RecName: Full=Phosphoprotein
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Paramyxo_P_V_N super family | cl16424 | Paramyxovirus structural protein V/P N-terminus; This family consists of several ... |
4-312 | 9.08e-143 | |||||
Paramyxovirus structural protein V/P N-terminus; This family consists of several Paramyxoviridae structural protein P and V sequences. From a structural point of view, P is the best-characterized protein of the replicative complex. P is organized into two moieties that are functionally and structurally distinct: a C-terminal moiety (PCT) and an N-terminal moiety (PNT). PCT is the most conserved in sequence and contains all regions required for virus transcription, whereas PNT, which is poorly conserved, provides several additional functions required for replication. P protein plays a crucial role in the enzyme by positioning L onto the N/RNA template through an interaction with the C-terminal domain of N. Without P, L is not functional. The N, P, and L proteins of SeV and measles and mumps viruses are functionally equivalent. However, sequence identity between proteins from these viruses is limited, and the viruses have been placed in different genera (Respirovirus, Morbilivirus, and Rubulavirus, respectively). SeV P protein (568 aa) is a modular protein with distinct functional domains. The N-terminal part of P (PNT) is a chaperone for N and prevents it from binding to non-viral RNA in the infected cell. The actual alignment was detected with superfamily member pfam13825: Pssm-ID: 372740 Cd Length: 309 Bit Score: 412.68 E-value: 9.08e-143
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| MEV_P-protein-C_like super family | cl03936 | C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes ... |
324-501 | 1.79e-29 | |||||
C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes the C-terminal domain of the P protein of plant viruses belonging to the Paramyxoviridae family such as measles virus and mumps virus. The family Paramyxoviridae belongs to the order Mononegavirales which are nonsegmented negative-stranded RNA viruses (NNVs). The genomes of NNVs are encapsidated by their nucleocapsid (N) proteins to form N-RNA complexes which serves as a template for transaction and replication. The C-terminus of P protein binds nucleocapsid. P protein plays multiple roles in transcription and translation, which include acting as a chaperone of nascent nucleoprotein (N), and as a cofactor of the viral polymerase (L) where P forms a two-subunit polymerase with a large catalytic subunit (L) and stabilizes the polymerase on its template of N-RNA. Paramyxoviruses have a polycistronic phosphoprotein (P) gene which encodes for proteins in addition to P protein; for example the measles virus P gene encodes for P protein and virulence factor V (MV-V). This domain family includes the unshared C-terminal domain of P protein not present in MV-V. The actual alignment was detected with superfamily member pfam03210: Pssm-ID: 413868 Cd Length: 154 Bit Score: 113.41 E-value: 1.79e-29
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| Name | Accession | Description | Interval | E-value | |||||
| Paramyxo_P_V_N | pfam13825 | Paramyxovirus structural protein V/P N-terminus; This family consists of several ... |
4-312 | 9.08e-143 | |||||
Paramyxovirus structural protein V/P N-terminus; This family consists of several Paramyxoviridae structural protein P and V sequences. From a structural point of view, P is the best-characterized protein of the replicative complex. P is organized into two moieties that are functionally and structurally distinct: a C-terminal moiety (PCT) and an N-terminal moiety (PNT). PCT is the most conserved in sequence and contains all regions required for virus transcription, whereas PNT, which is poorly conserved, provides several additional functions required for replication. P protein plays a crucial role in the enzyme by positioning L onto the N/RNA template through an interaction with the C-terminal domain of N. Without P, L is not functional. The N, P, and L proteins of SeV and measles and mumps viruses are functionally equivalent. However, sequence identity between proteins from these viruses is limited, and the viruses have been placed in different genera (Respirovirus, Morbilivirus, and Rubulavirus, respectively). SeV P protein (568 aa) is a modular protein with distinct functional domains. The N-terminal part of P (PNT) is a chaperone for N and prevents it from binding to non-viral RNA in the infected cell. Pssm-ID: 372740 Cd Length: 309 Bit Score: 412.68 E-value: 9.08e-143
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| Paramyx_P_V_C | pfam03210 | Paramyxovirus P/V phosphoprotein C-terminal; Paramyxoviridae P genes are able to generate more ... |
324-501 | 1.79e-29 | |||||
Paramyxovirus P/V phosphoprotein C-terminal; Paramyxoviridae P genes are able to generate more than one product, using alternative reading frames and RNA editing. The P gene encodes the structural phosphoprotein P. In addition, it encodes several non-structural proteins present in the infected cell but not in the virus particle. This family includes phosphoprotein P and the non-structural phosphoprotein V from different paramyxoviruses. Phosphoprotein P is essential for the activity of the RNA polymerase complex which it forms with another subunit, L pfam00946. Although all the catalytic activities of the polymerase are associated with the L subunit, its function requires specific interactions with phosphoprotein P. The P and V phosphoproteins are amino co-terminal, but diverge at their C-termini. This difference is generated by an RNA-editing mechanism in which one or two non-templated G residues are inserted into P-gene-derived mRNA. In measles virus and Sendai virus, one G residue is inserted and the edited transcript encodes the V protein. In mumps, simian virus type 5 and Newcastle disease virus, two G residues are inserted, and the edited transcript codes for the P protein. Being phosphoproteins, both P and V are rich in serine and threonine residues over their whole lengths. In addition, the V proteins are rich in cysteine residues at the C-termini. This C-terminal region of the P phosphoprotein is likely to be the nucleocapsid-binding domain, and is found to be intrinsically disordered and thus liable to induced folding. Pssm-ID: 281237 Cd Length: 154 Bit Score: 113.41 E-value: 1.79e-29
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| MEV_P-protein-C_like | cd21031 | C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes ... |
459-504 | 2.20e-07 | |||||
C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes the C-terminal domain of the P protein of plant viruses belonging to the Paramyxoviridae family such as measles virus and mumps virus. The family Paramyxoviridae belongs to the order Mononegavirales which are nonsegmented negative-stranded RNA viruses (NNVs). The genomes of NNVs are encapsidated by their nucleocapsid (N) proteins to form N-RNA complexes which serves as a template for transaction and replication. The C-terminus of P protein binds nucleocapsid. P protein plays multiple roles in transcription and translation, which include acting as a chaperone of nascent nucleoprotein (N), and as a cofactor of the viral polymerase (L) where P forms a two-subunit polymerase with a large catalytic subunit (L) and stabilizes the polymerase on its template of N-RNA. Paramyxoviruses have a polycistronic phosphoprotein (P) gene which encodes for proteins in addition to P protein; for example the measles virus P gene encodes for P protein and virulence factor V (MV-V). This domain family includes the unshared C-terminal domain of P protein not present in MV-V. Pssm-ID: 411026 Cd Length: 46 Bit Score: 47.31 E-value: 2.20e-07
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| Name | Accession | Description | Interval | E-value | |||||
| Paramyxo_P_V_N | pfam13825 | Paramyxovirus structural protein V/P N-terminus; This family consists of several ... |
4-312 | 9.08e-143 | |||||
Paramyxovirus structural protein V/P N-terminus; This family consists of several Paramyxoviridae structural protein P and V sequences. From a structural point of view, P is the best-characterized protein of the replicative complex. P is organized into two moieties that are functionally and structurally distinct: a C-terminal moiety (PCT) and an N-terminal moiety (PNT). PCT is the most conserved in sequence and contains all regions required for virus transcription, whereas PNT, which is poorly conserved, provides several additional functions required for replication. P protein plays a crucial role in the enzyme by positioning L onto the N/RNA template through an interaction with the C-terminal domain of N. Without P, L is not functional. The N, P, and L proteins of SeV and measles and mumps viruses are functionally equivalent. However, sequence identity between proteins from these viruses is limited, and the viruses have been placed in different genera (Respirovirus, Morbilivirus, and Rubulavirus, respectively). SeV P protein (568 aa) is a modular protein with distinct functional domains. The N-terminal part of P (PNT) is a chaperone for N and prevents it from binding to non-viral RNA in the infected cell. Pssm-ID: 372740 Cd Length: 309 Bit Score: 412.68 E-value: 9.08e-143
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| Paramyx_P_V_C | pfam03210 | Paramyxovirus P/V phosphoprotein C-terminal; Paramyxoviridae P genes are able to generate more ... |
324-501 | 1.79e-29 | |||||
Paramyxovirus P/V phosphoprotein C-terminal; Paramyxoviridae P genes are able to generate more than one product, using alternative reading frames and RNA editing. The P gene encodes the structural phosphoprotein P. In addition, it encodes several non-structural proteins present in the infected cell but not in the virus particle. This family includes phosphoprotein P and the non-structural phosphoprotein V from different paramyxoviruses. Phosphoprotein P is essential for the activity of the RNA polymerase complex which it forms with another subunit, L pfam00946. Although all the catalytic activities of the polymerase are associated with the L subunit, its function requires specific interactions with phosphoprotein P. The P and V phosphoproteins are amino co-terminal, but diverge at their C-termini. This difference is generated by an RNA-editing mechanism in which one or two non-templated G residues are inserted into P-gene-derived mRNA. In measles virus and Sendai virus, one G residue is inserted and the edited transcript encodes the V protein. In mumps, simian virus type 5 and Newcastle disease virus, two G residues are inserted, and the edited transcript codes for the P protein. Being phosphoproteins, both P and V are rich in serine and threonine residues over their whole lengths. In addition, the V proteins are rich in cysteine residues at the C-termini. This C-terminal region of the P phosphoprotein is likely to be the nucleocapsid-binding domain, and is found to be intrinsically disordered and thus liable to induced folding. Pssm-ID: 281237 Cd Length: 154 Bit Score: 113.41 E-value: 1.79e-29
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| MEV_P-protein-C_like | cd21031 | C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes ... |
459-504 | 2.20e-07 | |||||
C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes the C-terminal domain of the P protein of plant viruses belonging to the Paramyxoviridae family such as measles virus and mumps virus. The family Paramyxoviridae belongs to the order Mononegavirales which are nonsegmented negative-stranded RNA viruses (NNVs). The genomes of NNVs are encapsidated by their nucleocapsid (N) proteins to form N-RNA complexes which serves as a template for transaction and replication. The C-terminus of P protein binds nucleocapsid. P protein plays multiple roles in transcription and translation, which include acting as a chaperone of nascent nucleoprotein (N), and as a cofactor of the viral polymerase (L) where P forms a two-subunit polymerase with a large catalytic subunit (L) and stabilizes the polymerase on its template of N-RNA. Paramyxoviruses have a polycistronic phosphoprotein (P) gene which encodes for proteins in addition to P protein; for example the measles virus P gene encodes for P protein and virulence factor V (MV-V). This domain family includes the unshared C-terminal domain of P protein not present in MV-V. Pssm-ID: 411026 Cd Length: 46 Bit Score: 47.31 E-value: 2.20e-07
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