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Conserved domains on  [gi|33150714|gb|AAP97235|]
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ATP synthase inhibitor protein [Homo sapiens]

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 ...
36-87 2.25e-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: 62.96  E-value: 2.25e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 33150714    36 GAGSIREAGGAFGKREQAEEERYFRAQSREQLAALKKH------HEEEIVHHKKEIER 87
Cdd:pfam04568  41 GGGSIRSAGGAFGKREAAHEEEYIRQREAEKLATLKEKlaeqreHLQELEHHIEAITR 98
 
Name Accession Description Interval E-value
IATP pfam04568
Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from ...
36-87 2.25e-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: 62.96  E-value: 2.25e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 33150714    36 GAGSIREAGGAFGKREQAEEERYFRAQSREQLAALKKH------HEEEIVHHKKEIER 87
Cdd:pfam04568  41 GGGSIRSAGGAFGKREAAHEEEYIRQREAEKLATLKEKlaeqreHLQELEHHIEAITR 98
 
Name Accession Description Interval E-value
IATP pfam04568
Mitochondrial ATPase inhibitor, IATP; ATP synthase inhibitor prevents the enzyme from ...
36-87 2.25e-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: 62.96  E-value: 2.25e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 33150714    36 GAGSIREAGGAFGKREQAEEERYFRAQSREQLAALKKH------HEEEIVHHKKEIER 87
Cdd:pfam04568  41 GGGSIRSAGGAFGKREAAHEEEYIRQREAEKLATLKEKlaeqreHLQELEHHIEAITR 98
LCD1 pfam09798
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ...
61-103 7.38e-03

DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.


Pssm-ID: 462906  Cd Length: 615  Bit Score: 34.22  E-value: 7.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 33150714    61 AQSREQLAALKKHHEEEIVHHKKEIERLQKEIERHKQKIKMLK 103
Cdd:pfam09798  11 QEKEKELEKLKNSYEELKSSHEEELEKLKQEVQKLEDEKKFLL 53
LCD1 pfam09798
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ...
52-91 8.05e-03

DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.


Pssm-ID: 462906  Cd Length: 615  Bit Score: 34.22  E-value: 8.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 33150714    52 QAEEERyfrAQSREQLAALKKHHEEEIVHHKKEIERLQKE 91
Cdd:pfam09798  12 EKEKEL---EKLKNSYEELKSSHEEELEKLKQEVQKLEDE 48
 
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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