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Conserved domains on  [gi|1464310832|ref|YP_009508518|]
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P [Antarctic penguin virus C]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MEV_P-protein-C_like super family cl03936
C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes ...
 222-375 4.79e-36

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: 128.82  E-value: 4.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464310832 222 RMEQAVDSIHKGIAVIPNIRNDVQLIKTTVATMEGTLSMIKLMDPGNATISSLNDLRKSAVSTPVVISGPGDPAPYLHES 301
Cdd:pfam03210   1 KIHEDVDKVISQLSSIPLIKNEIESIKTSLATIEGHLSSMKIMDPGNPDLKPVIGLRRSGRAHAELVSGPGDTSGRTSSG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1464310832 302 QYMGLDKLARPVDDLRKLTTKSEPQGKDFVTEKETIASMIRAKPLQDATSKRLLSRLDQCTTMEELKKLKRGVL 375
Cdd:pfam03210  81 GQLLLDFLLKPVPHPSEKVSPAVQFVPDTGASRDVIRSMIKSSRLEPDRKRYLMTLLDDAKTAEELAKIKRMLM 154
Soyouz_module super family cl16791
N-terminal region of Paramyxovirinae phosphoprotein (P); The soyouz module moiety is the ...
 1-53 3.69e-09

N-terminal region of Paramyxovirinae phosphoprotein (P); The soyouz module moiety is the N-terminal region of the phosphoprotein (P) from the subfamily Paramyxovirinae of the family Paramyxoviridae viruses. The main genera in this subfamily include the Rubulaviruses, avulaviruses, respiroviruses, henipaviruses, and morbilliviruses, all of which are enveloped viruses with a non-segmented, negative, single-stranded RNA genome encapsidated by the nucleoprotein (N) within a helical nucleocapsid.


The actual alignment was detected with superfamily member pfam14313:

Pssm-ID: 316803  Cd Length: 58  Bit Score: 52.34  E-value: 3.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1464310832   1 MASFTDEEINELFDASDIIIDSIITPTPNVPSTVGKSAIPKGNTRVKTDAWEA 53
Cdd:pfam14313   1 MDSFSDAEIAELLELGLNVIESIQSAQGKPQKTLGKSAIPPGNTKALTKAWEK 53
 
Name Accession Description Interval E-value
Paramyx_P_V_C pfam03210
Paramyxovirus P/V phosphoprotein C-terminal; Paramyxoviridae P genes are able to generate more ...
 222-375 4.79e-36

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: 128.82  E-value: 4.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464310832 222 RMEQAVDSIHKGIAVIPNIRNDVQLIKTTVATMEGTLSMIKLMDPGNATISSLNDLRKSAVSTPVVISGPGDPAPYLHES 301
Cdd:pfam03210   1 KIHEDVDKVISQLSSIPLIKNEIESIKTSLATIEGHLSSMKIMDPGNPDLKPVIGLRRSGRAHAELVSGPGDTSGRTSSG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1464310832 302 QYMGLDKLARPVDDLRKLTTKSEPQGKDFVTEKETIASMIRAKPLQDATSKRLLSRLDQCTTMEELKKLKRGVL 375
Cdd:pfam03210  81 GQLLLDFLLKPVPHPSEKVSPAVQFVPDTGASRDVIRSMIKSSRLEPDRKRYLMTLLDDAKTAEELAKIKRMLM 154
Soyouz_module pfam14313
N-terminal region of Paramyxovirinae phosphoprotein (P); The soyouz module moiety is the ...
 1-53 3.69e-09

N-terminal region of Paramyxovirinae phosphoprotein (P); The soyouz module moiety is the N-terminal region of the phosphoprotein (P) from the subfamily Paramyxovirinae of the family Paramyxoviridae viruses. The main genera in this subfamily include the Rubulaviruses, avulaviruses, respiroviruses, henipaviruses, and morbilliviruses, all of which are enveloped viruses with a non-segmented, negative, single-stranded RNA genome encapsidated by the nucleoprotein (N) within a helical nucleocapsid.


Pssm-ID: 316803  Cd Length: 58  Bit Score: 52.34  E-value: 3.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1464310832   1 MASFTDEEINELFDASDIIIDSIITPTPNVPSTVGKSAIPKGNTRVKTDAWEA 53
Cdd:pfam14313   1 MDSFSDAEIAELLELGLNVIESIQSAQGKPQKTLGKSAIPPGNTKALTKAWEK 53
MEV_P-protein-C_like cd21031
C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes ...
 333-376 3.67e-04

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: 37.68  E-value: 3.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1464310832 333 EKETIASMIRAKPLQDATSKRLLSRLDQCTTMEELKKLKRGVLN 376
Cdd:cd21031     2 SRDVIRSMIRSSPLDREEKQALISLLDKAKTDEELNEIKQLVEE 45
 
Name Accession Description Interval E-value
Paramyx_P_V_C pfam03210
Paramyxovirus P/V phosphoprotein C-terminal; Paramyxoviridae P genes are able to generate more ...
 222-375 4.79e-36

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: 128.82  E-value: 4.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464310832 222 RMEQAVDSIHKGIAVIPNIRNDVQLIKTTVATMEGTLSMIKLMDPGNATISSLNDLRKSAVSTPVVISGPGDPAPYLHES 301
Cdd:pfam03210   1 KIHEDVDKVISQLSSIPLIKNEIESIKTSLATIEGHLSSMKIMDPGNPDLKPVIGLRRSGRAHAELVSGPGDTSGRTSSG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1464310832 302 QYMGLDKLARPVDDLRKLTTKSEPQGKDFVTEKETIASMIRAKPLQDATSKRLLSRLDQCTTMEELKKLKRGVL 375
Cdd:pfam03210  81 GQLLLDFLLKPVPHPSEKVSPAVQFVPDTGASRDVIRSMIKSSRLEPDRKRYLMTLLDDAKTAEELAKIKRMLM 154
Soyouz_module pfam14313
N-terminal region of Paramyxovirinae phosphoprotein (P); The soyouz module moiety is the ...
 1-53 3.69e-09

N-terminal region of Paramyxovirinae phosphoprotein (P); The soyouz module moiety is the N-terminal region of the phosphoprotein (P) from the subfamily Paramyxovirinae of the family Paramyxoviridae viruses. The main genera in this subfamily include the Rubulaviruses, avulaviruses, respiroviruses, henipaviruses, and morbilliviruses, all of which are enveloped viruses with a non-segmented, negative, single-stranded RNA genome encapsidated by the nucleoprotein (N) within a helical nucleocapsid.


Pssm-ID: 316803  Cd Length: 58  Bit Score: 52.34  E-value: 3.69e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1464310832   1 MASFTDEEINELFDASDIIIDSIITPTPNVPSTVGKSAIPKGNTRVKTDAWEA 53
Cdd:pfam14313   1 MDSFSDAEIAELLELGLNVIESIQSAQGKPQKTLGKSAIPPGNTKALTKAWEK 53
MEV_P-protein-C_like cd21031
C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes ...
 333-376 3.67e-04

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: 37.68  E-value: 3.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1464310832 333 EKETIASMIRAKPLQDATSKRLLSRLDQCTTMEELKKLKRGVLN 376
Cdd:cd21031     2 SRDVIRSMIRSSPLDREEKQALISLLDKAKTDEELNEIKQLVEE 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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