Chain A, Lethal factor
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Anthrax-tox_M super family | cl48044 | Anthrax toxin lethal factor, middle domain; Members of this family, which are predominantly ... |
2-287 | 4.58e-132 | |||||
Anthrax toxin lethal factor, middle domain; Members of this family, which are predominantly found in anthrax toxin lethal factor, adopt a structure consisting of a core of antiparallel beta sheets and alpha helices. They form a long deep groove within the protein that anchors the 16-residue N-terminal tail of MAPKK-2 before cleavage. It has been noted that this domain resembles the ADP-ribosylating toxin from Bacillus cereus, but the active site has been modified to augment substrate recognition. The actual alignment was detected with superfamily member pfam09156: Pssm-ID: 462694 Cd Length: 286 Bit Score: 384.91 E-value: 4.58e-132
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| ATLF super family | cl08465 | Anthrax toxin lethal factor, N- and C-terminal domain; The C-terminal domain is the ... |
293-514 | 2.61e-66 | |||||
Anthrax toxin lethal factor, N- and C-terminal domain; The C-terminal domain is the catalytically active domain whereas the N-terminal domain is likely to be inactive. The actual alignment was detected with superfamily member pfam07737: Pssm-ID: 285037 Cd Length: 218 Bit Score: 213.70 E-value: 2.61e-66
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| Name | Accession | Description | Interval | E-value | |||||
| Anthrax-tox_M | pfam09156 | Anthrax toxin lethal factor, middle domain; Members of this family, which are predominantly ... |
2-287 | 4.58e-132 | |||||
Anthrax toxin lethal factor, middle domain; Members of this family, which are predominantly found in anthrax toxin lethal factor, adopt a structure consisting of a core of antiparallel beta sheets and alpha helices. They form a long deep groove within the protein that anchors the 16-residue N-terminal tail of MAPKK-2 before cleavage. It has been noted that this domain resembles the ADP-ribosylating toxin from Bacillus cereus, but the active site has been modified to augment substrate recognition. Pssm-ID: 462694 Cd Length: 286 Bit Score: 384.91 E-value: 4.58e-132
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| ATLF | pfam07737 | Anthrax toxin lethal factor, N- and C-terminal domain; The C-terminal domain is the ... |
293-514 | 2.61e-66 | |||||
Anthrax toxin lethal factor, N- and C-terminal domain; The C-terminal domain is the catalytically active domain whereas the N-terminal domain is likely to be inactive. Pssm-ID: 285037 Cd Length: 218 Bit Score: 213.70 E-value: 2.61e-66
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| M34_peptidase | cd20171 | Peptidase family M34 includes the C-terminal catalytic domain of anthrax lethal factor (ATLF), ... |
356-508 | 9.60e-56 | |||||
Peptidase family M34 includes the C-terminal catalytic domain of anthrax lethal factor (ATLF), the protective antigen-binding domains of ATLF and edema factor, and Pro-Pro endopeptidase; Peptidase family M34 (also known as the anthrax lethal factor family) includes the C-terminal catalytic domain of anthrax lethal factor (ATLF, EC 3.4.24.83), and the N-terminal protective antigen-binding domains (PABDs) of ATLF and edema factor (EF). ATLF and EF are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). At its N-terminus, ATLF has a PABD domain which lacks the hallmark metalloprotease motif HEXXH, and, at its C-terminus, the related catalytic domain has the HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. EF acts as a Ca2+- and calmodulin-dependent adenylyl cyclase that can cause edema when associated with PA. EF is comprised of the PABD and an adenylyl cyclase domain. This family also includes Pro-Pro endopeptidase (PPEP-1; EC 3.4.24.89, also known as Zmp1) which is an extracellular metalloprotease that shows a unique specificity for hydrolyzing a Pro-Pro bond and is involved in bacterial adhesion. Pssm-ID: 380332 Cd Length: 156 Bit Score: 183.67 E-value: 9.60e-56
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| VIP2 | cd00233 | VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ... |
126-288 | 4.37e-04 | |||||
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative insecticidal proteins (VIPs) possesses high specificity against the major insect pest, corn rootworms, and belongs to a classs of binary toxins and regulators of biological pathways distinct from classical A-B toxins. A novel family of insecticidal ADP-ribosyltransferses were isolated from Bacillus cereus during vegetative growth, where VIP1 likely targets insect cells and VIP2 ribosylates actin. VIP2 shares significant sequence similarity with enzymatic components of other binary toxins, Clostridium botulinum C2 toxin, C. perfringens iota toxin, C. piroforme toxin, C. piroforme toxin and C. difficile toxin. Pssm-ID: 238144 [Multi-domain] Cd Length: 201 Bit Score: 41.62 E-value: 4.37e-04
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| Name | Accession | Description | Interval | E-value | |||||
| Anthrax-tox_M | pfam09156 | Anthrax toxin lethal factor, middle domain; Members of this family, which are predominantly ... |
2-287 | 4.58e-132 | |||||
Anthrax toxin lethal factor, middle domain; Members of this family, which are predominantly found in anthrax toxin lethal factor, adopt a structure consisting of a core of antiparallel beta sheets and alpha helices. They form a long deep groove within the protein that anchors the 16-residue N-terminal tail of MAPKK-2 before cleavage. It has been noted that this domain resembles the ADP-ribosylating toxin from Bacillus cereus, but the active site has been modified to augment substrate recognition. Pssm-ID: 462694 Cd Length: 286 Bit Score: 384.91 E-value: 4.58e-132
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| Anthrax-tox_M | pfam09156 | Anthrax toxin lethal factor, middle domain; Members of this family, which are predominantly ... |
4-289 | 5.06e-132 | |||||
Anthrax toxin lethal factor, middle domain; Members of this family, which are predominantly found in anthrax toxin lethal factor, adopt a structure consisting of a core of antiparallel beta sheets and alpha helices. They form a long deep groove within the protein that anchors the 16-residue N-terminal tail of MAPKK-2 before cleavage. It has been noted that this domain resembles the ADP-ribosylating toxin from Bacillus cereus, but the active site has been modified to augment substrate recognition. Pssm-ID: 462694 Cd Length: 286 Bit Score: 384.91 E-value: 5.06e-132
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| ATLF | pfam07737 | Anthrax toxin lethal factor, N- and C-terminal domain; The C-terminal domain is the ... |
293-514 | 2.61e-66 | |||||
Anthrax toxin lethal factor, N- and C-terminal domain; The C-terminal domain is the catalytically active domain whereas the N-terminal domain is likely to be inactive. Pssm-ID: 285037 Cd Length: 218 Bit Score: 213.70 E-value: 2.61e-66
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| M34_peptidase | cd20171 | Peptidase family M34 includes the C-terminal catalytic domain of anthrax lethal factor (ATLF), ... |
356-508 | 9.60e-56 | |||||
Peptidase family M34 includes the C-terminal catalytic domain of anthrax lethal factor (ATLF), the protective antigen-binding domains of ATLF and edema factor, and Pro-Pro endopeptidase; Peptidase family M34 (also known as the anthrax lethal factor family) includes the C-terminal catalytic domain of anthrax lethal factor (ATLF, EC 3.4.24.83), and the N-terminal protective antigen-binding domains (PABDs) of ATLF and edema factor (EF). ATLF and EF are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). At its N-terminus, ATLF has a PABD domain which lacks the hallmark metalloprotease motif HEXXH, and, at its C-terminus, the related catalytic domain has the HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. EF acts as a Ca2+- and calmodulin-dependent adenylyl cyclase that can cause edema when associated with PA. EF is comprised of the PABD and an adenylyl cyclase domain. This family also includes Pro-Pro endopeptidase (PPEP-1; EC 3.4.24.89, also known as Zmp1) which is an extracellular metalloprotease that shows a unique specificity for hydrolyzing a Pro-Pro bond and is involved in bacterial adhesion. Pssm-ID: 380332 Cd Length: 156 Bit Score: 183.67 E-value: 9.60e-56
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| M34_ATLF_C-like | cd20493 | C-terminal catalytically active domain of anthrax toxin lethal factor and similar domains; ... |
293-508 | 1.05e-55 | |||||
C-terminal catalytically active domain of anthrax toxin lethal factor and similar domains; belongs to peptidase family M34; This subfamily includes the C-terminal catalytic domain of anthrax toxin lethal factor (ATLF; EC 3.4.24.83). ATLF and edema factor are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is secreted by Bacillus anthracis to promote disease virulence through disruption of host signaling pathways. ATLF belongs to peptidase family M34 and has the hallmark metalloprotease motif HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). MKKs are cleaved by ATLF near their N-termini, removing the docking sequence for the downstream cognate mitogen-activated protein kinase. Preferred amino acids around the cleavage site can be denoted BBBBxHxH, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. At its N-terminus, ATLF has a related PABD domain which lacks the hallmark metalloprotease motif HEXXH. This subfamily also includes Bacillus thuringiensis Vip2Ac-like_2 which belongs to the Vip family of proteins that are secreted during the vegetative growth phase. Pssm-ID: 380336 Cd Length: 208 Bit Score: 185.61 E-value: 1.05e-55
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| M34_peptidase_like | cd20184 | uncharacterized subfamily of peptidase family M34; Peptidase family M34 (also known as the ... |
396-508 | 4.63e-16 | |||||
uncharacterized subfamily of peptidase family M34; Peptidase family M34 (also known as the anthrax lethal factor family) includes the C-terminal catalytic domain of anthrax lethal factor (ATLF, EC 3.4.24.83), and the N-terminal protective antigen-binding domains (PABDs) of ATLF and edema factor (EF). ATLF and EF are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). At its N-terminus, ATLF has a PABD domain which lacks the hallmark metalloprotease motif HEXXH, and, at its C-terminus, the related catalytic domain has the HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. EF acts as a Ca2+- and calmodulin-dependent adenylyl cyclase that can cause edema when associated with PA; it is comprised of the PABD and an adenylyl cyclase domain. Pro-Pro endopeptidase (PPEP-1; EC 3.4.24.89, also known as Zmp1) is an extracellular metalloprotease that shows a unique specificity for hydrolyzing a Pro-Pro bond and is involved in bacterial adhesion. This uncharacterized subfamily includes proteins which have an N-terminal SLH domain, and proteins which may have an N-terminal IG-like domain; these proteins have the hallmark metalloprotease motif HEXXH motif. Pssm-ID: 380334 Cd Length: 131 Bit Score: 74.63 E-value: 4.63e-16
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| M34_PPEP | cd20183 | Pro-Pro endopeptidase (PPEP) and similar proteins; belongs to peptidase family M34; This ... |
425-507 | 5.62e-09 | |||||
Pro-Pro endopeptidase (PPEP) and similar proteins; belongs to peptidase family M34; This subfamily includes the enzyme Pro-Pro endopeptidase (PPEP-1, EC 3.4.24.89, also known as Zmp1 (Clostridium difficile-type)), an extracellular metalloprotease showing a unique specificity for hydrolyzing a Pro-Pro bond. It belongs to peptidase family M34 and has the hallmark metalloprotease motif HEXXH, where the two His residues bind a single zinc atom, and the Glu has a catalytic role. PPEP-1 cleaves two C. difficile cell surface proteins (CD2831 and CD3246) involved in adhesion, one of which is encoded by the gene adjacent to the ppep-1 gene. There are multiple PPEP-1 cleavage sites located just above the site of attachment to the peptidoglycan layer. PPEP-1 may play a role in switching from an adhesive to a motile phenotype. Also included in this subfamily is Paenibacillus alvei PPEP-2, a secreted Pro-Pro endopeptidase. The cleavage motif of PPEP-2, PLP PVP, is distinct from that of PPEP-1 (VNP PVP). PPEP-2 cleavage sites in a cell-surface protein, with putative extracellular matrix-binding domains, and encoded by the adjacent gene, suggests a similar role of PPEP-2 in controlling bacterial adhesion. Pssm-ID: 380333 Cd Length: 184 Bit Score: 55.55 E-value: 5.62e-09
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| ADPrib_exo_Tox | pfam03496 | ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ... |
125-291 | 1.40e-06 | |||||
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ADP-ribosyltransferases, where, in Swiss:Q93Q17, E403 is the catalytic residue and E401 contributes to the transfer of ADP-ribose to the target protein. In clostridial species it is actin that is being ADP-ribosylated; this result is lethal and dermonecrotic in infected mammals. Pssm-ID: 427336 [Multi-domain] Cd Length: 199 Bit Score: 48.90 E-value: 1.40e-06
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| VIP2 | cd00233 | VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ... |
126-288 | 4.37e-04 | |||||
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative insecticidal proteins (VIPs) possesses high specificity against the major insect pest, corn rootworms, and belongs to a classs of binary toxins and regulators of biological pathways distinct from classical A-B toxins. A novel family of insecticidal ADP-ribosyltransferses were isolated from Bacillus cereus during vegetative growth, where VIP1 likely targets insect cells and VIP2 ribosylates actin. VIP2 shares significant sequence similarity with enzymatic components of other binary toxins, Clostridium botulinum C2 toxin, C. perfringens iota toxin, C. piroforme toxin, C. piroforme toxin and C. difficile toxin. Pssm-ID: 238144 [Multi-domain] Cd Length: 201 Bit Score: 41.62 E-value: 4.37e-04
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