ATP12 family chaperone protein similar to Homo sapiens ATP synthase mitochondrial F1 complex assembly factor 2 that may play a role in the assembly of the F1 component of the mitochondrial ATP synthase (ATPase)
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ...
46-265
3.61e-65
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.
The actual alignment was detected with superfamily member COG5387:
Pssm-ID: 470498 Cd Length: 235 Bit Score: 203.88 E-value: 3.61e-65
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ...
48-166
8.49e-55
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.
Pssm-ID: 462201 Cd Length: 121 Bit Score: 173.44 E-value: 8.49e-55
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ...
48-166
8.49e-55
ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesized as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.
Pssm-ID: 462201 Cd Length: 121 Bit Score: 173.44 E-value: 8.49e-55
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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