NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the product of the nervy gene in Drosophila and the human mtg8b protein, which is hypothesized to be a transcription factor.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188976 164 KLKRFLTTLQQFGNDISPEIGERVRSLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARMAK 243
Cdd:pfam07531   4 KCKNFLSTLIKLAGEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNSARFIQ 83

                  ....*..
gi 1207188976 244 QTPAQYL 250
Cdd:pfam07531  84 QCPPQYL 90

MYND finger;

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1207188976 573 CWNCGRKASET--CSGCNTARYCGSFCQHKDWEKHHHVC 609
Cdd:pfam01753   1 CAVCGKEALKLlrCSRCKSVYYCSKECQKADWPYHKKEC 39

NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the product of the nervy gene in Drosophila and the human mtg8b protein, which is hypothesized to be a transcription factor.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188976 164 KLKRFLTTLQQFGNDISPEIGERVRSLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARMAK 243
Cdd:pfam07531   4 KCKNFLSTLIKLAGEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNSARFIQ 83

                  ....*..
gi 1207188976 244 QTPAQYL 250
Cdd:pfam07531  84 QCPPQYL 90

NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it mediates oligomerization and protein-protein interactions. It forms an alpha-helical tetramer.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207188976 386 QEEVIDHRLTDREWAEEWKHLDNLLNCIMDMVEKTRRSLTVLRRCQEADREEMNHWIRRYSDVEDMK 452
Cdd:pfam08788   1 REEYIDTRLTDREWADEWRHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEELK 67

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207188976 507 AEEAVNEVKRQAMSELQKAVSDAERKAHEMIS---AERSKMERALAEAKRQ 554
Cdd:COG3599    74 AQETAEEVKENAEKEAELIIKEAELEAEKIIEeaqEKARKIVREIEELKRQ 124

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 1207188976 505 RKAEEAVNEVKRQAMSELQKAVSDAER-------KAHEMISAERskmERALAEAKRQASEDALTV 562
Cdd:cd06503    65 AEAQEIIEEARKEAEKIKEEILAEAKEeaerileQAKAEIEQEK---EKALAELRKEVADLAVEA 126

NHR1 homology to TAF; This corresponds to the region NHR1 that is conserved between the product of the nervy gene in Drosophila and the human mtg8b protein, which is hypothesized to be a transcription factor.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188976 164 KLKRFLTTLQQFGNDISPEIGERVRSLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARMAK 243
Cdd:pfam07531   4 KCKNFLSTLIKLAGEQSPETGENVKELVQGLLNGKIEPEEFTSKLQEELNSSPQPYLVPFLKKSLPALRQELLNSARFIQ 83

                  ....*..
gi 1207188976 244 QTPAQYL 250
Cdd:pfam07531  84 QCPPQYL 90

NHR2 domain like; The NHR2 (Nervy homology 2) domain is found in the ETO protein where it mediates oligomerization and protein-protein interactions. It forms an alpha-helical tetramer.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207188976 386 QEEVIDHRLTDREWAEEWKHLDNLLNCIMDMVEKTRRSLTVLRRCQEADREEMNHWIRRYSDVEDMK 452
Cdd:pfam08788   1 REEYIDTRLTDREWADEWRHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEELK 67

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207188976 507 AEEAVNEVKRQAMSELQKAVSDAERKAHEMIS---AERSKMERALAEAKRQ 554
Cdd:COG3599    74 AQETAEEVKENAEKEAELIIKEAELEAEKIIEeaqEKARKIVREIEELKRQ 124

V-type ATP synthase subunit E; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207188976 501 EEIWRKAEEAVNEVKRQAMSELQKAVSDAERKAHEMIsaerskmERALAEAKRQASEdaltvINQQEDSS 570
Cdd:PRK02292    8 EDIRDEARARASEIRAEADEEAEEIIAEAEADAEEIL-------EDREAEAEREIEQ-----LREQELSS 65

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207188976 501 EEIwRKAEEAVNEVKRQAMSELQKAVSDAERKAHEMIS-----AERSKmERALAEAKRQASEDALTVINQQE 567
Cdd:COG2811     8 KEI-KEAEEEADEIIEEAKEEREERIAEAREEAEEIIEqaeeeAEEEA-QERLEEAREEAEAEAEEIIEEGE 77

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 1207188976 505 RKAEEAVNEVKRQAMSELQKAVSDAER-------KAHEMISAERskmERALAEAKRQASEDALTV 562
Cdd:cd06503    65 AEAQEIIEEARKEAEKIKEEILAEAKEeaerileQAKAEIEQEK---EKALAELRKEVADLAVEA 126

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207188976 506 KAEEAVNEVKrQAMSELQKAVSDAERKAHEMISAERSKMERALAEAKRQASEDA 559
Cdd:COG0711    42 EAERAKEEAE-AALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEA 94

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207188976 501 EEIWRKAEEA---VNEVKRQAmsELQKAVSDAERKAHEMISAERskmeRALAEAKRQASEDAL 560
Cdd:TIGR02794 101 EKAAKQAEQAakqAEEKQKQA--EEAKAKQAAEAKAKAEAEAER----KAKEEAAKQAEEEAK 157