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Conserved domains on  [gi|2315907633|gb|UYB93555|]
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ATP synthase beta subunit, partial (chloroplast) [Ampelocissus africana]

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
 3-250 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: 564.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633   3 TSGPGVSTLEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLM 82
Cdd:CHL00060    3 PTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  83 RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGG 162
Cdd:CHL00060   83 RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633 163 KIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNISESKVALVYGQMNEPPGAR 242
Cdd:CHL00060  163 KIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGAR 242


                  ....*...
gi 2315907633 243 MRVGLTAL 250
Cdd:CHL00060  243 MRVGLTAL 250
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 3-250 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 564.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633   3 TSGPGVSTLEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLM 82
Cdd:CHL00060    3 PTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  83 RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGG 162
Cdd:CHL00060   83 RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633 163 KIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNISESKVALVYGQMNEPPGAR 242
Cdd:CHL00060  163 KIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGAR 242


                  ....*...
gi 2315907633 243 MRVGLTAL 250
Cdd:CHL00060  243 MRVGLTAL 250
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 12-250 1.04e-142

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: 407.94  E-value: 1.04e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  12 EKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 91
Cdd:COG0055     1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  92 APLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAG 171
Cdd:COG0055    77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2315907633 172 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqnisesKVALVYGQMNEPPGARMRVGLTAL 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 2.29e-124

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: 360.96  E-value: 2.29e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  15 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRdtvgQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
Cdd:TIGR01039   1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR----AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:TIGR01039  77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907633 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqnisesKVALVYGQMNEPPGARMRVGLTAL 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 1.52e-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: 286.42  E-value: 1.52e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:cd01133     1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907633 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqnISESKVALVYGQMNEPPGARMRVGLTAL 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 1.56e-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: 88.95  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633 148 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniseSK 227
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70

                          90       100
                  ....*....|....*....|...
gi 2315907633 228 VALVYGQMNEPPGARMRVGLTAL 250
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTAL 93
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 3-250 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 564.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633   3 TSGPGVSTLEKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLM 82
Cdd:CHL00060    3 PTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  83 RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGG 162
Cdd:CHL00060   83 RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633 163 KIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNISESKVALVYGQMNEPPGAR 242
Cdd:CHL00060  163 KIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGAR 242


                  ....*...
gi 2315907633 243 MRVGLTAL 250
Cdd:CHL00060  243 MRVGLTAL 250
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 12-250 1.04e-142

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: 407.94  E-value: 1.04e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  12 EKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 91
Cdd:COG0055     1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  92 APLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAG 171
Cdd:COG0055    77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2315907633 172 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqnisesKVALVYGQMNEPPGARMRVGLTAL 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 2.29e-124

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: 360.96  E-value: 2.29e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  15 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRdtvgQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
Cdd:TIGR01039   1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR----AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:TIGR01039  77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907633 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqnisesKVALVYGQMNEPPGARMRVGLTAL 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 1.52e-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: 286.42  E-value: 1.52e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:cd01133     1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907633 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqnISESKVALVYGQMNEPPGARMRVGLTAL 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 2.71e-75

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: 235.10  E-value: 2.71e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  17 GRIAQIIGPVLDVAFPpGKMPNIYNALvvkgrdTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSV 96
Cdd:TIGR03305   1 GHVVAVRGSIVDVRFD-GELPAIHSVL------RAGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  97 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 176
Cdd:TIGR03305  74 PVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2315907633 177 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqniseskVALVYGQMNEPPGARMRVGLTAL 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 9.56e-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: 194.98  E-value: 9.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:cd19476     1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907633 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVineqnisESKVALVYGQMNEPPGARMRVGLTAL 250
Cdd:cd19476    81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGL 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 1.42e-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: 1.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  15 NLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
Cdd:cd18115     1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDD----GKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 17-177 2.34e-24

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: 100.49  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  17 GRIAQIIGPVLDVAFPPGKMpniyNALV-VKGRDtvgqQINVTCEVqqlLG--NNRVRAVAMSATDGLMRGMEVIDTGAP 93
Cdd:COG1157    21 GRVTRVVGLLIEAVGPDASI----GELCeIETAD----GRPVLAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  94 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQ---LDTQLsifETGIKVVDLLAPYRRGGKIGLFGGA 170
Cdd:COG1157    90 LSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGS 166


                  ....*..
gi 2315907633 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 1.56e-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: 88.95  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633 148 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniseSK 227
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70

                          90       100
                  ....*....|....*....|...
gi 2315907633 228 VALVYGQMNEPPGARMRVGLTAL 250
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTAL 93
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 65-184 7.25e-20

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 88.05  E-value: 7.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSI 144
Cdd:PRK13343   66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2315907633 145 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
Cdd:PRK13343  146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN 185
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 19-91 3.01e-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: 78.74  E-value: 3.01e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2315907633  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 3.05e-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: 81.07  E-value: 3.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
Cdd:cd01136     1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2315907633 175 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYMEmkesGVINEQNISESkvALVYGQMNEPPGARMRVGLTA 249
Cdd:cd01136    81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGLKRS--VLVVATSDESPLLRVRAAYTA 145
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 70-161 4.22e-17

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 80.11  E-value: 4.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  70 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQldtQLSIFE--- 146
Cdd:PRK09281   71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEplq 147

                          90
                  ....*....|....*
gi 2315907633 147 TGIKVVDLLAPYRRG 161
Cdd:PRK09281  148 TGIKAIDAMIPIGRG 162
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 79-178 4.72e-17

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 79.81  E-value: 4.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  79 DGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQ---LDTQLSifeTGIKVVDLL 155
Cdd:PRK09099   81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGL 157

                          90       100
                  ....*....|....*....|...
gi 2315907633 156 APYRRGGKIGLFGGAGVGKTVLI 178
Cdd:PRK09099  158 MTLGEGQRMGIFAPAGVGKSTLM 180
fliI PRK08472
flagellar protein export ATPase FliI;
94-188 2.80e-14

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 71.64  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  94 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 173
Cdd:PRK08472   90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169

                          90
                  ....*....|....*
gi 2315907633 174 KTVLiMELINNIAKA 188
Cdd:PRK08472  170 KSTL-MGMIVKGCLA 183
fliI PRK08927
flagellar protein export ATPase FliI;
17-186 3.24e-14

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 71.55  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  17 GRIAQIIGPVLDVAFPPGKMpNIYNALVVKGRDTVGqqinVTCEVqqlLGNNRVRAVAM--SATDGLMRGMEVIDTGAPL 94
Cdd:PRK08927   19 GRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRP----VPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSI-FETGIKVVDLLAPYRRGGKIGLFGGAGVG 173
Cdd:PRK08927   91 AVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEpLDLGVRALNTFLTCCRGQRMGIFAGSGVG 170

                         170
                  ....*....|...
gi 2315907633 174 KTVLIMELINNIA 186
Cdd:PRK08927  171 KSVLLSMLARNAD 183
PRK08149 PRK08149
FliI/YscN family ATPase;
22-232 7.94e-14

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 70.02  E-value: 7.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  22 IIGPVLDVAFPP---GKMPNIYNALvvkgrdtvgQQINVTCEVQqLLGNNRVRAV--AMSATDGLMRGMEVIDTGAPLSV 96
Cdd:PRK08149   13 IQGPIIEAELPDvaiGEICEIRAGW---------HSNEVIARAQ-VVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  97 PVGGATLGRIFNVLGEPVDNLGPVDT----RTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV 172
Cdd:PRK08149   83 WVGEALLGAVLDPTGKIVERFDAPPTvgpiSEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGC 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633 173 GKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYMEMKESGvineqniSESKVALVY 232
Cdd:PRK08149  163 GKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS-------RREKCVLVY 212
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
80-184 1.07e-12

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 67.08  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQ---LDTQLSifeTGIKVVDLLA 156
Cdd:PRK06936   81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLL 157

                          90       100
                  ....*....|....*....|....*...
gi 2315907633 157 PYRRGGKIGLFGGAGVGKTVLIMELINN 184
Cdd:PRK06936  158 TCGEGQRMGIFAAAGGGKSTLLASLIRS 185
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 94-184 5.13e-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: 64.12  E-value: 5.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  94 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 173
Cdd:cd01132     2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81

                          90
                  ....*....|.
gi 2315907633 174 KTVLIMELINN 184
Cdd:cd01132    82 KTAIAIDTIIN 92
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
64-249 6.44e-11

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 61.75  E-value: 6.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  64 LLGNNRVRA--VAM----------SATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTSPIHRS 131
Cdd:PRK06820   55 RIEPQGMLAevVSIeqemallspfASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCP 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633 132 APAFIQ---LDTQLSifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELinnIAKAHGGVSVFGGVGERTREGNDL 208
Cdd:PRK06820  134 PPSPLTrqpIEQMLT---TGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGREVREF 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2315907633 209 YmemkesgvinEQNISE---SKVALVYGQMNEPPGARMRVGLTA 249
Cdd:PRK06820  208 L----------EQVLTPearARTVVVVATSDRPALERLKGLSTA 241
PRK05922 PRK05922
type III secretion system ATPase; Validated
 73-223 1.02e-10

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 61.07  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  73 VAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVV 152
Cdd:PRK05922   69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2315907633 153 DLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYMEMKESGVINEQNI 223
Cdd:PRK05922  149 DAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEGLAAQRTI 215
fliI PRK06002
flagellar protein export ATPase FliI;
104-178 1.95e-10

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 60.40  E-value: 1.95e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2315907633 104 GRIFNVLGEPVDNLGPVDTRTTS-PIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLI 178
Cdd:PRK06002  107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLL 182
atpA CHL00059
ATP synthase CF1 alpha subunit
 65-184 2.00e-10

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 60.36  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  65 LGNNRVRAVAMSatDGLM--RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTQL 142
Cdd:CHL00059   45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2315907633 143 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
Cdd:CHL00059  120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN 164
fliI PRK06793
flagellar protein export ATPase FliI;
51-217 4.91e-10

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 58.84  E-value: 4.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  51 VGQQiNVTCEVQQLLGNNRVrAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFN----VLGEPVDNLG----PVDT 122
Cdd:PRK06793   48 VGEH-NVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPlqkiKLDA 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633 123 rttSPIHrsapAFIQLDTQlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHggVSVFGGVGERT 202
Cdd:PRK06793  126 ---PPIH----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERG 194

                         170
                  ....*....|....*.
gi 2315907633 203 REGND-LYMEMKESGV 217
Cdd:PRK06793  195 REVKDfIRKELGEEGM 210
fliI PRK08972
flagellar protein export ATPase FliI;
80-178 4.97e-10

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 58.94  E-value: 4.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSApafIQLDTQLSIFE---TGIKVVDLLA 156
Cdd:PRK08972   81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPP---INPLSRRPITEpldVGVRAINAML 157

                          90       100
                  ....*....|....*....|..
gi 2315907633 157 PYRRGGKIGLFGGAGVGKTVLI 178
Cdd:PRK08972  158 TVGKGQRMGLFAGSGVGKSVLL 179
fliI PRK05688
flagellar protein export ATPase FliI;
55-178 7.19e-10

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 58.59  E-value: 7.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  55 INVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPV--------DTRTTS 126
Cdd:PRK05688   63 VQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMkaedwvpmDGPTIN 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2315907633 127 PIHRsAPAFIQLDTqlsifetGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLI 178
Cdd:PRK05688  142 PLNR-HPISEPLDV-------GIRSINGLLTVGRGQRLGLFAGTGVGKSVLL 185
fliI PRK07721
flagellar protein export ATPase FliI;
90-178 2.80e-09

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 56.65  E-value: 2.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  90 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGG 169
Cdd:PRK07721   87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166


                  ....*....
gi 2315907633 170 AGVGKTVLI 178
Cdd:PRK07721  167 SGVGKSTLM 175
fliI PRK07960
flagellum-specific ATP synthase FliI;
96-178 7.50e-09

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 55.56  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIhrSAPAF--IQLDTQLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 173
Cdd:PRK07960  110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFnpLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187


                  ....*
gi 2315907633 174 KTVLI 178
Cdd:PRK07960  188 KSVLL 192
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 19-171 2.43e-08

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 54.06  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  19 IAQIIGPVLDVAfppgKMPNI-YNALVV----KGRDTVGQQINVTCE--VQQLLGNnrvravamsaTDGLM-RGMEVIDT 90
Cdd:PRK04196    7 VSEIKGPLLFVE----GVEGVaYGEIVEielpNGEKRRGQVLEVSEDkaVVQVFEG----------TTGLDlKDTKVRFT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  91 GAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA--PA-------FIQldtqlsifeTGIKVVDLLAPYRRG 161
Cdd:PRK04196   73 GEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------TGISAIDGLNTLVRG 143

                         170
                  ....*....|
gi 2315907633 162 GKIGLFGGAG 171
Cdd:PRK04196  144 QKLPIFSGSG 153
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 93-171 6.11e-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: 52.22  E-value: 6.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  93 PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA--PA-------FIQldtqlsifeTGIKVVDLLAPYRRGGK 163
Cdd:cd01135     1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPinPVariypeeMIQ---------TGISAIDVMNTLVRGQK 71


                  ....*...
gi 2315907633 164 IGLFGGAG 171
Cdd:cd01135    72 LPIFSGSG 79
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
76-183 1.92e-07

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 51.11  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  76 SATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNL----GPVDTRTTSPihrsAPAFIQLDTQLSIFeTGIKV 151
Cdd:PRK07594   71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2315907633 152 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELIN 183
Cdd:PRK07594  146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN 177
fliI PRK07196
flagellar protein export ATPase FliI;
80-178 4.76e-07

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 49.89  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTQLSIFETGIKVVDLLAPYR 159
Cdd:PRK07196   74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153

                          90
                  ....*....|....*....
gi 2315907633 160 RGGKIGLFGGAGVGKTVLI 178
Cdd:PRK07196  154 KGQRVGLMAGSGVGKSVLL 172
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 90-172 1.49e-05

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: 45.48  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  90 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPV------DTRtTSPIHRSAPAFIQldtqlSIFETGIKVVDLLAPYRRGGK 163
Cdd:TIGR01040  70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedylDIN-GQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQK 143


                  ....*....
gi 2315907633 164 IGLFGGAGV 172
Cdd:TIGR01040 144 IPIFSAAGL 152
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 78-171 2.88e-05

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 44.64  E-value: 2.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  78 TDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNlGP------VDTRTTS--PIHRSAPAfiqldtqlSIFETGI 149
Cdd:PRK02118   58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPelegepIEIGGPSvnPVKRIVPR--------EMIRTGI 128

                          90       100
                  ....*....|....*....|..
gi 2315907633 150 KVVDLLAPYRRGGKIGLFGGAG 171
Cdd:PRK02118  129 PMIDVFNTLVESQKIPIFSVSG 150
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 16-184 1.09e-04

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 43.11  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  16 LGRIAQIIGPVLDVAFPPGKMPNIYNALVVKgrdTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
Cdd:PTZ00185   40 IGYVHSIDGTIATLIPAPGNPGVAYNTIIMI---QVSPTTFAAGLVFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315907633  96 VPVGGATLGRIFNVLGEPV---------------DNLGPVDTRTTSPIHRSAPAFIQLdtqlsifeTGIKVVDLLAPYRR 160
Cdd:PTZ00185  117 IPVGAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAPNIVSRSPVNYNLL--------TGFKAVDTMIPIGR 188

                         170       180
                  ....*....|....*....|....
gi 2315907633 161 GGKIGLFGGAGVGKTVLIMELINN 184
Cdd:PTZ00185  189 GQRELIVGDRQTGKTSIAVSTIIN 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 6.51e-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: 6.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2315907633  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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