DUF3800 domain-containing protein [Caenorhabditis elegans]
Protein Classification
ATP12 family chaperone protein( domain architecture ID 4941)
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)
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| ATP12 super family | cl02228 | ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ... |
1-61 | 3.24e-13 | ||
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 pfam07542: Pssm-ID: 470498 Cd Length: 121 Bit Score: 62.89 E-value: 3.24e-13
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| Name | Accession | Description | Interval | E-value | ||
| ATP12 | pfam07542 | ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ... |
1-61 | 3.24e-13 | ||
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: 62.89 E-value: 3.24e-13
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| Name | Accession | Description | Interval | E-value | ||
| ATP12 | pfam07542 | ATP12 chaperone protein; Mitochondrial F1-ATPase is an oligomeric enzyme composed of five ... |
1-61 | 3.24e-13 | ||
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: 62.89 E-value: 3.24e-13
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