost cell perinuclear region of cytoplasm
Cellular Componentmembrane
Molecular Function3'-5'-RNA exonuclease activity
Molecular Function5'-3' DNA helicase activity
Molecular FunctionATP binding
Molecular Functioncysteine-type deubiquitinase activity
Molecular Functioncysteine-type endopeptidase activity
Molecular Functionendonuclease activity
Molecular Functionlyase activity
Molecular FunctionmRNA (nucleoside-2'-O-)-methyltransferase activity
Molecular FunctionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
Molecular Functionomega peptidase activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionzinc ion binding
Biological ProcessDNA-templated transcription
Biological Processinduction by virus of host autophagy
Biological Processproteolysis
Biological Processsymbiont-mediated perturbation of host ubiquitin-like protein modification
Biological Processsymbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity
Biological Processviral genome replication
Biological Processviral protein processing
Biological Processviral translational frameshifting
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    ORF1ab polyprotein

Organism names

  • Taxonomic identifier
  • Strain
    • Xingguo-74
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae > Orthocoronavirinae > Alphacoronavirus > Sunacovirus > Suncus murinus coronavirus X74

Accessions

  • Primary accession
    A0A240FW11

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane1543-1561Helical
Transmembrane1608-1629Helical
Transmembrane1688-1711Helical
Transmembrane2091-2114Helical
Transmembrane2346-2373Helical
Transmembrane2385-2415Helical
Transmembrane2427-2458Helical
Transmembrane2875-2896Helical
Transmembrane2902-2921Helical
Transmembrane2928-2950Helical
Transmembrane2962-2982Helical
Transmembrane2994-3019Helical
Transmembrane3050-3072Helical

Keywords

PTM/Processing

Features

Showing features for disulfide bond.

TypeIDPosition(s)Description
Disulfide bond1648↔1654

Keywords

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain112-196CoV Nsp2 N-terminal
Domain554-669Ubiquitin-like
Domain947-1116Macro
Domain1282-1538Peptidase C16
Domain1614-16793Ecto
Region1748-1838Y1
Domain1748-2086CoV Nsp3 Y
Region1752-1765ZF1
Region1798-1808ZF2
Region1839-2086CoV-Y
Region1985-2086Y4
Domain2470-2565Nsp4C
Domain2566-2865Peptidase C30
Domain3132-3213RdRp Nsp7 cofactor
Domain3214-3406RdRp Nsp8 cofactor
Domain3407-3515Nsp9 ssRNA-binding
Domain3516-3655ExoN/MTase coactivator
Domain3658-3908NiRAN
Domain3914-4012Nsp12 Interface
Domain4013-4579Nsp12 RNA-dependent RNA polymerase
Domain4580-4663CV ZBD
Domain4827-5187+RNA virus helicase C-terminal
Domain5243-5457ExoN
Domain5466-5687N7-MTase
Region5578-5592GpppA-binding
Domain5691-5751Nsp15 N-terminal oligomerization
Domain5752-5869AV-Nsp11N/CoV-Nsp15M
Domain5886-6026NendoU
Domain6029-6324Nidovirus-type SAM-dependent 2'-O-MTase

Sequence similarities

Belongs to the coronaviruses polyprotein 1ab family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    6,324
  • Mass (Da)
    715,867
  • Last updated
    2017-10-25 v1
  • Checksum
    3DCCAF27F03EE762

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KY967715
EMBL· GenBank· DDBJ
ASF90443.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help