|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1-156 |
1.22e-59 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 181.90 E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 1 MNINLTLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQAN 80
Cdd:PRK05759 1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301799138 81 KRANQLIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 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 |
1.78e-40 |
|
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: 132.91 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 10 QMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQLIEE 89
Cdd:TIGR01144 1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301799138 90 AKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 156
Cdd:TIGR01144 81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
6-156 |
7.03e-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: 121.43 E-value: 7.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 6 TLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQ 85
Cdd:COG0711 2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301799138 86 LIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 156
Cdd:COG0711 82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 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 |
2.57e-33 |
|
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: 114.07 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 6 TLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQ 85
Cdd:cd06503 1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 301799138 86 LIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQ 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 |
6.22e-23 |
|
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: 87.75 E-value: 6.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 6 TLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQ 85
Cdd:pfam00430 1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 301799138 86 LIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQ 137
Cdd:pfam00430 81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1-156 |
1.22e-59 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 181.90 E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 1 MNINLTLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQAN 80
Cdd:PRK05759 1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301799138 81 KRANQLIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 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 |
1.78e-40 |
|
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: 132.91 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 10 QMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQLIEE 89
Cdd:TIGR01144 1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301799138 90 AKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 156
Cdd:TIGR01144 81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
6-156 |
7.03e-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: 121.43 E-value: 7.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 6 TLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQ 85
Cdd:COG0711 2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301799138 86 LIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 156
Cdd:COG0711 82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 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 |
2.57e-33 |
|
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: 114.07 E-value: 2.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 6 TLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQ 85
Cdd:cd06503 1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 301799138 86 LIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQ 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 |
6.22e-23 |
|
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: 87.75 E-value: 6.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 6 TLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQ 85
Cdd:pfam00430 1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 301799138 86 LIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQ 137
Cdd:pfam00430 81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
1-156 |
2.63e-19 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 79.20 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 1 MNINLTLF-GQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQA 79
Cdd:PRK14473 4 LGINLGLLiAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301799138 80 NKRANQLIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 156
Cdd:PRK14473 84 QERARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAAL 160
|
|
| PRK14472 |
PRK14472 |
F0F1 ATP synthase subunit B; Provisional |
7-156 |
7.60e-19 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172947 [Multi-domain] Cd Length: 175 Bit Score: 78.31 E-value: 7.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 7 LFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQL 86
Cdd:PRK14472 21 IFWTAVTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 87 IEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 156
Cdd:PRK14472 101 RAEITEKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDL 170
|
|
| PRK14471 |
PRK14471 |
F0F1 ATP synthase subunit B; Provisional |
7-152 |
3.35e-18 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184695 [Multi-domain] Cd Length: 164 Bit Score: 76.37 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 7 LFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQL 86
Cdd:PRK14471 11 FFWQTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEKM 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301799138 87 IEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSI-NQEAHSKMLEQL 152
Cdd:PRK14471 91 IADAKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRKELsNKEKQHKLVEKM 157
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
6-144 |
1.80e-16 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 75.16 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 6 TLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQ 85
Cdd:PRK13428 3 TFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAER 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 301799138 86 LIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEA 144
Cdd:PRK13428 83 IAEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGELVRNHVADPA 141
|
|
| PRK13461 |
PRK13461 |
F0F1 ATP synthase subunit B; Provisional |
1-150 |
7.77e-16 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184064 [Multi-domain] Cd Length: 159 Bit Score: 70.08 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 1 MNINL-TLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQA 79
Cdd:PRK13461 1 MEINIpTIIATIINFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301799138 80 NKRANQLIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLE 150
Cdd:PRK13461 81 KSKAENVYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIK 151
|
|
| PRK13453 |
PRK13453 |
F0F1 ATP synthase subunit B; Provisional |
6-155 |
8.38e-13 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184060 Cd Length: 173 Bit Score: 62.62 E-value: 8.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 6 TLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQ 85
Cdd:PRK13453 20 TVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 86 LIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAE 155
Cdd:PRK13453 100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
12-151 |
1.78e-11 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 58.81 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 12 IAFALFIWFCMKFIWppviNAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQLIEEAK 91
Cdd:PRK07352 31 IVIGLLYYFGRGFLG----KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 92 DNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQ 151
Cdd:PRK07352 107 KQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDR 166
|
|
| PRK06231 |
PRK06231 |
F0F1 ATP synthase subunit B; Validated |
10-156 |
1.79e-09 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180481 [Multi-domain] Cd Length: 205 Bit Score: 54.08 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 10 QMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQLIEE 89
Cdd:PRK06231 54 HLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLKSE 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301799138 90 AKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 156
Cdd:PRK06231 134 LEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIREL 200
|
|
| PRK13460 |
PRK13460 |
F0F1 ATP synthase subunit B; Provisional |
11-156 |
2.82e-08 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 139585 [Multi-domain] Cd Length: 173 Bit Score: 50.41 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 11 MIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQLIEEA 90
Cdd:PRK13460 23 LVTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDALKLKNKL 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301799138 91 KDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 156
Cdd:PRK13460 103 LEETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIETELAKL 168
|
|
| atpF |
CHL00019 |
ATP synthase CF0 B subunit |
31-148 |
3.47e-08 |
|
ATP synthase CF0 B subunit
Pssm-ID: 176962 [Multi-domain] Cd Length: 184 Bit Score: 50.25 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 31 NAMQERQRKIAEGLQEAD----RASKDLELAQKSatdtLREAKVQAAQLIEQANKRANQLIEEAKDNARAEGERIKVAAQ 106
Cdd:CHL00019 51 DLLDNRKQTILNTIRNSEerreEAIEKLEKARAR----LRQAELEADEIRVNGYSEIEREKENLINQAKEDLERLENYKN 126
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 301799138 107 ADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKM 148
Cdd:CHL00019 127 ETIRFEQQRAINQVRQQVFQLALQRALGTLNSCLNNELHLRT 168
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
28-136 |
2.18e-06 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 44.61 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 28 PVINAMQERQRKIAEGLQEA-DRASKDLELAQKSAtDTLREAKVQAAQLIEQANKRANQLIEEAKDNARAEGERIKVAAQ 106
Cdd:PRK07353 29 PVGKVVEEREDYIRTNRAEAkERLAEAEKLEAQYE-QQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQASKEKAR 107
|
90 100 110
....*....|....*....|....*....|
gi 301799138 107 ADIEQEVQRAKEALRAQLASLSLLGAEKIL 136
Cdd:PRK07353 108 REIEQQKQAALAQLEQQVDALSRQILEKLL 137
|
|
| PRK14474 |
PRK14474 |
F0F1 ATP synthase subunit B; Provisional |
5-156 |
2.83e-06 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184696 [Multi-domain] Cd Length: 250 Bit Score: 45.58 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 5 LTLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRAN 84
Cdd:PRK14474 6 FTVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEQQRASFMAQAQEAAD 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301799138 85 QLIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAEL 156
Cdd:PRK14474 86 EQRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAALADLANATLEQQIVGIFIARL 157
|
|
| atpG |
CHL00118 |
ATP synthase CF0 B' subunit; Validated |
3-136 |
2.01e-05 |
|
ATP synthase CF0 B' subunit; Validated
Pssm-ID: 214369 [Multi-domain] Cd Length: 156 Bit Score: 42.28 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 3 INLTLFGQMIAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEA-DRASKDLELAQKSATDtLREAKVQAAQLIEQANK 81
Cdd:CHL00118 21 FNATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKAsEILAKANELTKQYEQE-LSKARKEAQLEITQSQK 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 301799138 82 RANQLIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKIL 136
Cdd:CHL00118 100 EAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLL 154
|
|
| PRK08475 |
PRK08475 |
F0F1 ATP synthase subunit B; Validated |
12-120 |
3.96e-05 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 236272 [Multi-domain] Cd Length: 167 Bit Score: 41.54 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 12 IAFALFIWFCMKFIWPPVINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQLIEEAK 91
Cdd:PRK08475 30 INFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIVETAKKEAYILTQKIE 109
|
90 100
....*....|....*....|....*....
gi 301799138 92 DNARAEGERIKVAAQADIEQEVQRAKEAL 120
Cdd:PRK08475 110 KQTKDDIENLIKSFEELMEFEVRKMEREV 138
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
11-126 |
7.27e-05 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 40.44 E-value: 7.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 11 MIAFALFIWFCMKFIWPPVINAMQERQRKIAeglqeadrasKDLELAQKSATDTLrEAKVQAAQLIEQANKRANQLIEEA 90
Cdd:PRK08476 14 FVVFLLLIVILNSWLYKPLLKFMDNRNASIK----------NDLEKVKTNSSDVS-EIEHEIETILKNAREEANKIRQKA 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 301799138 91 KDNARAEGERIKVAAQADIEQE-------VQRAKEALRAQLAS 126
Cdd:PRK08476 83 IAKAKEEAEKKIEAKKAELESKyeafakqLANQKQELKEQLLS 125
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
34-95 |
2.42e-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: 2.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301799138 34 QERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQLIEEAKDNAR 95
Cdd:COG3599 51 EELEEELEEYRELEETLQKTLVVAQETAEEVKENAEKEAELIIKEAELEAEKIIEEAQEKAR 112
|
|
| SPFH_HflK |
cd03404 |
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ... |
29-124 |
6.82e-04 |
|
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.
Pssm-ID: 259802 [Multi-domain] Cd Length: 266 Bit Score: 38.65 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 29 VINAMQERQRKIAEglqeadraskdlelAQKSATDTLREAKVQAAQLIEQANKRANQLIeeakdnARAEGErikVAAQAD 108
Cdd:cd03404 179 VNAARQDKERLINE--------------AQAYANEVIPRARGEAARIIQEAEAYKAEVV------ARAEGD---AARFLA 235
|
90
....*....|....*.
gi 301799138 109 IEQEVQRAKEALRAQL 124
Cdd:cd03404 236 LLAEYRKAPEVTRERL 251
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-155 |
8.36e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 38.76 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 30 INAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQLIEEAKDNARAEGERIkvAAQADI 109
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA--EAEEEL 381
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 301799138 110 EQEVQRAKEALRAQLASLSLLGAEKILQTSINQEAHSKMLEQLAAE 155
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
54-155 |
1.64e-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: 37.23 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 54 LELAQKSATDTLREAKVQAAQLIEQANKRANQLIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAE 133
Cdd:COG1390 12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEEAL 91
|
90 100
....*....|....*....|..
gi 301799138 134 KILQTSINQEAHSKMLEQLAAE 155
Cdd:COG1390 92 EKLKNLPKDPEYKELLKKLLKE 113
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
63-142 |
1.77e-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: 37.23 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 63 DTLREAKVQAAQLIEQANKRANQLIEEAKDNARAEGERIKVAAQADIEQEVQRAKEALRAQLASLSLLGAEKILQTSINQ 142
Cdd:COG1390 10 EILEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEE 89
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
29-124 |
2.75e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 37.11 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 29 VINAMQERQRKIAEGLQEADRASKDLELAQKSATDTLREAKVQAAQLIEQANKRANQLIEEAKDNA----RAEGERIKVA 104
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAdeiiKELRQLQKGG 600
|
90 100
....*....|....*....|
gi 301799138 105 AQADIEQEVQRAKEALRAQL 124
Cdd:PRK00409 601 YASVKAHELIEARKRLNKAN 620
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
31-127 |
3.87e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 36.53 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 31 NAMQERQRKIAEGLQEADRASKDLElaqksatDTLREAKVQAAQLIEQANKRANQLIEEAKDNARAEGERikvAAQADIE 110
Cdd:PRK06669 67 DAFEIVEAAEEEAKEELLKKTDEAS-------SIIEKLQMQIEREQEEWEEELERLIEEAKAEGYEEGYE---KGREEGL 136
|
90
....*....|....*..
gi 301799138 111 QEVQRAKEALRAQLASL 127
Cdd:PRK06669 137 EEVRELIEQLNKIIEKL 153
|
|
| PRK01005 |
PRK01005 |
V-type ATP synthase subunit E; Provisional |
63-155 |
5.30e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 179204 [Multi-domain] Cd Length: 207 Bit Score: 35.92 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 63 DTLREAKVQAAQLIEQANKRANQLIEEAKDNAraegERIKVAAQADIEQEVQRAKEALrAQLASLSLLGAEKILQTSINQ 142
Cdd:PRK01005 20 ETLKPAEEEAGAIVHNAKEQAKRIIAEAQEEA----EKIIRSAEETADQKLKQGESAL-VQAGKRSLESLKQAVENKIFR 94
|
90
....*....|...
gi 301799138 143 EAHSKMLEQLAAE 155
Cdd:PRK01005 95 ESLGEWLEHVLTD 107
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
63-118 |
6.61e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 35.36 E-value: 6.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 301799138 63 DTLREAKVQAAQLIEQANKRANQLIEEAKDNAraegERIKVAAQADIEQEVQRAKE 118
Cdd:PRK02292 9 DIRDEARARASEIRAEADEEAEEIIAEAEADA----EEILEDREAEAEREIEQLRE 60
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
46-128 |
6.78e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 36.00 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 46 EADRASKDLELAQKSATDTLREAKVQAAQL--IEQANKRANQLIEEA----------KDNARAEGERIKVAAQA-DIEQE 112
Cdd:PRK12472 198 EAEDAARAADEAKTAAAAAAREAAPLKASLrkLERAKARADAELKRAdkalaaaktdEAKARAEERQQKAAQQAaEAATQ 277
|
90
....*....|....*.
gi 301799138 113 VQRAKEALRAQLASLS 128
Cdd:PRK12472 278 LDTAKADAEAKRAAAA 293
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
56-156 |
8.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 35.52 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301799138 56 LAQKSATDTLREAKVQAAQLIEQANKRANQLIEEAKDNARAEGERIKVAAQADI----------EQEVQRAKEALRAQLA 125
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrerrnelqklEKRLLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|..
gi 301799138 126 SLSLLgaEKILQTSINQEAHS-KMLEQLAAEL 156
Cdd:PRK12704 104 LLEKR--EEELEKKEKELEQKqQELEKKEEEL 133
|
|
| |
