Chain A, PROTEIN (TETANUS TOXIN HC)
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| Toxin_R_bind_C_TeNT | cd23397 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium tetani tetanus ... |
272-463 | 4.80e-128 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium tetani tetanus toxin (TeNT) and similar proteins; TeNT (EC 3.4.24.68), also called tentoxylysin, is tetanus toxin that inhibits neurotransmission of inhibitory interneurons, causing spastic paralysis in the tetanus disease. It binds to peripheral neuronal synapses. It is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of vesicle-associated membrane protein-2 (also known as synaptobrevin-2). TeNT comprises three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. : Pssm-ID: 467776 Cd Length: 192 Bit Score: 369.37 E-value: 4.80e-128
|
||||||||
| Toxin_R_bind_N | pfam07953 | Clostridium neurotoxin, N-terminal receptor binding; The Clostridium neurotoxin family is ... |
47-250 | 1.40e-63 | ||||
Clostridium neurotoxin, N-terminal receptor binding; The Clostridium neurotoxin family is composed of tetanus neurotoxin and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain (pfam01742), the central translocation domains and two receptor binding domains. This domains is the N-terminal receptor binding domain,which is comprised of two seven-stranded beta-sheets sandwiched together to form a jelly role motif. The role of this domain in receptor binding appears to be indirect. : Pssm-ID: 400348 Cd Length: 192 Bit Score: 204.17 E-value: 1.40e-63
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| Toxin_R_bind_C_TeNT | cd23397 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium tetani tetanus ... |
272-463 | 4.80e-128 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium tetani tetanus toxin (TeNT) and similar proteins; TeNT (EC 3.4.24.68), also called tentoxylysin, is tetanus toxin that inhibits neurotransmission of inhibitory interneurons, causing spastic paralysis in the tetanus disease. It binds to peripheral neuronal synapses. It is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of vesicle-associated membrane protein-2 (also known as synaptobrevin-2). TeNT comprises three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467776 Cd Length: 192 Bit Score: 369.37 E-value: 4.80e-128
|
||||||||
| Toxin_R_bind_C | pfam07951 | Clostridium neurotoxin, C-terminal receptor binding; The Clostridium neurotoxin family is ... |
259-468 | 7.23e-117 | ||||
Clostridium neurotoxin, C-terminal receptor binding; The Clostridium neurotoxin family is composed of tetanus neurotoxins and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain (pfam01742), the central translocation domains and two receptor binding domains. This domains is the C-terminal receptor binding domain, which adopts a modified beta-trefoil fold with a six stranded beta-barrel and a beta-hairpin triplet capping the domain. The first step in the intoxication process is a binding event between this domains and the pre-synaptic nerve ending. Pssm-ID: 285226 Cd Length: 217 Bit Score: 341.65 E-value: 7.23e-117
|
||||||||
| Toxin_R_bind_N | pfam07953 | Clostridium neurotoxin, N-terminal receptor binding; The Clostridium neurotoxin family is ... |
47-250 | 1.40e-63 | ||||
Clostridium neurotoxin, N-terminal receptor binding; The Clostridium neurotoxin family is composed of tetanus neurotoxin and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain (pfam01742), the central translocation domains and two receptor binding domains. This domains is the N-terminal receptor binding domain,which is comprised of two seven-stranded beta-sheets sandwiched together to form a jelly role motif. The role of this domain in receptor binding appears to be indirect. Pssm-ID: 400348 Cd Length: 192 Bit Score: 204.17 E-value: 1.40e-63
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| Toxin_R_bind_C_TeNT | cd23397 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium tetani tetanus ... |
272-463 | 4.80e-128 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium tetani tetanus toxin (TeNT) and similar proteins; TeNT (EC 3.4.24.68), also called tentoxylysin, is tetanus toxin that inhibits neurotransmission of inhibitory interneurons, causing spastic paralysis in the tetanus disease. It binds to peripheral neuronal synapses. It is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of vesicle-associated membrane protein-2 (also known as synaptobrevin-2). TeNT comprises three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467776 Cd Length: 192 Bit Score: 369.37 E-value: 4.80e-128
|
||||||||
| Toxin_R_bind_C | pfam07951 | Clostridium neurotoxin, C-terminal receptor binding; The Clostridium neurotoxin family is ... |
259-468 | 7.23e-117 | ||||
Clostridium neurotoxin, C-terminal receptor binding; The Clostridium neurotoxin family is composed of tetanus neurotoxins and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain (pfam01742), the central translocation domains and two receptor binding domains. This domains is the C-terminal receptor binding domain, which adopts a modified beta-trefoil fold with a six stranded beta-barrel and a beta-hairpin triplet capping the domain. The first step in the intoxication process is a binding event between this domains and the pre-synaptic nerve ending. Pssm-ID: 285226 Cd Length: 217 Bit Score: 341.65 E-value: 7.23e-117
|
||||||||
| Toxin_R_bind_N | pfam07953 | Clostridium neurotoxin, N-terminal receptor binding; The Clostridium neurotoxin family is ... |
47-250 | 1.40e-63 | ||||
Clostridium neurotoxin, N-terminal receptor binding; The Clostridium neurotoxin family is composed of tetanus neurotoxin and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain (pfam01742), the central translocation domains and two receptor binding domains. This domains is the N-terminal receptor binding domain,which is comprised of two seven-stranded beta-sheets sandwiched together to form a jelly role motif. The role of this domain in receptor binding appears to be indirect. Pssm-ID: 400348 Cd Length: 192 Bit Score: 204.17 E-value: 1.40e-63
|
||||||||
| Toxin_R_bind_C | cd23267 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium neurotoxin family; ... |
272-461 | 1.56e-60 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium neurotoxin family; The Clostridium neurotoxin (CNT) family is composed of tetanus neurotoxins (TeNT) and seven well-established serotypes (A-G) of botulinum neurotoxin (BoNT), which cause the diseases tetanus and botulism respectively. A new toxin serotype, BoNT/X, was recently identified. BoNTs are the primary virulence factors and vaccine components against botulism. They have been exploited as cosmetics and muscle-disorder treatment medicines for decades, are well known for their extreme neurotoxicity to humans. At motor neurons, BoNTs cleave neuronal soluble N-ethylmaleimide-sensitive-factor attachment protein receptor (SNARE) proteins that inhibits synaptic vesicle (SV) exocytosis, resulting in flaccid paralysis, whereas TeNT is subjected to retrograde transport into inhibitory neurons and blocks release of glycine and gamma-aminobutyric acid, which results in spastic paralysis. Uptake of BoNT/A, B, E, F, and G requires a dual interaction with complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles, such as synaptotagmin or SV2 (synaptic vesicle glycoprotein 2), whereas little is known about the cell entry mechanisms of the serotypes C and D. The family also includes Enterococcus botulinum-like toxin eBoNT/J and Paraclostridium bifermentans mosquitocidal protein 1 (PMP1). eBoNT/J might be a precursor of a toxin that binds to an unknown eukaryotic cell receptor(s) and be taken up into the host cell via the endocytic pathway. PMP1 is a clostridial-like neurotoxin that selectively targets anopheline mosquitoes. All family members comprise three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). The HCR domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. It is a proven target for anti-BoNT antibody and vaccine development. This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467766 Cd Length: 190 Bit Score: 196.13 E-value: 1.56e-60
|
||||||||
| Toxin_R_bind_C_BoNTA_like | cd23388 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum ... |
272-466 | 8.44e-16 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum neurotoxin type A (BoNT/A), type H (BoNT/H) and similar proteins; BoNT/A, also called bontoxilysin-A, or BOTOX, is a potent disease agent in botulism, a potential biological weapon and an effective therapeutic drug for a wide range of common medical conditions, such as migraines and a variety of ocular motility and movement disorders. It is also a licensed drug widely used for cosmetic applications. There are two types of BoNT/A receptor, gangliosides and members of the synaptic vesicle glycoprotein 2 (SV2) family. Both are required for BoNT/A toxicity and are therefore likely to cooperate with each other. SV2 family members are putative transporter proteins that are predicted to have 12 transmembrane domains, associate with the receptor-binding domain of the toxin. In addition, fibroblast growth factor receptor 3 (FGFR3) has also been reported to be a potential BoNT/A receptor. The family also includes BoNT/H, also known as BoNT/HA, or BoNT/FA, which shows high sequence/structure similarity to that of BoNT/A. However, they are different regarding their binding to cell-surface receptors including both polysialoganglioside (PSG) and SV2. BoNT/H also responds differently to some potent BoNT/A-neutralizing antibodies (e.g. CR2). Both BoNT/A and BoNT/H comprise three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). The HCR domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. It is a proven target for anti-BoNT antibody and vaccine development. This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467767 Cd Length: 196 Bit Score: 75.81 E-value: 8.44e-16
|
||||||||
| Toxin_R_bind_C_BoNTB | cd23389 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum ... |
272-461 | 1.07e-15 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum neurotoxin type B (BoNT/B) and similar proteins; BoNT/B, also called bontoxilysin-B, is botulinum toxin that causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. There are two co-receptors of BoNT/B precursor, complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles (e.g. synaptotagmin I and II). BoNT/B comprises three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). The HCR domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. It is a proven target for anti-BoNT antibody and vaccine development. This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467768 Cd Length: 198 Bit Score: 75.39 E-value: 1.07e-15
|
||||||||
| Toxin_R_bind_C_BoNTG | cd23394 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum ... |
272-461 | 1.41e-12 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum neurotoxin type G (BoNT/G) and similar proteins; BoNT/G, also called bontoxilysin-G, is botulinum toxin that causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. There are two co-receptors of BoNT/G precursor, complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles (e.g. synaptotagmin I and II). BoNT/G comprises three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). The HCR domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. It is a proven target for anti-BoNT antibody and vaccine development. This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467773 Cd Length: 195 Bit Score: 66.24 E-value: 1.41e-12
|
||||||||
| Laminin_G_3 | pfam13385 | Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
102-255 | 4.11e-11 | ||||
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily. Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 60.86 E-value: 4.11e-11
|
||||||||
| Toxin_R_bind_C_BoNTX_like | cd23396 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum ... |
272-461 | 1.52e-08 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum neurotoxin type X (BoNT/X) and similar proteins; BoNT/X, also called bontoxilysin-X, is a new serotype of botulinum toxin, which causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. There are two co-receptors of BoNT/X precursor, complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Like BoNT/B/D/F/G, BoNT/X cleaves vesicle-associated membrane proteins (VAMP) 1, 2 and 3, but at a novel site (Arg66-Ala67 in VAMP2). Unlike other BoNTs, BoNT/X is the only toxin that also cleaves non-canonical substrates VAMP4, VAMP5, and Ykt6. The family also includes Enterococcus botulinum-like toxin eBoNT/J and Paraclostridium bifermentans mosquitocidal protein 1 (PMP1). eBoNT/J might be a precursor of a toxin that binds to an unknown eukaryotic cell receptor(s) and be taken up into the host cell via the endocytic pathway. It strongly resembles a botulinum-type toxin, with the appropriate domains and residues to have proteolytic function, although its C-terminus (which binds to a eukaryotic host cell) is different enough from clostrial botulinum toxins that it might bind another cell target. eBoNT/J shows no toxicity to mice, although it cleaves human VAMP-2 and SNAP-25 in neurons. PMP1 is a clostridial-like neurotoxin that selectively targets anopheline mosquitoes. It cleaves mosquito syntaxin but does not cleave human syntaxin despite the cleavage site being conserved. PMP1 is not implicated in toxicity, although it has conserved SxWY motif. Members in this family comprise three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). The HCR domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. It is a proven target for anti-BoNT antibody and vaccine development. This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467775 Cd Length: 188 Bit Score: 54.58 E-value: 1.52e-08
|
||||||||
| Toxin_R_bind_C_BoNTE | cd23392 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum ... |
272-466 | 4.64e-07 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum neurotoxin type E (BoNT/E) and similar proteins; BoNT/E, also called bontoxilysin-E, is botulinum toxin that causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. There are two co-receptors of BoNT/E precursor, complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles (e.g. synaptic vesicle protein 2). BoNT/E comprises three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). The HCR domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. It is a proven target for anti-BoNT antibody and vaccine development. This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467771 Cd Length: 177 Bit Score: 49.99 E-value: 4.64e-07
|
||||||||
| Toxin_R_bind_C_BoNTF | cd23393 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum ... |
272-466 | 3.23e-05 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum neurotoxin type F (BoNT/F) and similar proteins; BoNT/F, also called bontoxilysin-F, is botulinum toxin that causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. There are two co-receptors of BoNT/F precursor, complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. BoNT/F was reported to bind synaptic vesicle protein 2 (SV2), but the functional relevance of SV2 for BoNT/F remains to be established. BoNT/F comprises three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). The HCR domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. It is a proven target for anti-BoNT antibody and vaccine development. This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467772 Cd Length: 184 Bit Score: 44.51 E-value: 3.23e-05
|
||||||||
| Toxin_R_bind_C_BoNTC | cd23390 | C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum ... |
272-361 | 6.14e-03 | ||||
C-terminal receptor binding domain, beta-trefoil fold, found in Clostridium botulinum neurotoxin type C (BoNT/C) and similar proteins; BoNT/C, also called bontoxilysin-C1, is botulinum toxin that causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of the eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. BoNT/C is unique among characterized BoNTs in having 2 substrates, syntaxin (STX) and SNAP25. Unlike most BoNTs, precursor of BoNT/C seems not to have a proteinaceous co-receptor, and instead recognizes 2 different complex polysialylated gangliosides found on neural tissue probably in synaptic vesicles. Moreover, BoNT/C usually does not cause diseases in humans, but type C strains can be responsible for infant botulism. It has been shown to be a suitable drug for the treatment of dystonia. BoNT/C comprises three domains which are involved in catalysis (LC), translocation (HCT), and host receptor binding (HCR). The HCR domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. It is a proven target for anti-BoNT antibody and vaccine development. This model corresponds to C-terminal HCR domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Pssm-ID: 467769 Cd Length: 188 Bit Score: 37.74 E-value: 6.14e-03
|
||||||||
| Blast search parameters | ||||
|
