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Conserved domains on  [gi|2315907287|gb|UYB93382|]
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ATP synthase beta subunit, partial (chloroplast) [Chamaecrista usambarensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
atpB super family cl33325
ATP synthase CF1 beta subunit
 2-250 0e+00

ATP synthase CF1 beta subunit


The actual alignment was detected with superfamily member CHL00060:

Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 530.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287   2 TTSGPEVSALEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGL 81
Cdd:CHL00060    2 NPTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  82 MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRG 161
Cdd:CHL00060   82 MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287 162 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGA 241
Cdd:CHL00060  162 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGA 241


                  ....*....
gi 2315907287 242 RMRVGLTAL 250
Cdd:CHL00060  242 RMRVGLTAL 250
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 2-250 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 530.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287   2 TTSGPEVSALEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGL 81
Cdd:CHL00060    2 NPTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  82 MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRG 161
Cdd:CHL00060   82 MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287 162 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGA 241
Cdd:CHL00060  162 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGA 241


                  ....*....
gi 2315907287 242 RMRVGLTAL 250
Cdd:CHL00060  242 RMRVGLTAL 250
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 12-250 3.14e-143

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 409.09  E-value: 3.14e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  12 EKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 91
Cdd:COG0055     1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  92 APLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAG 171
Cdd:COG0055    77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2315907287 172 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTAL 250
Cdd:COG0055   157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTAL 228
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 15-250 5.49e-125

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 362.50  E-value: 5.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  15 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRdtvgQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
Cdd:TIGR01039   1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR----AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  95 SVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:TIGR01039  77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907287 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTAL 250
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGL 225
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 95-250 2.04e-97

F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410877 [Multi-domain]  Cd Length: 277  Bit Score: 286.04  E-value: 2.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  95 SVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:cd01133     1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907287 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqnIAESKVALVYGQMNEPPGARMRVGLTAL 250
Cdd:cd01133    81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL--DGLSKVALVYGQMNEPPGARARVALTGL 154
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 148-250 1.86e-21

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 88.57  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287 148 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSK 227
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70

                          90       100
                  ....*....|....*....|...
gi 2315907287 228 VALVYGQMNEPPGARMRVGLTAL 250
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTAL 93
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 2-250 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 530.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287   2 TTSGPEVSALEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGL 81
Cdd:CHL00060    2 NPTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  82 MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRG 161
Cdd:CHL00060   82 MRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287 162 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGA 241
Cdd:CHL00060  162 GKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGA 241


                  ....*....
gi 2315907287 242 RMRVGLTAL 250
Cdd:CHL00060  242 RMRVGLTAL 250
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 12-250 3.14e-143

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 409.09  E-value: 3.14e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  12 EKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 91
Cdd:COG0055     1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  92 APLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAG 171
Cdd:COG0055    77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2315907287 172 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTAL 250
Cdd:COG0055   157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTAL 228
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 15-250 5.49e-125

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 362.50  E-value: 5.49e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  15 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRdtvgQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
Cdd:TIGR01039   1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR----AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  95 SVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:TIGR01039  77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907287 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTAL 250
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGL 225
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 95-250 2.04e-97

F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410877 [Multi-domain]  Cd Length: 277  Bit Score: 286.04  E-value: 2.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  95 SVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:cd01133     1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907287 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqnIAESKVALVYGQMNEPPGARMRVGLTAL 250
Cdd:cd01133    81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL--DGLSKVALVYGQMNEPPGARARVALTGL 154
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 17-250 7.06e-76

alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.


Pssm-ID: 132348 [Multi-domain]  Cd Length: 449  Bit Score: 236.65  E-value: 7.06e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  17 GRIAQIIGPVLDVAFPpGKMPNIYNALvvkgrdTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSV 96
Cdd:TIGR03305   1 GHVVAVRGSIVDVRFD-GELPAIHSVL------RAGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  97 PVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 176
Cdd:TIGR03305  74 PVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2315907287 177 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqniaeskVALVYGQMNEPPGARMRVGLTAL 250
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTAL 220
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 95-250 7.14e-62

RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410884 [Multi-domain]  Cd Length: 270  Bit Score: 195.37  E-value: 7.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  95 SVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:cd19476     1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907287 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGvineqniAESKVALVYGQMNEPPGARMRVGLTAL 250
Cdd:cd19476    81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG-------AMERTVVVANTANDPPGARMRVPYTGL 149
ATP-synt_F1_beta_N cd18115
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ...
 15-94 1.49e-39

F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.


Pssm-ID: 349739 [Multi-domain]  Cd Length: 76  Bit Score: 131.48  E-value: 1.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  15 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
Cdd:cd18115     1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDD----GKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 17-177 6.82e-25

Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440771 [Multi-domain]  Cd Length: 433  Bit Score: 101.65  E-value: 6.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  17 GRIAQIIGPVLDVAFPPGKMpniyNALV-VKGRDtvgqQINVTCEVqqlLG--NNRVRAVAMSATDGLMRGMEVIDTGAP 93
Cdd:COG1157    21 GRVTRVVGLLIEAVGPDASI----GELCeIETAD----GRPVLAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  94 LSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQ---LDTKLaifETGIKVVDLLAPYRRGGKIGLFGGA 170
Cdd:COG1157    90 LSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGS 166


                  ....*..
gi 2315907287 171 GVGKTVL 177
Cdd:COG1157   167 GVGKSTL 173
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 148-250 1.86e-21

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 88.57  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287 148 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSK 227
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70

                          90       100
                  ....*....|....*....|...
gi 2315907287 228 VALVYGQMNEPPGARMRVGLTAL 250
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTAL 93
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 65-184 4.54e-20

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 88.43  E-value: 4.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAI 144
Cdd:PRK13343   66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2315907287 145 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
Cdd:PRK13343  146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN 185
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
 65-184 1.43e-19

proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273365 [Multi-domain]  Cd Length: 501  Bit Score: 87.06  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAI 144
Cdd:TIGR00962  65 LEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEP 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2315907287 145 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
Cdd:TIGR00962 145 LQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIIN 184
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 19-91 1.96e-19

ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.


Pssm-ID: 427029 [Multi-domain]  Cd Length: 69  Bit Score: 79.51  E-value: 1.96e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2315907287  19 IAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 91
Cdd:pfam02874   1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 95-249 1.86e-18

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.


Pssm-ID: 410880 [Multi-domain]  Cd Length: 265  Bit Score: 81.84  E-value: 1.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  95 SVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:cd01136     1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2315907287 175 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYMEmkesGVINEQNIaeSKVALVYGQMNEPPGARMRVGLTA 249
Cdd:cd01136    81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGL--KRSVLVVATSDESPLLRVRAAYTA 145
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 65-161 5.49e-18

FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439826 [Multi-domain]  Cd Length: 504  Bit Score: 82.39  E-value: 5.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQ---LDTK 141
Cdd:COG0056    66 LEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDrqpVHEP 145

                          90       100
                  ....*....|....*....|
gi 2315907287 142 LaifETGIKVVDLLAPYRRG 161
Cdd:COG0056   146 L---QTGIKAIDAMIPIGRG 162
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 79-178 9.64e-18

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 81.74  E-value: 9.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  79 DGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQ---LDTKLAifeTGIKVVDLL 155
Cdd:PRK09099   81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGL 157

                          90       100
                  ....*....|....*....|...
gi 2315907287 156 APYRRGGKIGLFGGAGVGKTVLI 178
Cdd:PRK09099  158 MTLGEGQRMGIFAPAGVGKSTLM 180
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 70-161 1.30e-17

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 81.27  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  70 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQ---LDTKLaifE 146
Cdd:PRK09281   71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDrksVHEPL---Q 147

                          90
                  ....*....|....*
gi 2315907287 147 TGIKVVDLLAPYRRG 161
Cdd:PRK09281  148 TGIKAIDAMIPIGRG 162
fliI PRK08927
flagellar protein export ATPase FliI;
7-186 6.44e-15

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 73.47  E-value: 6.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287   7 EVSALEKKNL-GRIAQIIGPVLDVAFPPGKMpNIYNALVVKGRDTVGqqinVTCEVqqlLGNNRVRAVAM--SATDGLMR 83
Cdd:PRK08927    8 AIGDIDTLVIyGRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRP----VPCEV---VGFRGDRALLMpfGPLEGVRR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  84 GMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTS-PIHRSAP---AFIQLDTKLaifETGIKVVDLLAPYR 159
Cdd:PRK08927   80 GCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPpahSRARVGEPL---DLGVRALNTFLTCC 156

                         170       180
                  ....*....|....*....|....*..
gi 2315907287 160 RGGKIGLFGGAGVGKTVLIMELINNIA 186
Cdd:PRK08927  157 RGQRMGIFAGSGVGKSVLLSMLARNAD 183
fliI PRK08472
flagellar protein export ATPase FliI;
94-188 1.11e-14

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 72.80  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  94 LSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 173
Cdd:PRK08472   90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169

                          90
                  ....*....|....*
gi 2315907287 174 KTVLiMELINNIAKA 188
Cdd:PRK08472  170 KSTL-MGMIVKGCLA 183
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
80-184 6.09e-13

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 67.47  E-value: 6.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYR 159
Cdd:PRK06936   81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCG 160

                          90       100
                  ....*....|....*....|....*
gi 2315907287 160 RGGKIGLFGGAGVGKTVLIMELINN 184
Cdd:PRK06936  161 EGQRMGIFAAAGGGKSTLLASLIRS 185
PRK08149 PRK08149
FliI/YscN family ATPase;
22-232 8.27e-13

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 67.33  E-value: 8.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  22 IIGPVLDVAFPP---GKMPNIYNALvvkgrdtvgQQINVTCEVQqLLGNNRVRAV--AMSATDGLMRGMEVIDTGAPLSV 96
Cdd:PRK08149   13 IQGPIIEAELPDvaiGEICEIRAGW---------HSNEVIARAQ-VVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  97 PVGGATLGRIFNVLGEPIDNLGPVDT----RTTSPIHRSAPAFIQldtKLAI---FETGIKVVDLLAPYRRGGKIGLFGG 169
Cdd:PRK08149   83 WVGEALLGAVLDPTGKIVERFDAPPTvgpiSEERVIDVAPPSYAE---RRPIrepLITGVRAIDGLLTCGVGQRMGIFAS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2315907287 170 AGVGKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYMEMKESGvineqniAESKVALVY 232
Cdd:PRK08149  160 AGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS-------RREKCVLVY 212
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 94-184 1.58e-12

F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410876 [Multi-domain]  Cd Length: 274  Bit Score: 65.66  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  94 LSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 173
Cdd:cd01132     2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81

                          90
                  ....*....|.
gi 2315907287 174 KTVLIMELINN 184
Cdd:cd01132    82 KTAIAIDTIIN 92
fliI PRK08972
flagellar protein export ATPase FliI;
80-178 3.65e-11

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 62.41  E-value: 3.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHrsAPAFIQLDTKlAIFE---TGIKVVDLLA 156
Cdd:PRK08972   81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAML 157

                          90       100
                  ....*....|....*....|..
gi 2315907287 157 PYRRGGKIGLFGGAGVGKTVLI 178
Cdd:PRK08972  158 TVGKGQRMGLFAGSGVGKSVLL 179
fliI PRK06002
flagellar protein export ATPase FliI;
104-178 6.58e-11

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 61.55  E-value: 6.58e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907287 104 GRIFNVLGEPIDNLGPVDTRTTS-PIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLI 178
Cdd:PRK06002  107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLL 182
PRK05922 PRK05922
type III secretion system ATPase; Validated
 73-223 7.22e-11

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 61.46  E-value: 7.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  73 VAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVV 152
Cdd:PRK05922   69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2315907287 153 DLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYMEMKESGVINEQNI 223
Cdd:PRK05922  149 DAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEGLAAQRTI 215
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
64-249 1.16e-10

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 60.98  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  64 LLGNNRVRA--VAM----------SATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNlGPVDTRTTSPIHRS 131
Cdd:PRK06820   55 RIEPQGMLAevVSIeqemallspfASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCP 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287 132 APAFIQ---LDTKLAifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELinnIAKAHGGVSVFGGVGERTREGNDL 208
Cdd:PRK06820  134 PPSPLTrqpIEQMLT---TGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGREVREF 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2315907287 209 YmemkesgvinEQNI---AESKVALVYGQMNEPPGARMRVGLTA 249
Cdd:PRK06820  208 L----------EQVLtpeARARTVVVVATSDRPALERLKGLSTA 241
atpA CHL00059
ATP synthase CF1 alpha subunit
 65-184 3.02e-10

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 59.59  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  65 LGNNRVRAVAMSatDGLM--RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIqldTKL 142
Cdd:CHL00059   45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2315907287 143 AIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
Cdd:CHL00059  120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN 164
fliI PRK05688
flagellar protein export ATPase FliI;
55-178 7.12e-10

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 58.59  E-value: 7.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  55 INVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPV--------DTRTTS 126
Cdd:PRK05688   63 VQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMkaedwvpmDGPTIN 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2315907287 127 PIHRsAPAFIQLDTklaifetGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLI 178
Cdd:PRK05688  142 PLNR-HPISEPLDV-------GIRSINGLLTVGRGQRLGLFAGTGVGKSVLL 185
fliI PRK06793
flagellar protein export ATPase FliI;
51-217 1.47e-09

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 57.68  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  51 VGQQiNVTCEVQQLLGNNRVrAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFN----VLGEPIDNLG----PVDT 122
Cdd:PRK06793   48 VGEH-NVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPlqkiKLDA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287 123 rttSPIHrsapAFIQLDTKlAIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHggVSVFGGVGERT 202
Cdd:PRK06793  126 ---PPIH----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERG 194

                         170
                  ....*....|....*.
gi 2315907287 203 REGND-LYMEMKESGV 217
Cdd:PRK06793  195 REVKDfIRKELGEEGM 210
fliI PRK07721
flagellar protein export ATPase FliI;
90-178 2.33e-09

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 57.04  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  90 TGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSAPAFIQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGG 169
Cdd:PRK07721   87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166


                  ....*....
gi 2315907287 170 AGVGKTVLI 178
Cdd:PRK07721  167 SGVGKSTLM 175
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 19-171 4.12e-09

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 56.37  E-value: 4.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  19 IAQIIGPVLDVAfppgKMPNI-YNALVV----KGRDTVGQQINVTCE--VQQLLGNnrvravamsaTDGLM-RGMEVIDT 90
Cdd:PRK04196    7 VSEIKGPLLFVE----GVEGVaYGEIVEielpNGEKRRGQVLEVSEDkaVVQVFEG----------TTGLDlKDTKVRFT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  91 GAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSA--PA-------FIQldtklaifeTGIKVVDLLAPYRRG 161
Cdd:PRK04196   73 GEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------TGISAIDGLNTLVRG 143

                         170
                  ....*....|
gi 2315907287 162 GKIGLFGGAG 171
Cdd:PRK04196  144 QKLPIFSGSG 153
fliI PRK07960
flagellum-specific ATP synthase FliI;
96-178 1.02e-08

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 55.17  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  96 VPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIhrSAPAF--IQLDTKLAIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 173
Cdd:PRK07960  110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFnpLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187


                  ....*
gi 2315907287 174 KTVLI 178
Cdd:PRK07960  188 KSVLL 192
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 93-171 1.29e-08

V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.


Pssm-ID: 410879 [Multi-domain]  Cd Length: 282  Bit Score: 54.15  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  93 PLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTTSPIHRSA--PA-------FIQldtklaifeTGIKVVDLLAPYRRGGK 163
Cdd:cd01135     1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPinPVariypeeMIQ---------TGISAIDVMNTLVRGQK 71


                  ....*...
gi 2315907287 164 IGLFGGAG 171
Cdd:cd01135    72 LPIFSGSG 79
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
76-183 1.60e-07

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 51.49  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  76 SATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNL----GPVDTRTTSPihrsAPAFIQLDTKLAIFeTGIKV 151
Cdd:PRK07594   71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2315907287 152 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELIN 183
Cdd:PRK07594  146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN 177
fliI PRK07196
flagellar protein export ATPase FliI;
80-178 3.68e-07

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 50.27  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNLGPVDTRTtsPIHRSAPAFIQLDTKLA--IFETGIKVVDLLAP 157
Cdd:PRK07196   74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIHPLQRRAVdtPLDVGVNAINGLLT 151

                          90       100
                  ....*....|....*....|.
gi 2315907287 158 YRRGGKIGLFGGAGVGKTVLI 178
Cdd:PRK07196  152 IGKGQRVGLMAGSGVGKSVLL 172
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 90-172 5.68e-06

V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273410 [Multi-domain]  Cd Length: 466  Bit Score: 46.64  E-value: 5.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  90 TGAPLSVPVGGATLGRIFNVLGEPIDNLGPV------DTRtTSPIHRSAPAFIQldtklAIFETGIKVVDLLAPYRRGGK 163
Cdd:TIGR01040  70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedylDIN-GQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQK 143


                  ....*....
gi 2315907287 164 IGLFGGAGV 172
Cdd:TIGR01040 144 IPIFSAAGL 152
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 78-171 1.35e-05

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 45.80  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  78 TDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPIDNlGP------VDTRTTS--PIHRSAPAfiqldtklAIFETGI 149
Cdd:PRK02118   58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPelegepIEIGGPSvnPVKRIVPR--------EMIRTGI 128

                          90       100
                  ....*....|....*....|..
gi 2315907287 150 KVVDLLAPYRRGGKIGLFGGAG 171
Cdd:PRK02118  129 PMIDVFNTLVESQKIPIFSVSG 150
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 1-184 8.52e-05

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 43.49  E-value: 8.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287   1 STTSGPEVSALEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKgrdTVGQQINVTCEVQQLLGNNRVRAVAMSATDG 80
Cdd:PTZ00185   25 SAAPGQKSFFKATEMIGYVHSIDGTIATLIPAPGNPGVAYNTIIMI---QVSPTTFAAGLVFNLEKDGRIGIILMDNITE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907287  81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLG---------------EPIDNLGPVDTRTTSPIHRSAPAFIQLdtklaif 145
Cdd:PTZ00185  102 VQSGQKVMATGKLLYIPVGAGVLGKVVNPLGhevpvglltrsrallESEQTLGKVDAGAPNIVSRSPVNYNLL------- 174

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2315907287 146 eTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
Cdd:PTZ00185  175 -TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIIN 212
ATP-synt_F1_V1_A1_AB_FliI_N cd01426
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
 16-92 6.32e-04

ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases 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. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.


Pssm-ID: 349738 [Multi-domain]  Cd Length: 73  Bit Score: 37.29  E-value: 6.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2315907287  16 LGRIAQIIGPVLDVAFPPGKMpniYNALVVKGRDTVGQQINVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVIDTGA 92
Cdd:cd01426     1 KGRVIRVNGPLVEAELEGEVA---IGEVCEIERGDGNNETVLKAEVIGFRGD-RAILQLFESTRGLSRGALVEPTGR 73
 
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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