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Conserved domains on  [gi|3850958|gb|AAC72171|]
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ATP synthase beta subunit, partial (chloroplast) [Macadamia jansenii]

Protein Classification

F0F1 ATP synthase subunit beta( domain architecture ID 11414030)

F0F1 ATP synthase subunit beta is part of the catalytic core of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane and is found in bacterial, mitochondrial, and chloroplast membranes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
1-490 0e+00

ATP synthase CF1 beta subunit


:

Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 1162.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     1 GPGVSALEEKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRG 80
Cdd:CHL00060   5 GPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    81 MEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKI 160
Cdd:CHL00060  85 MEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   161 GLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMR 240
Cdd:CHL00060 165 GLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMR 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   241 VGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVY 320
Cdd:CHL00060 245 VGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVY 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   321 VPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAIL 400
Cdd:CHL00060 325 VPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAIL 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   401 GLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAM 480
Cdd:CHL00060 405 GLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAA 484
                        490
                 ....*....|
gi 3850958   481 NLEVESNLKK 490
Cdd:CHL00060 485 NLEVESKLKK 494
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
1-490 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 1162.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     1 GPGVSALEEKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRG 80
Cdd:CHL00060   5 GPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    81 MEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKI 160
Cdd:CHL00060  85 MEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   161 GLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMR 240
Cdd:CHL00060 165 GLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMR 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   241 VGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVY 320
Cdd:CHL00060 245 VGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVY 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   321 VPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAIL 400
Cdd:CHL00060 325 VPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAIL 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   401 GLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAM 480
Cdd:CHL00060 405 GLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAA 484
                        490
                 ....*....|
gi 3850958   481 NLEVESNLKK 490
Cdd:CHL00060 485 NLEVESKLKK 494
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
8-486 0e+00

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: 950.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    8 EEKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 87
Cdd:COG0055   1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   88 APLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAG 167
Cdd:COG0055  77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  168 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALT 247
Cdd:COG0055 157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALT 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  248 MAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLT 327
Cdd:COG0055 230 MAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLT 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  328 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSE 407
Cdd:COG0055 310 DPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSE 389
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3850958  408 EDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEVES 486
Cdd:COG0055 390 EDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
11-482 0e+00

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: 838.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     11 NLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRdtvgQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 90
Cdd:TIGR01039   1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR----AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     91 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:TIGR01039  77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    171 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    251 YFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 330
Cdd:TIGR01039 230 YFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    331 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 410
Cdd:TIGR01039 310 PATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDK 389
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3850958    411 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNL 482
Cdd:TIGR01039 390 LTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
91-369 0e+00

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: 579.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   91 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:cd01133   1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  171 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:cd01133  81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL--SKVALVYGQMNEPPGARARVALTGLTMAE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  251 YFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 330
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 3850958  331 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 369
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
144-364 5.43e-86

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: 263.06  E-value: 5.43e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    144 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSK 223
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    224 VALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 303
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3850958    304 RITSTKE--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
Cdd:pfam00006 150 RAGRVKGkgGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
156-284 4.28e-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: 37.74  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     156 RGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYmemkesgvineqniaeskvaLVYGQMNEPP 235
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL--------------------LIIVGGKKAS 60
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 3850958     236 GARMRVGLTALTMAEYFRdvneqDVLLFIDNIFRFVQAGSEVSALLGRM 284
Cdd:smart00382  61 GSGELRLRLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
1-490 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 1162.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     1 GPGVSALEEKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRG 80
Cdd:CHL00060   5 GPGVSTLEEKNLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    81 MEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKI 160
Cdd:CHL00060  85 MEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   161 GLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMR 240
Cdd:CHL00060 165 GLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMR 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   241 VGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVY 320
Cdd:CHL00060 245 VGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVY 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   321 VPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAIL 400
Cdd:CHL00060 325 VPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAIL 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   401 GLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAM 480
Cdd:CHL00060 405 GLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAA 484
                        490
                 ....*....|
gi 3850958   481 NLEVESNLKK 490
Cdd:CHL00060 485 NLEVESKLKK 494
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
8-486 0e+00

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: 950.68  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    8 EEKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 87
Cdd:COG0055   1 MAMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG----GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   88 APLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAG 167
Cdd:COG0055  77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  168 VGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALT 247
Cdd:COG0055 157 VGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALT 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  248 MAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLT 327
Cdd:COG0055 230 MAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLT 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  328 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSE 407
Cdd:COG0055 310 DPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSE 389
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3850958  408 EDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEVES 486
Cdd:COG0055 390 EDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
11-482 0e+00

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: 838.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     11 NLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRdtvgQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 90
Cdd:TIGR01039   1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNR----AESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     91 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:TIGR01039  77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    171 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    251 YFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 330
Cdd:TIGR01039 230 YFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPA 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    331 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 410
Cdd:TIGR01039 310 PATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDK 389
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3850958    411 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNL 482
Cdd:TIGR01039 390 LTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
13-475 0e+00

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: 581.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     13 GRIAQIIGPVLDVAFPpGKMPNIYNALIVkgrdtvGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSV 92
Cdd:TIGR03305   1 GHVVAVRGSIVDVRFD-GELPAIHSVLRA------GREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     93 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 172
Cdd:TIGR03305  74 PVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    173 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEqniaeskVALVYGQMNEPPGARMRVGLTALTMAEYF 252
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYF 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    253 RDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 332
Cdd:TIGR03305 227 RDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAV 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    333 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLT 412
Cdd:TIGR03305 307 HTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRV 386
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3850958    413 VARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEA 475
Cdd:TIGR03305 387 VNRARRLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
91-369 0e+00

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: 579.56  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   91 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:cd01133   1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  171 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:cd01133  81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL--SKVALVYGQMNEPPGARARVALTGLTMAE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  251 YFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 330
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 3850958  331 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 369
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
91-366 1.17e-133

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: 387.20  E-value: 1.17e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   91 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:cd19476   1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  171 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGvineqniAESKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:cd19476  81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSG-------AMERTVVVANTANDPPGARMRVPYTGLTIAE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  251 YFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK--EGSITSIQAVYVPADDLTD 328
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 3850958  329 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 366
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
144-364 5.43e-86

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: 263.06  E-value: 5.43e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    144 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSK 223
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    224 VALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 303
Cdd:pfam00006  71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3850958    304 RITSTKE--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
Cdd:pfam00006 150 RAGRVKGkgGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
ATP-synt_F1_beta_C cd18110
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ...
371-478 6.46e-77

F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-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: 349745 [Multi-domain]  Cd Length: 108  Bit Score: 235.84  E-value: 6.46e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  371 IVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGF 450
Cdd:cd18110   1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
                        90       100
                ....*....|....*....|....*...
gi 3850958  451 QLILSGELDGLPEQAFYLVGNIDEATAK 478
Cdd:cd18110  81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
13-454 3.20e-63

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: 211.43  E-value: 3.20e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   13 GRIAQIIGPVLDVAFPPGKMPNIynALIVKGRDTVgqqinVTCEVqqlLG--NNRVRAVAMSATDGLMRGMEVIDTGAPL 90
Cdd:COG1157  21 GRVTRVVGLLIEAVGPDASIGEL--CEIETADGRP-----VLAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   91 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQ---LDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAG 167
Cdd:COG1157  91 SVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGSG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  168 VGKTVLIMELINN----------IAkahggvsvfggvgERTREGNDlYME-------MKESGVIneqnIAESkvalvygq 230
Cdd:COG1157 168 VGKSTLLGMIARNteadvnvialIG-------------ERGREVRE-FIEddlgeegLARSVVV----VATS-------- 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  231 mNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE 310
Cdd:COG1157 222 -DEPPLMRLRAAYTATAIAEYFRDQG-KNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGK 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  311 GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPRIVGEEHYETAQRVKQTLQR 389
Cdd:COG1157 300 GSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISrVM--PDIVSPEHRALARRLRRLLAR 377
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3850958  390 YKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQpffvaevftgSPGKYVGLAETIRGFQLIL 454
Cdd:COG1157 378 YEENEDLIRI-GayqpgsdpeLDE-------AIALIPAIEAFLRQ----------GMDERVSFEESLAQLAELL 433
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
91-364 1.53e-52

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: 178.52  E-value: 1.53e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   91 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 170
Cdd:cd01136   1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  171 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYMEmkesGVINEQNIaeSKVALVYGQMNEPPGARMRVGLTALTMAE 250
Cdd:cd01136  81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGL--KRSVLVVATSDESPLLRVRAAYTATAIAE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  251 YFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 330
Cdd:cd01136 151 YFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
                       250       260       270
                ....*....|....*....|....*....|....
gi 3850958  331 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
76-425 3.66e-47

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 169.16  E-value: 3.66e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    76 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQ---LDTKLSifeTGIKVVDLLA 152
Cdd:PRK06936  81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   153 PYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREgndlYMEMKESGvINEQNIAESkvALVYGQMN 232
Cdd:PRK06936 158 TCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKA--VLVVATSD 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   233 EPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGS 312
Cdd:PRK06936 228 RPSMERAKAGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGS 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   313 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKE 392
Cdd:PRK06936 307 ITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEE 385
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 3850958   393 LQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 425
Cdd:PRK06936 386 VELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
60-425 5.57e-47

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 168.84  E-value: 5.57e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    60 LLGNNRVRA--VAM----------SATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTSPIHRS 127
Cdd:PRK06820  55 RIEPQGMLAevVSIeqemallspfASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCP 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   128 APAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELInniAKAHGGVSVFGGVGERTREGNDLYme 207
Cdd:PRK06820 134 PPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVREFL-- 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   208 mkesgvinEQNI---AESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRM 284
Cdd:PRK06820 209 --------EQVLtpeARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRG-KKVLLMADSLTRYARAAREIGLAAGEP 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   285 PSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
Cdd:PRK06820 280 PAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVS 359
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3850958   365 TMLqPRIVGEEHYETAQRVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 425
Cdd:PRK06820 360 RIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
PRK08149 PRK08149
FliI/YscN family ATPase;
59-427 5.00e-46

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 165.94  E-value: 5.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    59 QLLGNNRVRAV--AMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDT----RTTSPIHRSAPAFI 132
Cdd:PRK08149  47 QVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTvgpiSEERVIDVAPPSYA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   133 QLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYMEMKESG 212
Cdd:PRK08149 127 ERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   213 vineqniAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQP 292
Cdd:PRK08149 204 -------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQG-KRVVLFIDSMTRYARALRDVALAAGELPARRGYPA 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   293 TLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIV 372
Cdd:PRK08149 276 SVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVT 354
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 3850958   373 GEEHYETAQRVKQTLQRYKELQDIIAiLG---LDELSEEDRlTVARARKIERFLSQPF 427
Cdd:PRK08149 355 DPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDV 410
PRK09099 PRK09099
type III secretion system ATPase; Provisional
75-426 6.71e-45

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 163.02  E-value: 6.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    75 DGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQ---LDTKLSifeTGIKVVDLL 151
Cdd:PRK09099  81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   152 APYRRGGKIGLFGGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEMkesgVINEQNIAESKV 224
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMGMFargtqcdVNVIA----------LIGERGREVRE-FIEL----ILGEDGMARSVV 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   225 alVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER 304
Cdd:PRK09099 223 --VCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   305 ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVK 384
Cdd:PRK09099 300 AGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLR 378
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 3850958   385 QTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQP 426
Cdd:PRK09099 379 QLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
fliI PRK08972
flagellar protein export ATPase FliI;
76-399 1.74e-43

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 159.10  E-value: 1.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    76 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHrsAPAFIQLDTKlSIFE---TGIKVVDLLA 152
Cdd:PRK08972  81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAML 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   153 PYRRGGKIGLFGGAGVGKTVLI-MELINNIAKAhggvSVFGGVGERTREGNDLYMEmkesgVINEQNIAESKValVYGQM 231
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGREVKEFIEE-----ILGEEGRARSVV--VAAPA 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   232 NEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT--STK 309
Cdd:PRK08972 227 DTSPLMRLKGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPG 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   310 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQR 389
Cdd:PRK08972 306 QGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSL 384
                        330
                 ....*....|
gi 3850958   390 YKELQDIIAI 399
Cdd:PRK08972 385 YQQNRDLISI 394
fliI PRK08472
flagellar protein export ATPase FliI;
90-425 3.86e-43

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 157.92  E-value: 3.86e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    90 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 169
Cdd:PRK08472  90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   170 KTVLiMELINNIAKAhgGVSVFGGVGERTRE---------GNDLymemkESGVINEQNIAESKVALVYGqmneppgarmr 240
Cdd:PRK08472 170 KSTL-MGMIVKGCLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYG----------- 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   241 vGLTALTMAEYFRDVNEqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-EGSITSIQAV 319
Cdd:PRK08472 231 -AFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTV 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   320 YVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKELQDIIAI 399
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRI 387
                        330       340       350
                 ....*....|....*....|....*....|.
gi 3850958   400 ----LGLD-ELSEedrlTVARARKIERFLSQ 425
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ 414
fliI PRK08927
flagellar protein export ATPase FliI;
4-425 6.48e-43

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 157.83  E-value: 6.48e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     4 VSALEEKNL-GRIAQIIGPVLDVAFPPGkmpniynALIVKGRDTVGQQIN--VTCEVqqlLGNNRVRAVAM--SATDGLM 78
Cdd:PRK08927   9 IGDIDTLVIyGRVVAVRGLLVEVAGPIH-------ALSVGARIVVETRGGrpVPCEV---VGFRGDRALLMpfGPLEGVR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    79 RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTS-PIHRSAP---AFIQLDTKLsifETGIKVVDLLAPY 154
Cdd:PRK08927  79 RGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPPpahSRARVGEPL---DLGVRALNTFLTC 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   155 RRGGKIGLFGGAGVGKTVLIMELINNIAKAhggVSVFGGVGERTREGNDLYMEmkesgVINEQNIAESKValVYGQMNEP 234
Cdd:PRK08927 156 CRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQD-----DLGPEGLARSVV--VVATSDEP 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   235 PGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKEGS 312
Cdd:PRK08927 226 ALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGT 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   313 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPRIVGEEHYETAQRVKQTLQRYK 391
Cdd:PRK08927 305 ITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSrTM--PGCNDPEENPLVRRARQLMATYA 382
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 3850958   392 ELQDIIAI----LGLDelSEEDRlTVARARKIERFLSQ 425
Cdd:PRK08927 383 DMEELIRLgayrAGSD--PEVDE-AIRLNPALEAFLRQ 417
fliI PRK05688
flagellar protein export ATPase FliI;
51-425 3.60e-42

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 155.66  E-value: 3.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    51 INVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPV--------DTRTTS 122
Cdd:PRK05688  63 VQVEAEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMkaedwvpmDGPTIN 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   123 PIHRsAPAFIQLDTklsifetGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREgn 202
Cdd:PRK05688 142 PLNR-HPISEPLDV-------GIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVVGLIG--ERGRE-- 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   203 dlymeMKE--SGVINEQNIAESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSAL 280
Cdd:PRK05688 209 -----VKEfiEHILGEEGLKRSVV--VASPADDAPLMRLRAAMYCTRIAEYFRDKG-KNVLLLMDSLTRFAQAQREIALA 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   281 LGRMPSAVGYQPTLSTEMGSLQERITSTKEG--SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 358
Cdd:PRK05688 281 IGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAID 360
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3850958   359 PLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKELQDIIAI----LGLDelsEEDRLTVARARKIERFLSQ 425
Cdd:PRK05688 361 IEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
fliI PRK07721
flagellar protein export ATPase FliI;
86-399 2.23e-41

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 153.34  E-value: 2.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    86 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGG 165
Cdd:PRK07721  87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   166 AGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEmKESGvinEQNIAESKValVYGQMNEPPGAR 238
Cdd:PRK07721 167 SGVGKSTLMGMIarntsadLNVIA----------LIGERGREVRE-FIE-RDLG---PEGLKRSIV--VVATSDQPALMR 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   239 MRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQA 318
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQG-LNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYT 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   319 VYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTLQRYKELQDIIA 398
Cdd:PRK07721 309 VLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLIN 387

                 .
gi 3850958   399 I 399
Cdd:PRK07721 388 I 388
fliI PRK06002
flagellar protein export ATPase FliI;
100-401 2.25e-41

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 153.61  E-value: 2.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   100 GRIFNVLGEPVDNLGPVDTRTTS-PIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELi 178
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   179 nniAKA-HGGVSVFGGVGERTREgndlYMEMKEsGVINEqniAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNE 257
Cdd:PRK06002 186 ---ARAdAFDTVVIALVGERGRE----VREFLE-DTLAD---NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGE 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   258 qDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE--GSITSIQAVYVPADDLTDPAPATTF 335
Cdd:PRK06002 255 -NVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVADSIR 333
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3850958   336 AHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHyETAQRVKQTLQRYKELQDIIAILG 401
Cdd:PRK06002 334 GTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
fliI PRK06793
flagellar protein export ATPase FliI;
47-425 1.25e-40

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 151.28  E-value: 1.25e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    47 VGQQiNVTCEVQQLLGNNRVrAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFN----VLGEPVDNLG----PVDT 118
Cdd:PRK06793  48 VGEH-NVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPlqkiKLDA 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   119 rttSPIHrsapAFIQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGvgERT 198
Cdd:PRK06793 126 ---PPIH----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKADINVISLVG--ERG 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   199 REGND-LYMEMKESGVineqniaeSKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEV 277
Cdd:PRK06793 195 REVKDfIRKELGEEGM--------RKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSV 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   278 SALLGRMPSAvGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAV 357
Cdd:PRK06793 266 DIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAI 344
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3850958   358 DPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKElQDIIAILGLDELSEEDRLTVARARKIE---RFLSQ 425
Cdd:PRK06793 345 SVLDSVSRIME-EIVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
ATP-synt_F1_beta_N cd18115
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ...
11-90 1.27e-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: 134.95  E-value: 1.27e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   11 NLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 90
Cdd:cd18115   1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDD----GKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
fliI PRK07196
flagellar protein export ATPase FliI;
76-444 2.97e-34

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 133.48  E-value: 2.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    76 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTtsPIHRSAPAFIQLDTKL--SIFETGIKVVDLLAP 153
Cdd:PRK07196  74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLT 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   154 YRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREGNDLY-MEMKESGVineqniaeSKVALVYGQMN 232
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGLIG--ERGREVKEFIeHSLQAAGM--------AKSVVVAAPAD 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   233 EPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-TSTKEG 311
Cdd:PRK07196 221 ESPLMRIKATELCHAIATYYRDKG-HDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNG 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   312 SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYK 391
Cdd:PRK07196 300 TMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYM 378
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 3850958   392 ELQDIIA----ILGLDELSEEdrlTVARARKIERFLSQPFFVAEVFTGSPGKYVGLA 444
Cdd:PRK07196 379 AIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQEVGHPALFSASVEQLTGMF 432
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
72-399 1.06e-33

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 132.00  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    72 SATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNL----GPVDTRTTSPihrsAPAFIQLDTKLSIFeTGIKV 147
Cdd:PRK07594  71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   148 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFGGVGERTREgndlYMEMKESGVINEqniAESKVALV 227
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTLSEE---TRKRCVIV 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   228 YGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 307
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   308 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGEEHYETAQRVKQTL 387
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
                        330
                 ....*....|..
gi 3850958   388 QRYKELQDIIAI 399
Cdd:PRK07594 374 ALYQEVELLIRI 385
fliI PRK07960
flagellum-specific ATP synthase FliI;
92-428 3.75e-32

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 127.98  E-value: 3.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    92 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIhrSAPAF--IQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 169
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFnpLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   170 KTVLiMELINNIAKAHGGVSVFGGvgERTREGNDlYMEmkesGVINEQNIAESKValVYGQMNEPPGARMRVGLTALTMA 249
Cdd:PRK07960 188 KSVL-LGMMARYTQADVIVVGLIG--ERGREVKD-FIE----NILGAEGRARSVV--IAAPADVSPLLRMQGAAYATRIA 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   250 EYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS--TKEGSITSIQAVYVPADDLT 327
Cdd:PRK07960 258 EDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQ 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   328 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGEEHYETAQRVKQTLQRYKELQDIIAI----LGLD 403
Cdd:PRK07960 337 DPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSD 415
                        330       340
                 ....*....|....*....|....*
gi 3850958   404 ELSEEdrlTVARARKIERFLSQPFF 428
Cdd:PRK07960 416 PMLDK---AIALWPQLEAFLQQGIF 437
PRK05922 PRK05922
type III secretion system ATPase; Validated
69-457 1.73e-29

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 120.01  E-value: 1.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    69 VAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVV 148
Cdd:PRK05922  69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   149 DLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYMEMKESGvineqnIAESKVALV 227
Cdd:PRK05922 149 DAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEG------LAAQRTIII 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   228 YGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 307
Cdd:PRK05922 218 ASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   308 TKEGSITSIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQpRIVGEEHYETAQRVK 384
Cdd:PRK05922 297 NDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELR 370
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3850958   385 QTLQRYKELQDIIAI----LGLDElsEEDRlTVARARKIERFLSQPFfvaevftgspGKYVGLAETIRGFQLILSGE 457
Cdd:PRK05922 371 SLLKAYHEALDIIQLgayvPGQDA--HLDR-AVKLLPSIKQFLSQPL----------SSYCALHNTLKQLEALLKHE 434
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
61-428 1.09e-27

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 115.78  E-value: 1.09e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    61 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSI 140
Cdd:PRK13343  66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   141 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVIN 215
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   216 -----EQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 290
Cdd:PRK13343 208 vietlREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   291 QPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTStm 366
Cdd:PRK13343 287 PGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVS-- 364
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3850958   367 lqpRIVGEEHY----ETAQRVKQTLQRYKELQdIIAILGLDeLSEEDRLTVARARKIERFLSQPFF 428
Cdd:PRK13343 365 ---RVGGKAQHpairKESGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPRF 425
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
74-427 1.24e-27

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 114.92  E-value: 1.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    74 TDGLM-RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA--PA-------FIQldtklsifeT 143
Cdd:PRK04196  59 TTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------T 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   144 GIKVVDLLAPYRRGGKIGLFGGAGvgktvlimeLINNIAKAHGGVSVFGGVGE------------RTREGNDLYMEMKES 211
Cdd:PRK04196 130 GISAIDGLNTLVRGQKLPIFSGSG---------LPHNELAAQIARQAKVLGEEenfavvfaamgiTFEEANFFMEDFEET 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   212 GVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQ 291
Cdd:PRK04196 201 GALE-------RSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYP 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   292 PTLSTEMGSLQER--ITSTKEGSITSIQAVYVPADDLTDPAPattfahlDAT-------TVLSRGLAAKGIYPAVDPLDS 362
Cdd:PRK04196 274 GYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPS 346
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3850958   363 TSTMLQPRIvG-----EEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQPF 427
Cdd:PRK04196 347 LSRLMKDGI-GegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGF 416
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
89-368 2.55e-25

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: 105.00  E-value: 2.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   89 PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA--PA-------FIQldtklsifeTGIKVVDLLAPYRRGGK 159
Cdd:cd01135   1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPinPVariypeeMIQ---------TGISAIDVMNTLVRGQK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  160 IGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESgviNEQNIAESKVALVYGQMNEPPGARM 239
Cdd:cd01135  72 LPIFSGSGLPHNELAAQIARQ-AGVVGSEENFAIVFAAMGVTMEEARFFKDD---FEETGALERVVLFLNLANDPTIERI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  240 RVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER--ITSTKEGSITSIQ 317
Cdd:cd01135 148 ITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIP 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 3850958  318 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 368
Cdd:cd01135 228 ILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
89-364 5.54e-21

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: 93.02  E-value: 5.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   89 PLSVPVGGATLGRIFNVLGEPVDNLG----------------PVdtRTTSPIHRSAPAFIQLdtklsifETGIKVVDLLA 152
Cdd:cd01134   1 PLSVELGPGLLGSIFDGIQRPLEVIAetgsifiprgvnvqrwPV--RQPRPVKEKLPPNVPL-------LTGQRVLDTLF 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  153 PYRRGGKIGLFGGAGVGKTVlimeLINNIAK-AHGGVSVFGGVGERTREGNDLYMEMKE-SGVINEQNIAEsKVALVYGQ 230
Cdd:cd01134  72 PVAKGGTAAIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGERGNEMAEVLEEFPElKDPITGESLME-RTVLIANT 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  231 MNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI----- 305
Cdd:cd01134 147 SNMPVAAREASIYTGITIAEYFRDMG-YNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrc 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3850958  306 --TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
Cdd:cd01134 226 lgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
244-425 1.46e-20

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 94.85  E-value: 1.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   244 TALTMAEYFRDvneQ--DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER----IT-STKEGSITSI 316
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   317 QAVYVPADDLTDPapaTTFAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQP---RIVGEEHYETAQRVKQTL 387
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPwweENVDPDWRELRDEAMDLL 464
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 3850958   388 QRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 425
Cdd:PRK04192 465 QREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
86-425 2.33e-20

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: 93.63  E-value: 2.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     86 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPV------DTRTtSPIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 159
Cdd:TIGR01040  70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedylDING-QPINPYARIYPE-----EMIQTGISAIDVMNSIARGQK 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    160 IGLFGGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGNdLYMEMKESGViN-----------EQNIAESKVALVY 228
Cdd:TIGR01040 144 IPIFSAAGLPHN----EIAAQICRQAGLVKLPTKDVHDGHEDN-FAIVFAAMGV-NmetarffkqdfEENGSMERVCLFL 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    229 GQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--T 306
Cdd:TIGR01040 218 NLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrV 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    307 STKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----EHYETAQ 381
Cdd:TIGR01040 298 EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSN 376
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 3850958    382 RVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 425
Cdd:TIGR01040 377 QLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
15-87 1.88e-19

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


Pssm-ID: 427029 [Multi-domain]  Cd Length: 69  Bit Score: 82.21  E-value: 1.88e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3850958     15 IAQIIGPVLDVAFPPGKMPNIYNALIVKGRDtvgqQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTG 87
Cdd:pfam02874   1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
ATP-synt_F1_V1_A1_AB_FliI_C cd01429
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
376-439 2.50e-18

ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of 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, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that 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: 349744 [Multi-domain]  Cd Length: 70  Bit Score: 79.03  E-value: 2.50e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3850958  376 HYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGK 439
Cdd:cd01429   1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
196-437 2.91e-18

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 88.16  E-value: 2.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    196 ERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNeQDVLLFIDNIFRFVQAGS 275
Cdd:PRK14698  692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    276 EVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 348
Cdd:PRK14698  771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    349 AAKGIYPAVDPLDSTSTMLQP------RIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ER 421
Cdd:PRK14698  851 ARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
                         250
                  ....*....|....*.
gi 3850958    422 FLSQPFFvAEVFTGSP 437
Cdd:PRK14698  931 YLQQDAF-DEVDTYCP 945
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
90-364 4.35e-17

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: 81.07  E-value: 4.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   90 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 169
Cdd:cd01132   2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  170 KTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVINEQNIAESKVALVY-----GQMNEPPGARM 239
Cdd:cd01132  82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958  240 RVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE----GSITS 315
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTA 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 3850958  316 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 364
Cdd:cd01132 223 LPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
66-285 3.48e-16

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 80.88  E-value: 3.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    66 VRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQldtKLSIFE--- 142
Cdd:PRK09281  71 VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEplq 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   143 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESGVINEQ 217
Cdd:PRK09281 148 TGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN------------------QKGKDVIciyvaIGQKASTVAQVV 209
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3850958   218 NIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDvNEQDVLLFIDNIFRFVQAGSEVSALLGRMP 285
Cdd:PRK09281 210 RKLEEHGAMEYtivvaATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
74-334 4.08e-14

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 74.30  E-value: 4.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    74 TDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNlGP------VDTRTTS--PIHRSAPAfiqldtklSIFETGI 145
Cdd:PRK02118  58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPelegepIEIGGPSvnPVKRIVPR--------EMIRTGI 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   146 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMElINNIAKAHGGVSVFGGVGertregNDLYMEMKESgviNEQNIAESKVA 225
Cdd:PRK02118 129 PMIDVFNTLVESQKIPIFSVSGEPYNALLAR-IALQAEADIIILGGMGLT------FDDYLFFKDT---FENAGALDRTV 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   226 LVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI 305
Cdd:PRK02118 199 MFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA 278
                        250       260       270
                 ....*....|....*....|....*....|
gi 3850958   306 TSTKE-GSITSIQAVYVPADDLTDPAPATT 334
Cdd:PRK02118 279 VDFEDgGSITIIAVTTMPGDDVTHPVPDNT 308
atpA CHL00059
ATP synthase CF1 alpha subunit
61-358 1.19e-11

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 66.53  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    61 LGNNRVRAVAMSatDGLM--RGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKL 138
Cdd:CHL00059  45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   139 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGND---LYMEM--KE 210
Cdd:CHL00059 120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   211 SGVINEQNIAESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNEQDVLLFIDNIFRFVQAGSEVSALLGRMP 285
Cdd:CHL00059 182 SSVAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   286 SAVGY--------------QPTLSTEMGslqeritstkEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAK 351
Cdd:CHL00059 261 GREAYpgdvfylhsrllerAAKLSSQLG----------EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNA 330

                 ....*..
gi 3850958   352 GIYPAVD 358
Cdd:CHL00059 331 GIRPAIN 337
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
12-358 1.37e-08

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 57.36  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    12 LGRIAQIIGPVLDVAFPPGKMPNIYNALIVKgrdTVGQQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 91
Cdd:PTZ00185  40 IGYVHSIDGTIATLIPAPGNPGVAYNTIIMI---QVSPTTFAAGLVFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLY 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958    92 VPVGGATLGRIFNVLGEPV---------------DNLGPVDTRTTSPIHRSAPAFIQLdtklsifeTGIKVVDLLAPYRR 156
Cdd:PTZ00185 117 IPVGAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAPNIVSRSPVNYNLL--------TGFKAVDTMIPIGR 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   157 GGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGErtregndLYMEMKE--SGVINEQNIAESKVALVY-----G 229
Cdd:PTZ00185 189 GQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVIS-------IYVSIGQrcSNVARIHRLLRSYGALRYttvmaA 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958   230 QMNEPPGARMRVGLTALTMAEYFRDVNEQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK 309
Cdd:PTZ00185 262 TAAEPAGLQYLAPYSGVTMGEYFMNRGRH-CLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLS 340
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 3850958   310 E----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 358
Cdd:PTZ00185 341 PgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
T3SS_ATPase_C pfam18269
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ...
372-426 1.37e-04

T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.


Pssm-ID: 465691 [Multi-domain]  Cd Length: 70  Bit Score: 40.11  E-value: 1.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3850958    372 VGEEHYETAQRVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 426
Cdd:pfam18269   1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
ATP-synt_F1_V1_A1_AB_FliI_N cd01426
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
12-88 2.06e-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: 39.60  E-value: 2.06e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3850958   12 LGRIAQIIGPVLDVAFPPGkmPNIYNALIVKgRDTVGQQINVTCEVQQLLGNnRVRAVAMSATDGLMRGMEVIDTGA 88
Cdd:cd01426   1 KGRVIRVNGPLVEAELEGE--VAIGEVCEIE-RGDGNNETVLKAEVIGFRGD-RAILQLFESTRGLSRGALVEPTGR 73
ATP-synt_V_A-type_alpha_C cd18111
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ...
381-425 2.58e-04

V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.


Pssm-ID: 349746 [Multi-domain]  Cd Length: 105  Bit Score: 40.45  E-value: 2.58e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 3850958  381 QRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 425
Cdd:cd18111   6 TEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
ATP-synt_V_A-type_beta_C cd18112
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ...
391-425 3.65e-04

V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.


Pssm-ID: 349747 [Multi-domain]  Cd Length: 95  Bit Score: 39.72  E-value: 3.65e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 3850958  391 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 425
Cdd:cd18112  22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
156-284 4.28e-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: 37.74  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850958     156 RGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYmemkesgvineqniaeskvaLVYGQMNEPP 235
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL--------------------LIIVGGKKAS 60
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 3850958     236 GARMRVGLTALTMAEYFRdvneqDVLLFIDNIFRFVQAGSEVSALLGRM 284
Cdd:smart00382  61 GSGELRLRLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
 
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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