|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13453 |
PRK13453 |
F0F1 ATP synthase subunit B; Provisional |
1-173 |
9.41e-96 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184060 Cd Length: 173 Bit Score: 274.48 E-value: 9.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 1 MTETANLFVLGAAGGVEWGTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLK 80
Cdd:PRK13453 1 MTETANLFVLGAAGGVEWGTVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 81 ETQEEVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQK 160
Cdd:PRK13453 81 ETQEEVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQK 160
|
170
....*....|...
gi 995286833 161 ALVDKYLKEAGDK 173
Cdd:PRK13453 161 ALVDKYLKEAGDK 173
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
19-169 |
3.25e-37 |
|
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: 125.29 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 19 GTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQAR 98
Cdd:COG0711 1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 995286833 99 QQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
Cdd:COG0711 81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAE 151
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
20-151 |
1.18e-35 |
|
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: 120.62 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 20 TVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99
Cdd:cd06503 1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 995286833 100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLR 151
Cdd:cd06503 81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
24-169 |
1.91e-28 |
|
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: 102.87 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 24 QVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQQQEQ 103
Cdd:TIGR01144 1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 995286833 104 IIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
Cdd:TIGR01144 81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAE 146
|
|
| 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 ... |
20-151 |
1.67e-22 |
|
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: 86.98 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 20 TVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99
Cdd:pfam00430 1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 995286833 100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLR 151
Cdd:pfam00430 81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13453 |
PRK13453 |
F0F1 ATP synthase subunit B; Provisional |
1-173 |
9.41e-96 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184060 Cd Length: 173 Bit Score: 274.48 E-value: 9.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 1 MTETANLFVLGAAGGVEWGTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLK 80
Cdd:PRK13453 1 MTETANLFVLGAAGGVEWGTVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 81 ETQEEVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQK 160
Cdd:PRK13453 81 ETQEEVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQK 160
|
170
....*....|...
gi 995286833 161 ALVDKYLKEAGDK 173
Cdd:PRK13453 161 ALVDKYLKEAGDK 173
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
19-169 |
1.43e-38 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 129.13 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 19 GTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQAR 98
Cdd:PRK05759 5 GTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAA 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 995286833 99 QQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
Cdd:PRK05759 85 QIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAE 155
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
19-169 |
3.25e-37 |
|
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: 125.29 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 19 GTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQAR 98
Cdd:COG0711 1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 995286833 99 QQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
Cdd:COG0711 81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAE 151
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
20-151 |
1.18e-35 |
|
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: 120.62 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 20 TVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99
Cdd:cd06503 1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 995286833 100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLR 151
Cdd:cd06503 81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
|
|
| PRK14471 |
PRK14471 |
F0F1 ATP synthase subunit B; Provisional |
17-170 |
1.91e-30 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184695 [Multi-domain] Cd Length: 164 Bit Score: 108.73 E-value: 1.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 17 EWGTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQ 96
Cdd:PRK14471 7 DFGLFFWQTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREI 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 995286833 97 ARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQD-QKALVDKYLKEA 170
Cdd:PRK14471 87 KEKMIADAKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRKELSNKEkQHKLVEKMLGDV 161
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
24-169 |
1.91e-28 |
|
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: 102.87 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 24 QVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQQQEQ 103
Cdd:TIGR01144 1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 995286833 104 IIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
Cdd:TIGR01144 81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAE 146
|
|
| PRK13461 |
PRK13461 |
F0F1 ATP synthase subunit B; Provisional |
16-171 |
9.49e-27 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184064 [Multi-domain] Cd Length: 159 Bit Score: 98.97 E-value: 9.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 16 VEWGTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKV 95
Cdd:PRK13461 3 INIPTIIATIINFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEYKS 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 995286833 96 QARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEAG 171
Cdd:PRK13461 83 KAENVYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIKDFISKVG 158
|
|
| PRK14472 |
PRK14472 |
F0F1 ATP synthase subunit B; Provisional |
19-173 |
4.62e-24 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172947 [Multi-domain] Cd Length: 175 Bit Score: 92.56 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 19 GTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQAR 98
Cdd:PRK14472 19 GLIFWTAVTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 995286833 99 QQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEAGDK 173
Cdd:PRK14472 99 KLRAEITEKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDLSTK 173
|
|
| PRK13460 |
PRK13460 |
F0F1 ATP synthase subunit B; Provisional |
16-171 |
1.16e-22 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 139585 [Multi-domain] Cd Length: 173 Bit Score: 88.93 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 16 VEWGTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKV 95
Cdd:PRK13460 14 VNPGLVVWTLVTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKS 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 995286833 96 QARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEAG 171
Cdd:PRK13460 94 DALKLKNKLLEETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIETELAKLG 169
|
|
| 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 ... |
20-151 |
1.67e-22 |
|
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: 86.98 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 20 TVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99
Cdd:pfam00430 1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 995286833 100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLR 151
Cdd:pfam00430 81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
|
|
| PRK06231 |
PRK06231 |
F0F1 ATP synthase subunit B; Validated |
22-169 |
2.50e-17 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180481 [Multi-domain] Cd Length: 205 Bit Score: 75.65 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 22 IVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQQQ 101
Cdd:PRK06231 52 IAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLK 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 995286833 102 EQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
Cdd:PRK06231 132 SELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIRE 199
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
15-171 |
7.16e-17 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 73.42 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 15 GVEWGTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAK 94
Cdd:PRK14473 5 GINLGLLIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQAQ 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 995286833 95 VQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEAG 171
Cdd:PRK14473 85 ERARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAALG 161
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
19-150 |
1.06e-14 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 66.95 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 19 GTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQAR 98
Cdd:PRK07353 6 ATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEAEAEAD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 995286833 99 QQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVL 150
Cdd:PRK07353 86 KLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDALSRQILEKLL 137
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
30-173 |
8.35e-13 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 63.05 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 30 VLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQQQEQIIHEAN 109
Cdd:PRK07352 31 IVIGLLYYFGRGFLGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIEKQAI 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 995286833 110 VRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEAGDK 173
Cdd:PRK07352 111 EDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDRSIANLGGN 174
|
|
| PRK14474 |
PRK14474 |
F0F1 ATP synthase subunit B; Provisional |
16-151 |
8.95e-12 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184696 [Multi-domain] Cd Length: 250 Bit Score: 61.37 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 16 VEWGTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKV 95
Cdd:PRK14474 3 IDWFTVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEQQRASFMAQAQE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 995286833 96 QARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLR 151
Cdd:PRK14474 83 AADEQRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAALA 138
|
|
| atpG |
CHL00118 |
ATP synthase CF0 B' subunit; Validated |
19-152 |
4.27e-11 |
|
ATP synthase CF0 B' subunit; Validated
Pssm-ID: 214369 [Multi-domain] Cd Length: 156 Bit Score: 58.07 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 19 GTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQAR 98
Cdd:CHL00118 23 ATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEILAKANELTKQYEQELSKARKEAQLEITQSQKEAK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 995286833 99 QQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRK 152
Cdd:CHL00118 103 EIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLLIK 156
|
|
| PRK13455 |
PRK13455 |
F0F1 ATP synthase subunit B; Provisional |
20-173 |
1.43e-09 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184062 [Multi-domain] Cd Length: 184 Bit Score: 54.42 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 20 TVIVQVLTFIVLLALLKKFAW-GPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQAR 98
Cdd:PRK13455 28 TDFVVTLAFLLFIGILVYFKVpGMIGGMLDKRAEGIRSELEEARALREEAQTLLASYERKQREVQEQADRIVAAAKDEAQ 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 995286833 99 QQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEAGDK 173
Cdd:PRK13455 108 AAAEQAKADLEASIARRLAAAEDQIASAEAAAVKAVRDRAVSVAVAAAADVIAKQMTAADANALIDEAIKEVEAR 182
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
21-142 |
3.54e-08 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 49.69 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 21 VIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQQ 100
Cdd:PRK08476 10 MLATFVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQKAIAKAKEE 89
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 995286833 101 QEQIiheanvrangmIETAQSEINSQKERAIADINNQVSELS 142
Cdd:PRK08476 90 AEKK-----------IEAKKAELESKYEAFAKQLANQKQELK 120
|
|
| atpF |
CHL00019 |
ATP synthase CF0 B subunit |
25-141 |
2.64e-06 |
|
ATP synthase CF0 B subunit
Pssm-ID: 176962 [Multi-domain] Cd Length: 184 Bit Score: 45.24 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 25 VLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQ-KLEEENKQkLKETQEEVQKILEDAKVQARQQQEQ 103
Cdd:CHL00019 31 LINLSVVLGVLIYFGKGVLSDLLDNRKQTILNTIRNSEERREEAIeKLEKARAR-LRQAELEADEIRVNGYSEIEREKEN 109
|
90 100 110
....*....|....*....|....*....|....*...
gi 995286833 104 IIHEANVRANGMIETAQSEINSQKERAIADINNQVSEL 141
Cdd:CHL00019 110 LINQAKEDLERLENYKNETIRFEQQRAINQVRQQVFQL 147
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
19-169 |
1.12e-05 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 44.34 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 19 GTVIVQVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKlnaqkleeenkQKLKETQEEVQKILEDAKVQAR 98
Cdd:PRK13428 2 STFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAA-----------DRLAEADQAHTKAVEDAKAEAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 99 QQQEQIIHEANVRANGMIETAQSE---INSQKERAIADINNQV-----SEL---SVLIASKVLRKEIS-EQDQKALVDKY 166
Cdd:PRK13428 71 RVVEEAREDAERIAEQLRAQADAEaerIKVQGARQVQLLRAQLtrqlrLELgheSVRQAGELVRNHVAdPAQQSATVDRF 150
|
...
gi 995286833 167 LKE 169
Cdd:PRK13428 151 LDE 153
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
21-173 |
5.12e-05 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 41.46 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 21 VIVQVLTFIVLLALLKKfAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQQ 100
Cdd:PRK14475 14 VGAGLLIFFGILIALKV-LPKALAGALDAYAAKIQAELDEAQRLREEAQALLADVKAEREEAERQAAAMLAAAKADARRM 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 995286833 101 QEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEAGDK 173
Cdd:PRK14475 93 EAEAKEKLEEQIKRRAEMAERKIAQAEAQAAADVKAAAVDLAAQAAETVLAARLAGAKSDPLVDAAIGQMGAK 165
|
|
| PRK09173 |
PRK09173 |
F0F1 ATP synthase subunit B; Validated |
23-169 |
1.14e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 169691 [Multi-domain] Cd Length: 159 Bit Score: 37.80 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 23 VQVLTFIVLLALLKkfAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQArqqqE 102
Cdd:PRK09173 9 VGLVLFLALVVYLK--VPGMIARSLDARADRIKNELAEARRLREEAQQLLAEYQRKRKEAEKEAADIVAAAEREA----E 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 995286833 103 QIIHEANVRANGMIE--TAQSE--INSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
Cdd:PRK09173 83 ALTAEAKRKTEEYVArrNKLAEqkIAQAETDAINAVRSSAVDLAIAAAEKLLAEKVDAKAASELFKDALAQ 153
|
|
| PRK08475 |
PRK08475 |
F0F1 ATP synthase subunit B; Validated |
8-128 |
1.93e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 236272 [Multi-domain] Cd Length: 167 Bit Score: 36.91 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 8 FVLGAAGGVEWGTVIVQ-VLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAeQAKLNAQKLE-EENKQKLKETQEE 85
Cdd:PRK08475 11 YAFAASLGATEQYDIIErTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEI-QEKLKESKEKkEDALKKLEEAKEK 89
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 995286833 86 VQKILEDAKvqarQQQEQIIHEANVRANGMIETAQSEINSQKE 128
Cdd:PRK08475 90 AELIVETAK----KEAYILTQKIEKQTKDDIENLIKSFEELME 128
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
72-149 |
2.88e-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: 35.66 E-value: 2.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 995286833 72 EEENKQKLKETQEEVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKV 149
Cdd:COG2811 14 EEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAQERLEEAREEAEAEAEEIIEEGEKEAEALKKKAEDKL 91
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
44-168 |
4.39e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 36.73 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 44 KDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETqEEVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEi 123
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEA-EKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE- 585
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 995286833 124 nsqkeraIADINNQVSELSVLIASKVLRKEISEQdQKALVDKYLK 168
Cdd:PRK00409 586 -------ADEIIKELRQLQKGGYASVKAHELIEA-RKRLNKANEK 622
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
72-170 |
7.20e-03 |
|
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: 35.69 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 72 EEENKQKLKETQEEVQKILEDAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLR 151
Cdd:COG1390 16 EAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEEALEKLK 95
|
90
....*....|....*....
gi 995286833 152 KEISEQDQKALVDKYLKEA 170
Cdd:COG1390 96 NLPKDPEYKELLKKLLKEA 114
|
|
| PRK01005 |
PRK01005 |
V-type ATP synthase subunit E; Provisional |
76-164 |
9.42e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 179204 [Multi-domain] Cd Length: 207 Bit Score: 35.53 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 995286833 76 KQKLKETQEEVQKILEDAKVQArqqqEQIIHEANVRANGMIETAQSEIN---SQKERAIADINNQ-VSELSVLIASKVLR 151
Cdd:PRK01005 19 EETLKPAEEEAGAIVHNAKEQA----KRIIAEAQEEAEKIIRSAEETADqklKQGESALVQAGKRsLESLKQAVENKIFR 94
|
90
....*....|...
gi 995286833 152 KEISEQDQKALVD 164
Cdd:PRK01005 95 ESLGEWLEHVLTD 107
|
|
|