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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464315642 240 KVDHQLDLVLKQTSSIPMMRSEIQQLKTSVAIMEANLGMMKILDPGCANVSSLSDLRAVARSHPVLVSGPGDPSPYMTQG 319
Cdd:pfam03210   1 KIHEDVDKVISQLSSIPLIKNEIESIKTSLATIEGHLSSMKIMDPGNPDLKPVIGLRRSGRAHAELVSGPGDTSGRTSSG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1464315642 320 GEMTLNKLSQPVQHPSELIKSATASGPDMGVEKDTVRALITSRPMHPSSSAKLLSKLDAARSIEEIRKIKRLAL 393
Cdd:pfam03210  81 GQLLLDFLLKPVPHPSEKVSPAVQFVPDTGASRDVIRSMIKSSRLEPDRKRYLMTLLDDAKTAEELAKIKRMLM 154

DNA polymerase III subunit gamma/tau;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464315642  61 ASQDAPDQQDRTEKQPSTPEQATPHNNPP---ITSTEPPPTQAASETSDTQLKT--GASNSLLSMLDKLSNKSSNAKKgp 135
Cdd:PRK14949  561 SESYNALSDDEQHSANVQSAQSAAEAQPSsqsLSPISAVTTAAASLADDDILDAvlAARDSLLSDLDALSPKEGDGKK-- 638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464315642 136 wSGPQEGHHQPPAQQHGNQPSygSNQGRPQHQAKAVPGNRGTDENTAYHGQRKESQPSAGATPHAPQSGQSQDNTP---- 211
Cdd:PRK14949  639 -SSADRKPKTPPSRAPPASLS--KPASSPDASQTSASFDLDPDFELATHQSVPEAALASGSAPAPPPVPDPYDRPPweea 715

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1464315642 212 ---VPVDRVQLPADFAQAMMSMMEALSQKVSKVDHQLD-LVLKQTSSIP 256
Cdd:PRK14949  716 pevASANDGPNNAAEGNLSESVEDASNSELQAVEQQAThQPQVQAEAQS 764

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464315642 240 KVDHQLDLVLKQTSSIPMMRSEIQQLKTSVAIMEANLGMMKILDPGCANVSSLSDLRAVARSHPVLVSGPGDPSPYMTQG 319
Cdd:pfam03210   1 KIHEDVDKVISQLSSIPLIKNEIESIKTSLATIEGHLSSMKIMDPGNPDLKPVIGLRRSGRAHAELVSGPGDTSGRTSSG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1464315642 320 GEMTLNKLSQPVQHPSELIKSATASGPDMGVEKDTVRALITSRPMHPSSSAKLLSKLDAARSIEEIRKIKRLAL 393
Cdd:pfam03210  81 GQLLLDFLLKPVPHPSEKVSPAVQFVPDTGASRDVIRSMIKSSRLEPDRKRYLMTLLDDAKTAEELAKIKRMLM 154

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1464315642 350 VEKDTVRALITSRPMHPSSSAKLLSKLDAARSIEEIRKIKRLALNG 395
Cdd:cd21031     1 ASRDVIRSMIRSSPLDREEKQALISLLDKAKTDEELNEIKQLVEEI 46

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1464315642 240 KVDHQLDLVLKQTSSIPMMRSEIQQLKTSVAIMEANLGMMKILDPGCANVSSLSDLRAVARSHPVLVSGPGDPSPYMTQG 319
Cdd:pfam03210   1 KIHEDVDKVISQLSSIPLIKNEIESIKTSLATIEGHLSSMKIMDPGNPDLKPVIGLRRSGRAHAELVSGPGDTSGRTSSG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1464315642 320 GEMTLNKLSQPVQHPSELIKSATASGPDMGVEKDTVRALITSRPMHPSSSAKLLSKLDAARSIEEIRKIKRLAL 393
Cdd:pfam03210  81 GQLLLDFLLKPVPHPSEKVSPAVQFVPDTGASRDVIRSMIKSSRLEPDRKRYLMTLLDDAKTAEELAKIKRMLM 154

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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1464315642 350 VEKDTVRALITSRPMHPSSSAKLLSKLDAARSIEEIRKIKRLALNG 395
Cdd:cd21031     1 ASRDVIRSMIRSSPLDREEKQALISLLDKAKTDEELNEIKQLVEEI 46