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Conserved domains on  [gi|1728895377|gb|TXX15718|]
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ATP synthase F0 subunit B [Enterococcus gallinarum]

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
 33-167 2.49e-34

F0F1 ATP synthase subunit B; Validated


:

Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 118.34  E-value: 2.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:PRK05759   22 MKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAAQIIEEAKAEAEAEAARI 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGL 167
Cdd:PRK05759  102 KAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 33-167 2.49e-34

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 118.34  E-value: 2.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:PRK05759   22 MKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAAQIIEEAKAEAEAEAARI 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGL 167
Cdd:PRK05759  102 KAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 33-148 4.57e-32

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: 111.76  E-value: 4.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:cd06503    17 KKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERI 96

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILG 148
Cdd:cd06503    97 LEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 33-167 2.37e-31

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: 110.26  E-value: 2.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:COG0711    18 KKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERI 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGL 167
Cdd:COG0711    98 IAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 33-167 3.24e-24

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: 92.08  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:TIGR01144  13 MKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEEAKAEAREEREKI 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGL 167
Cdd:TIGR01144  93 KAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
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 ...
 35-148 3.67e-20

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: 81.20  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  35 FAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKE 114
Cdd:pfam00430  19 FAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIE 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1728895377 115 KAHSDITLEKEAALKEVKDDVADLSLQIAEKILG 148
Cdd:pfam00430  99 QAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 33-167 2.49e-34

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 118.34  E-value: 2.49e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:PRK05759   22 MKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAAQIIEEAKAEAEAEAARI 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGL 167
Cdd:PRK05759  102 KAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 33-148 4.57e-32

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: 111.76  E-value: 4.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:cd06503    17 KKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERI 96

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILG 148
Cdd:cd06503    97 LEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 33-167 2.37e-31

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: 110.26  E-value: 2.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:COG0711    18 KKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERI 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGL 167
Cdd:COG0711    98 IAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 33-167 3.24e-24

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: 92.08  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:TIGR01144  13 MKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEEAKAEAREEREKI 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGL 167
Cdd:TIGR01144  93 KAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 2-168 1.31e-22

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 88.81  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377   2 LNHLVLAEVKNAMLGNIILVSGSILLLLFLLKHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHS 81
Cdd:PRK13453    5 ANLFVLGAAGGVEWGTVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  82 EAAEIIKSAKDSGELSRQNILNETKEEVSRLKEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLIN 161
Cdd:PRK13453   85 EVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVD 164


                  ....*..
gi 1728895377 162 QYIEGLG 168
Cdd:PRK13453  165 KYLKEAG 171
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 ...
 35-148 3.67e-20

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: 81.20  E-value: 3.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  35 FAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKE 114
Cdd:pfam00430  19 FAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVAAAEAEAERIIE 98

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1728895377 115 KAHSDITLEKEAALKEVKDDVADLSLQIAEKILG 148
Cdd:pfam00430  99 QAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 33-171 9.10e-18

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 76.22  E-value: 9.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:PRK13460   34 KKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDALKLKNKLLEETNNEVKAQ 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGLGSVN 171
Cdd:PRK13460  114 KDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIETELAKLGKLS 172
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 33-169 1.22e-16

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 72.78  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:PRK13461   23 KHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEYKSKAENVYEEIVKEAHEEADLI 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGLGS 169
Cdd:PRK13461  103 IERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIKDFISKVGI 159
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 33-169 1.48e-16

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 72.92  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:PRK14472   36 KKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKLRAEITEKAHTEAKKM 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGLGS 169
Cdd:PRK14472  116 IASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDLST 172
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 43-168 5.46e-16

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 71.52  E-value: 5.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  43 MMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKEKAHSDITL 122
Cdd:PRK07352   47 ILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIEKQAIEDMARLKQTAAADLSA 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1728895377 123 EKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGLG 168
Cdd:PRK07352  127 EQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDRSIANLG 172
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 35-171 3.35e-15

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 69.18  E-value: 3.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  35 FAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKE 114
Cdd:PRK14473   28 FLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQAQERARAQEAEIIAQARREAEKIKE 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1728895377 115 KAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGLGSVN 171
Cdd:PRK14473  108 EARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAALGRRN 164
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 33-164 4.34e-15

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 68.66  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:PRK14471   26 AKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEKMIADAKEEAQVEGDKM 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELT-PENHESLINQYI 164
Cdd:PRK14471  106 IEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRKELSnKEKQHKLVEKML 158
atpF CHL00019
ATP synthase CF0 B subunit
 38-173 1.02e-10

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 57.57  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  38 DAISSMMQKREEKIANDLDSAEQsRLNAA--KLEKERQEkLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKEK 115
Cdd:CHL00019   47 GVLSDLLDNRKQTILNTIRNSEE-RREEAieKLEKARAR-LRQAELEADEIRVNGYSEIEREKENLINQAKEDLERLENY 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1728895377 116 AHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGLGSVNET 173
Cdd:CHL00019  125 KNETIRFEQQRAINQVRQQVFQLALQRALGTLNSCLNNELHLRTINANIGLLGAMKEI 182
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 46-150 1.79e-09

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 53.47  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  46 KREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKEKAHSDITLEKE 125
Cdd:PRK07353   36 EREDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKEKARREIEQQKQ 115

                          90       100
                  ....*....|....*....|....*
gi 1728895377 126 AALKEVKDDVADLSLQIAEKILGRE 150
Cdd:PRK07353  116 AALAQLEQQVDALSRQILEKLLAAK 140
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 40-148 1.02e-08

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 51.53  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  40 ISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKEKAHSD 119
Cdd:CHL00118   47 LLKVLDERKEYIRKNLTKASEILAKANELTKQYEQELSKARKEAQLEITQSQKEAKEIVENELKQAQKYIDSLLNEATKQ 126

                          90       100
                  ....*....|....*....|....*....
gi 1728895377 120 ITLEKEAALKEVKDDVADLSLQIAEKILG 148
Cdd:CHL00118  127 LEAQKEKALKSLEEQVDTLSDQIEEKLLI 155
PRK13455 PRK13455
F0F1 ATP synthase subunit B; Provisional
 40-165 2.73e-08

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184062 [Multi-domain]  Cd Length: 184  Bit Score: 50.95  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  40 ISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKEKAHSD 119
Cdd:PRK13455   52 IGGMLDKRAEGIRSELEEARALREEAQTLLASYERKQREVQEQADRIVAAAKDEAQAAAEQAKADLEASIARRLAAAEDQ 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1728895377 120 ITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIE 165
Cdd:PRK13455  132 IASAEAAAVKAVRDRAVSVAVAAAADVIAKQMTAADANALIDEAIK 177
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 33-172 3.21e-08

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 51.36  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  33 KHFAWDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:PRK14474   23 RRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEQQRASFMAQAQEAADEQRQHLLNEAREDVATA 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGLGSVNE 172
Cdd:PRK14474  103 RDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAALADLANATLEQQIVGIFIARLEHLSE 162
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 37-167 1.40e-07

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 49.07  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  37 WDAISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKEKA 116
Cdd:PRK06231   70 WKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLKSELEKEANRQANLIIFQA 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1728895377 117 HSDITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGL 167
Cdd:PRK06231  150 RQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIREL 200
PRK09173 PRK09173
F0F1 ATP synthase subunit B; Validated
 47-165 1.83e-07

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 169691 [Multi-domain]  Cd Length: 159  Bit Score: 48.20  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  47 REEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKEKAHSDITLEKEA 126
Cdd:PRK09173   34 RADRIKNELAEARRLREEAQQLLAEYQRKRKEAEKEAADIVAAAEREAEALTAEAKRKTEEYVARRNKLAEQKIAQAETD 113

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1728895377 127 ALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIE 165
Cdd:PRK09173  114 AINAVRSSAVDLAIAAAEKLLAEKVDAKAASELFKDALA 152
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
 39-169 1.00e-05

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 43.39  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  39 AISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRLKEKAHS 118
Cdd:PRK14475   34 ALAGALDAYAAKIQAELDEAQRLREEAQALLADVKAEREEAERQAAAMLAAAKADARRMEAEAKEKLEEQIKRRAEMAER 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1728895377 119 DITLEKEAALKEVKDDVADLSLQIAEKILGRELTPENHESLINQYIEGLGS 169
Cdd:PRK14475  114 KIAQAEAQAAADVKAAAVDLAAQAAETVLAARLAGAKSDPLVDAAIGQMGA 164
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 34-137 1.69e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 40.00  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  34 HFAWDAISSMMQKREEKIANDLDSAeQSRLNAAKLEKER-QEKLANSHSEAAEIIKSAKDSGELSRQNILNETKEEVSRL 112
Cdd:PRK08475   41 YFAAKPLKNFYKSRINKISKRLEEI-QEKLKESKEKKEDaLKKLEEAKEKAELIVETAKKEAYILTQKIEKQTKDDIENL 119

                          90       100
                  ....*....|....*....|....*
gi 1728895377 113 KEKAHSDITLEKEAALKEVKDDVAD 137
Cdd:PRK08475  120 IKSFEELMEFEVRKMEREVVEEVLN 144
PRK13454 PRK13454
F0F1 ATP synthase subunit B'; Provisional
 40-132 3.47e-03

F0F1 ATP synthase subunit B'; Provisional


Pssm-ID: 184061 [Multi-domain]  Cd Length: 181  Bit Score: 36.34  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  40 ISSMMQKREEKIANDLDSAEQSRLNAAKLEKERQEKLANSHSEAAEIIKSAKDSgelsrqnILNETKEEVSrlkeKAHSD 119
Cdd:PRK13454   56 IGAVLAERQGTITNDLAAAEELKQKAVEAEKAYNKALADARAEAQRIVAETRAE-------IQAELDVAIA----KADAE 124

                          90
                  ....*....|....*.
gi 1728895377 120 I---TLEKEAALKEVK 132
Cdd:PRK13454  125 IaakAAESEKRIAEIR 140
PRK09174 PRK09174
F0F1 ATP synthase subunit B;
40-132 5.20e-03

F0F1 ATP synthase subunit B;


Pssm-ID: 169692 [Multi-domain]  Cd Length: 204  Bit Score: 35.93  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728895377  40 ISSMMQKREEKIANDLDSAeqSRLNA------AKLEKERQEKLANSHSEAAEIIKSAKDSGELSRQNI-------LNETK 106
Cdd:PRK09174   78 IGGIIETRRDRIAQDLDQA--ARLKQeadaavAAYEQELAQARAKAHSIAQAAREAAKAKAEAERAAIeaslekkLKEAE 155

                          90       100
                  ....*....|....*....|....*..
gi 1728895377 107 EEVSRLKEKAHSDI-TLEKEAALKEVK 132
Cdd:PRK09174  156 ARIAAIKAKAMADVgSIAEETAAAIVE 182
 
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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