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Conserved domains on  [gi|4995067|emb|CAB43996|]
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H(+)-transporting ATP synthase, partial (chloroplast) [Christiana 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
 1-243 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: 524.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067     1 STLEKE*LGHISQIIGPVLDVAFPPGKMPNIYNALVVKGQDTLGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVT 80
Cdd:CHL00060   9 STLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    81 DTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFG 160
Cdd:CHL00060  89 DTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   161 GAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLT 240
Cdd:CHL00060 169 GAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLT 248


                 ...
gi 4995067   241 ALT 243
Cdd:CHL00060 249 ALT 251
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 1-243 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 524.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067     1 STLEKE*LGHISQIIGPVLDVAFPPGKMPNIYNALVVKGQDTLGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVT 80
Cdd:CHL00060   9 STLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    81 DTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFG 160
Cdd:CHL00060  89 DTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   161 GAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLT 240
Cdd:CHL00060 169 GAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLT 248


                 ...
gi 4995067   241 ALT 243
Cdd:CHL00060 249 ALT 251
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 4-243 3.44e-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: 408.71  E-value: 3.44e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    4 EKE*LGHISQIIGPVLDVAFPPGKMPNIYNALVVKGQDtlgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVTDTG 83
Cdd:COG0055   1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   84 APLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAG 163
Cdd:COG0055  77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067  164 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALT 243
Cdd:COG0055 157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALT 229
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 9-243 9.76e-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: 361.73  E-value: 9.76e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067      9 GHISQIIGPVLDVAFPPGKMPNIYNALVVKgqdtLGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVTDTGAPLSV 88
Cdd:TIGR01039   3 GKVVQVIGPVVDVEFEQGELPRIYNALKVQ----NRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067     89 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 168
Cdd:TIGR01039  79 PVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4995067    169 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALT 243
Cdd:TIGR01039 159 LIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLT 226
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 87-243 1.76e-98

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: 288.35  E-value: 1.76e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   87 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 166
Cdd:cd01133   1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4995067  167 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqnIAESKVALVYGQMNEPPGARMRVGLTALT 243
Cdd:cd01133  81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL--DGLSKVALVYGQMNEPPGARARVALTGLT 155
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 140-243 1.01e-22

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: 92.03  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    140 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSK 219
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70

                          90       100
                  ....*....|....*....|....
gi 4995067    220 VALVYGQMNEPPGARMRVGLTALT 243
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTALT 94
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 152-181 9.99e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.43  E-value: 9.99e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 4995067     152 RGGKIGLFGGAGVGKTVLIMELINNIAKAH 181
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPG 30
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 1-243 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 524.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067     1 STLEKE*LGHISQIIGPVLDVAFPPGKMPNIYNALVVKGQDTLGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVT 80
Cdd:CHL00060   9 STLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    81 DTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFG 160
Cdd:CHL00060  89 DTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   161 GAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLT 240
Cdd:CHL00060 169 GAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLT 248


                 ...
gi 4995067   241 ALT 243
Cdd:CHL00060 249 ALT 251
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 4-243 3.44e-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: 408.71  E-value: 3.44e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    4 EKE*LGHISQIIGPVLDVAFPPGKMPNIYNALVVKGQDtlgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVTDTG 83
Cdd:COG0055   1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   84 APLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAG 163
Cdd:COG0055  77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067  164 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALT 243
Cdd:COG0055 157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALT 229
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 9-243 9.76e-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: 361.73  E-value: 9.76e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067      9 GHISQIIGPVLDVAFPPGKMPNIYNALVVKgqdtLGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVTDTGAPLSV 88
Cdd:TIGR01039   3 GKVVQVIGPVVDVEFEQGELPRIYNALKVQ----NRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067     89 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 168
Cdd:TIGR01039  79 PVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4995067    169 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALT 243
Cdd:TIGR01039 159 LIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLT 226
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 87-243 1.76e-98

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: 288.35  E-value: 1.76e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   87 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 166
Cdd:cd01133   1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4995067  167 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqnIAESKVALVYGQMNEPPGARMRVGLTALT 243
Cdd:cd01133  81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL--DGLSKVALVYGQMNEPPGARARVALTGLT 155
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 9-243 2.71e-77

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: 240.11  E-value: 2.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067      9 GHISQIIGPVLDVAFPpGKMPNIYNALVVkgqdtlGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVTDTGAPLSV 88
Cdd:TIGR03305   1 GHVVAVRGSIVDVRFD-GELPAIHSVLRA------GREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067     89 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 168
Cdd:TIGR03305  74 PVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4995067    169 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqniaeskVALVYGQMNEPPGARMRVGLTALT 243
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALT 221
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 87-243 2.10e-63

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: 198.83  E-value: 2.10e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   87 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 166
Cdd:cd19476   1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4995067  167 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGvineqniAESKVALVYGQMNEPPGARMRVGLTALT 243
Cdd:cd19476  81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG-------AMERTVVVANTANDPPGARMRVPYTGLT 150
ATP-synt_F1_beta_N cd18115
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ...
 9-86 2.74e-38

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: 128.02  E-value: 2.74e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4995067    9 GHISQIIGPVLDVAFPPGKMPNIYNALVVKGQDtlgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVTDTGAPL 86
Cdd:cd18115   3 GKIVQVIGPVVDVEFPEGELPPIYNALEVKGDD----GKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 9-169 4.14e-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: 99.33  E-value: 4.14e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    9 GHISQIIGPVLDVAFPPGKMpniyNALV-VKGQDtlgqQINVTCEVqqlLG--NNRVRAVAMSATDGLMRGMEVTDTGAP 85
Cdd:COG1157  21 GRVTRVVGLLIEAVGPDASI----GELCeIETAD----GRPVLAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRP 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   86 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQ---LDTKLsifETGIKVVDLLAPYRRGGKIGLFGGA 162
Cdd:COG1157  90 LSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGS 166


                ....*..
gi 4995067  163 GVGKTVL 169
Cdd:COG1157 167 GVGKSTL 173
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 140-243 1.01e-22

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: 92.03  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    140 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSK 219
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70

                          90       100
                  ....*....|....*....|....
gi 4995067    220 VALVYGQMNEPPGARMRVGLTALT 243
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTALT 94
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 57-176 6.39e-21

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 90.75  E-value: 6.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    57 LGNNRVRAVAMSATDGLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSI 136
Cdd:PRK13343  66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 4995067   137 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 176
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN 185
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 11-83 4.94e-20

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: 80.67  E-value: 4.94e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4995067     11 ISQIIGPVLDVAFPPGKMPNIYNALVVKGQDtlgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVTDTG 83
Cdd:pfam02874   1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 87-243 1.11e-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: 82.22  E-value: 1.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   87 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 166
Cdd:cd01136   1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4995067  167 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYMEmkesGVINEQNIaeSKVALVYGQMNEPPGARMRVGLTALT 243
Cdd:cd01136  81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGL--KRSVLVVATSDESPLLRVRAAYTATA 147
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 62-153 2.36e-18

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 83.58  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    62 VRAVAMSATDGLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQldtKLSIFE--- 138
Cdd:PRK09281  71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEplq 147

                         90
                 ....*....|....*
gi 4995067   139 TGIKVVDLLAPYRRG 153
Cdd:PRK09281 148 TGIKAIDAMIPIGRG 162
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 71-170 1.94e-16

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 77.89  E-value: 1.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    71 DGLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQ---LDTKLSifeTGIKVVDLL 147
Cdd:PRK09099  81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGL 157

                         90       100
                 ....*....|....*....|...
gi 4995067   148 APYRRGGKIGLFGGAGVGKTVLI 170
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLM 180
fliI PRK08472
flagellar protein export ATPase FliI;
86-180 6.28e-15

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 73.18  E-value: 6.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    86 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 165
Cdd:PRK08472  90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169

                         90
                 ....*....|....*
gi 4995067   166 KTVLiMELINNIAKA 180
Cdd:PRK08472 170 KSTL-MGMIVKGCLA 183
PRK08149 PRK08149
FliI/YscN family ATPase;
8-224 2.04e-14

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 71.95  E-value: 2.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067     8 LGHISQIIGPVLDVAFPP---GKMPNIYNALvvkgqdtlgQQINVTCEVQqLLGNNRVRAV--AMSATDGLMRGMEVTDT 82
Cdd:PRK08149   7 LAHPLRIQGPIIEAELPDvaiGEICEIRAGW---------HSNEVIARAQ-VVGFQRERTIlsLIGNAQGLSRQVVLKPT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    83 GAPLSVPVGGATLGRIFNVLGEPVDNLGPVDT----RTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGL 158
Cdd:PRK08149  77 GKPLSVWVGEALLGAVLDPTGKIVERFDAPPTvgpiSEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGI 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4995067   159 FGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYMEMKESGvineqniAESKVALVY 224
Cdd:PRK08149 157 FASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS-------RREKCVLVY 212
fliI PRK08927
flagellar protein export ATPase FliI;
49-178 9.34e-14

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 70.01  E-value: 9.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    49 VTCEVqqlLGNNRVRAVAM--SATDGLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGP-------VDTRTTSP 119
Cdd:PRK08927  54 VPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPlpqgpvpYPLRAPPP 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4995067   120 ihkPAPAFIQLDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIA 178
Cdd:PRK08927 131 ---PAHSRARVGEPL---DLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNAD 183
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 86-176 5.43e-13

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: 66.81  E-value: 5.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   86 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 165
Cdd:cd01132   2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81

                        90
                ....*....|.
gi 4995067  166 KTVLIMELINN 176
Cdd:cd01132  82 KTAIAIDTIIN 92
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
56-243 2.32e-12

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 65.61  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    56 LLGNNRVRA--VAM----------SATDGLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTSPIHKP 123
Cdd:PRK06820  55 RIEPQGMLAevVSIeqemallspfASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   124 APAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELinnIAKAHGGVSVFGGVGERTREGNDLYme 203
Cdd:PRK06820 134 PPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGML---CADSAADVMVLALIGERGREVREFL-- 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 4995067   204 mkesgvinEQNI---AESKVALVYGQMNEPPGARMRVGLTALT 243
Cdd:PRK06820 209 --------EQVLtpeARARTVVVVATSDRPALERLKGLSTATT 243
atpA CHL00059
ATP synthase CF1 alpha subunit
 57-176 7.30e-12

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 64.21  E-value: 7.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    57 LGNNRVRAVAMSatDGLM--RGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIqldTKL 134
Cdd:CHL00059  45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 4995067   135 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 176
Cdd:CHL00059 120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN 164
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
72-176 1.36e-11

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 63.62  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    72 GLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQ---LDTKLSifeTGIKVVDLLA 148
Cdd:PRK06936  81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLL 157

                         90       100
                 ....*....|....*....|....*...
gi 4995067   149 PYRRGGKIGLFGGAGVGKTVLIMELINN 176
Cdd:PRK06936 158 TCGEGQRMGIFAAAGGGKSTLLASLIRS 185
fliI PRK08972
flagellar protein export ATPase FliI;
72-170 1.98e-11

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 63.18  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    72 GLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPApafIQLDTKLSIFE---TGIKVVDLLA 148
Cdd:PRK08972  81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPP---INPLSRRPITEpldVGVRAINAML 157

                         90       100
                 ....*....|....*....|..
gi 4995067   149 PYRRGGKIGLFGGAGVGKTVLI 170
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLL 179
PRK05922 PRK05922
type III secretion system ATPase; Validated
 65-243 2.49e-11

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 62.61  E-value: 2.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    65 VAMSATDGLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVV 144
Cdd:PRK05922  69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   145 DLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYMEMKESGvineqnIAESKVALV 223
Cdd:PRK05922 149 DAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEG------LAAQRTIII 217

                        170       180
                 ....*....|....*....|
gi 4995067   224 YGQMNEPPGARMRVGLTALT 243
Cdd:PRK05922 218 ASPAHETAPTKVIAGRAAMT 237
fliI PRK06002
flagellar protein export ATPase FliI;
96-170 6.76e-11

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 61.55  E-value: 6.76e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4995067    96 GRIFNVLGEPVDNLGPVDTRTTS-PIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLI 170
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLL 182
fliI PRK06793
flagellar protein export ATPase FliI;
48-209 1.04e-10

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 60.76  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    48 NVTCEVQQLLGNNRVrAVAMSATDGLMRGMEVTDTGAPLSVPVGGATLGRIFN----VLGEPVDNLGPVDTRTTSPihkP 123
Cdd:PRK06793  52 NVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPLQKIKLDAP---P 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   124 APAFIQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHggVSVFGGVGERTREGND-LYM 202
Cdd:PRK06793 128 IHAFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKDfIRK 203


                 ....*..
gi 4995067   203 EMKESGV 209
Cdd:PRK06793 204 ELGEEGM 210
fliI PRK07960
flagellum-specific ATP synthase FliI;
88-170 7.00e-10

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 58.26  E-value: 7.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    88 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 167
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189


                 ...
gi 4995067   168 VLI 170
Cdd:PRK07960 190 VLL 192
fliI PRK07721
flagellar protein export ATPase FliI;
76-170 3.25e-09

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 56.27  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    76 GMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGK 155
Cdd:PRK07721  81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160

                         90
                 ....*....|....*
gi 4995067   156 IGLFGGAGVGKTVLI 170
Cdd:PRK07721 161 VGIFAGSGVGKSTLM 175
fliI PRK05688
flagellar protein export ATPase FliI;
47-170 6.33e-09

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 55.51  E-value: 6.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    47 INVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPA 126
Cdd:PRK05688  63 VQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTIN 141

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 4995067   127 FIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLI 170
Cdd:PRK05688 142 PLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLL 185
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 11-163 1.34e-08

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 54.45  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    11 ISQIIGPVLDVAfppgKMPNI-YNALVV----KGQDTLGQQINVTCE--VQQLLGNnrvravamsaTDGLM-RGMEVTDT 82
Cdd:PRK04196   7 VSEIKGPLLFVE----GVEGVaYGEIVEielpNGEKRRGQVLEVSEDkaVVQVFEG----------TTGLDlKDTKVRFT 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    83 GAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPA--PA-------FIQldtklsifeTGIKVVDLLAPYRRG 153
Cdd:PRK04196  73 GEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------TGISAIDGLNTLVRG 143

                        170
                 ....*....|
gi 4995067   154 GKIGLFGGAG 163
Cdd:PRK04196 144 QKLPIFSGSG 153
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
68-175 1.35e-08

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 54.57  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    68 SATDGLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFeTGIKVVDLL 147
Cdd:PRK07594  71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPITQPLM-TGIRAIDSV 149

                         90       100
                 ....*....|....*....|....*...
gi 4995067   148 APYRRGGKIGLFGGAGVGKTVLIMELIN 175
Cdd:PRK07594 150 ATCGEGQRVGIFSAPGVGKSTLLAMLCN 177
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 85-163 2.35e-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: 53.38  E-value: 2.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   85 PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPA--PA-------FIQldtklsifeTGIKVVDLLAPYRRGGK 155
Cdd:cd01135   1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPinPVariypeeMIQ---------TGISAIDVMNTLVRGQK 71


                ....*...
gi 4995067  156 IGLFGGAG 163
Cdd:cd01135  72 LPIFSGSG 79
fliI PRK07196
flagellar protein export ATPase FliI;
72-170 8.65e-08

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 52.20  E-value: 8.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    72 GLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKPAPAFIQLDTKLSIFETGIKVVDLLAPYR 151
Cdd:PRK07196  74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153

                         90
                 ....*....|....*....
gi 4995067   152 RGGKIGLFGGAGVGKTVLI 170
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 ...
 82-164 2.49e-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: 44.71  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067     82 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPV------DTRtTSPIHKPAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 155
Cdd:TIGR01040  70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedylDIN-GQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQK 143


                  ....*....
gi 4995067    156 IGLFGGAGV 164
Cdd:TIGR01040 144 IPIFSAAGL 152
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 6-176 1.09e-04

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 42.72  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067     6 E*LGHISQIIGPVLDVAFPPGKMPNIYNALVvkgQDTLGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVTDTGAP 85
Cdd:PTZ00185  38 EMIGYVHSIDGTIATLIPAPGNPGVAYNTII---MIQVSPTTFAAGLVFNLEKDGRIGIILMDNITEVQSGQKVMATGKL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    86 LSVPVGGATLGRIFNVLGEPV---------------DNLGPVDTRTTSPIHKPAPAFIQLdtklsifeTGIKVVDLLAPY 150
Cdd:PTZ00185 115 LYIPVGAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAPNIVSRSPVNYNLL--------TGFKAVDTMIPI 186

                        170       180
                 ....*....|....*....|....*.
gi 4995067   151 RRGGKIGLFGGAGVGKTVLIMELINN 176
Cdd:PTZ00185 187 GRGQRELIVGDRQTGKTSIAVSTIIN 212
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 70-163 1.50e-04

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 42.33  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067    70 TDGLMRGMEVTDTGAPLSVPVGGATLGRIFNVLGEPVDNlGP------VDTRTTS--PIHKPAPAfiqldtklSIFETGI 141
Cdd:PRK02118  58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPelegepIEIGGPSvnPVKRIVPR--------EMIRTGI 128

                         90       100
                 ....*....|....*....|..
gi 4995067   142 KVVDLLAPYRRGGKIGLFGGAG 163
Cdd:PRK02118 129 PMIDVFNTLVESQKIPIFSVSG 150
ATP-synt_F1_V1_A1_AB_FliI_N cd01426
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
 8-84 3.09e-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: 38.06  E-value: 3.09e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4995067    8 LGHISQIIGPVLDVAFPPGkmPNIYNALVVKGQDTlGQQINVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVTDTGA 84
Cdd:cd01426   1 KGRVIRVNGPLVEAELEGE--VAIGEVCEIERGDG-NNETVLKAEVIGFRGD-RAILQLFESTRGLSRGALVEPTGR 73
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 85-169 6.12e-03

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. 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.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 37.17  E-value: 6.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4995067   85 PLSVPVGGATLGRIFNVLGEPVDNL----GPVDTRTTS----PIHKPAPAFIQLDTKLsIFETGIKVVDLLAPYRRGGKI 156
Cdd:cd01134   1 PLSVELGPGLLGSIFDGIQRPLEVIaetgSIFIPRGVNvqrwPVRQPRPVKEKLPPNV-PLLTGQRVLDTLFPVAKGGTA 79

                        90
                ....*....|...
gi 4995067  157 GLFGGAGVGKTVL 169
Cdd:cd01134  80 AIPGPFGCGKTVI 92
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 152-181 9.99e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.43  E-value: 9.99e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 4995067     152 RGGKIGLFGGAGVGKTVLIMELINNIAKAH 181
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPG 30
 
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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