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Conserved domains on  [gi|270267975|gb|ACZ65567|]
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ATP synthase subunit 4 (mitochondrion) [Zea mays]

Protein Classification

ATPase B chain family protein( domain architecture ID 10526936)

ATPase B chain family protein similar to human mitochondrial ATP synthase F(o) complex subunit B1 that is part of the membrane ATP synthase that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mt_ATP-synt_B pfam05405
Mitochondrial ATP synthase B chain precursor (ATP-synt_B); The Fo sector of the ATP synthase ...
 20-168 2.10e-57

Mitochondrial ATP synthase B chain precursor (ATP-synt_B); The Fo sector of the ATP synthase is a membrane bound complex which mediates proton transport. It is composed of nine different polypeptide subunits (a, b, c, d, e, f, g F6, A6L).


:

Pssm-ID: 368426 [Multi-domain]  Cd Length: 163  Bit Score: 179.01  E-value: 2.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267975   20 FICALSSKKILIYNEEMIVACCFIGFLILSRKSLGKTFKETLDGRIESIQESLQQFFNPNEVILEESNEQQRLLNLRISL 99
Cdd:pfam05405   1 LIAYLSSKEIYVVNEETIVALCFIGFLIFVYKSLGPSIKEWLDKRIEKIQDELNQSRNLHEEALKERIEQVKKLQSVVEL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 270267975  100 RICSTvkVVESLPAARCAPKCEKTVQALLCRNLNVKLATLLNAISSRRIRLQDDIVTGFHFSVSERLVS 168
Cdd:pfam05405  81 TKVLF--VVSKETVALEAEAFERELQAALAREIKSKLDTLVRKESSRRQREQDHLVNWVISSVLKELST 147
 
Name Accession Description Interval E-value
Mt_ATP-synt_B pfam05405
Mitochondrial ATP synthase B chain precursor (ATP-synt_B); The Fo sector of the ATP synthase ...
 20-168 2.10e-57

Mitochondrial ATP synthase B chain precursor (ATP-synt_B); The Fo sector of the ATP synthase is a membrane bound complex which mediates proton transport. It is composed of nine different polypeptide subunits (a, b, c, d, e, f, g F6, A6L).


Pssm-ID: 368426 [Multi-domain]  Cd Length: 163  Bit Score: 179.01  E-value: 2.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267975   20 FICALSSKKILIYNEEMIVACCFIGFLILSRKSLGKTFKETLDGRIESIQESLQQFFNPNEVILEESNEQQRLLNLRISL 99
Cdd:pfam05405   1 LIAYLSSKEIYVVNEETIVALCFIGFLIFVYKSLGPSIKEWLDKRIEKIQDELNQSRNLHEEALKERIEQVKKLQSVVEL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 270267975  100 RICSTvkVVESLPAARCAPKCEKTVQALLCRNLNVKLATLLNAISSRRIRLQDDIVTGFHFSVSERLVS 168
Cdd:pfam05405  81 TKVLF--VVSKETVALEAEAFERELQAALAREIKSKLDTLVRKESSRRQREQDHLVNWVISSVLKELST 147
 
Name Accession Description Interval E-value
Mt_ATP-synt_B pfam05405
Mitochondrial ATP synthase B chain precursor (ATP-synt_B); The Fo sector of the ATP synthase ...
 20-168 2.10e-57

Mitochondrial ATP synthase B chain precursor (ATP-synt_B); The Fo sector of the ATP synthase is a membrane bound complex which mediates proton transport. It is composed of nine different polypeptide subunits (a, b, c, d, e, f, g F6, A6L).


Pssm-ID: 368426 [Multi-domain]  Cd Length: 163  Bit Score: 179.01  E-value: 2.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270267975   20 FICALSSKKILIYNEEMIVACCFIGFLILSRKSLGKTFKETLDGRIESIQESLQQFFNPNEVILEESNEQQRLLNLRISL 99
Cdd:pfam05405   1 LIAYLSSKEIYVVNEETIVALCFIGFLIFVYKSLGPSIKEWLDKRIEKIQDELNQSRNLHEEALKERIEQVKKLQSVVEL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 270267975  100 RICSTvkVVESLPAARCAPKCEKTVQALLCRNLNVKLATLLNAISSRRIRLQDDIVTGFHFSVSERLVS 168
Cdd:pfam05405  81 TKVLF--VVSKETVALEAEAFERELQAALAREIKSKLDTLVRKESSRRQREQDHLVNWVISSVLKELST 147
 
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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