mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
38-162
1.08e-33
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain. In bacteria, which is lacking a eukaryotic epsilon subunit homolog, this subunit is called the epsilon subunit.
:
Pssm-ID: 213395 [Multi-domain] Cd Length: 123 Bit Score: 115.30 E-value: 1.08e-33
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
38-162
1.08e-33
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain. In bacteria, which is lacking a eukaryotic epsilon subunit homolog, this subunit is called the epsilon subunit.
Pssm-ID: 213395 [Multi-domain] Cd Length: 123 Bit Score: 115.30 E-value: 1.08e-33
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
38-168
1.32e-22
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP synthase, epsilon subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440124 [Multi-domain] Cd Length: 131 Bit Score: 87.17 E-value: 1.32e-22
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
44-168
2.13e-15
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five types of subunits in the F1 part of F1/F0 ATP synthases. Members of this family are designated epsilon in bacterial and chloroplast systems but designated delta in mitochondria, where the counterpart of the bacterial delta subunit is designated OSCP. In a few cases (Propionigenium modestum, Acetobacterium woodii) scoring above the trusted cutoff and designated here as exceptions, Na+ replaces H+ for translocation. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273506 [Multi-domain] Cd Length: 130 Bit Score: 68.43 E-value: 2.13e-15
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
38-119
2.49e-14
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These subunits are part of the head unit of the ATP synthase. The subunit is called epsilon in bacteria and delta in mitochondria. In bacteria the delta (D) subunit is equivalent to the mitochondrial Oligomycin sensitive subunit, OSCP (pfam00213).
Pssm-ID: 460714 [Multi-domain] Cd Length: 80 Bit Score: 64.38 E-value: 2.49e-14
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
38-162
1.08e-33
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain. In bacteria, which is lacking a eukaryotic epsilon subunit homolog, this subunit is called the epsilon subunit.
Pssm-ID: 213395 [Multi-domain] Cd Length: 123 Bit Score: 115.30 E-value: 1.08e-33
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
38-168
1.32e-22
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP synthase, epsilon subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440124 [Multi-domain] Cd Length: 131 Bit Score: 87.17 E-value: 1.32e-22
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
44-168
2.13e-15
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five types of subunits in the F1 part of F1/F0 ATP synthases. Members of this family are designated epsilon in bacterial and chloroplast systems but designated delta in mitochondria, where the counterpart of the bacterial delta subunit is designated OSCP. In a few cases (Propionigenium modestum, Acetobacterium woodii) scoring above the trusted cutoff and designated here as exceptions, Na+ replaces H+ for translocation. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273506 [Multi-domain] Cd Length: 130 Bit Score: 68.43 E-value: 2.13e-15
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
38-119
2.49e-14
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These subunits are part of the head unit of the ATP synthase. The subunit is called epsilon in bacteria and delta in mitochondria. In bacteria the delta (D) subunit is equivalent to the mitochondrial Oligomycin sensitive subunit, OSCP (pfam00213).
Pssm-ID: 460714 [Multi-domain] Cd Length: 80 Bit Score: 64.38 E-value: 2.49e-14
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic ...
41-151
3.62e-06
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 epsilon subunit of this apparent second ATP synthase.
Pssm-ID: 132210 [Multi-domain] Cd Length: 122 Bit Score: 43.88 E-value: 3.62e-06
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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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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