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MAG: polyprotein [Hubei virga-like virus 2]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||||
RdRP_2 | pfam00978 | RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ... |
2803-3225 | 1.83e-101 | |||||||
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The family also contains the following proteins: 2A protein from bromoviruses putative RNA dependent RNA polymerase from tobamoviruses Non structural polyprotein from togaviruses : Pssm-ID: 395779 Cd Length: 440 Bit Score: 334.61 E-value: 1.83e-101
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Viral_helicase1 | pfam01443 | Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ... |
2384-2646 | 8.96e-31 | |||||||
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated and NTPase activity. This helicase has multiple roles at different stages of viral RNA replication, as dissected by mutational analysis. : Pssm-ID: 366646 [Multi-domain] Cd Length: 227 Bit Score: 122.87 E-value: 8.96e-31
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Vmethyltransf super family | cl46422 | Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ... |
185-464 | 3.37e-20 | |||||||
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA viruses, including Hordei-, Tobra-, Tobamo-, Bromo-, Clostero- and Caliciviruses. This methyltransferase is involved in mRNA capping. Capping of mRNA enhances its stability. This usually occurs in the nucleus. Therefore, many viruses that replicate in the cytoplasm encode their own. This is a specific guanine-7-methyltransferase domain involved in viral mRNA cap0 synthesis. Specificity for guanine 7 position is shown by NMR in and in vivo role in cap synthesis. Based on secondary structure prediction, the basic fold is believed to be similar to the common AdoMet-dependent methyltransferase fold. A curious feature of this methyltransferase domain is that it together with flanking sequences seems to have guanylyltransferase activity coupled to the methyltransferase activity. The domain is found throughout the so-called Alphavirus superfamily, (including alphaviruses and several other groups). It forms the defining, unique feature of this superfamily. The actual alignment was detected with superfamily member pfam01660: Pssm-ID: 480762 Cd Length: 308 Bit Score: 94.29 E-value: 3.37e-20
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AdoMet_MTases super family | cl17173 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
984-1136 | 6.12e-11 | |||||||
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.). The actual alignment was detected with superfamily member pfam01728: Pssm-ID: 473071 Cd Length: 179 Bit Score: 63.76 E-value: 6.12e-11
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PHA03247 super family | cl33720 | large tegument protein UL36; Provisional |
1209-1378 | 1.99e-10 | |||||||
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247: Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 67.27 E-value: 1.99e-10
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OTU super family | cl45892 | OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ... |
803-871 | 1.04e-08 | |||||||
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. The actual alignment was detected with superfamily member cd22792: Pssm-ID: 459237 [Multi-domain] Cd Length: 108 Bit Score: 55.31 E-value: 1.04e-08
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Name | Accession | Description | Interval | E-value | |||||||
RdRP_2 | pfam00978 | RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ... |
2803-3225 | 1.83e-101 | |||||||
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The family also contains the following proteins: 2A protein from bromoviruses putative RNA dependent RNA polymerase from tobamoviruses Non structural polyprotein from togaviruses Pssm-ID: 395779 Cd Length: 440 Bit Score: 334.61 E-value: 1.83e-101
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Kitaviridae_RdRp | cd23254 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Kitaviridae of ... |
2909-3176 | 2.05e-99 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Kitaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Kitaviridae, order Martellivirales. The family Kitaviridae is composed of five recognized species among the three genera: Blueberry necrotic ring blotch virus and Tea plant necrotic ring blotch virus (genus Blunervirus); Citrus leprosis virus C and Citrus leprosis virus C2 (genus Cilevirus); and Hibiscus green spot virus 2 (genus Higrevirus). Although related, there are considerable physical and genetic distinctions between members of the different genera. For example, cile- and higreviruses are associated with a bacilliform virion, whereas a spherical virion has been observed for the lone blunervirus for which microscopy has been reported. Moreover, the replication-associated polyproteins are encoded by a single genomic RNA for cile- and higreviruses, but are split between two genomic RNAs for blunerviruses. 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: 438104 Cd Length: 267 Bit Score: 321.41 E-value: 2.05e-99
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Viral_helicase1 | pfam01443 | Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ... |
2384-2646 | 8.96e-31 | |||||||
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated and NTPase activity. This helicase has multiple roles at different stages of viral RNA replication, as dissected by mutational analysis. Pssm-ID: 366646 [Multi-domain] Cd Length: 227 Bit Score: 122.87 E-value: 8.96e-31
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Vmethyltransf | pfam01660 | Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ... |
185-464 | 3.37e-20 | |||||||
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA viruses, including Hordei-, Tobra-, Tobamo-, Bromo-, Clostero- and Caliciviruses. This methyltransferase is involved in mRNA capping. Capping of mRNA enhances its stability. This usually occurs in the nucleus. Therefore, many viruses that replicate in the cytoplasm encode their own. This is a specific guanine-7-methyltransferase domain involved in viral mRNA cap0 synthesis. Specificity for guanine 7 position is shown by NMR in and in vivo role in cap synthesis. Based on secondary structure prediction, the basic fold is believed to be similar to the common AdoMet-dependent methyltransferase fold. A curious feature of this methyltransferase domain is that it together with flanking sequences seems to have guanylyltransferase activity coupled to the methyltransferase activity. The domain is found throughout the so-called Alphavirus superfamily, (including alphaviruses and several other groups). It forms the defining, unique feature of this superfamily. Pssm-ID: 396298 Cd Length: 308 Bit Score: 94.29 E-value: 3.37e-20
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FtsJ | pfam01728 | FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
984-1136 | 6.12e-11 | |||||||
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: 63.76 E-value: 6.12e-11
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1209-1378 | 1.99e-10 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 67.27 E-value: 1.99e-10
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RlmE | COG0293 | 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
984-1136 | 3.14e-09 | |||||||
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 59.70 E-value: 3.14e-09
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OTU_RDRP-like | cd22792 | OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ... |
803-871 | 1.04e-08 | |||||||
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. Pssm-ID: 438613 [Multi-domain] Cd Length: 108 Bit Score: 55.31 E-value: 1.04e-08
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TALPID3 | pfam15324 | Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
1201-1419 | 2.94e-08 | |||||||
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for Hedgehog signalling. Mutations in this gene noticed first in chickens lead to multiple abnormalities of development. Pssm-ID: 434634 [Multi-domain] Cd Length: 1288 Bit Score: 59.90 E-value: 2.94e-08
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
984-1060 | 1.90e-04 | |||||||
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.). Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 43.19 E-value: 1.90e-04
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DEXXQc_SMUBP2 | cd18044 | DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
2379-2497 | 2.83e-04 | |||||||
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain] Cd Length: 191 Bit Score: 44.52 E-value: 2.83e-04
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SepH | NF040712 | septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1196-1361 | 9.33e-04 | |||||||
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments. Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 44.37 E-value: 9.33e-04
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RecD | COG0507 | ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
2599-2662 | 4.64e-03 | |||||||
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair]; Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 42.66 E-value: 4.64e-03
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Name | Accession | Description | Interval | E-value | |||||||
RdRP_2 | pfam00978 | RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The ... |
2803-3225 | 1.83e-101 | |||||||
RNA dependent RNA polymerase; This family may represent an RNA dependent RNA polymerase. The family also contains the following proteins: 2A protein from bromoviruses putative RNA dependent RNA polymerase from tobamoviruses Non structural polyprotein from togaviruses Pssm-ID: 395779 Cd Length: 440 Bit Score: 334.61 E-value: 1.83e-101
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Kitaviridae_RdRp | cd23254 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Kitaviridae of ... |
2909-3176 | 2.05e-99 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Kitaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Kitaviridae, order Martellivirales. The family Kitaviridae is composed of five recognized species among the three genera: Blueberry necrotic ring blotch virus and Tea plant necrotic ring blotch virus (genus Blunervirus); Citrus leprosis virus C and Citrus leprosis virus C2 (genus Cilevirus); and Hibiscus green spot virus 2 (genus Higrevirus). Although related, there are considerable physical and genetic distinctions between members of the different genera. For example, cile- and higreviruses are associated with a bacilliform virion, whereas a spherical virion has been observed for the lone blunervirus for which microscopy has been reported. Moreover, the replication-associated polyproteins are encoded by a single genomic RNA for cile- and higreviruses, but are split between two genomic RNAs for blunerviruses. 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: 438104 Cd Length: 267 Bit Score: 321.41 E-value: 2.05e-99
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Virgaviridae_RdRp | cd23251 | RNA-dependent RNA polymerase (RdRp) in the family Virgaviridae of positive-sense ... |
2764-3196 | 7.42e-92 | |||||||
RNA-dependent RNA polymerase (RdRp) in the family Virgaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Virgaviridae, order Martellivirales. The Virgaviridae is a family of plant viruses with rod-shaped virions, a (+)ssRNA genome with a 3'-terminal tRNA-like structure and a replication protein similar to those of the alpha-like supergroup. Plants serve as natural hosts. The name of the family is derived from the Latin word virga (rod), as all viruses in this family are rod-shaped. There are currently 59 species in this family, divided among seven genera: Goravirus, Furovirus, Hordeivirus, Pecluvirus, Pomovirus, Tobamovirus, and Tobravirus. 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: 438101 Cd Length: 427 Bit Score: 306.47 E-value: 7.42e-92
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Closteroviridae_RdRp | cd23253 | RNA-dependent RNA polymerase (RdRp) in the family Closteroviridae of positive-sense ... |
2909-3158 | 3.60e-59 | |||||||
RNA-dependent RNA polymerase (RdRp) in the family Closteroviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Closteroviridae, order Martellivirales. Viruses in the family Closteroviridae have a mono-, bi- or tripartite (+)ssRNA genome of 13-19 kb, and non-enveloped, filamentous particles 650-2200 nm long and 12 nm in diameter. They infect plants, mainly dicots, many of which are fruit crops. Members of the family are classified into four genera: Ampelovirus, Closterovirus, Crinivirus and Velarivirus. Their genetic diversity is primarily influenced by strong negative selection and recombination. Closteroviridae viruses are mostly phloem-restricted and induce specific cytoplasmic aggregates of virus particles intermingled with membranous vesicles derived from the endoplasmic reticulum and possibly mitochondria. Their transmission is by aphids, whiteflies, pseudococcid mealybugs or soft scale insects in a semi-persistent manner. 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: 438103 Cd Length: 266 Bit Score: 205.87 E-value: 3.60e-59
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ps-ssRNAv_Martellivirales_RdRp | cd23208 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Martellivirales of ... |
2909-3097 | 9.50e-57 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Martellivirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the order Martellivirales, class Alsuviricetes. The order Martellivirales consists of seven families: Bromoviridae, Closteroviridae, Endornaviridae, Kitaviridae, Mayoviridae, Togaviridae, and Virgaviridae. 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: 438058 [Multi-domain] Cd Length: 190 Bit Score: 196.05 E-value: 9.50e-57
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Mayoviridae_RdRp | cd23256 | RNA-dependent RNA polymerase (RdRp) in the family Mayoviridae of positive-sense ... |
2903-3198 | 2.06e-50 | |||||||
RNA-dependent RNA polymerase (RdRp) in the family Mayoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Mayoviridae, order Martellivirales. The Mayoviridae family consists of two genera, Idaeovirus and Pteridovirus. The genus Idaeovirus contains Raspberry bushy dwarf virus (RBDV), named after the host with which it was first associated (red raspberry, Rubus idaeu) and the disease which is characterized by bushiness (stunting and proliferation of canes); RBDV has recently been found causing an infection in grapevines. RBDV occurs in all tissues of the plant, including seed and pollen, and is transmitted in association with pollen, both vertically to the seed and horizontally to the pollinated plant; this is the only known method of natural spread of RBDV. 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: 438106 Cd Length: 329 Bit Score: 183.02 E-value: 2.06e-50
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Bromoviridae_RdRp | cd23252 | RNA-dependent RNA polymerase (RdRp) in the family Bromoviridae of positive-sense ... |
2801-3157 | 2.53e-42 | |||||||
RNA-dependent RNA polymerase (RdRp) in the family Bromoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Bromoviridae, order Martellivirales. The Bromoviridae family of plant viruses contains tri-segmented, (+)ssRNA viruses with a total genome size of about 8 kb. There are six genera in this family: Alfamovirus, Anulavirus, Bromovirus, Cucumovirus, Ilarvirus, and Oleavirus. Bromoviridae virions are variable in morphology (spherical or bacilliform) and are transmitted mechanically, in/on the pollen and non-persistently by insect vectors. Members of the family cause major disease epidemics in fruit, vegetable and fodder crops such as tomato, cucurbits, bananas, and alfalfa. 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: 438102 Cd Length: 332 Bit Score: 159.70 E-value: 2.53e-42
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Viral_helicase1 | pfam01443 | Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated ... |
2384-2646 | 8.96e-31 | |||||||
Viral (Superfamily 1) RNA helicase; Helicase activity for this family has been demonstrated and NTPase activity. This helicase has multiple roles at different stages of viral RNA replication, as dissected by mutational analysis. Pssm-ID: 366646 [Multi-domain] Cd Length: 227 Bit Score: 122.87 E-value: 8.96e-31
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Vmethyltransf | pfam01660 | Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA ... |
185-464 | 3.37e-20 | |||||||
Viral methyltransferase; This RNA methyltransferase domain is found in a wide range of ssRNA viruses, including Hordei-, Tobra-, Tobamo-, Bromo-, Clostero- and Caliciviruses. This methyltransferase is involved in mRNA capping. Capping of mRNA enhances its stability. This usually occurs in the nucleus. Therefore, many viruses that replicate in the cytoplasm encode their own. This is a specific guanine-7-methyltransferase domain involved in viral mRNA cap0 synthesis. Specificity for guanine 7 position is shown by NMR in and in vivo role in cap synthesis. Based on secondary structure prediction, the basic fold is believed to be similar to the common AdoMet-dependent methyltransferase fold. A curious feature of this methyltransferase domain is that it together with flanking sequences seems to have guanylyltransferase activity coupled to the methyltransferase activity. The domain is found throughout the so-called Alphavirus superfamily, (including alphaviruses and several other groups). It forms the defining, unique feature of this superfamily. Pssm-ID: 396298 Cd Length: 308 Bit Score: 94.29 E-value: 3.37e-20
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Endornaviridae_RdRp | cd23255 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Endornaviridae of ... |
2885-3117 | 1.74e-19 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Endornaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Endornaviridae, order Martellivirales. The family Endornaviridae includes viruses with linear (+)ssRNA genomes that range from 9.7 to 17.6 kb. The family consists of two genera, Alphaendornavirus and Betaendornavirus. Alphaendornavirus includes species whose members infect plants, fungi and oomycetes, while the genus Betaendornavirus includes species whose members infect ascomycete fungi. Plant endornaviruses are transmitted only through the gametes. A conserved RNA-dependent RNA polymerase domain located in the C-terminal region of the polyprotein is a feature common to all endornaviruses. 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: 438105 Cd Length: 237 Bit Score: 90.29 E-value: 1.74e-19
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Togaviridae_RdRp | cd23250 | RNA-dependent RNA polymerase (RdRp) in the family Togaviridae of positive-sense ... |
2798-3225 | 9.46e-18 | |||||||
RNA-dependent RNA polymerase (RdRp) in the family Togaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the RdRp of RNA viruses belonging to the family Togaviridae, order Martellivirales. Togaviridae is a family of small, enveloped viruses with [(+)ssRNA] genomes of 10-12 kb, and contains a single genus, Alphavirus. Alphavirus includes a large number of species that are mostly mosquito-borne and pathogenic in their vertebrate hosts. Many are important human and veterinary pathogens (e.g., chikungunya virus, eastern equine encephalitis virus). The genus Alphavirus mainly consists of mosquito-borne viruses although other hematophagous insects, including ticks, lice, and cliff swallow bugs, have been implicated in transmission. Vertebrate hosts include humans, non-human primates, equids, birds, amphibians, reptiles, rodents, and pigs. There are two aquatic alphaviruses, southern elephant seal virus and salmon pancreas disease virus, infecting sea mammals and fish respectively. Interestingly, Eilat virus (EILV) has been shown to only infect insect cells and is incapable of replicating in vertebrate cells. 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: 438100 Cd Length: 458 Bit Score: 89.44 E-value: 9.46e-18
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ps-ssRNAv_Alsuviricetes_RdRp | cd23182 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the class Alsuviricetes of ... |
2913-3097 | 6.31e-16 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the class Alsuviricetes of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the class Alsuviricetes, phylum: Kitrinoviricota. Alsuviricetes is a class of [(+)ssRNA] viruses which infect eukaryotes. The name of the group is a syllabic abbreviation of "alpha supergroup" with the suffix -viricetes indicating a virus class. The class Alsuviricetes includes three orders: Hepelivirales, Martellivirales, and Tymovirales. 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: 438032 [Multi-domain] Cd Length: 187 Bit Score: 78.79 E-value: 6.31e-16
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ps-ssRNAv_Hepelivirales_RdRp | cd23209 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Hepelivirales of ... |
2943-3099 | 8.74e-13 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Hepelivirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the order Hepelivirales, class Alsuviricetes. This Hepelivirales order consists of four families: Alphatetraviridae, Benyviridae, Hepeviridae, and Matonaviridae. 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: 438059 [Multi-domain] Cd Length: 183 Bit Score: 69.44 E-value: 8.74e-13
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FtsJ | pfam01728 | FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
984-1136 | 6.12e-11 | |||||||
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: 63.76 E-value: 6.12e-11
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1209-1378 | 1.99e-10 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 67.27 E-value: 1.99e-10
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1198-1376 | 1.87e-09 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.19 E-value: 1.87e-09
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RlmE | COG0293 | 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
984-1136 | 3.14e-09 | |||||||
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 59.70 E-value: 3.14e-09
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OTU_RDRP-like | cd22792 | OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; ... |
803-871 | 1.04e-08 | |||||||
OTU (ovarian tumor) domain of the potexviruses/carlaviruses RNA replication protein family; RNA replication polyprotein (RDRP) is a viral homolog of ovarian tumor protease (vOTU), which displays RNA helicase (EC 3.6.4.13), RNA-directed RNA polymerase (EC 2.7.7.48), viral methyltransferase, Fe(2+) 2-oxoglutarate dioxygenase and protease activities. The central part of this protein possibly functions as an ATP-binding helicase. It is an RNA-directed RNA polymerase involved in viral RNA replication. It also acts as a thiol protease that cleaves the polyprotein. This subfamily belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. Pssm-ID: 438613 [Multi-domain] Cd Length: 108 Bit Score: 55.31 E-value: 1.04e-08
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PHA02682 | PHA02682 | ORF080 virion core protein; Provisional |
1209-1408 | 2.05e-08 | |||||||
ORF080 virion core protein; Provisional Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 58.33 E-value: 2.05e-08
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TALPID3 | pfam15324 | Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for ... |
1201-1419 | 2.94e-08 | |||||||
Hedgehog signalling target; TALPID3 is a family of eukaryotic proteins that are targets for Hedgehog signalling. Mutations in this gene noticed first in chickens lead to multiple abnormalities of development. Pssm-ID: 434634 [Multi-domain] Cd Length: 1288 Bit Score: 59.90 E-value: 2.94e-08
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1196-1400 | 3.96e-08 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 59.95 E-value: 3.96e-08
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Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1207-1367 | 7.24e-07 | |||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 55.16 E-value: 7.24e-07
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PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
1209-1424 | 1.27e-06 | |||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 54.50 E-value: 1.27e-06
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1200-1394 | 2.74e-06 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 53.64 E-value: 2.74e-06
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Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1204-1360 | 2.89e-06 | |||||||
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity. Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 53.23 E-value: 2.89e-06
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1209-1376 | 3.17e-06 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.40 E-value: 3.17e-06
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Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1227-1399 | 6.22e-06 | |||||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 52.23 E-value: 6.22e-06
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1209-1404 | 6.58e-06 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 6.58e-06
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ps-ssRNAv_Nodaviridae_RdRp | cd23173 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Nodaviridae of ... |
2970-3096 | 8.84e-06 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Nodaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Nodaviridae, order Nodamuvirales. The family name Nodaviridae, derives from the Japanese village of Nodamura where Nodamura virus was first isolated from Culex tritaeniorhynchus mosquitoes. Virions are non-enveloped and spherical in shape with icosahedral symmetry and diameters ranging from 25 to 33 nm. The members of the two genera in this family infect insects (Alphanodavirus) or fish (Betanodavirus). Alphanodavirus infection results in the stunting, paralysis and death of the insect host. The infection of fish by betanodaviruses such as striped jack nervous necrosis virus or red-spotted grouper nervous necrosis virus causes neural necrosis, encephalopathy or retinopathy and is associated with behavioral abnormalities and high mortality, posing significant problems for marine aquaculture. The genome consists of two molecules of (+)ssRNA: RNA1 and RNA2. 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: 438023 Cd Length: 236 Bit Score: 49.82 E-value: 8.84e-06
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DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1190-1407 | 1.11e-05 | |||||||
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 51.11 E-value: 1.11e-05
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PHA03377 | PHA03377 | EBNA-3C; Provisional |
1179-1380 | 1.25e-05 | |||||||
EBNA-3C; Provisional Pssm-ID: 177614 [Multi-domain] Cd Length: 1000 Bit Score: 51.21 E-value: 1.25e-05
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OTU | cd22744 | OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved ... |
803-894 | 1.33e-05 | |||||||
OTU (ovarian tumor) domain family; The OTU family of cysteine proteases use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. OTU domains typically function as deubiquitinases (DUBs)/ubiquitin thiolesterases (EC 3.4.19.12) that catalyze the thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin, a small regulatory protein that can be conjugated to a large range of target proteins. Protein ubiquitination is a post-translational modification of mostly Lys residues that regulates many cellular processes, including protein degradation, intracellular trafficking, cell signaling, autophagy, transcription, translation, and the DNA damage response. These DUBs may play important regulatory roles at the level of protein turnover by preventing degradation. Pssm-ID: 438581 [Multi-domain] Cd Length: 128 Bit Score: 47.05 E-value: 1.33e-05
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DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1198-1403 | 1.33e-05 | |||||||
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 50.73 E-value: 1.33e-05
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PHA03291 | PHA03291 | envelope glycoprotein I; Provisional |
1235-1350 | 2.14e-05 | |||||||
envelope glycoprotein I; Provisional Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 49.95 E-value: 2.14e-05
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1196-1404 | 3.62e-05 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.78 E-value: 3.62e-05
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1215-1350 | 3.80e-05 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 3.80e-05
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DUF3729 | pfam12526 | Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
1223-1332 | 4.48e-05 | |||||||
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important. Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 45.07 E-value: 4.48e-05
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PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
1211-1377 | 5.09e-05 | |||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 49.10 E-value: 5.09e-05
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PHA03378 | PHA03378 | EBNA-3B; Provisional |
1208-1380 | 5.77e-05 | |||||||
EBNA-3B; Provisional Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 48.91 E-value: 5.77e-05
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SpeE | COG0421 | Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; |
974-1059 | 6.15e-05 | |||||||
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism]; Pssm-ID: 440190 [Multi-domain] Cd Length: 195 Bit Score: 46.75 E-value: 6.15e-05
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PRK14950 | PRK14950 | DNA polymerase III subunits gamma and tau; Provisional |
1226-1338 | 6.87e-05 | |||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 48.65 E-value: 6.87e-05
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PRK07003 | PRK07003 | DNA polymerase III subunit gamma/tau; |
1197-1351 | 8.82e-05 | |||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 48.31 E-value: 8.82e-05
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PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
1206-1352 | 1.07e-04 | |||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 47.95 E-value: 1.07e-04
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ps_ssRNAv_Tolivirales_RdRp | cd23179 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Toliovirales of ... |
2904-3133 | 1.15e-04 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Toliovirales of positive-sense single-stranded RNA (+ssRNA) viruses; This family contains the catalytic core domain of RdRp of Tolivirales, an order of (+)ssRNA viruses which infect insects and plants. The virions are non-enveloped, spherical, and have an icosahedral capsid. The name Tolivirales, is derived from "tombusvirus-like" with the suffix -virales indicating a virus order. This order includes two families: Carmotetraviridae and Tombusviridae. 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: 438029 Cd Length: 227 Bit Score: 46.36 E-value: 1.15e-04
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
984-1060 | 1.90e-04 | |||||||
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.). Pssm-ID: 100107 [Multi-domain] Cd Length: 107 Bit Score: 43.19 E-value: 1.90e-04
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Matonaviridae_RdRp | cd23260 | catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Matonaviridae of ... |
2959-3104 | 2.24e-04 | |||||||
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Matonaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Matonaviridae, order Hepelivirales. Members of the family Matonaviridae have a (+)ssRNA genome enclosed by an icosahedral capsid. Matonaviridae has a single genus, Rubivirus, which contains three species: Rubivirus rubella (commonly called rubella virus), Rubivirus ruteetense (commonly called ruhugu virus), and Rubivirus strelense (commonly called rustrela virus). Rubella virus (RuV) is the etiologic agent of the disease rubella (also called German measles). RuV is transmitted only between humans via the respiratory route, and is the main cause of congenital rubella syndrome (severe congenital birth defects, miscarriage, and stillbirth) when infection occurs during the first trimester of pregnancy. In vitro studies with cell lines showed that RuV has an apoptotic effect on certain cell types; there is evidence for a p53-dependent mechanism. 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: 438110 Cd Length: 257 Bit Score: 45.74 E-value: 2.24e-04
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PRK14951 | PRK14951 | DNA polymerase III subunits gamma and tau; Provisional |
1229-1353 | 2.56e-04 | |||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 46.63 E-value: 2.56e-04
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1196-1358 | 2.68e-04 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.09 E-value: 2.68e-04
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DEXXQc_SMUBP2 | cd18044 | DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, ... |
2379-2497 | 2.83e-04 | |||||||
DEXXQ-box helicase domain of SMUBP2; SMUBP2 (also called immunoglobulin mu-binding protein 2, or IGHMBP2) is a 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction. It is a DNA-binding protein specific to 5'-phosphorylated single-stranded guanine-rich sequence (5'-GGGCT-3') related to the immunoglobulin mu chain switch region. The IGHMBP2 gene is responsible for Charcot-Marie-Tooth disease (CMT) type 2S and spinal muscular atrophy with respiratory distress type 1 (SMARD1). It is also thought to play a role in frontotemporal dementia (FTD) with amyotrophic lateral sclerosis (ALS) and major depressive disorder (MDD). SMUBP2 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: 350802 [Multi-domain] Cd Length: 191 Bit Score: 44.52 E-value: 2.83e-04
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SmtA | COG0500 | SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
980-1057 | 3.81e-04 | |||||||
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]; Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 44.52 E-value: 3.81e-04
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COG4262 | COG4262 | Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ... |
951-1068 | 4.53e-04 | |||||||
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only]; Pssm-ID: 443404 [Multi-domain] Cd Length: 426 Bit Score: 45.63 E-value: 4.53e-04
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PHA03269 | PHA03269 | envelope glycoprotein C; Provisional |
1214-1378 | 5.69e-04 | |||||||
envelope glycoprotein C; Provisional Pssm-ID: 165527 [Multi-domain] Cd Length: 566 Bit Score: 45.49 E-value: 5.69e-04
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PRK07003 | PRK07003 | DNA polymerase III subunit gamma/tau; |
1198-1360 | 6.65e-04 | |||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 45.61 E-value: 6.65e-04
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AAA_19 | pfam13245 | AAA domain; |
2367-2499 | 8.87e-04 | |||||||
AAA domain; Pssm-ID: 433059 [Multi-domain] Cd Length: 136 Bit Score: 42.21 E-value: 8.87e-04
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SepH | NF040712 | septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ... |
1196-1361 | 9.33e-04 | |||||||
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments. Pssm-ID: 468676 [Multi-domain] Cd Length: 346 Bit Score: 44.37 E-value: 9.33e-04
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
1210-1351 | 1.51e-03 | |||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 44.21 E-value: 1.51e-03
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PRK14951 | PRK14951 | DNA polymerase III subunits gamma and tau; Provisional |
1175-1316 | 2.35e-03 | |||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 43.55 E-value: 2.35e-03
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PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1207-1314 | 2.37e-03 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 2.37e-03
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COG4976 | COG4976 | Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
974-1059 | 2.58e-03 | |||||||
Predicted methyltransferase, contains TPR repeat [General function prediction only]; Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 41.52 E-value: 2.58e-03
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1204-1361 | 4.00e-03 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 43.24 E-value: 4.00e-03
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RecD | COG0507 | ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
2599-2662 | 4.64e-03 | |||||||
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair]; Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 42.66 E-value: 4.64e-03
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PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1196-1361 | 6.35e-03 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 6.35e-03
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PRK14951 | PRK14951 | DNA polymerase III subunits gamma and tau; Provisional |
1241-1355 | 7.15e-03 | |||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 237865 [Multi-domain] Cd Length: 618 Bit Score: 42.01 E-value: 7.15e-03
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kgd | PRK12270 | multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ... |
1253-1351 | 7.17e-03 | |||||||
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit; Pssm-ID: 237030 [Multi-domain] Cd Length: 1228 Bit Score: 42.18 E-value: 7.17e-03
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DEXSc_RecD-like | cd17933 | DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
2384-2500 | 7.32e-03 | |||||||
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD 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: 350691 [Multi-domain] Cd Length: 155 Bit Score: 39.85 E-value: 7.32e-03
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
1229-1361 | 7.73e-03 | |||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.90 E-value: 7.73e-03
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PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
1195-1350 | 8.56e-03 | |||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 41.90 E-value: 8.56e-03
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TrmR | COG4122 | tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
962-1126 | 8.72e-03 | |||||||
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 443298 Cd Length: 173 Bit Score: 39.78 E-value: 8.72e-03
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Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
984-1057 | 9.84e-03 | |||||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 37.93 E-value: 9.84e-03
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Blast search parameters | ||||
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