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Conserved domains on  [gi|1851233220|gb|KAF5120624|]
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hypothetical protein DV495_004495 [Geotrichum candidum]

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 ...
70-230 7.13e-49

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: 157.82  E-value: 7.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233220  70 IYTISNGLYVVNAETCIAGVFGVLVLLASKTVAPAYKEWADTYISNVKKVLNQARETHTLAVKERIESVSLAKDVVPITQ 149
Cdd:pfam05405   3 AYLSSKEIYVVNEETIVALCFIGFLIFVYKSLGPSIKEWLDKRIEKIQDELNQSRNLHEEALKERIEQVKKLQSVVELTK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233220 150 SLFAVSKETAELEAEAFVLKQKVDFAAEAKSVLDSWVRYEAQVRKREQQALAESVIAKVNKQLGDNKFQKQILAQAVADV 229
Cdd:pfam05405  83 VLFVVSKETVALEAEAFERELQAALAREIKSKLDTLVRKESSRRQREQDHLVNWVISSVLKELSTPKFQKESLQESIADL 162

                  .
gi 1851233220 230 E 230
Cdd:pfam05405 163 E 163
 
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 ...
70-230 7.13e-49

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: 157.82  E-value: 7.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233220  70 IYTISNGLYVVNAETCIAGVFGVLVLLASKTVAPAYKEWADTYISNVKKVLNQARETHTLAVKERIESVSLAKDVVPITQ 149
Cdd:pfam05405   3 AYLSSKEIYVVNEETIVALCFIGFLIFVYKSLGPSIKEWLDKRIEKIQDELNQSRNLHEEALKERIEQVKKLQSVVELTK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233220 150 SLFAVSKETAELEAEAFVLKQKVDFAAEAKSVLDSWVRYEAQVRKREQQALAESVIAKVNKQLGDNKFQKQILAQAVADV 229
Cdd:pfam05405  83 VLFVVSKETVALEAEAFERELQAALAREIKSKLDTLVRKESSRRQREQDHLVNWVISSVLKELSTPKFQKESLQESIADL 162

                  .
gi 1851233220 230 E 230
Cdd:pfam05405 163 E 163
 
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 ...
70-230 7.13e-49

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: 157.82  E-value: 7.13e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233220  70 IYTISNGLYVVNAETCIAGVFGVLVLLASKTVAPAYKEWADTYISNVKKVLNQARETHTLAVKERIESVSLAKDVVPITQ 149
Cdd:pfam05405   3 AYLSSKEIYVVNEETIVALCFIGFLIFVYKSLGPSIKEWLDKRIEKIQDELNQSRNLHEEALKERIEQVKKLQSVVELTK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851233220 150 SLFAVSKETAELEAEAFVLKQKVDFAAEAKSVLDSWVRYEAQVRKREQQALAESVIAKVNKQLGDNKFQKQILAQAVADV 229
Cdd:pfam05405  83 VLFVVSKETVALEAEAFERELQAALAREIKSKLDTLVRKESSRRQREQDHLVNWVISSVLKELSTPKFQKESLQESIADL 162

                  .
gi 1851233220 230 E 230
Cdd:pfam05405 163 E 163
 
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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