MYND finger;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2462621453 272 CWNCGRKASET--CSGCNTARYCGSFCQHKDWEKHHHIC 308
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39

MYND finger;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2462621453 272 CWNCGRKASET--CSGCNTARYCGSFCQHKDWEKHHHIC 308
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462621453 200 EEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQAA---EDALAVINQQ 265
Cdd:cd06503    50 EELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEqekEKALAELRKE 118

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462621453 160 KKGGGSSSSHSRQQSPVNPDPVALDAHREFLHRPAsgyVPEEIWKKAEEA---VNEVKRQAmtELQKAVSEAERKAHDMI 236
Cdd:TIGR02794  64 KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA---AAEKAAKQAEQAakqAEEKQKQA--EEAKAKQAAEAKAKAEA 138

                          90       100
                  ....*....|....*....|....
gi 2462621453 237 TTERAKMErtvaEAKRQAAEDALA 260
Cdd:TIGR02794 139 EAERKAKE----EAAKQAEEEAKA 158

MYND finger;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2462621453 272 CWNCGRKASET--CSGCNTARYCGSFCQHKDWEKHHHIC 308
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39

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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462621453 200 EEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQAA---EDALAVINQQ 265
Cdd:cd06503    50 EELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEqekEKALAELRKE 118

V-type ATP synthase subunit E; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462621453 198 VPEEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQA 254
Cdd:PRK02292    6 VVEDIRDEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLREQE 62

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462621453 203 WKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKmERTVAEAKRQAAEDALAVINQQEDSSE 270
Cdd:COG3064    79 LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAE-KEKAEEAKRKAEEEAKRKAEEERKAAE 145

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462621453 200 EEIWKKAE--------EAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQAAEDALA 260
Cdd:COG1390    20 EEILEEAEeeaekileEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFE 88