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Conserved domains on  [gi|122324596|sp|Q0BK80|]
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RecName: Full=ATP synthase subunit b; AltName: Full=ATP synthase F(0) sector subunit b; AltName: Full=ATPase subunit I; AltName: Full=F-type ATPase subunit b; Short=F-ATPase subunit b

Protein Classification

F0F1 ATP synthase subunit B( domain architecture ID 11481619)

F0F1 ATP synthase subunit B is part of the membrane proton channel of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane

Gene Ontology:  GO:0015986|GO:0015078|GO:0045263
PubMed:  7961438|15473999|15078220

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 4.14e-42

F0F1 ATP synthase subunit B; Validated


:

Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 137.21  E-value: 4.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   1 MDINITLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAY 80
Cdd:PRK05759   1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122324596  81 VRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV 156
Cdd:PRK05759  81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 4.14e-42

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 137.21  E-value: 4.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   1 MDINITLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAY 80
Cdd:PRK05759   1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122324596  81 VRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV 156
Cdd:PRK05759  81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 6-127 1.53e-26

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: 96.74  E-value: 1.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   6 TLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHK 85
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 122324596  86 VDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADL 122
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 10-156 1.40e-25

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 94.78  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   10 QMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQ 89
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122324596   90 AKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV 156
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 6-156 4.36e-25

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: 93.70  E-value: 4.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   6 TLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHK 85
Cdd:COG0711    2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122324596  86 VDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV 156
Cdd:COG0711   82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
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 ...
 6-127 2.43e-17

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: 73.12  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596    6 TLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHK 85
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 122324596   86 VDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVAL 122
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 4.14e-42

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 137.21  E-value: 4.14e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   1 MDINITLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAY 80
Cdd:PRK05759   1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122324596  81 VRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV 156
Cdd:PRK05759  81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 6-127 1.53e-26

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: 96.74  E-value: 1.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   6 TLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHK 85
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 122324596  86 VDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADL 122
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 10-156 1.40e-25

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 94.78  E-value: 1.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   10 QMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQ 89
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122324596   90 AKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV 156
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 6-156 4.36e-25

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: 93.70  E-value: 4.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   6 TLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHK 85
Cdd:COG0711    2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122324596  86 VDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV 156
Cdd:COG0711   82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
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 ...
 6-127 2.43e-17

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: 73.12  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596    6 TLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHK 85
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 122324596   86 VDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVAL 122
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 1-156 2.49e-15

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 68.92  E-value: 2.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   1 MDINI-TLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENA 79
Cdd:PRK13461   1 MEINIpTIIATIINFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 122324596  80 YVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV 156
Cdd:PRK13461  81 KSKAENVYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIKDFISKV 157
PRK13428 PRK13428
F0F1 ATP synthase subunit delta; Provisional
 6-124 3.05e-13

F0F1 ATP synthase subunit delta; Provisional


Pssm-ID: 184048 [Multi-domain]  Cd Length: 445  Bit Score: 65.91  E-value: 3.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   6 TLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHK 85
Cdd:PRK13428   3 TFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAER 82

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 122324596  86 VDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQEL 124
Cdd:PRK13428  83 IAEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLEL 121
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 10-127 5.76e-13

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 62.50  E-value: 5.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596  10 QMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQ 89
Cdd:PRK14471  14 QTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEKMIAD 93

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 122324596  90 AKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:PRK14471  94 AKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANL 131
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 12-154 6.95e-13

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 62.52  E-value: 6.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596  12 ITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAK 91
Cdd:PRK14472  26 VTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKLRAEIT 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122324596  92 EEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVE 154
Cdd:PRK14472 106 EKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQ 168
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 6-156 4.57e-11

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 58.00  E-value: 4.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   6 TLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHK 85
Cdd:PRK13453  20 TVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 122324596  86 VDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFVEKV 156
Cdd:PRK13453 100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEA 170
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 8-153 6.12e-10

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 55.23  E-value: 6.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   8 IGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVD 87
Cdd:PRK06231  52 IAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLK 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122324596  88 EQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLEDFV 153
Cdd:PRK06231 132 SELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFI 197
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 7-127 2.14e-09

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 53.00  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   7 LIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKV 86
Cdd:PRK14473  11 LIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQAQERARAQ 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 122324596  87 DEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:PRK14473  91 EAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADL 131
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 12-150 2.35e-09

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 53.04  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596  12 ITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAK 91
Cdd:PRK07352  27 INLAIVIGLLYYFGRGFLGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIE 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 122324596  92 EEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNLAMAAASKIIAASVDEKASKKVLE 150
Cdd:PRK07352 107 KQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLID 165
atpF CHL00019
ATP synthase CF0 B subunit
 12-127 1.68e-07

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 48.32  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596  12 ITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASAD----RASRELEVAKRQsaeiLREAKAKATEIVENAYVRAhkvd 87
Cdd:CHL00019  32 INLSVVLGVLIYFGKGVLSDLLDNRKQTILNTIRNSEerreEAIEKLEKARAR----LRQAELEADEIRVNGYSEI---- 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 122324596  88 EQAKEEAIAAADK----IKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:CHL00019 104 EREKENLINQAKEdlerLENYKNETIRFEQQRAINQVRQQVFQL 147
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 7-127 1.86e-07

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 48.10  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   7 LIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYVRAHKV 86
Cdd:PRK13460  19 VVWTLVTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDALKL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 122324596  87 DEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:PRK13460  99 KNKLLEETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEM 139
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 2-127 4.54e-06

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 43.84  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   2 DINITLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYV 81
Cdd:PRK07353   3 DFDATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEAEA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 122324596  82 RAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:PRK07353  83 EADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDAL 128
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 8-123 5.72e-05

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 41.15  E-value: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   8 IGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENayvrahkvd 87
Cdd:PRK08475  26 IERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIVET--------- 96

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 122324596  88 eqAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQE 123
Cdd:PRK08475  97 --AKKEAYILTQKIEKQTKDDIENLIKSFEELMEFE 130
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 54-126 2.94e-04

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 39.16  E-value: 2.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 122324596  54 LEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVN 126
Cdd:COG1390   12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIE 84
PRK09174 PRK09174
F0F1 ATP synthase subunit B;
12-117 2.07e-03

F0F1 ATP synthase subunit B;


Pssm-ID: 169692 [Multi-domain]  Cd Length: 204  Bit Score: 37.08  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596  12 ITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAyvrahkvDEQAK 91
Cdd:PRK09174  61 ITFGLFYLFMSRVILPRIGGIIETRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSIAQAA-------REAAK 133

                         90       100       110
                 ....*....|....*....|....*....|.
gi 122324596  92 EEAIAAADKI-----KSMAIAEIEQEKVKAK 117
Cdd:PRK09174 134 AKAEAERAAIeasleKKLKEAEARIAAIKAK 164
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 2-127 3.03e-03

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 36.12  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   2 DINITLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVENAYV 81
Cdd:CHL00118  20 DFNATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEILAKANELTKQYEQELSKARKEAQLEITQSQK 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 122324596  82 RAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQELVNL 127
Cdd:CHL00118 100 EAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTL 145
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 5-123 6.82e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 35.56  E-value: 6.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   5 ITLIGQMITFAIFIGFTMKFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVenayvrah 84
Cdd:PRK14474   6 FTVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEQQRASFM-------- 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 122324596  85 kvdEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQE 123
Cdd:PRK14474  78 ---AQAQEAADEQRQHLLNEAREDVATARDEWLEQLERE 113
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 1-124 7.02e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 35.05  E-value: 7.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122324596   1 MDINITLIGQMITFAIFIGFTM---KFVWPPLRKALEERREKIAEGLASADRASRELEVAKRQSAEILREAKAKATEIVE 77
Cdd:PRK08476   1 MMLDVNPYLMLATFVVFLLLIVilnSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 122324596  78 NAYVRAHKVDEQAKEEAIAAADKIKSMAIAEIEQEKVKAKEQLKQEL 124
Cdd:PRK08476  81 KAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQELKEQLLSQM 127
PRK01558 PRK01558
V-type ATP synthase subunit E; Provisional
 54-111 8.17e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179302  Cd Length: 198  Bit Score: 35.12  E-value: 8.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 122324596  54 LEVAKRQSAEILREAKAKATEIVENAYVRAHKVDEQAKEEaiaaADKIKSMAIAEIEQ 111
Cdd:PRK01558  17 LEEAERLANEIILEAKEEAEEIIAKAEEEAKELKAKAEKE----ANDYKRHALEASRQ 70
 
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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