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Late protein which is part of a large complex required for early virion morphogenesis. This complex participates in the formation of virosomes and the incorporation of virosomal contents into nascent immature virions.
Lipid-bound viral membrane assembly protein that plays an essential role in immature virion (IV) to mature virion (MV) transition. Functions in both crescent-shaped viral membranes formation and its enclosure to form immature virions. In addition, participates in targeting mature virion proteins to sites of virion assembly to ensure their correct localization.
Major component of the virion core that undergoes proteolytic processing during the immature virion (IV) to mature virion (MV) transition. Essential for the formation of a structurally normal core.
Core protein 4a is the most abundant virion protein. Major component of the virion core that undergoes proteolytic processing during the immature virion (IV) to mature virion (MV) transition.
Late protein which is part of a large complex required for early virion morphogenesis. This complex participates in the formation of virosomes and the incorporation of virosomal contents into nascent immature virions.
Required for viral crescent formation early during virus morphogenesis.
Plays an essential role in viral replication as a component of the DNA polymerase processivity factor. Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Serine/tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the OPG144 protein.
DNA-binding protein which binds to the hairpin form of the viral telomeric sequence. Required for the production of mature virions (MV).
Binds to the hairpin form of the viral telomeric sequence. Might direct genome encapsidation into the virus particle.
Nuclease that is responsible for viral evasion of host cGAS-STING innate immunity (PubMed:30728498).
Cleaves 2',3'-cGAMP which is produced by host cGAS following recognition of intracellular foreign DNA and blocks the subsequent 2',3'-cGAMP-mediated activation of TMEM173/STING which normally spreads to adjacent cells and activates the interferon and NF-kappa-B immune responses (PubMed:30728498)
Late protein which probably participates in disulfide bond formation by functioning as a thiol-disulfide transfer protein between membrane-associated OPG072 and OPG08. The complete pathway for formation of disulfide bonds in intracellular virion membrane proteins sequentially involves oxidation of OPG072, OPG128 and OPG08 .
Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.
NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for replication and propagation of viral particles.
Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.automatic annotation
Ribonucleoside-diphosphate reductase holoenzyme provides the precursors necessary for viral DNA synthesis. Allows virus growth in non-dividing cells. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Plays a role in the inhibition of host protein synthesis. Specifically, inhibits the initiation of cap-dependent and cap-independent translation. In turn, affects the outcome of infection by decreasing recruitment of inflammatory leukocytes and reducing the memory CD8+ T-cell response.
Probably involved in maturation of some viral proteins by processing them preferentially at Ala-Gly-|-Ser/Thr/Lys motifs. Does not seem to be responsible for the cleavage of major core proteins.
Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
Acts with RNA polymerase to initiate transcription from late gene promoters.
Associates with RNA polymerase to initiate transcription from late gene promoters.
Involved in postreplicative transcription elongation on intermediate and late genes.
Might be required to be present in the virion for transcription of early genes after primo infection.
Acts with RNA polymerase to initiate transcription from intermediate gene promoters.
Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
Plays an essential role for maintaining proper localization of the seven-protein complex and the viroplasm during assembly.
Required for the association between the dense viroplasm and the viral membranes to form the mature virion (MV).
Envelope protein which is a major component of the mature virion (MV) membrane. Essential for membrane biogenesis. Is required, together with OPG144, to form bona fide crescents, which can progress to form the immature virion (IV) membrane. OPG140 and OPG144 form a lattice that is stabilized by disulfide bonds and serves as an anchor within the viral membrane to which several other proteins important in virion structure and morphogenesis attach.
Essential for the encapsidation of DNA into immature virions (IV) and the subsequent maturation of IV into mature virions (MV).
Envelope protein. Required for an early step in virion morphogenesis.
Catalyzes the oxidative conversion of Delta5-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. During viral infection, steroid production contributes to virulence by inhibiting the host inflammatory response.
Plays a role in DNA replication by cleaving viral DNA concatamers to yield unit-length viral genomes. The concatamer junctions contain inverted repeat sequences that can be extruded as cruciforms, yielding Holliday junctions that A22 protein cleaves.
Glutaredoxin necessary for virion morphogenesis and virus replication. Functions as a thiol-disulfide transfer protein between membrane-associated OPG128 and substrates OPG095 or OPG053. The complete pathway for formation of disulfide bonds in intracellular virion membrane proteins sequentially involves oxidation of OPG072, OPG128 and OPG088. Exhibit thioltransferase and dehydroascorbate reductase activities in vitro.
Putative nuclease that seems to be required for double-strand break repair, homologous recombination, and production of full-length viral genomic DNA.
Envelope protein required for virus entry into host cell and for cell-cell fusion (syncytium formation).
Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation.
Envelope protein part of the entry-fusion complex responsible for the virus membrane fusion with host cell membrane during virus entry. Also plays a role in cell-cell fusion (syncytium formation).
Acts with RNA polymerase to initiate transcription from early gene promoters. Is recruited by the RPO-associated protein of 94 kDa RAP94/OPG109 to form the early transcription complex, which also contains the core RNA polymerase. ETF heterodimer binds to early gene promoters.
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
DNA helicase which seems to act as a postreplicative transcription termination factor. Involved in ATP-dependent release of nascent RNA. Forms a stable complex with single-stranded DNA, and to a lesser extent RNA.
Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.
Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.
Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.
Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG134, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase.
Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of D6 and A7, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase (By similarity).
Plays an essential role in viral DNA replication. Binds to ssDNA with high affinity and localizes to cytoplasmic factories where nascent viral genomes accumulate. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation.
Plays an essential role in virion assembly and morphogenesis. Also plays a role in the inhibition of host immune response by dysregulating mTOR. Sequesters host RICTOR and RPTOR, thereby disrupting mTORC1 and mTORC2 crosstalk. In turn, blocks the host antiviral response in part through mTOR-dependent degradation of cGAS, the primary poxvirus sensor.
Late protein which is a part of a large complex required for early virion morphogenesis. This complex participates in the formation of virosomes and the incorporation of virosomal contents into nascent immature virions. Required for the stability and kinase activity of OPG054.
Binds to chondroitin sulfate on the cell surface to provide virion attachment to target cell.
Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase OPG063 that creates mRNA's poly(A) tail. In the presence of OPG102, OPG063 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.
Assembly protein G7
Late protein which is a part of a large complex required for early virion morphogenesis. This complex participates in the formation of virosomes
MPXV ankyrin-like proteins are known to inhibit host antiviral signaling and inflammatory responses by disrupting activation of NF-κB22
plays a significant role in the virus's ability to evade the host's immune response.
plays a significant role in the virus's ability to evade the host's immune response.
plays a significant role in the virus's ability to evade the host's immune response.
plays a significant role in the virus's ability to evade the host's immune response.
MPXV ankyrin-like proteins are known to inhibit host antiviral signaling and inflammatory responses by disrupting activation of NF-κB22
Plays a role in the inhibition of host immune repsonse by counteracting the action of interferons on early events in the viral replication cycle.
inhibit host antiviral signaling and inflammatory responses by disrupting activation of NF-κB22
Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin
ankyrin-like; ANK-containing protein; apoptosis inhibitor; start of ORF is missing approx. 31 AA compared to CPXVs; similar to VACV-WR O1L and VACV-Cop M1L
Component of the virion core that undergoes proteolytic processing during the immature virion (IV) to mature virion (MV) transition. Essential for the formation of a structurally normal core
immunodominant virion core protein needed for the progression of IV to infectious IMV