catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Flavivirus, within ...
2812-3375
0e+00
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Flavivirus, within the family Flaviviridae of positive-sense single-stranded RNA (+ssRNA) viruses; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Flavivirus genus within the family Flaviviridae, order Amarillovirales. The genus Flavivirus consists of more than 50 species of arthropod-borne viruses, with distinct groups infecting mosquitoes or ticks. Mammals and birds are the usual primary hosts, in which infections range from asymptomatic to severe or fatal hemorrhagic fever or neurological disease. Important human pathogens include yellow fever virus, dengue virus, Japanese encephalitis virus, West Nile virus and tick-borne encephalitis virus. Other members cause economically important diseases in domestic or wild animals. Virions of Flavivirus have a single, small, basic capsid (C) protein and two envelope proteins. They contain a single, long ORF flanked by 5'- and 3'-terminal non-coding regions, which form specific secondary structures required for genome replication and translation. Translational initiation of genomic RNA is cap dependent in the case of members of the genus Flavivirus. 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: 438054 [Multi-domain] Cd Length: 565 Bit Score: 1320.64 E-value: 0e+00
Flavivirus non-structural Protein NS1; The NS1 protein is well conserved amongst the ...
777-1130
0e+00
Flavivirus non-structural Protein NS1; The NS1 protein is well conserved amongst the flaviviruses. It contains 12 cysteines, and undergoes glycosylation in a similar manner to other NS proteins. Mutational analysis has strongly implied a role for NS1 in the early stages of RNA replication.
The actual alignment was detected with superfamily member pfam00948:
Pssm-ID: 279316 Cd Length: 360 Bit Score: 717.98 E-value: 0e+00
Flavivirus non-structural protein NS4B; Flaviviruses encode a single polyprotein. This is ...
2245-2486
5.84e-143
Flavivirus non-structural protein NS4B; Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. The NS4B protein is small and poorly conserved among the Flaviviruses. NS4B contains multiple hydrophobic potential membrane spanning regions. NS4B may form membrane components of the viral replication complex and could be involved in membrane localization of NS3 and pfam00972.
:
Pssm-ID: 279665 Cd Length: 248 Bit Score: 445.63 E-value: 5.84e-143
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific ...
2501-2734
1.59e-131
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Flaviviridae viruses, comprise a family of ss(+)RNA viruses, cap their mRNAs. The 2'OMTase activity is located in the non-structural protein 5 (NS5).
:
Pssm-ID: 467736 Cd Length: 225 Bit Score: 411.62 E-value: 1.59e-131
Flavivirus non-structural protein NS2A; NS2A is a hydrophobic protein about 25 kDa is size. ...
1138-1320
5.84e-91
Flavivirus non-structural protein NS2A; NS2A is a hydrophobic protein about 25 kDa is size. NS2A is cleaved from NS1 by a membrane bound host protease. NS2A has been found to associate with the dsRNA within the vesicle packages. It has also been found that NS2A associates with the known replicase components and so NS2A has been postulated to be part of this replicase complex.
The actual alignment was detected with superfamily member pfam01005:
Pssm-ID: 279359 Cd Length: 215 Bit Score: 295.21 E-value: 5.84e-91
Flavivirus non-structural protein NS4A; Flaviviruses encode a single polyprotein. This is ...
2099-2242
1.66e-76
Flavivirus non-structural protein NS4A; Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. The NS4A protein is small and poorly conserved among the Flaviviruses. NS4A contains multiple hydrophobic potential membrane spanning regions. NS4A has only been found in cells infected by Kunjin virus.
The actual alignment was detected with superfamily member pfam01350:
Pssm-ID: 279666 Cd Length: 144 Bit Score: 250.59 E-value: 1.66e-76
C-terminal helicase domain of viral helicase; Viral helicases in this family here are ...
1808-1952
5.20e-75
C-terminal helicase domain of viral helicase; Viral helicases in this family here are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
:
Pssm-ID: 350193 [Multi-domain] Cd Length: 145 Bit Score: 246.40 E-value: 5.20e-75
Flavivirus non-structural protein NS2B; Flaviviruses encode a single polyprotein. This is ...
1349-1475
2.33e-69
Flavivirus non-structural protein NS2B; Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. All, but two, are cleaved by the NS2B-NS3 protease complex.
:
Pssm-ID: 279357 Cd Length: 127 Bit Score: 229.51 E-value: 2.33e-69
Peptidase S7, Flavivirus NS3 serine protease; The viral genome is a positive strand RNA that ...
1493-1642
9.75e-50
Peptidase S7, Flavivirus NS3 serine protease; The viral genome is a positive strand RNA that encodes a single polyprotein precursor. Processing of the polyprotein precursor into mature proteins is carried out by the host signal peptidase and by NS3 serine protease, which requires NS2B (pfam01002) as a cofactor.
:
Pssm-ID: 395758 Cd Length: 129 Bit Score: 173.39 E-value: 9.75e-50
flavivirus envelope glycoprotein E, stem/anchor domain; This model describes the C-terminal ...
679-775
5.84e-44
flavivirus envelope glycoprotein E, stem/anchor domain; This model describes the C-terminal domain, containing a stem region followed by two transmembrane anchor domains, of the envelope protein E. This protein is cleaved from the large flavivirus polyprotein, which yields three structural and seven nonstructural proteins.
:
Pssm-ID: 213897 Cd Length: 97 Bit Score: 155.49 E-value: 5.84e-44
Flavivirus polyprotein propeptide; The flaviviruses are small enveloped animal viruses ...
120-198
4.76e-43
Flavivirus polyprotein propeptide; The flaviviruses are small enveloped animal viruses containing a single positive strand genomic RNA. The genome encodes one large ORF a polyprotein which undergos proteolytic processing into mature viral peptide chains. This family consists of a propeptide region of approximately 90 amino acid length.
:
Pssm-ID: 366710 Cd Length: 78 Bit Score: 152.27 E-value: 4.76e-43
Flavivirus capsid protein C; Flaviviruses are small enveloped viruses with virions comprised ...
5-113
7.63e-39
Flavivirus capsid protein C; Flaviviruses are small enveloped viruses with virions comprised of 3 proteins called C, M and E. Multiple copies of the C protein form the nucleocapsid, which contains the ssRNA molecule.
:
Pssm-ID: 366413 Cd Length: 117 Bit Score: 141.70 E-value: 7.63e-39
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with virions ...
207-280
1.13e-36
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with virions comprised of 3 proteins called C, M and E. The envelope glycoprotein M is made as a precursor, called prM. The precursor portion of the protein is the signal peptide for the proteins entry into the membrane. prM is cleaved to form M in a late-stage cleavage event. Associated with this cleavage is a change in the infectivity and fusion activity of the virus.
:
Pssm-ID: 460022 Cd Length: 74 Bit Score: 133.86 E-value: 1.13e-36
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Flavivirus, within ...
2812-3375
0e+00
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Flavivirus, within the family Flaviviridae of positive-sense single-stranded RNA (+ssRNA) viruses; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Flavivirus genus within the family Flaviviridae, order Amarillovirales. The genus Flavivirus consists of more than 50 species of arthropod-borne viruses, with distinct groups infecting mosquitoes or ticks. Mammals and birds are the usual primary hosts, in which infections range from asymptomatic to severe or fatal hemorrhagic fever or neurological disease. Important human pathogens include yellow fever virus, dengue virus, Japanese encephalitis virus, West Nile virus and tick-borne encephalitis virus. Other members cause economically important diseases in domestic or wild animals. Virions of Flavivirus have a single, small, basic capsid (C) protein and two envelope proteins. They contain a single, long ORF flanked by 5'- and 3'-terminal non-coding regions, which form specific secondary structures required for genome replication and translation. Translational initiation of genomic RNA is cap dependent in the case of members of the genus Flavivirus. 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: 438054 [Multi-domain] Cd Length: 565 Bit Score: 1320.64 E-value: 0e+00
Flavivirus RNA-directed RNA polymerase, fingers and palm domains; Flaviviruses produce a large ...
2743-3192
0e+00
Flavivirus RNA-directed RNA polymerase, fingers and palm domains; Flaviviruses produce a large polyprotein from the ssRNA genome, encoding structural proteins required for virus assembly and non-structural (NS1-5) proteins involved in replication of the viral genome. This polyprotein is cleaved by viral and cellular proteases to produce mature viral proteins. NS5 is the largest mature viral protein and contains a N-terminal methyltransferase (MTase) domain separated by a short linker from the C-terminal RNA-directed RNA polymerase domain (RdRp) that adopts a characteriztic right-handed fingers-palm-thumb fold and possesses a number of short regions and motifs homologous to other RNA-directed RNA polymerases. This entry covers the fingers and palm domains of RNA-directed RNA polymerase (RdRp) from Flavivirus NS5. NS5 binds to a the stem loop A (SLA) at the 5' extremity of Flavivirus genome and regulates translation of the viral genome.
Pssm-ID: 460013 Cd Length: 451 Bit Score: 942.06 E-value: 0e+00
Flavivirus non-structural Protein NS1; The NS1 protein is well conserved amongst the ...
777-1130
0e+00
Flavivirus non-structural Protein NS1; The NS1 protein is well conserved amongst the flaviviruses. It contains 12 cysteines, and undergoes glycosylation in a similar manner to other NS proteins. Mutational analysis has strongly implied a role for NS1 in the early stages of RNA replication.
Pssm-ID: 279316 Cd Length: 360 Bit Score: 717.98 E-value: 0e+00
Flavivirus non-structural protein NS4B; Flaviviruses encode a single polyprotein. This is ...
2245-2486
5.84e-143
Flavivirus non-structural protein NS4B; Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. The NS4B protein is small and poorly conserved among the Flaviviruses. NS4B contains multiple hydrophobic potential membrane spanning regions. NS4B may form membrane components of the viral replication complex and could be involved in membrane localization of NS3 and pfam00972.
Pssm-ID: 279665 Cd Length: 248 Bit Score: 445.63 E-value: 5.84e-143
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific ...
2501-2734
1.59e-131
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Flaviviridae viruses, comprise a family of ss(+)RNA viruses, cap their mRNAs. The 2'OMTase activity is located in the non-structural protein 5 (NS5).
Pssm-ID: 467736 Cd Length: 225 Bit Score: 411.62 E-value: 1.59e-131
Flavivirus non-structural protein NS2A; NS2A is a hydrophobic protein about 25 kDa is size. ...
1138-1320
5.84e-91
Flavivirus non-structural protein NS2A; NS2A is a hydrophobic protein about 25 kDa is size. NS2A is cleaved from NS1 by a membrane bound host protease. NS2A has been found to associate with the dsRNA within the vesicle packages. It has also been found that NS2A associates with the known replicase components and so NS2A has been postulated to be part of this replicase complex.
Pssm-ID: 279359 Cd Length: 215 Bit Score: 295.21 E-value: 5.84e-91
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
1662-1812
5.37e-83
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350689 [Multi-domain] Cd Length: 151 Bit Score: 269.42 E-value: 5.37e-83
Flavivirus non-structural protein NS4A; Flaviviruses encode a single polyprotein. This is ...
2099-2242
1.66e-76
Flavivirus non-structural protein NS4A; Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. The NS4A protein is small and poorly conserved among the Flaviviruses. NS4A contains multiple hydrophobic potential membrane spanning regions. NS4A has only been found in cells infected by Kunjin virus.
Pssm-ID: 279666 Cd Length: 144 Bit Score: 250.59 E-value: 1.66e-76
C-terminal helicase domain of viral helicase; Viral helicases in this family here are ...
1808-1952
5.20e-75
C-terminal helicase domain of viral helicase; Viral helicases in this family here are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350193 [Multi-domain] Cd Length: 145 Bit Score: 246.40 E-value: 5.20e-75
Flavivirus non-structural protein NS2B; Flaviviruses encode a single polyprotein. This is ...
1349-1475
2.33e-69
Flavivirus non-structural protein NS2B; Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. All, but two, are cleaved by the NS2B-NS3 protease complex.
Pssm-ID: 279357 Cd Length: 127 Bit Score: 229.51 E-value: 2.33e-69
Peptidase S7, Flavivirus NS3 serine protease; The viral genome is a positive strand RNA that ...
1493-1642
9.75e-50
Peptidase S7, Flavivirus NS3 serine protease; The viral genome is a positive strand RNA that encodes a single polyprotein precursor. Processing of the polyprotein precursor into mature proteins is carried out by the host signal peptidase and by NS3 serine protease, which requires NS2B (pfam01002) as a cofactor.
Pssm-ID: 395758 Cd Length: 129 Bit Score: 173.39 E-value: 9.75e-50
flavivirus envelope glycoprotein E, stem/anchor domain; This model describes the C-terminal ...
679-775
5.84e-44
flavivirus envelope glycoprotein E, stem/anchor domain; This model describes the C-terminal domain, containing a stem region followed by two transmembrane anchor domains, of the envelope protein E. This protein is cleaved from the large flavivirus polyprotein, which yields three structural and seven nonstructural proteins.
Pssm-ID: 213897 Cd Length: 97 Bit Score: 155.49 E-value: 5.84e-44
Flavivirus polyprotein propeptide; The flaviviruses are small enveloped animal viruses ...
120-198
4.76e-43
Flavivirus polyprotein propeptide; The flaviviruses are small enveloped animal viruses containing a single positive strand genomic RNA. The genome encodes one large ORF a polyprotein which undergos proteolytic processing into mature viral peptide chains. This family consists of a propeptide region of approximately 90 amino acid length.
Pssm-ID: 366710 Cd Length: 78 Bit Score: 152.27 E-value: 4.76e-43
Immunoglobulin-like domain III (C-terminal domain) of Flavivirus envelope glycoprotein E; The ...
585-674
1.42e-42
Immunoglobulin-like domain III (C-terminal domain) of Flavivirus envelope glycoprotein E; The C-terminal domain (domain III) of Flavivirus glycoprotein E appears to be involved in low-affinity interactions with negatively charged glycoaminoglycans on the host cell surface. Domain III may also play a role in interactions with alpha-v-beta-3 integrins in West Nile virus, Japanese encephalitis virus, and Dengue virus. The interface between domain I and domain III appears to be destabilized by the low-pH environment of the endosome, and domain III may play a vital role in the conformational changes of envelope glycoprotein E that follow the clathrin-mediated endocytosis of viral particles and are a prerequisite to membrane fusion.
Pssm-ID: 213392 Cd Length: 91 Bit Score: 151.30 E-value: 1.42e-42
Flavivirus capsid protein C; Flaviviruses are small enveloped viruses with virions comprised ...
5-113
7.63e-39
Flavivirus capsid protein C; Flaviviruses are small enveloped viruses with virions comprised of 3 proteins called C, M and E. Multiple copies of the C protein form the nucleocapsid, which contains the ssRNA molecule.
Pssm-ID: 366413 Cd Length: 117 Bit Score: 141.70 E-value: 7.63e-39
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with virions ...
207-280
1.13e-36
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with virions comprised of 3 proteins called C, M and E. The envelope glycoprotein M is made as a precursor, called prM. The precursor portion of the protein is the signal peptide for the proteins entry into the membrane. prM is cleaved to form M in a late-stage cleavage event. Associated with this cleavage is a change in the infectivity and fusion activity of the virus.
Pssm-ID: 460022 Cd Length: 74 Bit Score: 133.86 E-value: 1.13e-36
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with a ...
206-280
1.38e-29
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with a membrane-anchored envelope comprised of 3 proteins called C, M and E. The envelope glycoprotein M is translated as a precursor, called prM. The precursor portion of the protein is the signal peptide for the protein's entry into the membrane. prM is cleaved to form M by the proprotein convertase furin in a late-stage cleavage event. Associated with this cleavage is a change in the infectivity and fusion activity of the virus.
Pssm-ID: 341208 Cd Length: 75 Bit Score: 113.88 E-value: 1.38e-29
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
2548-2714
2.27e-20
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 91.11 E-value: 2.27e-20
Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator ...
1137-1327
5.90e-03
Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily; This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340882 [Multi-domain] Cd Length: 370 Bit Score: 42.15 E-value: 5.90e-03
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Flavivirus, within ...
2812-3375
0e+00
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the genus Flavivirus, within the family Flaviviridae of positive-sense single-stranded RNA (+ssRNA) viruses; This group contains the catalytic core domain of the RdRp of RNA viruses belonging to the Flavivirus genus within the family Flaviviridae, order Amarillovirales. The genus Flavivirus consists of more than 50 species of arthropod-borne viruses, with distinct groups infecting mosquitoes or ticks. Mammals and birds are the usual primary hosts, in which infections range from asymptomatic to severe or fatal hemorrhagic fever or neurological disease. Important human pathogens include yellow fever virus, dengue virus, Japanese encephalitis virus, West Nile virus and tick-borne encephalitis virus. Other members cause economically important diseases in domestic or wild animals. Virions of Flavivirus have a single, small, basic capsid (C) protein and two envelope proteins. They contain a single, long ORF flanked by 5'- and 3'-terminal non-coding regions, which form specific secondary structures required for genome replication and translation. Translational initiation of genomic RNA is cap dependent in the case of members of the genus Flavivirus. 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: 438054 [Multi-domain] Cd Length: 565 Bit Score: 1320.64 E-value: 0e+00
Flavivirus RNA-directed RNA polymerase, fingers and palm domains; Flaviviruses produce a large ...
2743-3192
0e+00
Flavivirus RNA-directed RNA polymerase, fingers and palm domains; Flaviviruses produce a large polyprotein from the ssRNA genome, encoding structural proteins required for virus assembly and non-structural (NS1-5) proteins involved in replication of the viral genome. This polyprotein is cleaved by viral and cellular proteases to produce mature viral proteins. NS5 is the largest mature viral protein and contains a N-terminal methyltransferase (MTase) domain separated by a short linker from the C-terminal RNA-directed RNA polymerase domain (RdRp) that adopts a characteriztic right-handed fingers-palm-thumb fold and possesses a number of short regions and motifs homologous to other RNA-directed RNA polymerases. This entry covers the fingers and palm domains of RNA-directed RNA polymerase (RdRp) from Flavivirus NS5. NS5 binds to a the stem loop A (SLA) at the 5' extremity of Flavivirus genome and regulates translation of the viral genome.
Pssm-ID: 460013 Cd Length: 451 Bit Score: 942.06 E-value: 0e+00
Flavivirus non-structural Protein NS1; The NS1 protein is well conserved amongst the ...
777-1130
0e+00
Flavivirus non-structural Protein NS1; The NS1 protein is well conserved amongst the flaviviruses. It contains 12 cysteines, and undergoes glycosylation in a similar manner to other NS proteins. Mutational analysis has strongly implied a role for NS1 in the early stages of RNA replication.
Pssm-ID: 279316 Cd Length: 360 Bit Score: 717.98 E-value: 0e+00
Flavivirus non-structural protein NS4B; Flaviviruses encode a single polyprotein. This is ...
2245-2486
5.84e-143
Flavivirus non-structural protein NS4B; Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. The NS4B protein is small and poorly conserved among the Flaviviruses. NS4B contains multiple hydrophobic potential membrane spanning regions. NS4B may form membrane components of the viral replication complex and could be involved in membrane localization of NS3 and pfam00972.
Pssm-ID: 279665 Cd Length: 248 Bit Score: 445.63 E-value: 5.84e-143
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific ...
2501-2734
1.59e-131
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Flaviviridae viruses, comprise a family of ss(+)RNA viruses, cap their mRNAs. The 2'OMTase activity is located in the non-structural protein 5 (NS5).
Pssm-ID: 467736 Cd Length: 225 Bit Score: 411.62 E-value: 1.59e-131
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Flaviviridae of ...
2942-3257
7.34e-99
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Flaviviridae of positive-sense single-stranded RNA (+ssRNA) viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Flaviviridae, order Amarillovirales. Flaviviridae, is a family of small, enveloped viruses with RNA genomes of 9-13 kb. Most infect mammals and birds. Many flaviviruses are host-specific and pathogenic, such as hepatitis C virus in the genus Hepacivirus. The majority of known members in the genus Flavivirus are arthropod borne, and many are important human and veterinary pathogens (e.g., yellow fever virus, dengue virus). Virions are typically spherical in shape with a lipid envelope. Virions have a single, small, basic capsid (C) protein and two (genera Flavivirus, Hepacivirus and Pegivirus) or three (genus Pestivirus) envelope proteins. They contain a single, long ORF flanked by 5'- and 3'-terminal non-coding regions, which form specific secondary structures required for genome replication and translation. Translational initiation of genomic RNA is cap dependent in the case of members of the genus Flavivirus. 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: 438028 Cd Length: 284 Bit Score: 320.62 E-value: 7.34e-99
Flavivirus RNA-directed RNA polymerase, thumb domain; Flaviviruses produce a large polyprotein ...
3196-3359
1.48e-95
Flavivirus RNA-directed RNA polymerase, thumb domain; Flaviviruses produce a large polyprotein from the ssRNA genome, encoding structural proteins required for virus assembly and non-structural (NS1-5) proteins involved in replication of the viral genome. This polyprotein is cleaved by viral and cellular proteases to produce mature viral proteins. NS5 is the largest mature viral protein and contains a N-terminal methyltransferase (MTase) domain separated by a short linker from the C-terminal RNA-directed RNA polymerase domain (RdRp) that adopts a characteriztic right-handed fingers-palm-thumb fold and possesses a number of short regions and motifs homologous to other RNA-directed RNA polymerases. This entry represents the thumb domain of NS5 RdRp. NS5 binds to a the stem loop A (SLA) at the 5' extremity of Flavivirus genome and regulates translation of the viral genome.
Pssm-ID: 466632 Cd Length: 164 Bit Score: 305.95 E-value: 1.48e-95
Flavivirus non-structural protein NS2A; NS2A is a hydrophobic protein about 25 kDa is size. ...
1138-1320
5.84e-91
Flavivirus non-structural protein NS2A; NS2A is a hydrophobic protein about 25 kDa is size. NS2A is cleaved from NS1 by a membrane bound host protease. NS2A has been found to associate with the dsRNA within the vesicle packages. It has also been found that NS2A associates with the known replicase components and so NS2A has been postulated to be part of this replicase complex.
Pssm-ID: 279359 Cd Length: 215 Bit Score: 295.21 E-value: 5.84e-91
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional ...
1662-1812
5.37e-83
DEXH-box helicase domain of NS3 protease-helicase; NS3 is a nonstructural multifunctional protein found in pestiviruses that contains an N-terminal protease and a C-terminal helicase. The N-terminal domain is a chymotrypsin-like serine protease, which is responsible for most of the maturation cleavages of the polyprotein precursor in the cytosolic side of the endoplasmic reticulum membrane. The C-terminal domain, about two-thirds of NS3, is a helicase belonging to superfamily 2 (SF2) thought to be important for unwinding highly structured regions of the RNA genome during replication. NS3 plays an essential role in viral polyprotein processing and genome replication. NS3 is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350689 [Multi-domain] Cd Length: 151 Bit Score: 269.42 E-value: 5.37e-83
Flavivirus non-structural protein NS4A; Flaviviruses encode a single polyprotein. This is ...
2099-2242
1.66e-76
Flavivirus non-structural protein NS4A; Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. The NS4A protein is small and poorly conserved among the Flaviviruses. NS4A contains multiple hydrophobic potential membrane spanning regions. NS4A has only been found in cells infected by Kunjin virus.
Pssm-ID: 279666 Cd Length: 144 Bit Score: 250.59 E-value: 1.66e-76
C-terminal helicase domain of viral helicase; Viral helicases in this family here are ...
1808-1952
5.20e-75
C-terminal helicase domain of viral helicase; Viral helicases in this family here are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350193 [Multi-domain] Cd Length: 145 Bit Score: 246.40 E-value: 5.20e-75
Flavivirus non-structural protein NS2B; Flaviviruses encode a single polyprotein. This is ...
1349-1475
2.33e-69
Flavivirus non-structural protein NS2B; Flaviviruses encode a single polyprotein. This is cleaved into three structural and seven non-structural proteins. All, but two, are cleaved by the NS2B-NS3 protease complex.
Pssm-ID: 279357 Cd Length: 127 Bit Score: 229.51 E-value: 2.33e-69
Peptidase S7, Flavivirus NS3 serine protease; The viral genome is a positive strand RNA that ...
1493-1642
9.75e-50
Peptidase S7, Flavivirus NS3 serine protease; The viral genome is a positive strand RNA that encodes a single polyprotein precursor. Processing of the polyprotein precursor into mature proteins is carried out by the host signal peptidase and by NS3 serine protease, which requires NS2B (pfam01002) as a cofactor.
Pssm-ID: 395758 Cd Length: 129 Bit Score: 173.39 E-value: 9.75e-50
flavivirus envelope glycoprotein E, stem/anchor domain; This model describes the C-terminal ...
679-775
5.84e-44
flavivirus envelope glycoprotein E, stem/anchor domain; This model describes the C-terminal domain, containing a stem region followed by two transmembrane anchor domains, of the envelope protein E. This protein is cleaved from the large flavivirus polyprotein, which yields three structural and seven nonstructural proteins.
Pssm-ID: 213897 Cd Length: 97 Bit Score: 155.49 E-value: 5.84e-44
Flavivirus polyprotein propeptide; The flaviviruses are small enveloped animal viruses ...
120-198
4.76e-43
Flavivirus polyprotein propeptide; The flaviviruses are small enveloped animal viruses containing a single positive strand genomic RNA. The genome encodes one large ORF a polyprotein which undergos proteolytic processing into mature viral peptide chains. This family consists of a propeptide region of approximately 90 amino acid length.
Pssm-ID: 366710 Cd Length: 78 Bit Score: 152.27 E-value: 4.76e-43
Immunoglobulin-like domain III (C-terminal domain) of Flavivirus envelope glycoprotein E; The ...
585-674
1.42e-42
Immunoglobulin-like domain III (C-terminal domain) of Flavivirus envelope glycoprotein E; The C-terminal domain (domain III) of Flavivirus glycoprotein E appears to be involved in low-affinity interactions with negatively charged glycoaminoglycans on the host cell surface. Domain III may also play a role in interactions with alpha-v-beta-3 integrins in West Nile virus, Japanese encephalitis virus, and Dengue virus. The interface between domain I and domain III appears to be destabilized by the low-pH environment of the endosome, and domain III may play a vital role in the conformational changes of envelope glycoprotein E that follow the clathrin-mediated endocytosis of viral particles and are a prerequisite to membrane fusion.
Pssm-ID: 213392 Cd Length: 91 Bit Score: 151.30 E-value: 1.42e-42
Flavivirus capsid protein C; Flaviviruses are small enveloped viruses with virions comprised ...
5-113
7.63e-39
Flavivirus capsid protein C; Flaviviruses are small enveloped viruses with virions comprised of 3 proteins called C, M and E. Multiple copies of the C protein form the nucleocapsid, which contains the ssRNA molecule.
Pssm-ID: 366413 Cd Length: 117 Bit Score: 141.70 E-value: 7.63e-39
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with virions ...
207-280
1.13e-36
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with virions comprised of 3 proteins called C, M and E. The envelope glycoprotein M is made as a precursor, called prM. The precursor portion of the protein is the signal peptide for the proteins entry into the membrane. prM is cleaved to form M in a late-stage cleavage event. Associated with this cleavage is a change in the infectivity and fusion activity of the virus.
Pssm-ID: 460022 Cd Length: 74 Bit Score: 133.86 E-value: 1.13e-36
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with a ...
206-280
1.38e-29
Flavivirus envelope glycoprotein M; Flaviviruses are small enveloped viruses with a membrane-anchored envelope comprised of 3 proteins called C, M and E. The envelope glycoprotein M is translated as a precursor, called prM. The precursor portion of the protein is the signal peptide for the protein's entry into the membrane. prM is cleaved to form M by the proprotein convertase furin in a late-stage cleavage event. Associated with this cleavage is a change in the infectivity and fusion activity of the virus.
Pssm-ID: 341208 Cd Length: 75 Bit Score: 113.88 E-value: 1.38e-29
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
1665-1793
1.48e-21
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 93.62 E-value: 1.48e-21
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
2548-2714
2.27e-20
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 91.11 E-value: 2.27e-20
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-) ...
2552-2714
7.71e-20
viral Cap-0 specific (nucleoside-2'-O-)-methyltransferase; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Some dsDNA and dsRNA viruses, like the bluetongue virus (BTV), a member of the Reoviridae family, and Vaccinia virus, a member of the Poxviridae family, as well as some ss(+)RNA viruses, like Flaviviridae and Nidovirales, cap their mRNAs and encode their own 2'OMTase. In BTV, all four reactions are catalyzed by a single protein, VP4. In Vaccinia, the activity is located in the processing factor of the poly(A) polymerase, VP39.
Pssm-ID: 467730 Cd Length: 179 Bit Score: 89.81 E-value: 7.71e-20
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) ...
1662-1794
2.67e-14
DEXH-box helicase domain of DEAD-like helicase RHA family proteins; The RNA helicase A (RHA) family includes RHA, also called DEAH-box helicase 9 (DHX9), DHX8, DHX15-16, DHX32-38, and many others. The RHA family belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438707 [Multi-domain] Cd Length: 159 Bit Score: 72.88 E-value: 2.67e-14
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
1672-1801
8.78e-07
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 51.47 E-value: 8.78e-07
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
1666-1794
9.93e-05
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 44.99 E-value: 9.93e-05
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA ...
1648-1763
8.45e-04
DEXH-box helicase domain of ATP-dependent helicase HrpB; HrpB is part of the HrpB-HrpA two-partner secretion (TPS) system, a secretion pathway important to the secretion of large virulence-associated proteins. HrpB belongs to the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 438711 [Multi-domain] Cd Length: 174 Bit Score: 43.09 E-value: 8.45e-04
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 39.61 E-value: 1.70e-03
Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator ...
1137-1327
5.90e-03
Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily; This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340882 [Multi-domain] Cd Length: 370 Bit Score: 42.15 E-value: 5.90e-03
23S rRNA C2498 (ribose-2'-O)-methylase RlmM [Translation, ribosomal structure and biogenesis]; 23S rRNA C2498 (ribose-2'-O)-methylase RlmM is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 442177 [Multi-domain] Cd Length: 356 Bit Score: 41.38 E-value: 9.02e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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