|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1-156 |
1.12e-62 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 189.60 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 1 MNINATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAK 80
Cdd:PRK05759 1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1499951224 81 KRGTQIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 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 |
2.72e-41 |
|
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: 134.84 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 10 QSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDE 89
Cdd:TIGR01144 1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499951224 90 ARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 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 |
2.70e-36 |
|
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: 122.20 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 5 ATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGT 84
Cdd:COG0711 1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1499951224 85 QIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 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 |
5.48e-34 |
|
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: 116.00 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:cd06503 1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1499951224 86 IVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILG 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 |
6.71e-24 |
|
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: 90.06 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:pfam00430 1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1499951224 86 IVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILG 137
Cdd:pfam00430 81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1-156 |
1.12e-62 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 189.60 E-value: 1.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 1 MNINATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAK 80
Cdd:PRK05759 1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1499951224 81 KRGTQIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 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 |
2.72e-41 |
|
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: 134.84 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 10 QSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDE 89
Cdd:TIGR01144 1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499951224 90 ARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 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 |
2.70e-36 |
|
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: 122.20 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 5 ATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGT 84
Cdd:COG0711 1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1499951224 85 QIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 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 |
5.48e-34 |
|
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: 116.00 E-value: 5.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:cd06503 1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1499951224 86 IVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILG 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 |
6.71e-24 |
|
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: 90.06 E-value: 6.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:pfam00430 1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1499951224 86 IVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILG 137
Cdd:pfam00430 81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
|
|
| PRK14472 |
PRK14472 |
F0F1 ATP synthase subunit B; Provisional |
11-156 |
2.80e-22 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172947 [Multi-domain] Cd Length: 175 Bit Score: 87.17 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 11 SVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEA 90
Cdd:PRK14472 25 AVTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKLRAEI 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1499951224 91 RETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK14472 105 TEKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDL 170
|
|
| PRK14471 |
PRK14471 |
F0F1 ATP synthase subunit B; Provisional |
10-156 |
3.94e-18 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184695 [Multi-domain] Cd Length: 164 Bit Score: 76.37 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 10 QSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDE 89
Cdd:PRK14471 14 QTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEKMIAD 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1499951224 90 ARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATI-DQNAHAELVNKLAAEI 156
Cdd:PRK14471 94 AKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRKELsNKEKQHKLVEKMLGDV 161
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
1-156 |
5.42e-17 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 73.42 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 1 MNINATLIGQSVAFFIFVIFCMK-FVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQA 79
Cdd:PRK14473 4 LGINLGLLIAQLINFLLLIFLLRtFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499951224 80 KKRGTQIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK14473 84 QERARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAAL 160
|
|
| PRK13461 |
PRK13461 |
F0F1 ATP synthase subunit B; Provisional |
1-150 |
8.46e-16 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184064 [Multi-domain] Cd Length: 159 Bit Score: 70.08 E-value: 8.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 1 MNINATLIGQSVAFFIFVIFCMK-FVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQA 79
Cdd:PRK13461 1 MEINIPTIIATIINFIILLLILKhFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1499951224 80 KKRGTQIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVN 150
Cdd:PRK13461 81 KSKAENVYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIK 151
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
6-135 |
5.01e-15 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 70.92 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:PRK13428 3 TFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAER 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1499951224 86 IVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKI 135
Cdd:PRK13428 83 IAEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGEL 132
|
|
| PRK06231 |
PRK06231 |
F0F1 ATP synthase subunit B; Validated |
8-156 |
3.43e-13 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180481 [Multi-domain] Cd Length: 205 Bit Score: 64.09 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 8 IGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIV 87
Cdd:PRK06231 52 IAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLK 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1499951224 88 DEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK06231 132 SELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIREL 200
|
|
| PRK13453 |
PRK13453 |
F0F1 ATP synthase subunit B; Provisional |
6-155 |
2.50e-09 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184060 Cd Length: 173 Bit Score: 52.99 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:PRK13453 20 TVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 86 IVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAE 155
Cdd:PRK13453 100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
7-151 |
2.83e-09 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 53.04 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 7 LIGQSVAFFIFVIFCMKFVWppviAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQI 86
Cdd:PRK07352 26 LINLAIVIGLLYYFGRGFLG----KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAI 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1499951224 87 VDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNK 151
Cdd:PRK07352 102 RAEIEKQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDR 166
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
3-138 |
1.24e-08 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 50.77 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 3 INATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGL-DAASRAARDLELAQEKAgQQLREAKAQAAEIIEQAKK 81
Cdd:PRK07353 4 FDATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRaEAKERLAEAEKLEAQYE-QQLASARKQAQAVIAEAEA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1499951224 82 RGTQIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGA 138
Cdd:PRK07353 83 EADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDALSRQILEKLLAA 139
|
|
| PRK14474 |
PRK14474 |
F0F1 ATP synthase subunit B; Provisional |
6-156 |
1.56e-07 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184696 [Multi-domain] Cd Length: 250 Bit Score: 49.04 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:PRK14474 7 TVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEQQRASFMAQAQEAADE 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1499951224 86 IVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK14474 87 QRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAALADLANATLEQQIVGIFIARL 157
|
|
| PRK13460 |
PRK13460 |
F0F1 ATP synthase subunit B; Provisional |
12-151 |
3.44e-07 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 139585 [Multi-domain] Cd Length: 173 Bit Score: 47.33 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 12 VAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEAR 91
Cdd:PRK13460 24 VTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDALKLKNKLL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 92 ETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNK 151
Cdd:PRK13460 104 EETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIET 163
|
|
| PRK09173 |
PRK09173 |
F0F1 ATP synthase subunit B; Validated |
12-156 |
7.62e-07 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 169691 [Multi-domain] Cd Length: 159 Bit Score: 46.27 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 12 VAFFIFVIFCMKFVWPPVIA-ALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEA 90
Cdd:PRK09173 9 VGLVLFLALVVYLKVPGMIArSLDARADRIKNELAEARRLREEAQQLLAEYQRKRKEAEKEAADIVAAAEREAEALTAEA 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1499951224 91 RETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK09173 89 KRKTEEYVARRNKLAEQKIAQAETDAINAVRSSAVDLAIAAAEKLLAEKVDAKAASELFKDALAQV 154
|
|
| atpG |
CHL00118 |
ATP synthase CF0 B' subunit; Validated |
3-137 |
4.64e-06 |
|
ATP synthase CF0 B' subunit; Validated
Pssm-ID: 214369 [Multi-domain] Cd Length: 156 Bit Score: 43.82 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 3 INATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAardLELAQEKAGQ---QLREAKAQAAEIIEQA 79
Cdd:CHL00118 21 FNATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEI---LAKANELTKQyeqELSKARKEAQLEITQS 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1499951224 80 KKRGTQIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAEKILG 137
Cdd:CHL00118 98 QKEAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLLI 155
|
|
| PRK09174 |
PRK09174 |
F0F1 ATP synthase subunit B; |
12-155 |
7.57e-06 |
|
F0F1 ATP synthase subunit B;
Pssm-ID: 169692 [Multi-domain] Cd Length: 204 Bit Score: 44.02 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 12 VAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEAR 91
Cdd:PRK09174 61 ITFGLFYLFMSRVILPRIGGIIETRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSIAQAAREAAKAKAEAER 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1499951224 92 ETARVEADRVKAQAHAEIEqelnGVKDALRAQLGSLAVNGA----EKILGATIDQNAHAELVNKLAAE 155
Cdd:PRK09174 141 AAIEASLEKKLKEAEARIA----AIKAKAMADVGSIAEETAaaivEQLIGGTADKASVAAAVKAARAS 204
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
54-155 |
2.77e-05 |
|
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: 42.24 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 54 LELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQLGSLAVNGAE 133
Cdd:COG1390 12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEEAL 91
|
90 100
....*....|....*....|..
gi 1499951224 134 KILGATIDQNAHAELVNKLAAE 155
Cdd:COG1390 92 EKLKNLPKDPEYKELLKKLLKE 113
|
|
| PRK08475 |
PRK08475 |
F0F1 ATP synthase subunit B; Validated |
8-111 |
5.67e-05 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 236272 [Multi-domain] Cd Length: 167 Bit Score: 41.15 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 8 IGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIV 87
Cdd:PRK08475 26 IERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIVETAKKEAYILT 105
|
90 100
....*....|....*....|....
gi 1499951224 88 DEaretarveadrVKAQAHAEIEQ 111
Cdd:PRK08475 106 QK-----------IEKQTKDDIEN 118
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
33-104 |
2.08e-04 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 38.68 E-value: 2.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1499951224 33 LHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARETAR---VEADRVKAQ 104
Cdd:COG3599 50 LEELEEELEEYRELEETLQKTLVVAQETAEEVKENAEKEAELIIKEAELEAEKIIEEAQEKARkivREIEELKRQ 124
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
3-123 |
2.49e-04 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 38.90 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 3 INATLIGQSVAFFIFVIFCM-KFVWPPVIAALHERQKKIADGLDAASraardlelaqeKAGQQLREAKAQAAEIIEQAKK 81
Cdd:PRK08476 5 VNPYLMLATFVVFLLLIVILnSWLYKPLLKFMDNRNASIKNDLEKVK-----------TNSSDVSEIEHEIETILKNARE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1499951224 82 RGTQIVDEARETARVEADRVKAQAHAEIEQELNGVKDALRAQ 123
Cdd:PRK08476 74 EANKIRQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQ 115
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
46-144 |
7.34e-04 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 38.05 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 46 AASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARE----TARVEADRVKAQAHAEIeqeLNGVKDALR 121
Cdd:PRK02292 14 ARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLREqelsSAKLEAKRERLNARKEV---LEDVRNQVE 90
|
90 100
....*....|....*....|...
gi 1499951224 122 AQLGSLAVNGAEKILGATIDQNA 144
Cdd:PRK02292 91 DEIASLDGDKREELTKSLLDAAD 113
|
|
| PRK01005 |
PRK01005 |
V-type ATP synthase subunit E; Provisional |
35-111 |
7.37e-04 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 179204 [Multi-domain] Cd Length: 207 Bit Score: 38.23 E-value: 7.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1499951224 35 ERQKKIADGLDAASraardLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEAREtarvEADRVKAQAHAEIEQ 111
Cdd:PRK01005 8 DKLKQICDALREET-----LKPAEEEAGAIVHNAKEQAKRIIAEAQEEAEKIIRSAEE----TADQKLKQGESALVQ 75
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
66-112 |
9.81e-04 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 37.67 E-value: 9.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1499951224 66 REAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAHAEIEQE 112
Cdd:PRK02292 12 DEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQL 58
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
29-114 |
3.87e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 36.73 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 29 VIAALHERQKKIADGLDAASRAARDLE-----LAQEKAGQQLREAKA------QAAEIIEQAKKRGTQIVDEARETARVE 97
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEklkeeLEEKKEKLQEEEDKLleeaekEAQQAIKEAKKEADEIIKELRQLQKGG 600
|
90
....*....|....*..
gi 1499951224 98 ADRVKAQAHAEIEQELN 114
Cdd:PRK00409 601 YASVKAHELIEARKRLN 617
|
|
| fliH |
PRK06032 |
flagellar assembly protein H; Validated |
66-149 |
3.98e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235679 [Multi-domain] Cd Length: 199 Bit Score: 36.12 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 66 REAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAHAEIEQ-------ELNGVKDALRAQLGSLAVNGAEKILGA 138
Cdd:PRK06032 24 RAAAEFAQAVAEAEAAAYAQGFAAGQREAAAQSERRLADALERIAQaaagllaALAAVEHEMETEAADLALAVARKIAGA 103
|
90
....*....|.
gi 1499951224 139 TIDQNAHAELV 149
Cdd:PRK06032 104 ALAAEPLAEIT 114
|
|
| V_ATP_synt_G |
TIGR01147 |
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ... |
57-108 |
4.69e-03 |
|
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. V-ATPases are multi-subunit enzymes composed of two functional domains: A transmembrane Vo domain and a peripheral catalytic domain V1. The G subunit is one of the subunits of the catalytic domain. V-ATPases are responsible for the acidification of endosomes and lysosomes, which are part of the central vacuolar system. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130217 [Multi-domain] Cd Length: 113 Bit Score: 34.81 E-value: 4.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1499951224 57 AQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAHAE 108
Cdd:TIGR01147 3 SQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKE 54
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
30-117 |
5.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 36.43 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1499951224 30 IAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRgTQIVDEARETARVEADRVKAQaHAEI 109
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE-LEALEEALAEAEAALRDLRRE-LREL 424
|
....*...
gi 1499951224 110 EQELNGVK 117
Cdd:COG4913 425 EAEIASLE 432
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
56-118 |
7.78e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 35.52 E-value: 7.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1499951224 56 LAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAHAEIEQELNGVKD 118
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK 86
|
|
| |
