|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1-156 |
1.03e-65 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 197.31 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 1 MNMNATILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQAN 80
Cdd:PRK05759 1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2094593737 81 KRRSQILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 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 |
7.52e-54 |
|
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: 166.81 E-value: 7.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 10 QAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQILDE 89
Cdd:TIGR01144 1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2094593737 90 AKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 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 |
1.59e-35 |
|
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: 120.28 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 5 ATILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRS 84
Cdd:COG0711 1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2094593737 85 QILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 156
Cdd:COG0711 81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
6-137 |
2.33e-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: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 6 TILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQ 85
Cdd:cd06503 1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2094593737 86 ILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIE 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 |
9.11e-27 |
|
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: 97.38 E-value: 9.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 6 TILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQ 85
Cdd:pfam00430 1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2094593737 86 ILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIE 137
Cdd:pfam00430 81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1-156 |
1.03e-65 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 197.31 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 1 MNMNATILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQAN 80
Cdd:PRK05759 1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2094593737 81 KRRSQILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 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 |
7.52e-54 |
|
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: 166.81 E-value: 7.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 10 QAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQILDE 89
Cdd:TIGR01144 1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2094593737 90 AKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 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 |
1.59e-35 |
|
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: 120.28 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 5 ATILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRS 84
Cdd:COG0711 1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2094593737 85 QILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 156
Cdd:COG0711 81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
6-137 |
2.33e-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: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 6 TILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQ 85
Cdd:cd06503 1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2094593737 86 ILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIE 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 |
9.11e-27 |
|
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: 97.38 E-value: 9.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 6 TILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQ 85
Cdd:pfam00430 1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2094593737 86 ILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIE 137
Cdd:pfam00430 81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
|
|
| PRK14472 |
PRK14472 |
F0F1 ATP synthase subunit B; Provisional |
7-156 |
3.78e-21 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172947 [Multi-domain] Cd Length: 175 Bit Score: 84.48 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 7 ILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQI 86
Cdd:PRK14472 21 IFWTAVTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 87 LDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 156
Cdd:PRK14472 101 RAEITEKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDL 170
|
|
| PRK14471 |
PRK14471 |
F0F1 ATP synthase subunit B; Provisional |
10-156 |
2.44e-20 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184695 [Multi-domain] Cd Length: 164 Bit Score: 81.76 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 10 QAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQILDE 89
Cdd:PRK14471 14 QTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEKMIAD 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2094593737 90 AKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIErsvDEAANSDIVDKLVAEL 156
Cdd:PRK14471 94 AKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLR---KELSNKEKQHKLVEKM 157
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
6-156 |
1.61e-15 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 72.46 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 6 TILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQ 85
Cdd:PRK13428 3 TFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAER 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2094593737 86 ILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSV-DEAANSDIVDKLVAEL 156
Cdd:PRK13428 83 IAEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGELVRNHVaDPAQQSATVDRFLDEL 154
|
|
| PRK13453 |
PRK13453 |
F0F1 ATP synthase subunit B; Provisional |
6-155 |
7.86e-15 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184060 Cd Length: 173 Bit Score: 67.63 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 6 TILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQ 85
Cdd:PRK13453 20 TVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 86 ILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAE 155
Cdd:PRK13453 100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
|
|
| PRK13461 |
PRK13461 |
F0F1 ATP synthase subunit B; Provisional |
1-154 |
1.75e-14 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184064 [Multi-domain] Cd Length: 159 Bit Score: 66.61 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 1 MNMN-ATILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQA 79
Cdd:PRK13461 1 MEINiPTIIATIINFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2094593737 80 NKRRSQILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVA 154
Cdd:PRK13461 81 KSKAENVYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIKDFIS 155
|
|
| PRK14473 |
PRK14473 |
F0F1 ATP synthase subunit B; Provisional |
7-156 |
5.91e-14 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 172948 [Multi-domain] Cd Length: 164 Bit Score: 65.33 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 7 ILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQI 86
Cdd:PRK14473 11 LIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQAQERARAQ 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 87 LDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 156
Cdd:PRK14473 91 EAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAAL 160
|
|
| PRK06231 |
PRK06231 |
F0F1 ATP synthase subunit B; Validated |
8-156 |
3.68e-12 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180481 [Multi-domain] Cd Length: 205 Bit Score: 61.40 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 8 LGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQIL 87
Cdd:PRK06231 52 IAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLK 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2094593737 88 DEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 156
Cdd:PRK06231 132 SELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIREL 200
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
11-156 |
1.67e-10 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 56.12 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 11 AIAFILFVWFCMKYvwppLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQILDEA 90
Cdd:PRK07352 30 AIVIGLLYYFGRGF----LGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2094593737 91 KAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 156
Cdd:PRK07352 106 EKQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDRSIANL 171
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
4-138 |
3.91e-09 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 51.93 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 4 NATILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAeraKKDLDLAQANATD---QLKKAKAEAQVIIEQAN 80
Cdd:PRK07353 5 DATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRAEA---KERLAEAEKLEAQyeqQLASARKQAQAVIAEAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2094593737 81 KRRSQILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILavagAEKIIER 138
Cdd:PRK07353 82 AEADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDAL----SRQILEK 135
|
|
| atpG |
CHL00118 |
ATP synthase CF0 B' subunit; Validated |
4-136 |
1.63e-08 |
|
ATP synthase CF0 B' subunit; Validated
Pssm-ID: 214369 [Multi-domain] Cd Length: 156 Bit Score: 50.76 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 4 NATILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAkkdldLAQANAT-----DQLKKAKAEAQVIIEQ 78
Cdd:CHL00118 22 NATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEI-----LAKANELtkqyeQELSKARKEAQLEITQ 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2094593737 79 ANKRRSQILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKII 136
Cdd:CHL00118 97 SQKEAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLL 154
|
|
| PRK13460 |
PRK13460 |
F0F1 ATP synthase subunit B; Provisional |
12-156 |
2.84e-08 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 139585 [Multi-domain] Cd Length: 173 Bit Score: 50.41 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 12 IAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQILDEAK 91
Cdd:PRK13460 24 VTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDALKLKNKLL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2094593737 92 AEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 156
Cdd:PRK13460 104 EETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIETELAKL 168
|
|
| PRK14474 |
PRK14474 |
F0F1 ATP synthase subunit B; Provisional |
6-140 |
7.43e-07 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184696 [Multi-domain] Cd Length: 250 Bit Score: 47.12 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 6 TILGQAIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERakkdldlAQANATDQLKKAKAEAQVIIEQankrRSQ 85
Cdd:PRK14474 7 TVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQ-------RQQEAGQEAERYRQKQQSLEQQ----RAS 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2094593737 86 ILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSV 140
Cdd:PRK14474 76 FMAQAQEAADEQRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMV 130
|
|
| PRK09174 |
PRK09174 |
F0F1 ATP synthase subunit B; |
11-115 |
3.32e-06 |
|
F0F1 ATP synthase subunit B;
Pssm-ID: 169692 [Multi-domain] Cd Length: 204 Bit Score: 44.79 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 11 AIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANkrrsqilDEA 90
Cdd:PRK09174 60 AITFGLFYLFMSRVILPRIGGIIETRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSIAQAAR-------EAA 132
|
90 100
....*....|....*....|....*
gi 2094593737 91 KAEAEQERTKIVTQAQAEIDAERKR 115
Cdd:PRK09174 133 KAKAEAERAAIEASLEKKLKEAEAR 157
|
|
| atpF |
CHL00019 |
ATP synthase CF0 B subunit |
61-132 |
4.79e-06 |
|
ATP synthase CF0 B subunit
Pssm-ID: 176962 [Multi-domain] Cd Length: 184 Bit Score: 44.09 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 61 ATDQLKKAKAEaqviIEQANKRRSQILDEAKAEAEQERTKIVTQA-----------QAEIDAERKRAREELRKQVAILAV 129
Cdd:CHL00019 74 AIEKLEKARAR----LRQAELEADEIRVNGYSEIEREKENLINQAkedlerlenykNETIRFEQQRAINQVRQQVFQLAL 149
|
...
gi 2094593737 130 AGA 132
Cdd:CHL00019 150 QRA 152
|
|
| PRK09173 |
PRK09173 |
F0F1 ATP synthase subunit B; Validated |
12-156 |
5.85e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 169691 [Multi-domain] Cd Length: 159 Bit Score: 43.58 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 12 IAFILFVWFCMKYVWPPLMA-AIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQILDEA 90
Cdd:PRK09173 9 VGLVLFLALVVYLKVPGMIArSLDARADRIKNELAEARRLREEAQQLLAEYQRKRKEAEKEAADIVAAAEREAEALTAEA 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2094593737 91 KAEAE---QERTKIVTQ--AQAEIDAERkrareELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 156
Cdd:PRK09173 89 KRKTEeyvARRNKLAEQkiAQAETDAIN-----AVRSSAVDLAIAAAEKLLAEKVDAKAASELFKDALAQV 154
|
|
| PRK02292 |
PRK02292 |
V-type ATP synthase subunit E; Provisional |
63-147 |
1.34e-04 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 235026 [Multi-domain] Cd Length: 188 Bit Score: 40.37 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 63 DQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIVTQAQAEIDAERKRA---------REELRKQVAILavagaE 133
Cdd:PRK02292 9 DIRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLREQElssakleakRERLNARKEVL-----E 83
|
90
....*....|....
gi 2094593737 134 KIIERSVDEAANSD 147
Cdd:PRK02292 84 DVRNQVEDEIASLD 97
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
29-101 |
1.48e-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: 39.45 E-value: 1.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2094593737 29 LMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKI 101
Cdd:COG3599 46 LKEKLEELEEELEEYRELEETLQKTLVVAQETAEEVKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREI 118
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
65-143 |
1.69e-04 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 39.93 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2094593737 65 LKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKIIERSVDEA 143
Cdd:COG1390 12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEEA 90
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
11-112 |
4.72e-04 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 38.13 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 11 AIAFILFVWFCMKYVWPPLMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQAnkrrsqiLDEA 90
Cdd:PRK08476 14 FVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQKA-------IAKA 86
|
90 100
....*....|....*....|..
gi 2094593737 91 KAEAEQErtkiVTQAQAEIDAE 112
Cdd:PRK08476 87 KEEAEKK----IEAKKAELESK 104
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
32-144 |
7.32e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 38.70 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 32 AIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQViiEQANKRRSQILDEAKAEAEQERTKIVTQA--QAEI 109
Cdd:COG2268 215 AIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREA--ETARAEAEAAYEIAEANAEREVQRQLEIAerEREI 292
|
90 100 110
....*....|....*....|....*....|....*...
gi 2094593737 110 DAERKRA---REELRKQVAILAVAGAEKIIERSVDEAA 144
Cdd:COG2268 293 ELQEKEAereEAELEADVRKPAEAEKQAAEAEAEAEAE 330
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
27-122 |
8.24e-04 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 38.28 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 27 PPLMAAIEKRQKeiadglasAERAKKDLDL-AQANATDQLKKAKAEAQVIIEQAN-KRRSQILdeaKAEAEQERTKIVTQ 104
Cdd:COG0330 167 EEVQDAMEDRMK--------AEREREAAILeAEGYREAAIIRAEGEAQRAIIEAEaYREAQIL---RAEGEAEAFRIVAE 235
|
90
....*....|....*....
gi 2094593737 105 A-QAEIDAERKRAREELRK 122
Cdd:COG0330 236 AySAAPFVLFYRSLEALEE 254
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
61-123 |
1.45e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 37.84 E-value: 1.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2094593737 61 ATDQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIvtqaQAEIDAERKRAREELRKQ 123
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKL----RNEFEKELRERRNELQKL 87
|
|
| PRK01005 |
PRK01005 |
V-type ATP synthase subunit E; Provisional |
63-114 |
2.22e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 179204 [Multi-domain] Cd Length: 207 Bit Score: 36.69 E-value: 2.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2094593737 63 DQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQertkIVTQAQAEIDAERK 114
Cdd:PRK01005 20 ETLKPAEEEAGAIVHNAKEQAKRIIAEAQEEAEK----IIRSAEETADQKLK 67
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
57-135 |
3.29e-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: 35.27 E-value: 3.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2094593737 57 AQANATDQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKI 135
Cdd:COG2811 13 AEEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAQERLEEAREEAEAEAEEIIEEGEKEAEALKKKAEDKL 91
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
57-155 |
3.93e-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: 36.08 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 57 AQANATDQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQVAILAVAGAEKII 136
Cdd:COG1390 15 AEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEEALEKL 94
|
90
....*....|....*....
gi 2094593737 137 ERSVDEAANSDIVDKLVAE 155
Cdd:COG1390 95 KNLPKDPEYKELLKKLLKE 113
|
|
| PRK03963 |
PRK03963 |
V-type ATP synthase subunit E; Provisional |
65-124 |
4.07e-03 |
|
V-type ATP synthase subunit E; Provisional
Pssm-ID: 167649 [Multi-domain] Cd Length: 198 Bit Score: 35.89 E-value: 4.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2094593737 65 LKKAKAEAQVIIEQANKR----RSQILDEAKAEAEQERTKIVTQAQAEIDAERKRAREELRKQV 124
Cdd:PRK03963 23 LEEAQKEAEKIKEEARKRaeskAEWILRKAKTQAELEKQRIIANAKLEVRRKRLAVQEELISEV 86
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
30-140 |
4.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 36.29 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 30 MAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVI----IEQAnkrRSQILDEAKAEAEQERTKIVTQA 105
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltAEEA---KEILLEKVEEEARHEAAVLIKEI 178
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2094593737 106 QAEIDAE-RKRAREelrkqvaILAVA----GAEKIIERSV 140
Cdd:PRK12704 179 EEEAKEEaDKKAKE-------ILAQAiqrcAADHVAETTV 211
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-156 |
5.97e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 36.07 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 29 LMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIVTQAQAE 108
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2094593737 109 IDAERKRAREELRKQVAILAVAGAEKIIERSVDEAANSDIVDKLVAEL 156
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
29-125 |
6.92e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 35.96 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 29 LMAAIEKRQKEIADGLASAERAKKDLDLAQANATDQLKKAKAEAQVIIEQANKRRSQILDEAKAEAEQERTKIVTQAQAE 108
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGG 600
|
90
....*....|....*..
gi 2094593737 109 IDAERKRAREELRKQVA 125
Cdd:PRK00409 601 YASVKAHELIEARKRLN 617
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
34-125 |
8.16e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 35.89 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2094593737 34 EKRQKEIADGLASAERAKKDLDLAQANATDQLKKA----KAEAQVIIEQANKRRSQILDEAKAE----AEQERTKIVTQA 105
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkKAEEENKIKAAEEAKKAEEDKKKAEeakkAEEDEKKAAEAL 1694
|
90 100
....*....|....*....|
gi 2094593737 106 QAEidAERKRAREELRKQVA 125
Cdd:PTZ00121 1695 KKE--AEEAKKAEELKKKEA 1712
|
|
| |
