A0A0X9JEX8 · A0A0X9JEX8_PRRSV

Function

function

Cleaves the majority of cleavage sites present in the C-terminus of the polyprotein. Triggers host apoptosis through caspase-3, -8, and -9 activations. Subverts host innate immune responses through its protease activity. Targets the NF-kappa-B essential modulator NEMO and mediates its cleavage. Blocks host interferon beta induction and downstream signaling by cleaving mitochondrial MAVS, dislodging it from the mitochondria. Impairs host defense by cleaving host mRNA-decapping enzyme DCP1A to attenuate its antiviral activity.
Plays a role in the inhibition of the immune response by interacting with host IFITM1. This interaction leads to the proteasomal degradation of the IFN-induced antiviral protein IFITM1.
Plays a role in viral transcription/replication and prevents the simultaneous activation of host cell dsRNA sensors, such as MDA5/IFIH1, OAS, PKR (By similarity) and NLRP3 inflammasome (By similarity).
Acts by degrading the 5'-polyuridines generated during replication of the poly(A) region of viral genomic and subgenomic RNAs. Catalyzes a two-step reaction in which a 2'3'-cyclic phosphate (2'3'-cP) is first generated by 2'-O transesterification, which is then hydrolyzed to a 3'-phosphate (3'-P) (By similarity).
If not degraded, poly(U) RNA would hybridize with poly(A) RNA tails and activate host dsRNA sensors (By similarity).
Also plays a role in the inhibition of host type I interferon production by recruiting host OTULIN to promote removal of linear ubiquitination targeting host NEMO

Catalytic activity

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site1213
Active site1228
Active site1257

GO annotations

AspectTerm
Cellular Componenthost cell membrane
Cellular Componenthost cell perinuclear region of cytoplasm
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular Functionendonuclease activity
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Molecular FunctionRNA nuclease activity
Molecular FunctionRNA-dependent RNA polymerase activity
Molecular Functionzinc ion binding
Biological ProcessDNA-templated transcription
Biological Processviral RNA genome replication
Biological Processviral translational frameshifting

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Replicase polyprotein 1ab
  • Alternative names
    • ORF1ab polyprotein

Gene names

    • Name
      ORF1b

Organism names

Accessions

  • Primary accession
    A0A0X9JEX8

Proteomes

Subcellular Location

Host membrane
; Multi-pass membrane protein
Membrane
; Multi-pass membrane protein

Keywords

Interaction

Subunit

Interacts with host DDX18; this interaction redistributes host DDX18 to the cytoplasm.
Interacts with host DDX5.
Interacts with host IFITM1.
Interacts with host LGALS3.
Interacts with host OTULIN.
Nsp1-alpha papain-like: Interacts with host RNF31.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-150NiRAN
Domain389-523RdRp catalytic
Domain644-707AV ZBD
Domain764-1045+RNA virus helicase C-terminal
Domain1084-1180AV-Nsp11N/CoV-Nsp15M
Domain1182-1304NendoU

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    1,460
  • Mass (Da)
    161,617
  • Last updated
    2016-04-13 v1
  • Checksum
    7E30E085B9545F9C
FKLLAASGLTRCGRGGLVVTETAVKIVKFHNRTFTLGPVNLKVASEVELKDAVEHNQHPVASPLDGGVVLLRSAVPSLVDVLISGADASPKLLARHGPGNTGIDGTLWDFETEATKEEVALSAQIIQACDIRRGDAPNIGLPYKLYPVRGNPERVKGVLKNTRFGDIPYKTPSDTGSPVHAAACLTPNATPVTDGRSILATTMPSGFELYVPTIPASVLDYLDSRPDCPKQLTEHGCEDAALRDLSKYDLSTQGFVLPGVLRLVRKYLFAHVGRCPPVHRPSTYPAKNSMAGINGNRFPTKDIQSVPEIDVLCAQAVRENWQTVTPCTLKKQYCGKKKTRTILGTNNFVALAHRAALSGITQGFMKKAFNSPIALGKNKFKELHTPVLGRCLEADLASCDRSTPAIVRWFAAHLLYELACAEDHLPSYVLNCCHDLLVTQSGAVTKRGGLSSGDPITSVSNTIYSLVIYAQHMVLSYFKSGHPHGLLFLQDQLKFEDMLKVQPLIVYSDDLVLYAESPSMPNYHWWVEHLNLMLGFQTDPRKTAITDSPSFLGCRIINGRQLVPHRDRILAALAYHMKASNVSEYYASAAAILMDSCACLEYDPEWFEELVVGIAQCARKDGYSFPGPPFFLSMWEKLRSNYEGKKSRVCGYCGASAPYATACGLDVCVYHTHFHQHCPVIIWCGHPAGSGSCDECKSPIGKGTSPLDEILRQVPYKPPRTVLMHVEQGLTPLDPGRYQTRRGLVAVRRGIRGNEVDLPDGDYASTALLPTCKEINMVAVASNVLRSRFIIGPPGAGKTYWLLQQVQDGDVIYTPTHQTMLDMIKALGTCRFNIPAGTTLQFPAPSRTGPWVRILAGGWCPGKNSFLDEAAYCNHLDVLRLLSKTTLTCLGDFKQLHPVGFDSHCYVFDVMPQTQLKTIWRFGQNICDAIQPDYRDKLMSMVNTTRVTYVEKPVKYGQVLTPYHRDREDGAITIDSSQGATFDVVTLHLPTENSLNKQRALVAITRARHAIFVYDPHRQLQSLFNLPAKSTPVNLAVHRDGQLIVLDRNNKECTVAQALGNGDKFRATDKRVVDSLRAICADLEGSSSPLPKVAHNLGFYFSPDLTQFAKLPAELAPHWPVVTTQNNEKWPDRLVASLRPVHKYSRACIGAGYMVGPSVFLGTPGVVSYYLTKFIRGEAQMLPETVFSTGRIEVDCREYLDDREREIAESLPHAFIGDVKGTTVGGCHHVTSKYLPRFLPKESVAVVGVSSPGKAAKAVCTLTDVYLPDLEAYLHPETQSRCWKMMLDFKEVRLMVWKDRTAYFQLEGRHFTWYQLASYASYIRVPINSTVYLDPCMGPALCNRRVVGSTHWGADLAVTPYDYGARTILSSAYHGEMPPGYKILACAEFSLDDPVRYKHTWGFESDTAYLYEFTGNGEDWEDYNEAFRARQKGKIYRAIATSLKFHFPPGPVIEPTLGSN

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KT945017
EMBL· GenBank· DDBJ
ALU09384.1
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.
FeedbackHelp