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Conserved domains on  [gi|152002461|dbj|BAF73486|]
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phosphoprotein [Respirovirus muris]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Paramyxo_P super family cl03361
Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the ...
320-566 1.25e-106

Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the family Paramyxoviridae now contains as main genera the Rubulaviruses, avulaviruses, respiroviruses, Henipavirus-es and morbilliviruses. Protein P is the best characterized, structurally of the replicative complex of N, P and L proteins and consists of two functionally distinct moieties, an N-terminal PNT, and a C-terminal PCT. The P protein is an essential part of the viral RNA polymerase complex formed from the P and L proteins. 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 C-terminal part of P (PCT) is only functional as an oligomer and forms with L the polymerase complex. PNT is poorly conserved and unstructured in solution while PCT contains the oligomerization domain (PMD) that folds as a homotetrameric coiled coil (40) containing the L binding region and a C-terminal partially folded domain, PX (residues 474 to 568), identified as the nucleocapsid binding site. Interestingly, PX is also expressed as an independent polypeptide in infected cells. PX has a C-subdomain (residues 516 to 568) that consists of three {alpha}-helices arranged in an antiparallel triple-helical bundle linked to an unfolded flexible N-subdomain (residues 474 to 515).


The actual alignment was detected with superfamily member pfam01806:

Pssm-ID: 460340  Cd Length: 248  Bit Score: 320.25  E-value: 1.25e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  320 ENTSSMKDMATLLTSLGVIQSAQEFESSRDASYVFARRALKSANYAEMTFNVCGLILSAEKSSARKVDENKQLLKQIQES 399
Cdd:pfam01806   2 DNDALIKEEASELEREASGGRAQEFDSIGDADAVFAKEALDIAGDAEMAFNTCGLILRAEKSFANKGDEEGELLKQIQED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  400 VESFRDIYKRFSEYQKEQNSLLMSNLSTLHIITDRGGKTDNTDSLTRSPSVFAKSKENKTKATRFDPSMETLEDMKYKPD 479
Cdd:pfam01806  82 NESFEDIRKRFGESEKEAEAHAMNNDKQLHHIADGGGASDDPDPPDLGNGRDAGIKEDKPKAGGFDPSGAEDEDMEMAAD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  480 LIREDEFRDEIRNPVYQERDTEPRASNASRLFPSKEKHTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELV 559
Cdd:pfam01806 162 LDKEDEDQAEGLNEEIQERAPEPDAREARADLNGREKEPGHPHKARIEGSLLIPAEEAAEAKLLRKCKRDAESGARMELP 241

                  ....*..
gi 152002461  560 EEDIESL 566
Cdd:pfam01806 242 EEDIESL 248
Paramyxo_P super family cl03361
Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the ...
1-248 3.43e-93

Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the family Paramyxoviridae now contains as main genera the Rubulaviruses, avulaviruses, respiroviruses, Henipavirus-es and morbilliviruses. Protein P is the best characterized, structurally of the replicative complex of N, P and L proteins and consists of two functionally distinct moieties, an N-terminal PNT, and a C-terminal PCT. The P protein is an essential part of the viral RNA polymerase complex formed from the P and L proteins. 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 C-terminal part of P (PCT) is only functional as an oligomer and forms with L the polymerase complex. PNT is poorly conserved and unstructured in solution while PCT contains the oligomerization domain (PMD) that folds as a homotetrameric coiled coil (40) containing the L binding region and a C-terminal partially folded domain, PX (residues 474 to 568), identified as the nucleocapsid binding site. Interestingly, PX is also expressed as an independent polypeptide in infected cells. PX has a C-subdomain (residues 516 to 568) that consists of three {alpha}-helices arranged in an antiparallel triple-helical bundle linked to an unfolded flexible N-subdomain (residues 474 to 515).


The actual alignment was detected with superfamily member pfam01806:

Pssm-ID: 460340  Cd Length: 248  Bit Score: 285.58  E-value: 3.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461    1 MDQDAFILKEDSEVERKAPGGRESLSDVIGFLDAVLSNEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQ 80
Cdd:pfam01806   1 EDNDALIKEEASELEREASGGRAQEFDSIGDADAVFAKEALDIAGDAEMAFNTCGLILRAEKSFANKGDEEGELLKQIQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461   81 DNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHWAFRGRTGTNSVSQDLDDGGDSGILENPPNERGYPRSGIEDENREMAA 160
Cdd:pfam01806  81 DNESFEDIRKRFGESEKEAEAHAMNNDKQLHHIADGGGASDDPDPPDLGNGRDAGIKEDKPKAGGFDPSGAEDEDMEMAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  161 HPDKRGEDQAEGLPEEVRGGTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLT 240
Cdd:pfam01806 161 DLDKEDEDQAEGLNEEIQERAPEPDAREARADLNGREKEPGHPHKARIEGSLLIPAEEAAEAKLLRKCKRDAESGARMEL 240

                  ....*...
gi 152002461  241 PATVPGTR 248
Cdd:pfam01806 241 PEEDIESL 248
 
Name Accession Description Interval E-value
Paramyxo_P pfam01806
Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the ...
320-566 1.25e-106

Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the family Paramyxoviridae now contains as main genera the Rubulaviruses, avulaviruses, respiroviruses, Henipavirus-es and morbilliviruses. Protein P is the best characterized, structurally of the replicative complex of N, P and L proteins and consists of two functionally distinct moieties, an N-terminal PNT, and a C-terminal PCT. The P protein is an essential part of the viral RNA polymerase complex formed from the P and L proteins. 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 C-terminal part of P (PCT) is only functional as an oligomer and forms with L the polymerase complex. PNT is poorly conserved and unstructured in solution while PCT contains the oligomerization domain (PMD) that folds as a homotetrameric coiled coil (40) containing the L binding region and a C-terminal partially folded domain, PX (residues 474 to 568), identified as the nucleocapsid binding site. Interestingly, PX is also expressed as an independent polypeptide in infected cells. PX has a C-subdomain (residues 516 to 568) that consists of three {alpha}-helices arranged in an antiparallel triple-helical bundle linked to an unfolded flexible N-subdomain (residues 474 to 515).


Pssm-ID: 460340  Cd Length: 248  Bit Score: 320.25  E-value: 1.25e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  320 ENTSSMKDMATLLTSLGVIQSAQEFESSRDASYVFARRALKSANYAEMTFNVCGLILSAEKSSARKVDENKQLLKQIQES 399
Cdd:pfam01806   2 DNDALIKEEASELEREASGGRAQEFDSIGDADAVFAKEALDIAGDAEMAFNTCGLILRAEKSFANKGDEEGELLKQIQED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  400 VESFRDIYKRFSEYQKEQNSLLMSNLSTLHIITDRGGKTDNTDSLTRSPSVFAKSKENKTKATRFDPSMETLEDMKYKPD 479
Cdd:pfam01806  82 NESFEDIRKRFGESEKEAEAHAMNNDKQLHHIADGGGASDDPDPPDLGNGRDAGIKEDKPKAGGFDPSGAEDEDMEMAAD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  480 LIREDEFRDEIRNPVYQERDTEPRASNASRLFPSKEKHTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELV 559
Cdd:pfam01806 162 LDKEDEDQAEGLNEEIQERAPEPDAREARADLNGREKEPGHPHKARIEGSLLIPAEEAAEAKLLRKCKRDAESGARMELP 241

                  ....*..
gi 152002461  560 EEDIESL 566
Cdd:pfam01806 242 EEDIESL 248
Paramyxo_P pfam01806
Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the ...
1-248 3.43e-93

Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the family Paramyxoviridae now contains as main genera the Rubulaviruses, avulaviruses, respiroviruses, Henipavirus-es and morbilliviruses. Protein P is the best characterized, structurally of the replicative complex of N, P and L proteins and consists of two functionally distinct moieties, an N-terminal PNT, and a C-terminal PCT. The P protein is an essential part of the viral RNA polymerase complex formed from the P and L proteins. 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 C-terminal part of P (PCT) is only functional as an oligomer and forms with L the polymerase complex. PNT is poorly conserved and unstructured in solution while PCT contains the oligomerization domain (PMD) that folds as a homotetrameric coiled coil (40) containing the L binding region and a C-terminal partially folded domain, PX (residues 474 to 568), identified as the nucleocapsid binding site. Interestingly, PX is also expressed as an independent polypeptide in infected cells. PX has a C-subdomain (residues 516 to 568) that consists of three {alpha}-helices arranged in an antiparallel triple-helical bundle linked to an unfolded flexible N-subdomain (residues 474 to 515).


Pssm-ID: 460340  Cd Length: 248  Bit Score: 285.58  E-value: 3.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461    1 MDQDAFILKEDSEVERKAPGGRESLSDVIGFLDAVLSNEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQ 80
Cdd:pfam01806   1 EDNDALIKEEASELEREASGGRAQEFDSIGDADAVFAKEALDIAGDAEMAFNTCGLILRAEKSFANKGDEEGELLKQIQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461   81 DNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHWAFRGRTGTNSVSQDLDDGGDSGILENPPNERGYPRSGIEDENREMAA 160
Cdd:pfam01806  81 DNESFEDIRKRFGESEKEAEAHAMNNDKQLHHIADGGGASDDPDPPDLGNGRDAGIKEDKPKAGGFDPSGAEDEDMEMAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  161 HPDKRGEDQAEGLPEEVRGGTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLT 240
Cdd:pfam01806 161 DLDKEDEDQAEGLNEEIQERAPEPDAREARADLNGREKEPGHPHKARIEGSLLIPAEEAAEAKLLRKCKRDAESGARMEL 240

                  ....*...
gi 152002461  241 PATVPGTR 248
Cdd:pfam01806 241 PEEDIESL 248
MEV_P-protein-C_like cd21031
C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes ...
517-562 1.06e-12

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: 62.34  E-value: 1.06e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 152002461 517 HTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELVEED 562
Cdd:cd21031    1 ASRDVIRSMIRSSPLDREEKQALISLLDKAKTDEELNEIKQLVEEI 46
 
Name Accession Description Interval E-value
Paramyxo_P pfam01806
Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the ...
320-566 1.25e-106

Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the family Paramyxoviridae now contains as main genera the Rubulaviruses, avulaviruses, respiroviruses, Henipavirus-es and morbilliviruses. Protein P is the best characterized, structurally of the replicative complex of N, P and L proteins and consists of two functionally distinct moieties, an N-terminal PNT, and a C-terminal PCT. The P protein is an essential part of the viral RNA polymerase complex formed from the P and L proteins. 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 C-terminal part of P (PCT) is only functional as an oligomer and forms with L the polymerase complex. PNT is poorly conserved and unstructured in solution while PCT contains the oligomerization domain (PMD) that folds as a homotetrameric coiled coil (40) containing the L binding region and a C-terminal partially folded domain, PX (residues 474 to 568), identified as the nucleocapsid binding site. Interestingly, PX is also expressed as an independent polypeptide in infected cells. PX has a C-subdomain (residues 516 to 568) that consists of three {alpha}-helices arranged in an antiparallel triple-helical bundle linked to an unfolded flexible N-subdomain (residues 474 to 515).


Pssm-ID: 460340  Cd Length: 248  Bit Score: 320.25  E-value: 1.25e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  320 ENTSSMKDMATLLTSLGVIQSAQEFESSRDASYVFARRALKSANYAEMTFNVCGLILSAEKSSARKVDENKQLLKQIQES 399
Cdd:pfam01806   2 DNDALIKEEASELEREASGGRAQEFDSIGDADAVFAKEALDIAGDAEMAFNTCGLILRAEKSFANKGDEEGELLKQIQED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  400 VESFRDIYKRFSEYQKEQNSLLMSNLSTLHIITDRGGKTDNTDSLTRSPSVFAKSKENKTKATRFDPSMETLEDMKYKPD 479
Cdd:pfam01806  82 NESFEDIRKRFGESEKEAEAHAMNNDKQLHHIADGGGASDDPDPPDLGNGRDAGIKEDKPKAGGFDPSGAEDEDMEMAAD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  480 LIREDEFRDEIRNPVYQERDTEPRASNASRLFPSKEKHTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELV 559
Cdd:pfam01806 162 LDKEDEDQAEGLNEEIQERAPEPDAREARADLNGREKEPGHPHKARIEGSLLIPAEEAAEAKLLRKCKRDAESGARMELP 241

                  ....*..
gi 152002461  560 EEDIESL 566
Cdd:pfam01806 242 EEDIESL 248
Paramyxo_P pfam01806
Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the ...
1-248 3.43e-93

Paramyxovirinae P phosphoprotein C-terminal region; The subfamily Paramyxovirinae of the family Paramyxoviridae now contains as main genera the Rubulaviruses, avulaviruses, respiroviruses, Henipavirus-es and morbilliviruses. Protein P is the best characterized, structurally of the replicative complex of N, P and L proteins and consists of two functionally distinct moieties, an N-terminal PNT, and a C-terminal PCT. The P protein is an essential part of the viral RNA polymerase complex formed from the P and L proteins. 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 C-terminal part of P (PCT) is only functional as an oligomer and forms with L the polymerase complex. PNT is poorly conserved and unstructured in solution while PCT contains the oligomerization domain (PMD) that folds as a homotetrameric coiled coil (40) containing the L binding region and a C-terminal partially folded domain, PX (residues 474 to 568), identified as the nucleocapsid binding site. Interestingly, PX is also expressed as an independent polypeptide in infected cells. PX has a C-subdomain (residues 516 to 568) that consists of three {alpha}-helices arranged in an antiparallel triple-helical bundle linked to an unfolded flexible N-subdomain (residues 474 to 515).


Pssm-ID: 460340  Cd Length: 248  Bit Score: 285.58  E-value: 3.43e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461    1 MDQDAFILKEDSEVERKAPGGRESLSDVIGFLDAVLSNEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQ 80
Cdd:pfam01806   1 EDNDALIKEEASELEREASGGRAQEFDSIGDADAVFAKEALDIAGDAEMAFNTCGLILRAEKSFANKGDEEGELLKQIQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461   81 DNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHWAFRGRTGTNSVSQDLDDGGDSGILENPPNERGYPRSGIEDENREMAA 160
Cdd:pfam01806  81 DNESFEDIRKRFGESEKEAEAHAMNNDKQLHHIADGGGASDDPDPPDLGNGRDAGIKEDKPKAGGFDPSGAEDEDMEMAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152002461  161 HPDKRGEDQAEGLPEEVRGGTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLT 240
Cdd:pfam01806 161 DLDKEDEDQAEGLNEEIQERAPEPDAREARADLNGREKEPGHPHKARIEGSLLIPAEEAAEAKLLRKCKRDAESGARMEL 240

                  ....*...
gi 152002461  241 PATVPGTR 248
Cdd:pfam01806 241 PEEDIESL 248
MEV_P-protein-C_like cd21031
C-terminal domain of Measles virus phosphoprotein and related proteins; This family includes ...
517-562 1.06e-12

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: 62.34  E-value: 1.06e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 152002461 517 HTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELVEED 562
Cdd:cd21031    1 ASRDVIRSMIRSSPLDREEKQALISLLDKAKTDEELNEIKQLVEEI 46
 
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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