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Conserved domains on  [gi|338856159|gb|AEJ32358|]
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ATP synthase beta subunit, partial [Synechococcus sp. A15-48A1]

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
 1-200 1.21e-125

ATP synthase CF1 beta subunit


The actual alignment was detected with superfamily member CHL00060:

Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 363.21  E-value: 1.21e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159   1 PAGKLPKILNALRIEGTNTAGQPVALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLG 80
Cdd:CHL00060  32 PPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  81 EPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEHGG 160
Cdd:CHL00060 112 EPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGG 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 338856159 161 VSVFGGVGERTREGNDLYEEFKDSGVINAEDLSKSKVALC 200
Cdd:CHL00060 192 VSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALV 231
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 1-200 1.21e-125

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 363.21  E-value: 1.21e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159   1 PAGKLPKILNALRIEGTNTAGQPVALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLG 80
Cdd:CHL00060  32 PPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  81 EPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEHGG 160
Cdd:CHL00060 112 EPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGG 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 338856159 161 VSVFGGVGERTREGNDLYEEFKDSGVINAEDLSKSKVALC 200
Cdd:CHL00060 192 VSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALV 231
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-188 4.28e-110

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: 322.81  E-value: 4.28e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159   1 PAGKLPKILNALRIEGTNtagqPVALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLG 80
Cdd:COG0055   21 PEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  81 EPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEHGG 160
Cdd:COG0055   97 EPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGG 176

                        170       180
                 ....*....|....*....|....*...
gi 338856159 161 VSVFGGVGERTREGNDLYEEFKDSGVIN 188
Cdd:COG0055  177 VSVFAGVGERTREGNDLYREMKESGVLD 204
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-200 7.99e-99

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: 293.93  E-value: 7.99e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159    1 PAGKLPKILNALRIEGTNTAgqpvALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLG 80
Cdd:TIGR01039  18 EQGELPRIYNALKVQNRAES----ELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159   81 EPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEHGG 160
Cdd:TIGR01039  94 EPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 338856159  161 VSVFGGVGERTREGNDLYEEFKDSGVINaedlsksKVALC 200
Cdd:TIGR01039 174 YSVFAGVGERTREGNDLYHEMKESGVID-------KTALV 206
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 64-200 2.24e-75

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: 227.87  E-value: 2.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  64 SVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGK 143
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 338856159 144 TVLIQELINNIAKEHGGVSVFGGVGERTREGNDLYEEFKDSGVINAEDLskSKVALC 200
Cdd:cd01133   81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL--SKVALV 135
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 117-187 1.26e-15

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: 72.00  E-value: 1.26e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338856159  117 GIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEhggVSVFGGVGERTREGNDLYEEFKDSGVI 187
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD---VVVYALIGERGREVREFIEELLGSGAL 68
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 1-200 1.21e-125

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 363.21  E-value: 1.21e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159   1 PAGKLPKILNALRIEGTNTAGQPVALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLG 80
Cdd:CHL00060  32 PPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  81 EPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEHGG 160
Cdd:CHL00060 112 EPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGG 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 338856159 161 VSVFGGVGERTREGNDLYEEFKDSGVINAEDLSKSKVALC 200
Cdd:CHL00060 192 VSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALV 231
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-188 4.28e-110

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: 322.81  E-value: 4.28e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159   1 PAGKLPKILNALRIEGTNtagqPVALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLG 80
Cdd:COG0055   21 PEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  81 EPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEHGG 160
Cdd:COG0055   97 EPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGG 176

                        170       180
                 ....*....|....*....|....*...
gi 338856159 161 VSVFGGVGERTREGNDLYEEFKDSGVIN 188
Cdd:COG0055  177 VSVFAGVGERTREGNDLYREMKESGVLD 204
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-200 7.99e-99

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: 293.93  E-value: 7.99e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159    1 PAGKLPKILNALRIEGTNTAgqpvALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLG 80
Cdd:TIGR01039  18 EQGELPRIYNALKVQNRAES----ELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159   81 EPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEHGG 160
Cdd:TIGR01039  94 EPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 338856159  161 VSVFGGVGERTREGNDLYEEFKDSGVINaedlsksKVALC 200
Cdd:TIGR01039 174 YSVFAGVGERTREGNDLYHEMKESGVID-------KTALV 206
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 64-200 2.24e-75

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: 227.87  E-value: 2.24e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  64 SVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGK 143
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 338856159 144 TVLIQELINNIAKEHGGVSVFGGVGERTREGNDLYEEFKDSGVINAEDLskSKVALC 200
Cdd:cd01133   81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL--SKVALV 135
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 64-186 1.08e-43

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: 146.83  E-value: 1.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  64 SVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGK 143
Cdd:cd19476    1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 338856159 144 TVLIQELINNIAKEHGGVSVFGGVGERTREGNDLYEEFKDSGV 186
Cdd:cd19476   81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA 123
ATP-synt_F1_beta_N cd18115
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ...
 1-63 4.14e-26

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: 95.66  E-value: 4.14e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 338856159   1 PAGKLPKILNALRIEGtntaGQPVALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEALDTGAPI 63
Cdd:cd18115   18 PEGELPPIYNALEVKG----DDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 13-153 2.18e-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: 98.95  E-value: 2.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  13 RIEGTNtaGQPVAltAEVqqlLG--DHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVN 90
Cdd:COG1157   45 EIETAD--GRPVL--AEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLP 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 338856159  91 ASATAPIHRSAPKltELETKP--KVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINN 153
Cdd:COG1157  118 GEERRPLDAPPPN--PLERARitEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARN 180
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 64-153 1.22e-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: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  64 SVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGK 143
Cdd:cd01136    1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                         90
                 ....*....|
gi 338856159 144 TVLIQELINN 153
Cdd:cd01136   81 STLLGMIARN 90
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 34-152 1.26e-18

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 83.04  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  34 LGDHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTE--LETKP 111
Cdd:PRK13343  66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIErdFVTEP 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 338856159 112 kvFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVL-IQELIN 152
Cdd:PRK13343 146 --LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIaIDAIIN 185
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 45-147 5.19e-17

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 78.27  E-value: 5.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  45 SGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLL 124
Cdd:PRK09099  78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGL 157

                         90       100
                 ....*....|....*....|...
gi 338856159 125 APYRQGGKVGLFGGAGVGKTVLI 147
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLM 180
fliI PRK08472
flagellar protein export ATPase FliI;
63-147 4.15e-16

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 75.49  E-value: 4.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  63 ISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVG 142
Cdd:PRK08472  90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169


                 ....*
gi 338856159 143 KTVLI 147
Cdd:PRK08472 170 KSTLM 174
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 39-132 7.44e-16

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 74.72  E-value: 7.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  39 VRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLteLETKPkVFE--- 115
Cdd:PRK09281  71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGV--IDRKS-VHEplq 147

                         90       100
                 ....*....|....*....|....*...
gi 338856159 116 TGIKVIDLLAPY-----------RQGGK 132
Cdd:PRK09281 148 TGIKAIDAMIPIgrgqreliigdRQTGK 175
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 117-187 1.26e-15

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: 72.00  E-value: 1.26e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338856159  117 GIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIAKEhggVSVFGGVGERTREGNDLYEEFKDSGVI 187
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD---VVVYALIGERGREVREFIEELLGSGAL 68
PRK08149 PRK08149
FliI/YscN family ATPase;
32-153 2.43e-14

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 70.41  E-value: 2.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  32 QLLGDHRVRAV--AMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHR----SAPKLT 105
Cdd:PRK08149  47 QVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGPISEERvidvAPPSYA 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 338856159 106 ELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINN 153
Cdd:PRK08149 127 ERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH 174
fliI PRK08927
flagellar protein export ATPase FliI;
13-155 9.15e-14

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 68.85  E-value: 9.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  13 RIEGTNTAGQPVAltAEVqqlLGDHRVRAVAM--SGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVN 90
Cdd:PRK08927  43 RIVVETRGGRPVP--CEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLP 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338856159  91 ASATA-PIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINNIA 155
Cdd:PRK08927 118 QGPVPyPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNAD 183
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
20-153 4.96e-13

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 66.70  E-value: 4.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  20 AGQPVALTAEV---QQllgdHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAP 96
Cdd:PRK06936  53 PDNSLSLQAEVigfAQ----HQALLTPLGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYP 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 338856159  97 IHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELINN 153
Cdd:PRK06936 129 VYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRS 185
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 63-152 7.06e-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: 65.27  E-value: 7.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  63 ISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVG 142
Cdd:cd01132    2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81

                         90
                 ....*....|.
gi 338856159 143 KT-VLIQELIN 152
Cdd:cd01132   82 KTaIAIDTIIN 92
fliI PRK08972
flagellar protein export ATPase FliI;
65-147 7.65e-12

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 63.18  E-value: 7.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  65 VPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHrsAPKLTELETKP--KVFETGIKVIDLLAPYRQGGKVGLFGGAGVG 142
Cdd:PRK08972  97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRRPitEPLDVGVRAINAMLTVGKGQRMGLFAGSGVG 174


                 ....*
gi 338856159 143 KTVLI 147
Cdd:PRK08972 175 KSVLL 179
fliI PRK07721
flagellar protein export ATPase FliI;
59-197 1.51e-11

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 62.43  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  59 TGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGG 138
Cdd:PRK07721  87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338856159 139 AGVGKTVLIQEL-------INNIAkehggvsvfgGVGERTREGNDLYEefKDSGvinAEDLSKSKV 197
Cdd:PRK07721 167 SGVGKSTLMGMIarntsadLNVIA----------LIGERGREVREFIE--RDLG---PEGLKRSIV 217
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
22-147 1.93e-11

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 62.14  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  22 QPVALTAEVQQLLGDHrVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEqGPVNASATAPIHRSA 101
Cdd:PRK06820  57 EPQGMLAEVVSIEQEM-ALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPP 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 338856159 102 PKLTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLI 147
Cdd:PRK06820 135 PSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLL 180
fliI PRK07196
flagellar protein export ATPase FliI;
49-147 6.79e-11

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 60.29  E-value: 6.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  49 GLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASatAPIHRSAPKLTELETKP--KVFETGIKVIDLLAP 126
Cdd:PRK07196  74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGS--TPLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLT 151

                         90       100
                 ....*....|....*....|.
gi 338856159 127 YRQGGKVGLFGGAGVGKTVLI 147
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVLL 172
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 1-60 1.46e-10

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: 54.86  E-value: 1.46e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159    1 PAGKLPKILNALRIEGTNtagqPVALTAEVQQLLGDHRVRAVAMSGTDGLVRGMEALDTG 60
Cdd:pfam02874  14 GIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
PRK05922 PRK05922
type III secretion system ATPase; Validated
 26-183 1.92e-10

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 59.15  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  26 LTAEVqqlLGDHRVRAVAMSGTD--GLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPK 103
Cdd:PRK05922  54 ILAEV---IGFHNRTTLLMSLSPihYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPS 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159 104 LTELETKPKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLI-------QELINNIAkehggvsvfgGVGERTREGND 176
Cdd:PRK05922 131 PMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLstiakgsKSTINVIA----------LIGERGREVRE 200


                 ....*..
gi 338856159 177 LYEEFKD 183
Cdd:PRK05922 201 YIEQHKE 207
fliI PRK05688
flagellar protein export ATPase FliI;
23-147 2.08e-10

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 58.97  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  23 PVALTAEVQQLLGDhRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIhrSAP 102
Cdd:PRK05688  62 PVQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPM--DGP 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 338856159 103 KLTELETKP--KVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLI 147
Cdd:PRK05688 139 TINPLNRHPisEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLL 185
fliI PRK06002
flagellar protein export ATPase FliI;
73-147 2.94e-10

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 58.47  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  73 GRIFNVLGEPVDEQGP-------VNASATAPihrsaPKLTELETKpKVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTV 145
Cdd:PRK06002 107 GRVINALGEPIDGLGPlapgtrpMSIDATAP-----PAMTRARVE-TGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKST 180


                 ..
gi 338856159 146 LI 147
Cdd:PRK06002 181 LL 182
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
28-152 1.46e-09

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 56.50  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  28 AEVQQLLGDhRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDE----QGPVNASATAPihrsAPK 103
Cdd:PRK07594  55 AEVVGINGS-KALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGrelpDVCWKDYDAMP----PPA 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 338856159 104 LTELE-TKPKVfeTGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLIQELIN 152
Cdd:PRK07594 130 MVRQPiTQPLM--TGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN 177
fliI PRK06793
flagellar protein export ATPase FliI;
63-153 2.15e-09

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 56.14  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  63 ISVPVGEATLGRIFNVLGEPVDEQgpvnaSATAPIHR---SAPKLT--ELETKPKVFETGIKVIDLLAPYRQGGKVGLFG 137
Cdd:PRK06793  89 VVIPRGNHLLGKVLSANGEVLNEE-----AENIPLQKiklDAPPIHafEREEITDVFETGIKSIDSMLTIGIGQKIGIFA 163

                         90
                 ....*....|....*.
gi 338856159 138 GAGVGKTVLIQELINN 153
Cdd:PRK06793 164 GSGVGKSTLLGMIAKN 179
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 62-140 1.19e-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: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  62 PISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTELEtKPKVF-ETGIKVIDLLAPYRQGGKVGLFGGAG 140
Cdd:cd01135    1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARI-YPEEMiQTGISAIDVMNTLVRGQKLPIFSGSG 79
fliI PRK07960
flagellum-specific ATP synthase FliI;
29-147 2.59e-08

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 52.86  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  29 EVQQLLGDHRVRAVAMSGtDGLVRGMEaldtgapisVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIhrSAPKLTELE 108
Cdd:PRK07960  84 EVEGILPGARVYARNISG-EGLQSGKQ---------LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFNPLQ 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 338856159 109 TKP--KVFETGIKVIDLLAPYRQGGKVGLFGGAGVGKTVLI 147
Cdd:PRK07960 152 RTPieHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLL 192
atpA CHL00059
ATP synthase CF1 alpha subunit
 39-152 5.32e-08

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 51.89  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  39 VRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSAPKLTeleTKPKVFE--- 115
Cdd:CHL00059  50 VGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRRSVYEplq 126

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 338856159 116 TGIKVIDLLAPYRQGGKVGLFGGAGVGKT-VLIQELIN 152
Cdd:CHL00059 127 TGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILN 164
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 46-140 1.18e-07

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 50.98  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  46 GTDGL-VRGMEALDTGAPISVPVGEATLGRIFNVLGEPVDEQGPVNASATAPIHRSA--PKLTEletKPKVF-ETGIKVI 121
Cdd:PRK04196  58 GTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVARE---YPEEFiQTGISAI 134

                         90
                 ....*....|....*....
gi 338856159 122 DLLAPYRQGGKVGLFGGAG 140
Cdd:PRK04196 135 DGLNTLVRGQKLPIFSGSG 153
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 4-141 5.86e-07

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: 48.95  E-value: 5.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159    4 KLPK---ILNALRIEGTNTAGQpvaltaeVQQLLGDHRVRAVaMSGTDGL-VRGMEALDTGAPISVPVGEATLGRIFNVL 79
Cdd:TIGR01040  19 KFPRfaeIVNLTLPDGTVRSGQ-------VLEVSGNKAVVQV-FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGS 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159   80 GEPVDEQGPV--------NASATAPIHRSAPKlteletkpKVFETGIKVIDLLAPYRQGGKVGLFGGAGV 141
Cdd:TIGR01040  91 GKPIDKGPPVlaedyldiNGQPINPYARIYPE--------EMIQTGISAIDVMNSIARGQKIPIFSAAGL 152
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 28-140 3.12e-06

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 46.57  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  28 AEVQQLLGDhRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPVD-------EQGPVNASATAPIHRS 100
Cdd:PRK02118  40 AQVIRLDGD-KVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDggpelegEPIEIGGPSVNPVKRI 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 338856159 101 APKlteletkpKVFETGIKVIDLLAPYRQGGKVGLFGGAG 140
Cdd:PRK02118 119 VPR--------EMIRTGIPMIDVFNTLVESQKIPIFSVSG 150
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 62-150 2.59e-04

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: 40.64  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  62 PISVPVGEATLGRIFNVLGEPV----DEQGP-----VNASaTAPIHRSAPKLTELE-TKPkvFETGIKVIDLLAPYRQGG 131
Cdd:cd01134    1 PLSVELGPGLLGSIFDGIQRPLeviaETGSIfiprgVNVQ-RWPVRQPRPVKEKLPpNVP--LLTGQRVLDTLFPVAKGG 77

                         90
                 ....*....|....*....
gi 338856159 132 KVGLFGGAGVGKTVLIQEL 150
Cdd:cd01134   78 TAAIPGPFGCGKTVISQSL 96
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 30-154 6.22e-03

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 36.94  E-value: 6.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338856159  30 VQQLLGDHRVRAVAMSGTDGLVRGMEALDTGAPISVPVGEATLGRIFNVLGEPV---------------DEQGPVNASAT 94
Cdd:PTZ00185  82 VFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAP 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338856159  95 APIHRSAPKLTELetkpkvfeTGIKVIDLLAPYRQGGKVGLFGGAGVGKT-VLIQELINNI 154
Cdd:PTZ00185 162 NIVSRSPVNYNLL--------TGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINQV 214
 
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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