putative P1-P2 fusion protein, partial [Pepper vein yellows virus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| ps-ssRNAv_RdRp-like super family | cl40470 | conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense ... |
270-713 | 0e+00 | |||||||
conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense single-stranded RNA [(+)ssRNA] viruses and closely related viruses; This family contains the catalytic core domain of RdRp of RNA viruses which belong to Group IV of the Baltimore classification system, and are a group of related viruses that have positive-sense (+), single-stranded (ss) genomes made of ribonucleic acid (RNA). RdRp (also known as RNA replicase) catalyzes the replication of RNA from an RNA template; specifically, it catalyzes the synthesis of the RNA strand complementary to a given RNA template. The Baltimore Classification is divided into 7 classes, 3 of which include RNA viruses: Group IV (+) RNA viruses, Group III double-stranded (ds) RNA viruses, and Group V negative-sense (-) RNA viruses. Baltimore groups of viruses differ with respect to the nature of their genome (i.e., the nucleic acid form that is packaged into virions) and correspond to distinct strategies of genome replication and expression. (+) viral RNA is similar to mRNA and thus can be immediately translated by the host cell. (+)ssRNA viruses can also produce (+) copies of the genome from (-) strands of an intermediate dsRNA genome. This acts as both a transcription and a replication process since the replicated RNA is also mRNA. RdRps belong to the expansive class of polymerases containing so-called palm catalytic domains along with the accessory fingers and thumb domains. All RdRps also have six conserved structural motifs (A-F), located in its majority in the palm subdomain (A-E motifs) and the F motif is located on the finger subdomain. All these motifs have been shown to be implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. In addition to Group IV viruses, this model also includes Picobirnaviruses (PBVs), members of the family Picobirnaviridae of dsRNA viruses (Baltimore classification Group III), which are bi-segmented dsRNA viruses. The phylogenetic tree of the RdRps of RNA viruses (realm Riboviria) showed that picobirnaviruses are embedded in the branch of diverse (+)RNA viruses; sometimes they are collectively referred to as the picornavirus supergroup. RdRps of members of the family Permutatetraviridae, a distinct group of RNA viruses that encompass a circular permutation within the RdRp palm domain, are not included in this model. The actual alignment was detected with superfamily member cd23180: Pssm-ID: 477363 Cd Length: 447 Bit Score: 569.21 E-value: 0e+00
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| Peptidase_S39 super family | cl09540 | Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses. |
2-74 | 8.30e-28 | |||||||
Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses. The actual alignment was detected with superfamily member pfam02122: Pssm-ID: 111059 Cd Length: 203 Bit Score: 111.32 E-value: 8.30e-28
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| Name | Accession | Description | Interval | E-value | |||||||
| ps-ssRNAv_Solemoviridae_RdRp | cd23180 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Solemoviridae of ... |
270-713 | 0e+00 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Solemoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Solemoviridae, order Sobelivirales. Plant viruses in the family Solemoviridae have stable icosahedral particles assembled on T=3 symmetry and a relatively small (4-4.6 kb) monopartite (+)ssRNA genome with 4-5 open reading frames (ORFs). The natural host range is relatively narrow for each virus. Viral transmission occurs via mechanical wounding, by vegetative propagation or abiotically through soil; insects (beetles, aphids, thrips, hoppers, mirid bugs, moths) can also be vectors. Viruses infecting legumes or plants from the family Chenopodiaceae may be seed-transmissible. Members of the family are classified into four genera: Sobemovirus, Polemovirus, Polerovirus, Enamovirus. The viral polyprotein contains domains of the membrane anchor, a serine protease, a genome-linked viral protein (VPg) and C-terminal protein(s) or an RdRp, expressed by means of ribosomal frameshifting. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. Pssm-ID: 438030 Cd Length: 447 Bit Score: 569.21 E-value: 0e+00
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| RdRP_4 | pfam02123 | Viral RNA-directed RNA-polymerase; This family includes RNA-dependent RNA polymerase proteins ... |
292-685 | 2.98e-96 | |||||||
Viral RNA-directed RNA-polymerase; This family includes RNA-dependent RNA polymerase proteins (RdRPs) from Luteovirus, Totivirus and Rotavirus. Pssm-ID: 280316 Cd Length: 465 Bit Score: 305.54 E-value: 2.98e-96
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| Peptidase_S39 | pfam02122 | Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses. |
2-74 | 8.30e-28 | |||||||
Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses. Pssm-ID: 111059 Cd Length: 203 Bit Score: 111.32 E-value: 8.30e-28
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| alphaLP-like | cd21112 | alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ... |
11-40 | 3.62e-03 | |||||||
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases. Pssm-ID: 411050 Cd Length: 188 Bit Score: 39.21 E-value: 3.62e-03
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| Name | Accession | Description | Interval | E-value | |||||||
| ps-ssRNAv_Solemoviridae_RdRp | cd23180 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Solemoviridae of ... |
270-713 | 0e+00 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Solemoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Solemoviridae, order Sobelivirales. Plant viruses in the family Solemoviridae have stable icosahedral particles assembled on T=3 symmetry and a relatively small (4-4.6 kb) monopartite (+)ssRNA genome with 4-5 open reading frames (ORFs). The natural host range is relatively narrow for each virus. Viral transmission occurs via mechanical wounding, by vegetative propagation or abiotically through soil; insects (beetles, aphids, thrips, hoppers, mirid bugs, moths) can also be vectors. Viruses infecting legumes or plants from the family Chenopodiaceae may be seed-transmissible. Members of the family are classified into four genera: Sobemovirus, Polemovirus, Polerovirus, Enamovirus. The viral polyprotein contains domains of the membrane anchor, a serine protease, a genome-linked viral protein (VPg) and C-terminal protein(s) or an RdRp, expressed by means of ribosomal frameshifting. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. Pssm-ID: 438030 Cd Length: 447 Bit Score: 569.21 E-value: 0e+00
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| RdRP_4 | pfam02123 | Viral RNA-directed RNA-polymerase; This family includes RNA-dependent RNA polymerase proteins ... |
292-685 | 2.98e-96 | |||||||
Viral RNA-directed RNA-polymerase; This family includes RNA-dependent RNA polymerase proteins (RdRPs) from Luteovirus, Totivirus and Rotavirus. Pssm-ID: 280316 Cd Length: 465 Bit Score: 305.54 E-value: 2.98e-96
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| ps-ssRNAv_Barnaviridae_RdRp | cd23184 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Barnaviridae of ... |
438-675 | 7.70e-55 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Barnaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Barnaviridae, order Sobelivirales, and related viruses. Barnaviridae is a family of non-enveloped, (+)ssRNA viruses. Cultivated mushrooms serve as natural hosts. The family has one genus, Barnavirus, which contains one species: Mushroom bacilliform virus (MBV) which infects the common cultivated button mushroom (Agaricus bisporus), and Bacilliform particles, which are morphologically similar to MBV, have been observed in the field mushroom Agaricus campestris. MBV viral transmission is horizontal via mycelium and possibly basidiospores. Distribution of MBV coincides with that of the commercial cultivation of Agaricus bisporus; the virus has been reported to occur in most major mushroom-growing countries. MBV is capable of autonomous replication, but commonly occurs as a double infection with a double-stranded RNA (dsRNA) virus (LaFrance isometric virus, LFIV) in mushrooms afflicted with La France disease. MBV is not required in pathogenesis involving LFIV, but it remains to be determined if it is a second, minor causal agent of LaFrance disease. MBV ssRNA and LFIV dsRNA do not share sequence homology. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. Pssm-ID: 438034 Cd Length: 261 Bit Score: 188.88 E-value: 7.70e-55
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| Peptidase_S39 | pfam02122 | Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses. |
2-74 | 8.30e-28 | |||||||
Peptidase S39; This family contains polyprotein processing endopeptidases from RNA viruses. Pssm-ID: 111059 Cd Length: 203 Bit Score: 111.32 E-value: 8.30e-28
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| ps-ssRNAv_Alvernaviridae_RdRp | cd23181 | RNA-dependent RNA polymerase (RdRp) in the family Alvernaviridae of positive-sense ... |
455-679 | 2.26e-07 | |||||||
RNA-dependent RNA polymerase (RdRp) in the family Alvernaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Alvernaviridae, order Sobelivirales. Alvernaviridae is a family of non-enveloped [(+)ssRNA] viruses. Dinoflagellates serve as natural hosts. There is one genus in this family, Dinornavirus, which contains one species: Heterocapsa circularisquama RNA virus 01. Diseases associated with this family include host population control, possibly through lysis of the host cell. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. Pssm-ID: 438031 Cd Length: 304 Bit Score: 53.18 E-value: 2.26e-07
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| RNA_dep_RNAP | cd01699 | RNA_dep_RNAP: RNA-dependent RNA polymerase (RdRp) is an essential protein encoded in the ... |
427-676 | 8.66e-07 | |||||||
RNA_dep_RNAP: RNA-dependent RNA polymerase (RdRp) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage. RdRp catalyzes synthesis of the RNA strand complementary to a given RNA template. RdRps of many viruses are products of processing of polyproteins. Some RdRps consist of one polypeptide chain, and others are complexes of several subunits. The domain organization and the 3D structure of the catalytic center of a wide range of RdRps, including those with a low overall sequence homology, are conserved. The catalytic center is formed by several motifs containing a number of conserved amino acid residues. This subfamily represents the RNA-dependent RNA polymerases from all positive-strand RNA eukaryotic viruses with no DNA stage. Pssm-ID: 238843 [Multi-domain] Cd Length: 278 Bit Score: 51.13 E-value: 8.66e-07
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| RdRP_1 | pfam00680 | Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase ... |
343-705 | 1.58e-05 | |||||||
Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase found in many positive strand RNA eukaryotic viruses. Structural studies indicate that these proteins form the "right hand" structure found in all oligonucleotide polymerases, containing thumb, finger and palm domains, and also the additional bridging finger and thumb domains unique to RNA-directed RNA polymerases. Pssm-ID: 425815 Cd Length: 450 Bit Score: 47.79 E-value: 1.58e-05
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| Alphanecrovirus_RdRp | cd23237 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Alphanecrovirus of ... |
528-671 | 3.71e-05 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Alphanecrovirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the Procedovirinae subfamily; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the Alphanecrovirus genus within the subfamily Procedovirinae, family Tombusviridae, order Tolivirales. Alphanecroviruses are non-enveloped, with icosahedral and spherical geometries, and T=3 symmetry, and a diameter of around 28 nm. Their genomes are linear, around 4 kb in length. In the Alphanecrovirus genus plants serve as natural hosts. There are 4 species in this genus: Olive latent virus 1, Olive mild mosaic virus, Potato necrosis virus, and Tobacco necrosis virus A. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. Pssm-ID: 438087 Cd Length: 439 Bit Score: 46.95 E-value: 3.71e-05
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| ps-ssRNAv_RdRp-like | cd23167 | conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense ... |
610-649 | 5.24e-04 | |||||||
conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense single-stranded RNA [(+)ssRNA] viruses and closely related viruses; This family contains the catalytic core domain of RdRp of RNA viruses which belong to Group IV of the Baltimore classification system, and are a group of related viruses that have positive-sense (+), single-stranded (ss) genomes made of ribonucleic acid (RNA). RdRp (also known as RNA replicase) catalyzes the replication of RNA from an RNA template; specifically, it catalyzes the synthesis of the RNA strand complementary to a given RNA template. The Baltimore Classification is divided into 7 classes, 3 of which include RNA viruses: Group IV (+) RNA viruses, Group III double-stranded (ds) RNA viruses, and Group V negative-sense (-) RNA viruses. Baltimore groups of viruses differ with respect to the nature of their genome (i.e., the nucleic acid form that is packaged into virions) and correspond to distinct strategies of genome replication and expression. (+) viral RNA is similar to mRNA and thus can be immediately translated by the host cell. (+)ssRNA viruses can also produce (+) copies of the genome from (-) strands of an intermediate dsRNA genome. This acts as both a transcription and a replication process since the replicated RNA is also mRNA. RdRps belong to the expansive class of polymerases containing so-called palm catalytic domains along with the accessory fingers and thumb domains. All RdRps also have six conserved structural motifs (A-F), located in its majority in the palm subdomain (A-E motifs) and the F motif is located on the finger subdomain. All these motifs have been shown to be implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. In addition to Group IV viruses, this model also includes Picobirnaviruses (PBVs), members of the family Picobirnaviridae of dsRNA viruses (Baltimore classification Group III), which are bi-segmented dsRNA viruses. The phylogenetic tree of the RdRps of RNA viruses (realm Riboviria) showed that picobirnaviruses are embedded in the branch of diverse (+)RNA viruses; sometimes they are collectively referred to as the picornavirus supergroup. RdRps of members of the family Permutatetraviridae, a distinct group of RNA viruses that encompass a circular permutation within the RdRp palm domain, are not included in this model. Pssm-ID: 438017 [Multi-domain] Cd Length: 73 Bit Score: 38.86 E-value: 5.24e-04
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| Enterovirus_RdRp | cd23213 | RNA-dependent RNA polymerase (RdRp) in the Enterovirus genus of positive-sense single-stranded ... |
387-647 | 2.07e-03 | |||||||
RNA-dependent RNA polymerase (RdRp) in the Enterovirus genus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Enterovirus genus within the family Picornaviridae, order Picornavirales. Enteroviruses have small, non-enveloped (+)ssRNA genomes, and replicate within the gastrointestinal tract or other mucosal surfaces. The genus Enterovirus has been divided into 15 species based on genetic divergence (EV A-L and Rhinovirus A-C), and its major members include poliovirus, coxsackievirus and rhinovirus. More than 100 enterovirus types have been associated with several human diseases, all of which are classified into four species (Enterovirus A, Enterovirus B, Enterovirus C, and Enterovirus D). RdRps are multi-domain proteins that play a pivotal role in enterovirus replication. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of enteroviruses. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. Pssm-ID: 438063 Cd Length: 453 Bit Score: 41.36 E-value: 2.07e-03
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| alphaLP-like | cd21112 | alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ... |
11-40 | 3.62e-03 | |||||||
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases. Pssm-ID: 411050 Cd Length: 188 Bit Score: 39.21 E-value: 3.62e-03
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