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Conserved domains on  [gi|1034583842|ref|XP_016875885|]
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dachshund homolog 1 isoform X3 [Homo sapiens]

Protein Classification

ATP synthase subunit B family protein( domain architecture ID 229537)

ATP synthase subunit B family protein such as subunits b and b' from the F(o) complex in F-type ATP synthase (FoF1-ATPase) found in chloroplasts and in bacterial plasma membranes; the b subunits are part of the peripheral stalk that links the F(1) and F(o) complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element

EC:  7.1.2.2
Gene Ontology:  GO:0045263|GO:0046933|GO:0015986
PubMed:  30901262|29074581|30240940|15473999
SCOP:  4002710

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_b super family cl21478
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 274-389 3.84e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


The actual alignment was detected with superfamily member CHL00019:

Pssm-ID: 473877 [Multi-domain]  Cd Length: 184  Bit Score: 38.31  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034583842 274 LSSI-----ETLLTNIQ---GLLKVAIDnaRAQEKQVQLEKTELKMDflrerELREtlEKQLAMEQKNRAIVQKRLKKEK 345
Cdd:CHL00019   49 LSDLldnrkQTILNTIRnseERREEAIE--KLEKARARLRQAELEAD-----EIRV--NGYSEIEREKENLINQAKEDLE 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034583842 346 KAKRKLQEALEFETKR-REQAEQTLKQAASTDSLRVLNDSLTPEI 389
Cdd:CHL00019  120 RLENYKNETIRFEQQRaINQVRQQVFQLALQRALGTLNSCLNNEL 164
 
Name Accession Description Interval E-value
atpF CHL00019
ATP synthase CF0 B subunit
 274-389 3.84e-03

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 38.31  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034583842 274 LSSI-----ETLLTNIQ---GLLKVAIDnaRAQEKQVQLEKTELKMDflrerELREtlEKQLAMEQKNRAIVQKRLKKEK 345
Cdd:CHL00019   49 LSDLldnrkQTILNTIRnseERREEAIE--KLEKARARLRQAELEAD-----EIRV--NGYSEIEREKENLINQAKEDLE 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034583842 346 KAKRKLQEALEFETKR-REQAEQTLKQAASTDSLRVLNDSLTPEI 389
Cdd:CHL00019  120 RLENYKNETIRFEQQRaINQVRQQVFQLALQRALGTLNSCLNNEL 164
 
Name Accession Description Interval E-value
atpF CHL00019
ATP synthase CF0 B subunit
 274-389 3.84e-03

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 38.31  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034583842 274 LSSI-----ETLLTNIQ---GLLKVAIDnaRAQEKQVQLEKTELKMDflrerELREtlEKQLAMEQKNRAIVQKRLKKEK 345
Cdd:CHL00019   49 LSDLldnrkQTILNTIRnseERREEAIE--KLEKARARLRQAELEAD-----EIRV--NGYSEIEREKENLINQAKEDLE 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1034583842 346 KAKRKLQEALEFETKR-REQAEQTLKQAASTDSLRVLNDSLTPEI 389
Cdd:CHL00019  120 RLENYKNETIRFEQQRaINQVRQQVFQLALQRALGTLNSCLNNEL 164
 
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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