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Conserved domains on  [gi|218519656|gb|ACK80242|]
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ATP synthase F0, B subunit [Acidithiobacillus ferrooxidans ATCC 23270]

Protein Classification

similar to ATP synthase subunit b( domain architecture ID 11490213)

protein similar to ATP synthase subunit b

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 13-159 3.17e-59

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: 180.68  E-value: 3.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   13 QLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELREE 92
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218519656   93 AQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
 
Name Accession Description Interval E-value
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 13-159 3.17e-59

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: 180.68  E-value: 3.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   13 QLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELREE 92
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218519656   93 AQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 6-159 5.35e-53

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 164.95  E-value: 5.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   6 INGTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERR 85
Cdd:PRK05759   3 LNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218519656  86 GVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:PRK05759  83 AAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 8-159 3.94e-40

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: 132.22  E-value: 3.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   8 GTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGV 87
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218519656  88 ELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
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 ...
 9-139 5.85e-37

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: 123.70  E-value: 5.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   9 TLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVE 88
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 218519656  89 LREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRIL 139
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKIL 131
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 ...
 9-139 8.75e-34

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: 115.49  E-value: 8.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656    9 TLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVE 88
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 218519656   89 LREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRIL 139
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLL 131
 
Name Accession Description Interval E-value
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 13-159 3.17e-59

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: 180.68  E-value: 3.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   13 QLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELREE 92
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218519656   93 AQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 6-159 5.35e-53

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 164.95  E-value: 5.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   6 INGTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERR 85
Cdd:PRK05759   3 LNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKR 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218519656  86 GVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:PRK05759  83 AAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 8-159 3.94e-40

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: 132.22  E-value: 3.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   8 GTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGV 87
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218519656  88 ELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
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 ...
 9-139 5.85e-37

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: 123.70  E-value: 5.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   9 TLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVE 88
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 218519656  89 LREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRIL 139
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKIL 131
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 ...
 9-139 8.75e-34

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: 115.49  E-value: 8.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656    9 TLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVE 88
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 218519656   89 LREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRIL 139
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLL 131
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 8-156 1.16e-22

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 88.43  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   8 GTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGV 87
Cdd:PRK13453  19 GTVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQAR 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218519656  88 ELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMV 156
Cdd:PRK13453  99 QQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYL 167
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 15-159 1.63e-21

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 85.25  E-value: 1.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  15 VTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELREEAQ 94
Cdd:PRK14472  26 VTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKLRAEIT 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218519656  95 GKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:PRK14472 106 EKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDL 170
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 8-157 1.27e-18

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 77.52  E-value: 1.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   8 GTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGV 87
Cdd:PRK14471   9 GLFFWQTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKE 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218519656  88 ELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDD-QTHRDIIDRMVG 157
Cdd:PRK14471  89 KMIADAKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRKELSNkEKQHKLVEKMLG 159
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 1-159 2.09e-18

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 76.89  E-value: 2.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   1 MNPVGIN-GTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEII 79
Cdd:PRK14473   1 MEKLGINlGLLIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  80 ANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:PRK14473  81 AQAQERARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAAL 160
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 14-159 1.98e-17

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 74.61  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  14 LVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELREEA 93
Cdd:PRK07352  26 LINLAIVIGLLYYFGRGFLGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEI 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218519656  94 QGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:PRK07352 106 EKQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDRSIANL 171
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 9-153 4.18e-17

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 73.55  E-value: 4.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   9 TLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVE 88
Cdd:PRK13461   7 TIIATIINFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEYKSKAEN 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218519656  89 LREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIID 153
Cdd:PRK13461  87 VYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIK 151
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 11-159 1.67e-16

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 72.95  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  11 IVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELR 90
Cdd:PRK06231  52 IAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLK 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 218519656  91 EEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:PRK06231 132 SELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIREL 200
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 6-130 2.29e-14

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 65.80  E-value: 2.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   6 INGTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAergKEEMALAQKRATEL---LREAKDKAAEIIANA 82
Cdd:PRK07353   4 FDATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRAEA---KERLAEAEKLEAQYeqqLASARKQAQAVIAEA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 218519656  83 ERRGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVEL 130
Cdd:PRK07353  81 EAEADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDAL 128
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 10-130 4.68e-12

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 59.70  E-value: 4.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  10 LIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIianaerrgvel 89
Cdd:PRK08476  10 MLATFVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKI----------- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 218519656  90 REEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVEL 130
Cdd:PRK08476  79 RQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQEL 119
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 8-159 1.88e-11

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 58.88  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   8 GTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGV 87
Cdd:PRK13460  17 GLVVWTLVTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDAL 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218519656  88 ELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:PRK13460  97 KLKNKLLEETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIETELAKL 168
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 9-159 5.62e-11

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 58.67  E-value: 5.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   9 TLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVE 88
Cdd:PRK14474   7 TVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEQQRASFMAQAQEAADE 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218519656  89 LREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:PRK14474  87 QRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAALADLANATLEQQIVGIFIARL 157
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 6-139 3.36e-10

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 55.38  E-value: 3.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   6 INGTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEM-ALAQKRATELLrEAKDKAAEIIANAER 84
Cdd:CHL00118  21 FNATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEILAKAnELTKQYEQELS-KARKEAQLEITQSQK 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 218519656  85 RGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRIL 139
Cdd:CHL00118 100 EAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLL 154
PRK13428 PRK13428
F0F1 ATP synthase subunit delta; Provisional
 8-159 1.43e-08

F0F1 ATP synthase subunit delta; Provisional


Pssm-ID: 184048 [Multi-domain]  Cd Length: 445  Bit Score: 52.43  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   8 GTLIVQLVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGV 87
Cdd:PRK13428   2 STFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218519656  88 ELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREI-DDQTHRDIIDRMVGQL 159
Cdd:PRK13428  82 RIAEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGELVRNHVaDPAQQSATVDRFLDEL 154
PRK09173 PRK09173
F0F1 ATP synthase subunit B; Validated
 12-159 4.54e-08

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 169691 [Multi-domain]  Cd Length: 159  Bit Score: 49.74  E-value: 4.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  12 VQLVTFVILVAllYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEmalAQKRATELLR---EAKDKAAEIIANAERRGVE 88
Cdd:PRK09173   9 VGLVLFLALVV--YLKVPGMIARSLDARADRIKNELAEARRLREE---AQQLLAEYQRkrkEAEKEAADIVAAAEREAEA 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218519656  89 LREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:PRK09173  84 LTAEAKRKTEEYVARRNKLAEQKIAQAETDAINAVRSSAVDLAIAAAEKLLAEKVDAKAASELFKDALAQV 154
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 5-122 5.32e-07

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 46.93  E-value: 5.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   5 GINGTLIVQ-LVTFVILVALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAE 83
Cdd:PRK08475  19 ATEQYDIIErTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIVETAK 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 218519656  84 RRGVELREEAQGKAREEADRIIASARAEIDVETNRA-REV 122
Cdd:PRK08475  99 KEAYILTQKIEKQTKDDIENLIKSFEELMEFEVRKMeREV 138
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
 55-121 8.42e-06

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 41.75  E-value: 8.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218519656   55 EEMALAQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRARE 121
Cdd:TIGR02926   2 EEIKKAEEDAEELIEEAEEERKQRIAEAREEARELLEEAEEEASKLGEEIIKEAEEEIEKEAEKIRE 68
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 60-158 1.42e-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: 43.01  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  60 AQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRIL 139
Cdd:COG1390   15 AEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEEALEKL 94

                         90
                 ....*....|....*....
gi 218519656 140 HREIDDQTHRDIIDRMVGQ 158
Cdd:COG1390   95 KNLPKDPEYKELLKKLLKE 113
HrpE_YscL_not TIGR02499
type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, ...
 54-159 1.56e-05

type III secretion apparatus protein, HrpE/YscL family; This model is related to pfam06188, but is broader. pfam06188 describes HrpE-like proteins, components of bacterial type III secretion systems primarily in bacteria that infect plants. This model includes also the homologous proteins of animal pathogens, such as YscL of Yersinia pestis. This model excludes the related protein FliH of the bacterial flagellar apparatus (see pfam02108) [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274165 [Multi-domain]  Cd Length: 166  Bit Score: 42.67  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   54 KEEMALAQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVN 133
Cdd:TIGR02499   5 RAEDLAALAQAQAILAAARQRAEAILADAEEEAEASRQLGYEQGLEQFWQEAAAQLAEWQQEAEQLEASLEERLAELVLQ 84

                          90       100
                  ....*....|....*....|....*.
gi 218519656  134 GTQRILHREIDDQTHRDIIDRMVGQL 159
Cdd:TIGR02499  85 ALEQILGEYDEPERLVRLLRQLLRAV 110
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 55-121 2.69e-05

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: 41.05  E-value: 2.69e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 218519656  55 EEMALAQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRARE 121
Cdd:COG2811    8 KEIKEAEEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAQERLEEAREEAEAEAEEIIE 74
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 49-140 2.86e-05

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: 41.05  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  49 AAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELR----EEAQGKAREEADRIIASARAEIDVETNRAREVLR 124
Cdd:COG2811   13 AEEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEEAqerlEEAREEAEAEAEEIIEEGEKEAEALKKKAEDKLD 92

                         90
                 ....*....|....*.
gi 218519656 125 gQVVELVVNGTQRILH 140
Cdd:COG2811   93 -KAVELLVEEFEEAVH 107
PRK01558 PRK01558
V-type ATP synthase subunit E; Provisional
 54-113 1.42e-04

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179302  Cd Length: 198  Bit Score: 40.13  E-value: 1.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  54 KEEMALAQKRATELLREAKDKAAEIIANAERRGVELREeaqgKAREEADRIIASARAEID 113
Cdd:PRK01558  14 KDGLEEAERLANEIILEAKEEAEEIIAKAEEEAKELKA----KAEKEANDYKRHALEASR 69
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 54-133 3.95e-04

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 38.83  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  54 KEEMALAQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRI----IASARAEIDVET-NRAREVL---RG 125
Cdd:PRK02292   8 EDIRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLreqeLSSAKLEAKRERlNARKEVLedvRN 87


                 ....*...
gi 218519656 126 QVVELVVN 133
Cdd:PRK02292  88 QVEDEIAS 95
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 32-104 6.27e-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: 37.53  E-value: 6.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218519656  32 LRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRI 104
Cdd:COG3599   46 LKEKLEELEEELEEYRELEETLQKTLVVAQETAEEVKENAEKEAELIIKEAELEAEKIIEEAQEKARKIVREI 118
PTZ00121 PTZ00121
MAEBL; Provisional
 32-136 9.54e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 9.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   32 LRKVMDDRraKIADGLAAAERGK--EEMALAQ--KRATELLR-EAKDKAAEIIANAERRGVELREEAQGKAREEADRIIA 106
Cdd:PTZ00121 1502 AKKAAEAK--KKADEAKKAEEAKkaDEAKKAEeaKKADEAKKaEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579

                          90       100       110
                  ....*....|....*....|....*....|..
gi 218519656  107 SARAEI--DVETNRAREVLRGQVVELVVNGTQ 136
Cdd:PTZ00121 1580 LRKAEEakKAEEARIEEVMKLYEEEKKMKAEE 1611
PLN02316 PLN02316
synthase/transferase
 59-124 1.10e-03

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 38.31  E-value: 1.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218519656   59 LAQKRATELLREAKDKAAEiianaERRGVELREEAQGKAREEADRiiASARAEIDVETNRAREVLR 124
Cdd:PLN02316  250 LLEEKRRELEKLAKEEAER-----ERQAEEQRRREEEKAAMEADR--AQAKAEVEKRREKLQNLLK 308
PRK01005 PRK01005
V-type ATP synthase subunit E; Provisional
 37-117 1.80e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179204 [Multi-domain]  Cd Length: 207  Bit Score: 37.07  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  37 DDRRAKIADGLAaaergKEEMALAQKRATELLREAKDKAAEIIANaerrgvelreeaqgkAREEADRIIASARAEIDVET 116
Cdd:PRK01005   7 QDKLKQICDALR-----EETLKPAEEEAGAIVHNAKEQAKRIIAE---------------AQEEAEKIIRSAEETADQKL 66


                 .
gi 218519656 117 N 117
Cdd:PRK01005  67 K 67
PTZ00121 PTZ00121
MAEBL; Provisional
 33-126 2.75e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.43  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656   33 RKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKD-KAAEIIANAE--RRGVELREEAQGKAREEADRIIASAR 109
Cdd:PTZ00121 1128 RKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEaRKAEDAKKAEaaRKAEEVRKAEELRKAEDARKAEAARK 1207

                          90
                  ....*....|....*..
gi 218519656  110 AEidvETNRAREVLRGQ 126
Cdd:PTZ00121 1208 AE---EERKAEEARKAE 1221
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
 60-131 4.43e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 35.89  E-value: 4.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 218519656  60 AQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEAD----RIIASARAEIDVETNRAREVLRGQVVELV 131
Cdd:PRK03963  15 AEQKIEYILEEAQKEAEKIKEEARKRAESKAEWILRKAKTQAElekqRIIANAKLEVRRKRLAVQEELISEVLEAV 90
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
 66-119 6.07e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 35.50  E-value: 6.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 218519656  66 ELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRA 119
Cdd:PRK03963  10 EINREAEQKIEYILEEAQKEAEKIKEEARKRAESKAEWILRKAKTQAELEKQRI 63
PRK08404 PRK08404
V-type ATP synthase subunit H; Validated
 56-137 6.25e-03

V-type ATP synthase subunit H; Validated


Pssm-ID: 169428 [Multi-domain]  Cd Length: 103  Bit Score: 34.38  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  56 EMALAQKRATELLREAKDKAAEIIANAERRGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGT 135
Cdd:PRK08404   7 EIVKAEKEAEERIEKAKEEAKKIIRKAKEEAKKIEEEIIKKAEEEAQKLIEKKKKEGEEEAKKILEEGEKEIEELKVKAE 86


                 ..
gi 218519656 136 QR 137
Cdd:PRK08404  87 EN 88
NhaP COG0025
NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];
10-146 7.05e-03

NhaP-type Na+/H+ or K+/H+ antiporter [Inorganic ion transport and metabolism];


Pssm-ID: 439796 [Multi-domain]  Cd Length: 506  Bit Score: 35.71  E-value: 7.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  10 LIVQLVTFVILV-----ALLYKYMYGPLRKVMDDRRAKIADGLAAAERGKEEMALAQKRATELLREAKDKAAEIIANAER 84
Cdd:COG0025  363 LILALAFGVILLtlvlqGLTLPPLARRLGLREDEPEGEELEAALARAALLELLAAELLADDEEVVLRAARRARRRREAAE 442

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218519656  85 RGVELREEAQGKAREEADRIIASARAEIDVETNRAREVLRGQVVELVVNGTQRILHREIDDQ 146
Cdd:COG0025  443 LLSEEAEEELDEDLLRLLLALLRLRLLNALAAARLERLLLRRRVEELLRLLERLLRERELEE 504
PRK01558 PRK01558
V-type ATP synthase subunit E; Provisional
 59-144 8.46e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179302  Cd Length: 198  Bit Score: 35.12  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218519656  59 LAQKRATELLREAKDKAAEIIANAERRgvelREEAQGKAREEADRIIASARAEIDVETNRAREVLRgQVVELVVNGTQRI 138
Cdd:PRK01558   8 LINKIKKDGLEEAERLANEIILEAKEE----AEEIIAKAEEEAKELKAKAEKEANDYKRHALEASR-QAGRDLLISFEKS 82


                 ....*.
gi 218519656 139 LHREID 144
Cdd:PRK01558  83 IKSLFK 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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