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Conserved domains on  [gi|1815807629|gb|QIE73118|]
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F0F1 ATP synthase subunit B [Glaesserella parasuis]

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 7.73e-60

F0F1 ATP synthase subunit B; Validated


:

Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 182.28  E-value: 7.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   1 MNLNATLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLAT 80
Cdd:PRK05759    1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1815807629  81 KRRNEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:PRK05759   81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 7.73e-60

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 182.28  E-value: 7.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   1 MNLNATLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLAT 80
Cdd:PRK05759    1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1815807629  81 KRRNEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:PRK05759   81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 10-156 2.58e-47

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: 150.25  E-value: 2.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  10 QLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNEILES 89
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1815807629  90 VQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 5-156 4.34e-32

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: 111.80  E-value: 4.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   5 ATLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRN 84
Cdd:COG0711     1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1815807629  85 EILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:COG0711    81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 6-137 2.86e-30

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: 106.37  E-value: 2.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   6 TLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNE 85
Cdd:cd06503     1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1815807629  86 ILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVG 137
Cdd:cd06503    81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
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 ...
 6-137 2.83e-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: 83.52  E-value: 2.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   6 TLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNE 85
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1815807629  86 ILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVG 137
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 7.73e-60

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 182.28  E-value: 7.73e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   1 MNLNATLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLAT 80
Cdd:PRK05759    1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1815807629  81 KRRNEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:PRK05759   81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 10-156 2.58e-47

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: 150.25  E-value: 2.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  10 QLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNEILES 89
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1815807629  90 VQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 5-156 4.34e-32

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: 111.80  E-value: 4.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   5 ATLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRN 84
Cdd:COG0711     1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1815807629  85 EILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:COG0711    81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 6-137 2.86e-30

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: 106.37  E-value: 2.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   6 TLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNE 85
Cdd:cd06503     1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1815807629  86 ILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVG 137
Cdd:cd06503    81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
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 ...
 6-137 2.83e-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: 83.52  E-value: 2.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   6 TLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNE 85
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1815807629  86 ILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVG 137
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 12-156 7.28e-20

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 81.01  E-value: 7.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  12 IAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHII----DLATKRRNEIL 87
Cdd:PRK14472   26 VTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIregkEYAEKLRAEIT 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1815807629  88 ESVQAEAeaekAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:PRK14472  106 EKAHTEA----KKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDL 170
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 7-156 1.92e-18

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 76.89  E-value: 1.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   7 LIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNEI 86
Cdd:PRK14473   11 LIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQAQERARAQ 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  87 LESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:PRK14473   91 EAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAAL 160
PRK13428 PRK13428
F0F1 ATP synthase subunit delta; Provisional
 6-156 3.36e-18

F0F1 ATP synthase subunit delta; Provisional


Pssm-ID: 184048 [Multi-domain]  Cd Length: 445  Bit Score: 80.16  E-value: 3.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   6 TLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNE 85
Cdd:PRK13428    3 TFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAER 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1815807629  86 ILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSV-DAAANNDIIDKLVAEL 156
Cdd:PRK13428   83 IAEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGELVRNHVaDPAQQSATVDRFLDEL 154
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 10-136 3.57e-16

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 70.98  E-value: 3.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  10 QLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNEILES 89
Cdd:PRK14471   14 QTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEKMIAD 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1815807629  90 VQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIV 136
Cdd:PRK14471   94 AKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVL 140
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 8-156 1.24e-12

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 62.55  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   8 IGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNEIL 87
Cdd:PRK06231   52 IAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLK 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1815807629  88 ESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:PRK06231  132 SELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIREL 200
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 1-154 2.34e-12

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 60.83  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   1 MNLN-ATLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLA 79
Cdd:PRK13461    1 MEINiPTIIATIINFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1815807629  80 TKRRNEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVA 154
Cdd:PRK13461   81 KSKAENVYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIKDFIS 155
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 6-155 8.31e-12

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 59.92  E-value: 8.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   6 TLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNE 85
Cdd:PRK13453   20 TVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  86 ILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAE 155
Cdd:PRK13453  100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 3-156 1.29e-11

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 59.20  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   3 LNATLIGQLIAFALFVWFCMKFvwppLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKR 82
Cdd:PRK07352   22 LETNLINLAIVIGLLYYFGRGF----LGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKAR 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1815807629  83 RNEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:PRK07352   98 AEAIRAEIEKQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDRSIANL 171
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 4-137 8.65e-08

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 48.83  E-value: 8.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   4 NATLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRR 83
Cdd:CHL00118   22 NATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEILAKANELTKQYEQELSKARKEAQLEITQSQKEA 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1815807629  84 NEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVG 137
Cdd:CHL00118  102 KEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLLI 155
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 6-135 2.45e-07

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 48.27  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   6 TLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEqadtkvlVEQELAKAREEAQHIidlaTKRRNE 85
Cdd:PRK14474    7 TVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQE-------AGQEAERYRQKQQSL----EQQRAS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1815807629  86 ILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKI 135
Cdd:PRK14474   76 FMAQAQEAADEQRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQT 125
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 7-156 5.64e-07

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 46.94  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   7 LIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDL----ATKR 82
Cdd:PRK13460   19 VVWTLVTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEaksdALKL 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1815807629  83 RNEILESVQAEAEAEKakiiEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:PRK13460   99 KNKLLEETNNEVKAQK----DQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIETELAKL 168
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 3-139 2.51e-06

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 44.22  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   3 LNATLIGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKR 82
Cdd:PRK07353    4 FDATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEAEAE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1815807629  83 RNEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRS 139
Cdd:PRK07353   84 ADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDALSRQILEKLLAAK 140
PRK09174 PRK09174
F0F1 ATP synthase subunit B;
12-145 6.73e-06

F0F1 ATP synthase subunit B;


Pssm-ID: 169692 [Multi-domain]  Cd Length: 204  Bit Score: 44.02  E-value: 6.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  12 IAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEqADTKVLV-EQELAKAREEAQHIIDLATkrrneilESV 90
Cdd:PRK09174   61 ITFGLFYLFMSRVILPRIGGIIETRRDRIAQDLDQAARLKQE-ADAAVAAyEQELAQARAKAHSIAQAAR-------EAA 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1815807629  91 QAEAEAEKAKI---IEQGYAEVENERRRVQEELRQKVAALAVAGAEKIVGRSVDAAAN 145
Cdd:PRK09174  133 KAKAEAERAAIeasLEKKLKEAEARIAAIKAKAMADVGSIAEETAAAIVEQLIGGTAD 190
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 11-127 1.15e-05

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 42.75  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  11 LIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEqadtkvlveqeLAKAREEAQHIIDLATKRRNEILESV 90
Cdd:PRK08476   14 FVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSD-----------VSEIEHEIETILKNAREEANKIRQKA 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1815807629  91 QAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAAL 127
Cdd:PRK08476   83 IAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQEL 119
PRK09173 PRK09173
F0F1 ATP synthase subunit B; Validated
 7-156 1.72e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 169691 [Multi-domain]  Cd Length: 159  Bit Score: 39.72  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   7 LIGQLIAFALFVWFCmkfVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNEI 86
Cdd:PRK09173    8 FVGLVLFLALVVYLK---VPGMIARSLDARADRIKNELAEARRLREEAQQLLAEYQRKRKEAEKEAADIVAAAEREAEAL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1815807629  87 LESVQAEAE---AEKAKIIEQGYAEVENERRRvqeELRQKVAALAVAGAEKIVGRSVDAAANNDIIDKLVAEL 156
Cdd:PRK09173   85 TAEAKRKTEeyvARRNKLAEQKIAQAETDAIN---AVRSSAVDLAIAAAEKLLAEKVDAKAASELFKDALAQV 154
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 60-124 3.93e-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: 38.77  E-value: 3.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1815807629  60 LVEQELAKAREEAQHIIDLATKRRNEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKV 124
Cdd:COG1390     7 IIEEILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEA 71
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
 61-124 1.09e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 37.81  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1815807629  61 VEQELAKAREEAQHIIDLATKR----RNEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKV 124
Cdd:PRK03963   19 IEYILEEAQKEAEKIKEEARKRaeskAEWILRKAKTQAELEKQRIIANAKLEVRRKRLAVQEELISEV 86
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 62-135 1.35e-03

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


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 36.43  E-value: 1.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1815807629  62 EQELAKAREEAQHIIDLATKRRNEILESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKVAALAVAGAEKI 135
Cdd:COG2811    18 DEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAQERLEEAREEAEAEAEEIIEEGEKEAEALKKKAEDKL 91
PTZ00121 PTZ00121
MAEBL; Provisional
 31-122 1.82e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   31 KAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNEILESVQAEAEAEKAKIIEQGYAEVE 110
Cdd:PTZ00121  1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712

                           90
                   ....*....|..
gi 1815807629  111 NERRRVqEELRQ 122
Cdd:PTZ00121  1713 EEKKKA-EELKK 1723
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 8-124 2.77e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 36.14  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629   8 IGQLIAFALFVWFCMKFVWPPLIKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNEIL 87
Cdd:PRK08475   26 IERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIVETAKKEAYILT 105

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1815807629  88 ESVQAEAEAEKAKIIEQGYAEVENERRRVQEELRQKV 124
Cdd:PRK08475  106 QKIEKQTKDDIENLIKSFEELMEFEVRKMEREVVEEV 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 30-135 4.68e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 36.45  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  30 IKAIETRQANIADALASAEKAKQEQADTKVLVEQELAKAREEAQHIIDLATKRRNEILESVQAEAEAEKAKIIE-QGYAE 108
Cdd:COG1196   234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLeERRRE 313

                          90       100
                  ....*....|....*....|....*..
gi 1815807629 109 VENERRRVQEELRQKVAALAVAGAEKI 135
Cdd:COG1196   314 LEERLEELEEELAELEEELEELEEELE 340
PRK12472 PRK12472
hypothetical protein; Provisional
 40-144 7.58e-03

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 35.62  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1815807629  40 IADALASAEKAKQEQAD-TKVLVEQELAKAREEAQHIIDLATKRRneiLESVQAEAEAEKAKIIEQGYAEVENERRRVQE 118
Cdd:PRK12472  185 LAAAPARAETLAREAEDaARAADEAKTAAAAAAREAAPLKASLRK---LERAKARADAELKRADKALAAAKTDEAKARAE 261

                          90       100
                  ....*....|....*....|....*.
gi 1815807629 119 ELRQKVAALAVAGAEKIVGRSVDAAA 144
Cdd:PRK12472  262 ERQQKAAQQAAEAATQLDTAKADAEA 287
 
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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