Papain-like auto-proteinase; The replicase polyproteins of the Nidoviruses such as, porcine ...
1-249
0e+00
Papain-like auto-proteinase; The replicase polyproteins of the Nidoviruses such as, porcine arterivirus PRRSV, equine arterivirus EAV, human coronavirus 229E, and severe acute respiratory syndrome coronavirus (SARS-CoV), are predicted to be cleaved into 14 non-structural proteins (nsps) by the nsp4 main proteinase pfam05579 and three accessory proteinases residing in nsp1-alpha, nsp1-beta and nsp2. This family is the two nsp1 proteins that together act in a papain-like way to separate off the rest of the various functional domains of the polyprotein. Once inside the host cell, this nsp1 interferes with the regulation of interferon, thereby enabling the virus to replicate.
The actual alignment was detected with superfamily member pfam14754:
Pssm-ID: 291424 Cd Length: 249 Bit Score: 542.72 E-value: 0e+00
Nsp2, transmembrane domain; This domain is found in Nsp2 protein of the RNA-arteriviruses, ...
361-508
1.57e-84
Nsp2, transmembrane domain; This domain is found in Nsp2 protein of the RNA-arteriviruses, such as porcine arterivirus PRRSV and equine arterivirus EAV, which is a tetraspanning transmembrane protein. This domain resides adjacent to the peptidase C33 catalytic domain of Nsp2.
:
Pssm-ID: 373271 [Multi-domain] Cd Length: 148 Bit Score: 273.01 E-value: 1.57e-84
intracellular membrane remodeller motif of arterivirus non-structural protein 3 (Nsp3); This ...
846-902
7.78e-22
intracellular membrane remodeller motif of arterivirus non-structural protein 3 (Nsp3); This domain is present in subunit Nsp3 of RNA-arteriviruses, such as porcine arterivirus PRRSV and equine arterivirus EAV. Nsp3 proteins are localized to the ER and appear to be essential for formation of double-membrane vesicles that originate from the ER during the life-cycle of the virus. Arterivirus Nsp3 is a predicted tetra-spanning transmembrane protein containing four transmembrane helices, with the N- and C-termini of the protein residing in the cytoplasm. It contains a cluster of four highly conserved cysteine residues that are predicted to reside in the first luminal domain of the protein. These conserved cysteines play a key role in the formation of double-membrane vesicles (DMVs); mutagenesis of each completely blocked DMV formation.
:
Pssm-ID: 412095 Cd Length: 57 Bit Score: 90.07 E-value: 7.78e-22
Equine arterivirus Nsp2-type cysteine proteinase; Corresponds to Merops family C33. These ...
261-357
8.62e-15
Equine arterivirus Nsp2-type cysteine proteinase; Corresponds to Merops family C33. These peptidases are involved in viral polyprotein processing in replication.
The actual alignment was detected with superfamily member pfam05412:
Pssm-ID: 114153 Cd Length: 108 Bit Score: 71.87 E-value: 8.62e-15
Papain-like auto-proteinase; The replicase polyproteins of the Nidoviruses such as, porcine ...
1-249
0e+00
Papain-like auto-proteinase; The replicase polyproteins of the Nidoviruses such as, porcine arterivirus PRRSV, equine arterivirus EAV, human coronavirus 229E, and severe acute respiratory syndrome coronavirus (SARS-CoV), are predicted to be cleaved into 14 non-structural proteins (nsps) by the nsp4 main proteinase pfam05579 and three accessory proteinases residing in nsp1-alpha, nsp1-beta and nsp2. This family is the two nsp1 proteins that together act in a papain-like way to separate off the rest of the various functional domains of the polyprotein. Once inside the host cell, this nsp1 interferes with the regulation of interferon, thereby enabling the virus to replicate.
Pssm-ID: 291424 Cd Length: 249 Bit Score: 542.72 E-value: 0e+00
Nsp2, transmembrane domain; This domain is found in Nsp2 protein of the RNA-arteriviruses, ...
361-508
1.57e-84
Nsp2, transmembrane domain; This domain is found in Nsp2 protein of the RNA-arteriviruses, such as porcine arterivirus PRRSV and equine arterivirus EAV, which is a tetraspanning transmembrane protein. This domain resides adjacent to the peptidase C33 catalytic domain of Nsp2.
Pssm-ID: 373271 [Multi-domain] Cd Length: 148 Bit Score: 273.01 E-value: 1.57e-84
intracellular membrane remodeller motif of arterivirus non-structural protein 3 (Nsp3); This ...
846-902
7.78e-22
intracellular membrane remodeller motif of arterivirus non-structural protein 3 (Nsp3); This domain is present in subunit Nsp3 of RNA-arteriviruses, such as porcine arterivirus PRRSV and equine arterivirus EAV. Nsp3 proteins are localized to the ER and appear to be essential for formation of double-membrane vesicles that originate from the ER during the life-cycle of the virus. Arterivirus Nsp3 is a predicted tetra-spanning transmembrane protein containing four transmembrane helices, with the N- and C-termini of the protein residing in the cytoplasm. It contains a cluster of four highly conserved cysteine residues that are predicted to reside in the first luminal domain of the protein. These conserved cysteines play a key role in the formation of double-membrane vesicles (DMVs); mutagenesis of each completely blocked DMV formation.
Pssm-ID: 412095 Cd Length: 57 Bit Score: 90.07 E-value: 7.78e-22
Equine arterivirus Nsp2-type cysteine proteinase; Corresponds to Merops family C33. These ...
261-357
8.62e-15
Equine arterivirus Nsp2-type cysteine proteinase; Corresponds to Merops family C33. These peptidases are involved in viral polyprotein processing in replication.
Pssm-ID: 114153 Cd Length: 108 Bit Score: 71.87 E-value: 8.62e-15
Papain-like auto-proteinase; The replicase polyproteins of the Nidoviruses such as, porcine ...
1-249
0e+00
Papain-like auto-proteinase; The replicase polyproteins of the Nidoviruses such as, porcine arterivirus PRRSV, equine arterivirus EAV, human coronavirus 229E, and severe acute respiratory syndrome coronavirus (SARS-CoV), are predicted to be cleaved into 14 non-structural proteins (nsps) by the nsp4 main proteinase pfam05579 and three accessory proteinases residing in nsp1-alpha, nsp1-beta and nsp2. This family is the two nsp1 proteins that together act in a papain-like way to separate off the rest of the various functional domains of the polyprotein. Once inside the host cell, this nsp1 interferes with the regulation of interferon, thereby enabling the virus to replicate.
Pssm-ID: 291424 Cd Length: 249 Bit Score: 542.72 E-value: 0e+00
Nsp2, transmembrane domain; This domain is found in Nsp2 protein of the RNA-arteriviruses, ...
361-508
1.57e-84
Nsp2, transmembrane domain; This domain is found in Nsp2 protein of the RNA-arteriviruses, such as porcine arterivirus PRRSV and equine arterivirus EAV, which is a tetraspanning transmembrane protein. This domain resides adjacent to the peptidase C33 catalytic domain of Nsp2.
Pssm-ID: 373271 [Multi-domain] Cd Length: 148 Bit Score: 273.01 E-value: 1.57e-84
intracellular membrane remodeller motif of arterivirus non-structural protein 3 (Nsp3); This ...
846-902
7.78e-22
intracellular membrane remodeller motif of arterivirus non-structural protein 3 (Nsp3); This domain is present in subunit Nsp3 of RNA-arteriviruses, such as porcine arterivirus PRRSV and equine arterivirus EAV. Nsp3 proteins are localized to the ER and appear to be essential for formation of double-membrane vesicles that originate from the ER during the life-cycle of the virus. Arterivirus Nsp3 is a predicted tetra-spanning transmembrane protein containing four transmembrane helices, with the N- and C-termini of the protein residing in the cytoplasm. It contains a cluster of four highly conserved cysteine residues that are predicted to reside in the first luminal domain of the protein. These conserved cysteines play a key role in the formation of double-membrane vesicles (DMVs); mutagenesis of each completely blocked DMV formation.
Pssm-ID: 412095 Cd Length: 57 Bit Score: 90.07 E-value: 7.78e-22
Equine arterivirus Nsp2-type cysteine proteinase; Corresponds to Merops family C33. These ...
261-357
8.62e-15
Equine arterivirus Nsp2-type cysteine proteinase; Corresponds to Merops family C33. These peptidases are involved in viral polyprotein processing in replication.
Pssm-ID: 114153 Cd Length: 108 Bit Score: 71.87 E-value: 8.62e-15
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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