Chain C, ATPASE INHIBITOR
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| IATP super family | cl04596 | Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from ... |
11-62 | 1.78e-10 | ||
Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from switching to ATP hydrolysis during collapse of the electrochemical gradient, for example during oxygen deprivation ATP synthase inhibitor forms a one to one complex with the F1 ATPase, possibly by binding at the alpha-beta interface. It is thought to inhibit ATP synthesis by preventing the release of ATP. The minimum inhibitory region for bovine inhibitor is from residues 39 to 72. The inhibitor has two oligomeric states, dimer (the active state) and tetramer. At low pH, the inhibitor forms a dimer via antiparallel coiled coil interactions between the C terminal regions of two monomers. At high pH, the inhibitor forms tetramers and higher oligomers by coiled coil interactions involving the N terminus and inhibitory region, thus preventing the inhibitory activity. The actual alignment was detected with superfamily member pfam04568: Pssm-ID: 428014 Cd Length: 98 Bit Score: 52.18 E-value: 1.78e-10
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| Name | Accession | Description | Interval | E-value | ||
| IATP | pfam04568 | Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from ... |
11-62 | 1.78e-10 | ||
Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from switching to ATP hydrolysis during collapse of the electrochemical gradient, for example during oxygen deprivation ATP synthase inhibitor forms a one to one complex with the F1 ATPase, possibly by binding at the alpha-beta interface. It is thought to inhibit ATP synthesis by preventing the release of ATP. The minimum inhibitory region for bovine inhibitor is from residues 39 to 72. The inhibitor has two oligomeric states, dimer (the active state) and tetramer. At low pH, the inhibitor forms a dimer via antiparallel coiled coil interactions between the C terminal regions of two monomers. At high pH, the inhibitor forms tetramers and higher oligomers by coiled coil interactions involving the N terminus and inhibitory region, thus preventing the inhibitory activity. Pssm-ID: 428014 Cd Length: 98 Bit Score: 52.18 E-value: 1.78e-10
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| Name | Accession | Description | Interval | E-value | ||
| IATP | pfam04568 | Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from ... |
11-62 | 1.78e-10 | ||
Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from switching to ATP hydrolysis during collapse of the electrochemical gradient, for example during oxygen deprivation ATP synthase inhibitor forms a one to one complex with the F1 ATPase, possibly by binding at the alpha-beta interface. It is thought to inhibit ATP synthesis by preventing the release of ATP. The minimum inhibitory region for bovine inhibitor is from residues 39 to 72. The inhibitor has two oligomeric states, dimer (the active state) and tetramer. At low pH, the inhibitor forms a dimer via antiparallel coiled coil interactions between the C terminal regions of two monomers. At high pH, the inhibitor forms tetramers and higher oligomers by coiled coil interactions involving the N terminus and inhibitory region, thus preventing the inhibitory activity. Pssm-ID: 428014 Cd Length: 98 Bit Score: 52.18 E-value: 1.78e-10
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