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Conserved domains on  [gi|2150810581|gb|UEX91591|]
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ATP synthase CF0 B subunit (chloroplast) [Acer pseudoplatanus]

Protein Classification

ATP synthase subunit b( domain architecture ID 10000014)

ATP synthase subunit b is a component of the Fo complex of FoF1-ATP synthase found in chloroplasts, and which acts as a stator to prevent certain subunits from rotating with the central rotary element

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
atpF CHL00019
ATP synthase CF0 B subunit
 1-184 6.80e-95

ATP synthase CF0 B subunit


:

Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 273.28  E-value: 6.80e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581   1 MKNITDSFVSLVRWSFAGSFGFNTDILATNPINLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEK 80
Cdd:CHL00019    1 MKNVTDSFVSLGHWPSAGSFGFNTDILETNLINLSVVLGVLIYFGKGVLSDLLDNRKQTILNTIRNSEERREEAIEKLEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  81 ARARLRKVEREADQFRVNGYSEIEREKLNLIKSTYKTLEELENYKNETIRFDHQRAIQQVRQQVFQQVLKGARGTLNSSL 160
Cdd:CHL00019   81 ARARLRQAELEADEIRVNGYSEIEREKENLINQAKEDLERLENYKNETIRFEQQRAINQVRQQVFQLALQRALGTLNSCL 160

                         170       180
                  ....*....|....*....|....
gi 2150810581 161 NKELHLRTVSENIDTFEAMAEITD 184
Cdd:CHL00019  161 NNELHLRTINANIGLLGAMKEITD 184
 
Name Accession Description Interval E-value
atpF CHL00019
ATP synthase CF0 B subunit
 1-184 6.80e-95

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 273.28  E-value: 6.80e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581   1 MKNITDSFVSLVRWSFAGSFGFNTDILATNPINLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEK 80
Cdd:CHL00019    1 MKNVTDSFVSLGHWPSAGSFGFNTDILETNLINLSVVLGVLIYFGKGVLSDLLDNRKQTILNTIRNSEERREEAIEKLEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  81 ARARLRKVEREADQFRVNGYSEIEREKLNLIKSTYKTLEELENYKNETIRFDHQRAIQQVRQQVFQQVLKGARGTLNSSL 160
Cdd:CHL00019   81 ARARLRQAELEADEIRVNGYSEIEREKENLINQAKEDLERLENYKNETIRFEQQRAINQVRQQVFQLALQRALGTLNSCL 160

                         170       180
                  ....*....|....*....|....
gi 2150810581 161 NKELHLRTVSENIDTFEAMAEITD 184
Cdd:CHL00019  161 NNELHLRTINANIGLLGAMKEITD 184
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 26-157 1.27e-21

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 85.06  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  26 ILATNPINLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEKARARLRKVEREADQFRVNGYSEIER 105
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2150810581 106 EKLNLIKSTYKTLEELENYKNETIRFDHQRAIQQVRQQVFQQVLKGARGTLN 157
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 26-139 4.71e-11

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.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 57.45  E-value: 4.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  26 ILATNPINLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEKARARLRKVEREADQFRVNGYSEIER 105
Cdd:cd06503     1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2150810581 106 EKLNLIKSTYKTLEELENYKNETIRFDHQRAIQQ 139
Cdd:cd06503    81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAE 114
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 32-174 8.36e-05

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.93  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  32 INLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEKARARLRKVEREADQFRVNGYSEIEREKLNLI 111
Cdd:COG0711     8 INFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2150810581 112 KSTYKTLEELENYKNETIRFDHQRAIQQVRQQVFQQVLKGARGTLNSSLNKELHLRTVSENID 174
Cdd:COG0711    88 AEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIA 150
 
Name Accession Description Interval E-value
atpF CHL00019
ATP synthase CF0 B subunit
 1-184 6.80e-95

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 273.28  E-value: 6.80e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581   1 MKNITDSFVSLVRWSFAGSFGFNTDILATNPINLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEK 80
Cdd:CHL00019    1 MKNVTDSFVSLGHWPSAGSFGFNTDILETNLINLSVVLGVLIYFGKGVLSDLLDNRKQTILNTIRNSEERREEAIEKLEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  81 ARARLRKVEREADQFRVNGYSEIEREKLNLIKSTYKTLEELENYKNETIRFDHQRAIQQVRQQVFQQVLKGARGTLNSSL 160
Cdd:CHL00019   81 ARARLRQAELEADEIRVNGYSEIEREKENLINQAKEDLERLENYKNETIRFEQQRAINQVRQQVFQLALQRALGTLNSCL 160

                         170       180
                  ....*....|....*....|....
gi 2150810581 161 NKELHLRTVSENIDTFEAMAEITD 184
Cdd:CHL00019  161 NNELHLRTINANIGLLGAMKEITD 184
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 26-157 1.27e-21

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 85.06  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  26 ILATNPINLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEKARARLRKVEREADQFRVNGYSEIER 105
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2150810581 106 EKLNLIKSTYKTLEELENYKNETIRFDHQRAIQQVRQQVFQQVLKGARGTLN 157
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 17-177 9.10e-20

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 81.54  E-value: 9.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  17 AGSFGFNTDILATNPINLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEKARARLRKVEREADQFR 96
Cdd:PRK07352   12 EGGFGLNLNLLETNLINLAIVIGLLYYFGRGFLGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  97 VNGYSEIEREKLNLIKSTYKTLEELENYKNETIRFDHQRAIQQVRQQVFQQVLKGARGTLNSSLNKELHLRTVSENIDTF 176
Cdd:PRK07352   92 ADAKARAEAIRAEIEKQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDRSIANL 171


                  .
gi 2150810581 177 E 177
Cdd:PRK07352  172 G 172
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 26-139 4.71e-11

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.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 57.45  E-value: 4.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  26 ILATNPINLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEKARARLRKVEREADQFRVNGYSEIER 105
Cdd:cd06503     1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2150810581 106 EKLNLIKSTYKTLEELENYKNETIRFDHQRAIQQ 139
Cdd:cd06503    81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAE 114
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 32-174 8.36e-05

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.93  E-value: 8.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2150810581  32 INLSVVLGVLIFFGKGVRSDLLDNRKRKILNTIRNSEELQGGAIQRLEKARARLRKVEREADQFRVNGYSEIEREKLNLI 111
Cdd:COG0711     8 INFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2150810581 112 KSTYKTLEELENYKNETIRFDHQRAIQQVRQQVFQQVLKGARGTLNSSLNKELHLRTVSENID 174
Cdd:COG0711    88 AEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIA 150
 
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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