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Conserved domains on  [gi|6320020|ref|NP_010100|]
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ATPase inhibitor [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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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 ...
 4-85 3.93e-14

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: 61.42  E-value: 3.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320020     4 RSALARSLQLQRGVAARFYS-------EGSTGTPRGSGSE-------DSFVKRERATEDFFVRQREKEQLRHLKEQLEKQ 69
Cdd:pfam04568  3 RQTLAKTATASRPVSARSFSvaarrmgEGDSGAPKGGGGGgsirsagGAFGKREAAHEEEYIRQREAEKLATLKEKLAEQ 82

                         90
                 ....*....|....*.
gi 6320020    70 RKKIDSLENKIDSMTK 85
Cdd:pfam04568 83 REHLQELEHHIEAITR 98
 
Name Accession Description Interval E-value
IATP pfam04568
Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from ...
 4-85 3.93e-14

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: 61.42  E-value: 3.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320020     4 RSALARSLQLQRGVAARFYS-------EGSTGTPRGSGSE-------DSFVKRERATEDFFVRQREKEQLRHLKEQLEKQ 69
Cdd:pfam04568  3 RQTLAKTATASRPVSARSFSvaarrmgEGDSGAPKGGGGGgsirsagGAFGKREAAHEEEYIRQREAEKLATLKEKLAEQ 82

                         90
                 ....*....|....*.
gi 6320020    70 RKKIDSLENKIDSMTK 85
Cdd:pfam04568 83 REHLQELEHHIEAITR 98
 
Name Accession Description Interval E-value
IATP pfam04568
Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from ...
 4-85 3.93e-14

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: 61.42  E-value: 3.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320020     4 RSALARSLQLQRGVAARFYS-------EGSTGTPRGSGSE-------DSFVKRERATEDFFVRQREKEQLRHLKEQLEKQ 69
Cdd:pfam04568  3 RQTLAKTATASRPVSARSFSvaarrmgEGDSGAPKGGGGGgsirsagGAFGKREAAHEEEYIRQREAEKLATLKEKLAEQ 82

                         90
                 ....*....|....*.
gi 6320020    70 RKKIDSLENKIDSMTK 85
Cdd:pfam04568 83 REHLQELEHHIEAITR 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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