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Conserved domains on  [gi|387165999|gb|AFJ64462|]
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ATP synthase beta chain, partial [Desmacella pumilio]

Protein Classification

F0F1 ATP synthase subunit beta( domain architecture ID 11414600)

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

CATH:  1.10.1140.10
EC:  7.1.2.2
Gene Ontology:  GO:0005524|GO:0016020|GO:0045261|GO:0046933|GO:0046961
PubMed:  10838044|27373333|11533724
SCOP:  3002019

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 2-303 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: 610.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   2 LPPILNSLEVEN-RKPRLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGP 80
Cdd:COG0055   25 LPAIYNALEVENeGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  81 VGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRR-LIMELINNVANAHGGCSVFAGVG 159
Cdd:COG0055  105 IEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTvLIMELIHNIAKEHGGVSVFAGVG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 160 ERTREGNDLYHEMIQSGVISlkddksKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSE 239
Cdd:COG0055  185 ERTREGNDLYREMKESGVLD------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSE 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387165999 240 VSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:COG0055  259 VSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 2-303 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: 610.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   2 LPPILNSLEVEN-RKPRLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGP 80
Cdd:COG0055   25 LPAIYNALEVENeGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  81 VGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRR-LIMELINNVANAHGGCSVFAGVG 159
Cdd:COG0055  105 IEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTvLIMELIHNIAKEHGGVSVFAGVG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 160 ERTREGNDLYHEMIQSGVISlkddksKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSE 239
Cdd:COG0055  185 ERTREGNDLYREMKESGVLD------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSE 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387165999 240 VSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:COG0055  259 VSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 2-303 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: 549.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999    2 LPPILNSLEVENRK-PRLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGP 80
Cdd:TIGR01039  22 LPRIYNALKVQNRAeSELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   81 VGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRR-LIMELINNVANAHGGCSVFAGVG 159
Cdd:TIGR01039 102 IPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTvLIQELINNIAKEHGGYSVFAGVG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  160 ERTREGNDLYHEMIQSGVISlkddksKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSE 239
Cdd:TIGR01039 182 ERTREGNDLYHEMKESGVID------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSE 255

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387165999  240 VSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:TIGR01039 256 VSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDA 319
atpB CHL00060
ATP synthase CF1 beta subunit
 2-303 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 540.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   2 LPPILNSLEVENRKP-----RLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPID 76
Cdd:CHL00060  36 MPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVD 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  77 ERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRR-LIMELINNVANAHGGCSVF 155
Cdd:CHL00060 116 NLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTvLIMELINNIAKAHGGVSVF 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 156 AGVGERTREGNDLYHEMIQSGVISLKD-DKSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFT 234
Cdd:CHL00060 196 GGVGERTREGNDLYMEMKESGVINEQNiAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFV 275

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387165999 235 QAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:CHL00060 276 QAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDA 344
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 56-303 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: 518.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  56 KIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGR 135
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 136 R-LIMELINNVANAHGGCSVFAGVGERTREGNDLYHEMIQSGVISLkDDKSKVALVYGQMNEPPGARARVALTGLTVAEY 214
Cdd:cd01133   81 TvLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL-DGLSKVALVYGQMNEPPGARARVALTGLTMAEY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 215 FRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAP 294
Cdd:cd01133  160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239


                 ....*....
gi 387165999 295 ATTFAHLDA 303
Cdd:cd01133  240 ATTFAHLDA 248
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 109-303 1.39e-75

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: 229.94  E-value: 1.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  109 GIKVVDLLAPYAKGGKIGLFGRAGVGRRLIMELINNvaNAHGGCSVFAGVGERTREGNDLYHEMIQSGVISlkddksKVA 188
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIAR--QASADVVVYALIGERGREVREFIEELLGSGALK------RTV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  189 LVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI 268
Cdd:pfam00006  73 VVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 387165999  269 TTT--QKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:pfam00006 152 GRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDG 188
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 2-303 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: 610.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   2 LPPILNSLEVEN-RKPRLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGP 80
Cdd:COG0055   25 LPAIYNALEVENeGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  81 VGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRR-LIMELINNVANAHGGCSVFAGVG 159
Cdd:COG0055  105 IEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTvLIMELIHNIAKEHGGVSVFAGVG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 160 ERTREGNDLYHEMIQSGVISlkddksKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSE 239
Cdd:COG0055  185 ERTREGNDLYREMKESGVLD------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSE 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387165999 240 VSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:COG0055  259 VSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 2-303 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: 549.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999    2 LPPILNSLEVENRK-PRLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGP 80
Cdd:TIGR01039  22 LPRIYNALKVQNRAeSELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGP 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   81 VGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRR-LIMELINNVANAHGGCSVFAGVG 159
Cdd:TIGR01039 102 IPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTvLIQELINNIAKEHGGYSVFAGVG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  160 ERTREGNDLYHEMIQSGVISlkddksKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSE 239
Cdd:TIGR01039 182 ERTREGNDLYHEMKESGVID------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSE 255

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387165999  240 VSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:TIGR01039 256 VSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDA 319
atpB CHL00060
ATP synthase CF1 beta subunit
 2-303 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 540.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   2 LPPILNSLEVENRKP-----RLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPID 76
Cdd:CHL00060  36 MPNIYNALVVKGRDTagqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVD 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  77 ERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRR-LIMELINNVANAHGGCSVF 155
Cdd:CHL00060 116 NLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTvLIMELINNIAKAHGGVSVF 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 156 AGVGERTREGNDLYHEMIQSGVISLKD-DKSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFT 234
Cdd:CHL00060 196 GGVGERTREGNDLYMEMKESGVINEQNiAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFV 275

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387165999 235 QAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:CHL00060 276 QAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDA 344
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 56-303 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: 518.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  56 KIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGR 135
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 136 R-LIMELINNVANAHGGCSVFAGVGERTREGNDLYHEMIQSGVISLkDDKSKVALVYGQMNEPPGARARVALTGLTVAEY 214
Cdd:cd01133   81 TvLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL-DGLSKVALVYGQMNEPPGARARVALTGLTMAEY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 215 FRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAP 294
Cdd:cd01133  160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239


                 ....*....
gi 387165999 295 ATTFAHLDA 303
Cdd:cd01133  240 ATTFAHLDA 248
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 1-303 2.12e-127

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: 370.69  E-value: 2.12e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999    1 GLPPILNSLEVENRKPRLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGP 80
Cdd:TIGR03305  17 GELPAIHSVLRAGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGNTIDRREP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   81 VGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRR-LIMELINNVANAHGGCSVFAGVG 159
Cdd:TIGR03305  97 PKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTvLLTEMIHNMVGQHQGVSIFCGIG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  160 ERTREGNDLYHEMIQSGVISlkddksKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSE 239
Cdd:TIGR03305 177 ERCREGEELYREMKEAGVLD------NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIFRFIQAGSE 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387165999  240 VSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:TIGR03305 251 VSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSA 314
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 56-303 5.54e-114

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: 329.80  E-value: 5.54e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  56 KIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGR 135
Cdd:cd19476    1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 136 R-LIMELINNVANAHGGCSVFAGVGERTREGNDLYHEMIQSGVIslkddkSKVALVYGQMNEPPGARARVALTGLTVAEY 214
Cdd:cd19476   81 TvLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAM------ERTVVVANTANDPPGARMRVPYTGLTIAEY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 215 FRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQ--KGSITSVQAVFVPADDLTDP 292
Cdd:cd19476  155 FRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDP 233

                        250
                 ....*....|.
gi 387165999 293 APATTFAHLDA 303
Cdd:cd19476  234 IPDNTFAILDG 244
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 109-303 1.39e-75

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: 229.94  E-value: 1.39e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  109 GIKVVDLLAPYAKGGKIGLFGRAGVGRRLIMELINNvaNAHGGCSVFAGVGERTREGNDLYHEMIQSGVISlkddksKVA 188
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIAR--QASADVVVYALIGERGREVREFIEELLGSGALK------RTV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  189 LVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI 268
Cdd:pfam00006  73 VVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 387165999  269 TTT--QKGSITSVQAVFVPADDLTDPAPATTFAHLDA 303
Cdd:pfam00006 152 GRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDG 188
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 56-302 4.01e-44

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: 151.17  E-value: 4.01e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  56 KIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGR 135
Cdd:cd01136    1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 136 RLIMELINNVANAHggCSVFAGVGERTREGNDLYHEMIQSGVISlkddksKVALVYGQMNEPPGARARVALTGLTVAEYF 215
Cdd:cd01136   81 STLLGMIARNTDAD--VNVIALIGERGREVREFIEKDLGEEGLK------RSVLVVATSDESPLLRVRAAYTATAIAEYF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 216 RDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDPAPA 295
Cdd:cd01136  153 RDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIAD 231


                 ....*..
gi 387165999 296 TTFAHLD 302
Cdd:cd01136  232 EVRSILD 238
fliI PRK08472
flagellar protein export ATPase FliI;
57-292 2.75e-37

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 137.51  E-value: 2.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  57 IPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRR 136
Cdd:PRK08472  92 IPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 137 LIMELInnVANAHGGCSVFAGVGERTREgndlYHEMIQSgviSLKDDKSKVALVYGQMNEPPGARARVALTGLTVAEYFR 216
Cdd:PRK08472 172 TLMGMI--VKGCLAPIKVVALIGERGRE----IPEFIEK---NLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK 242

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387165999 217 DQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQ-KGSITSVQAVFVPADDLTDP 292
Cdd:PRK08472 243 NQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVEGDDMSDP 318
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
37-292 8.74e-37

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 136.10  E-value: 8.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  37 DGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSsIHADAPEFVEMNVKQEILVTGIKVVDLL 116
Cdd:PRK06820  79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWRE-LDCPPPSPLTRQPIEQMLTTGIRAIDGI 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 117 APYAKGGKIGLFGRAGVGRRLIMELInnVANAHGGCSVFAGVGERTREGNDLYHEMIQsgvislKDDKSKVALVYGQMNE 196
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTLLGML--CADSAADVMVLALIGERGREVREFLEQVLT------PEARARTVVVVATSDR 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 197 PPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSI 276
Cdd:PRK06820 230 PALERLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSI 308

                        250
                 ....*....|....*.
gi 387165999 277 TSVQAVFVPADDLTDP 292
Cdd:PRK06820 309 TAFYTVLVEGDDMNEP 324
fliI PRK06002
flagellar protein export ATPase FliI;
25-302 9.70e-37

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 136.28  E-value: 9.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  25 HLGEntvrTIAMDGTEGLIRGQVC--NDTGSPIK--------------IPVGPKTL-------GRIINVIGEPIDERGPV 81
Cdd:PRK06002  48 RLGD----FVAIRADGGTHLGEVVrvDPDGVTVKpfeprieiglgdavFRKGPLRIrpdpswkGRVINALGEPIDGLGPL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  82 GE-EMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRlimELINNVANAHGGCSV-FAGVG 159
Cdd:PRK06002 124 APgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKS---TLLAMLARADAFDTVvIALVG 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 160 ERTREgndlYHEMIQSgviSLKDDKSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSE 239
Cdd:PRK06002 201 ERGRE----VREFLED---TLADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR-GENVLLIVDSVTRFAHAARE 272

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 387165999 240 VSALLGRIPSAVGYQPTLATDMGTMQERI--TTTQKGSITSVQAVFVPADDLTDPAPATTFAHLD 302
Cdd:PRK06002 273 VALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLD 337
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 32-292 3.79e-35

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: 131.69  E-value: 3.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  32 RTIAM--DGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTG 109
Cdd:COG1157   65 RVLLMplGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTG 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 110 IKVVDLLAPYAKGGKIGLFGRAGVGRRLIMELINNVANAHggCSVFAGVGERTREGNdlyhEMIQSgviSLKDDK-SKVA 188
Cdd:COG1157  145 VRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEAD--VNVIALIGERGREVR----EFIED---DLGEEGlARSV 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 189 LVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI 268
Cdd:COG1157  216 VVVATSDEPPLMRLRAAYTATAIAEYFRDQ-GKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA 294

                        250       260
                 ....*....|....*....|....
gi 387165999 269 TTTQKGSITSVQAVFVPADDLTDP 292
Cdd:COG1157  295 GNGGKGSITAFYTVLVEGDDMNDP 318
PRK08149 PRK08149
FliI/YscN family ATPase;
19-292 7.02e-34

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 128.19  E-value: 7.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  19 VLEVAQHLGENTVRTI--AMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEpIDER--GPVGEEMKSS---IHA 91
Cdd:PRK08149  42 VIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdAPPTVGPISEervIDV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  92 DAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRLIMELInnVANAHGGCSVFAGVGERTREGNDLYHE 171
Cdd:PRK08149 121 APPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNML--IEHSEADVFVIGLIGERGREVTEFVES 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 172 MIQSGvislkdDKSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAV 251
Cdd:PRK08149 199 LRASS------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARR 271

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 387165999 252 GYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDLTDP 292
Cdd:PRK08149 272 GYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDP 312
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
51-302 2.19e-33

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 126.79  E-value: 2.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  51 TGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGR 130
Cdd:PRK06936  91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 131 AGVGRRLIMELInnVANAHGGCSVFAGVGERTREGND-LYHEMIQSGVislkddkSKVALVYGQMNEPPGARARVALTGL 209
Cdd:PRK06936 171 AGGGKSTLLASL--IRSAEVDVTVLALIGERGREVREfIESDLGEEGL-------RKAVLVVATSDRPSMERAKAGFVAT 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 210 TVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFVPADDL 289
Cdd:PRK06936 242 SIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDM 320

                        250
                 ....*....|...
gi 387165999 290 TDPAPATTFAHLD 302
Cdd:PRK06936 321 TEPVADETRSILD 333
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 40-292 1.78e-32

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 124.50  E-value: 1.78e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  40 EGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPY 119
Cdd:PRK09099  81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 120 AKGGKIGLFGRAGVGRRLIMELInnVANAHGGCSVFAGVGERTREGNDLYHE------MIQSGVISLKDDKSKValvygq 193
Cdd:PRK09099 161 GEGQRMGIFAPAGVGKSTLMGMF--ARGTQCDVNVIALIGERGREVREFIELilgedgMARSVVVCATSDRSSI------ 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 194 mneppgARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQK 273
Cdd:PRK09099 233 ------ERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET 305

                        250
                 ....*....|....*....
gi 387165999 274 GSITSVQAVFVPADDLTDP 292
Cdd:PRK09099 306 GSITALYTVLAEDESGSDP 324
fliI PRK07721
flagellar protein export ATPase FliI;
51-302 1.88e-31

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 121.75  E-value: 1.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  51 TGSPIKIPVGPKTLGRIINVIGEPIDERgPVGEEMKS-SIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFG 129
Cdd:PRK07721  87 TGKPLEVKVGSGLIGQVLDALGEPLDGS-ALPKGLAPvSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 130 RAGVGRRLIMELINNVANAHggCSVFAGVGERTRE-----GNDLYHEMIQSGVIslkddkskvalVYGQMNEPPGARARV 204
Cdd:PRK07721 166 GSGVGKSTLMGMIARNTSAD--LNVIALIGERGREvrefiERDLGPEGLKRSIV-----------VVATSDQPALMRIKG 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 205 ALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVFV 284
Cdd:PRK07721 233 AYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLV 311

                        250
                 ....*....|....*...
gi 387165999 285 PADDLTDPAPATTFAHLD 302
Cdd:PRK07721 312 DGDDMNEPIADTVRGILD 329
fliI PRK08972
flagellar protein export ATPase FliI;
52-302 1.19e-28

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 114.03  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  52 GSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRA 131
Cdd:PRK08972  92 GEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 132 GVGRRLIMELINNVANAHggCSVFAGVGERTREGNDLYHEmiqsgvISLKDDKSKVALVYGQMNEPPGARARVALTGLTV 211
Cdd:PRK08972 172 GVGKSVLLGMMTRGTTAD--VIVVGLVGERGREVKEFIEE------ILGEEGRARSVVVAAPADTSPLMRLKGCETATTI 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 212 AEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITT--TQKGSITSVQAVFVPADDL 289
Cdd:PRK08972 244 AEYFRDQ-GLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGDDL 322

                        250
                 ....*....|...
gi 387165999 290 TDPAPATTFAHLD 302
Cdd:PRK08972 323 QDPIADASRAILD 335
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
39-292 3.21e-28

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 112.74  E-value: 3.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  39 TEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERgPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAP 118
Cdd:PRK07594  73 TIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVAT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 119 YAKGGKIGLFGRAGVGRRLIMELINNVANAHggCSVFAGVGERTREGNDLYHEMIQsgvislKDDKSKVALVYGQMNEPP 198
Cdd:PRK07594 152 CGEGQRVGIFSAPGVGKSTLLAMLCNAPDAD--SNVLVLIGERGREVREFIDFTLS------EETRKRCVIVVATSDRPA 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 199 GARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITS 278
Cdd:PRK07594 224 LERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITA 302

                        250
                 ....*....|....
gi 387165999 279 VQAVFVPADDLTDP 292
Cdd:PRK07594 303 FYTVLVEGDDMNEP 316
fliI PRK06793
flagellar protein export ATPase FliI;
39-302 5.14e-28

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 111.99  E-value: 5.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  39 TEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDErgPVGEEMKSSIHADAPEF--VEMNVKQEILVTGIKVVDLL 116
Cdd:PRK06793  73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREEITDVFETGIKSIDSM 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 117 APYAKGGKIGLFGRAGVGRRLIMELInnVANAHGGCSVFAGVGERTREGND-LYHEMIQSGVislkddkSKVALVYGQMN 195
Cdd:PRK06793 151 LTIGIGQKIGIFAGSGVGKSTLLGMI--AKNAKADINVISLVGERGREVKDfIRKELGEEGM-------RKSVVVVATSD 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 196 EPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvGYQPTLATDMGTMQERITTTQKGS 275
Cdd:PRK06793 222 ESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGS 299

                        250       260
                 ....*....|....*....|....*..
gi 387165999 276 ITSVQAVFVPADDLTDPAPATTFAHLD 302
Cdd:PRK06793 300 ITGIYTVLVDGDDLNGPVPDLARGILD 326
fliI PRK08927
flagellar protein export ATPase FliI;
9-292 6.20e-27

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 109.30  E-value: 6.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   9 LEVENRKPRLVL-EVaqhLGENTVRTIAM--DGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGE-E 84
Cdd:PRK08927  44 IVVETRGGRPVPcEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQgP 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  85 MKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRLIMELInnVANAHGGCSVFAGVGERTRE 164
Cdd:PRK08927 121 VPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSML--ARNADADVSVIGLIGERGRE 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 165 gndlYHEMIQS--GVISLKddKSKValVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSA 242
Cdd:PRK08927 199 ----VQEFLQDdlGPEGLA--RSVV--VVATSDEPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGL 269

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 387165999 243 LLGRIPSAVGYQPTLATDMGTMQERI--TTTQKGSITSVQAVFVPADDLTDP 292
Cdd:PRK08927 270 SAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEP 321
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 54-297 7.07e-27

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: 106.15  E-value: 7.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  54 PIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGV 133
Cdd:cd01135    1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 134 GRRLIMELINNVANAHGGCS----VFAGVGERTREGNDLYHEMIQSGVISlkddksKVALVYGQMNEPPGARARVALTGL 209
Cdd:cd01135   81 PHNELAAQIARQAGVVGSEEnfaiVFAAMGVTMEEARFFKDDFEETGALE------RVVLFLNLANDPTIERIITPRMAL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 210 TVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER--ITTTQKGSITSVQAVFVPAD 287
Cdd:cd01135  155 TTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPND 234

                        250
                 ....*....|
gi 387165999 288 DLTDPAPATT 297
Cdd:cd01135  235 DITHPIPDLT 244
fliI PRK05688
flagellar protein export ATPase FliI;
56-302 3.17e-25

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 104.43  E-value: 3.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  56 KIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGR 135
Cdd:PRK05688 102 RLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 136 RLIMELINNVANAHggCSVFAGVGERTREGNDLYHEMIqsGVISLKddksKVALVYGQMNEPPGARARVALTGLTVAEYF 215
Cdd:PRK05688 182 SVLLGMMTRFTEAD--IIVVGLIGERGREVKEFIEHIL--GEEGLK----RSVVVASPADDAPLMRLRAAMYCTRIAEYF 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 216 RDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQK--GSITSVQAVFVPADDLTDPA 293
Cdd:PRK05688 254 RDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGDDQQDPI 332


                 ....*....
gi 387165999 294 PATTFAHLD 302
Cdd:PRK05688 333 ADSARGVLD 341
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 22-248 9.52e-24

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 100.76  E-value: 9.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  22 VAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNV 101
Cdd:PRK13343  62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDF 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 102 KQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRLIMelINNVANAHGG---CsVFAGVGERTregndlyhEMIQSGVI 178
Cdd:PRK13343 142 VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIA--IDAIINQKDSdviC-VYVAIGQKA--------SAVARVIE 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387165999 179 SLK----DDKSKValVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIP 248
Cdd:PRK13343 211 TLRehgaLEYTTV--VVAEASDPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPP 281
ATP-synt_F1_beta_N cd18115
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ...
 2-55 1.72e-23

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: 91.42  E-value: 1.72e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 387165999   2 LPPILNSLEVENRKP-RLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPI 55
Cdd:cd18115   22 LPPIYNALEVKGDDGkKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
PRK05922 PRK05922
type III secretion system ATPase; Validated
 54-283 3.96e-23

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 98.44  E-value: 3.96e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  54 PIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGV 133
Cdd:PRK05922  89 PPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGS 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 134 GRRLIMELInnVANAHGGCSVFAGVGERTREGNDlYHEMIQSGVislkdDKSKVALVYGQMNEPPGARARVALTGLTVAE 213
Cdd:PRK05922 169 GKSSLLSTI--AKGSKSTINVIALIGERGREVRE-YIEQHKEGL-----AAQRTIIIASPAHETAPTKVIAGRAAMTIAE 240

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 214 YFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQKGSITSVQAVF 283
Cdd:PRK05922 241 YFRDQ-GHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIL 309
fliI PRK07196
flagellar protein export ATPase FliI;
59-302 1.72e-22

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 96.50  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  59 VGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRLI 138
Cdd:PRK07196  92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 139 MELINNVANAHggCSVFAGVGERTREGNDLY-HEMIQSGVislkddkSKVALVYGQMNEPPGARARVALTGLTVAEYFRD 217
Cdd:PRK07196 172 LGMITRYTQAD--VVVVGLIGERGREVKEFIeHSLQAAGM-------AKSVVVAAPADESPLMRIKATELCHAIATYYRD 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 218 QeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTQ-KGSITSVQAVFVPADDLTDPAPAT 296
Cdd:PRK07196 243 K-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTMTAIYTVLAEGDDQQDPIVDC 321


                 ....*.
gi 387165999 297 TFAHLD 302
Cdd:PRK07196 322 ARAVLD 327
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
 19-248 3.78e-22

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


Pssm-ID: 273365 [Multi-domain]  Cd Length: 501  Bit Score: 95.92  E-value: 3.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   19 VLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVE 98
Cdd:TIGR00962  58 VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIE 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   99 MNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRLI-MELINNVANAHGGCsVFAGVGERTREGNDLYHEMIQSGV 177
Cdd:TIGR00962 138 RKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVaIDTIINQKDSDVYC-IYVAIGQKASTVAQVVRKLEEHGA 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387165999  178 IslkdDKSKValVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIP 248
Cdd:TIGR00962 217 M----AYTIV--VAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPP 280
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 38-294 3.52e-21

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 92.97  E-value: 3.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  38 GTEGL-IRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLL 116
Cdd:PRK04196  58 GTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 117 APYAKGGKIGLFGRAGVGRRLIMELINNVANAHGG----CSVFAGVGERTREGNDLYHEMIQSGVIslkddkSKVALVYG 192
Cdd:PRK04196 138 NTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLGEeenfAVVFAAMGITFEEANFFMEDFEETGAL------ERSVVFLN 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 193 QMNEPPGAR---ARVAltgLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER-- 267
Cdd:PRK04196 212 LADDPAIERiltPRMA---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERag 288

                        250       260
                 ....*....|....*....|....*..
gi 387165999 268 ITTTQKGSITSVQAVFVPADDLTDPAP 294
Cdd:PRK04196 289 RIKGKKGSITQIPILTMPDDDITHPIP 315
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 104-292 4.09e-20

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: 88.02  E-value: 4.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 104 EILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRLIMELINNVANAHggCSVFAGVGERtreGNdlyhEMIQsgVIS---- 179
Cdd:cd01134   58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSD--VVIYVGCGER---GN----EMAE--VLEefpe 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 180 LKDDKS------KVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGY 253
Cdd:cd01134  127 LKDPITgeslmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGY 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 387165999 254 QPTLATDMGTMQERI-------TTTQKGSITSVQAVFVPADDLTDP 292
Cdd:cd01134  206 PAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEP 251
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 19-297 3.28e-18

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: 84.39  E-value: 3.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   19 VLEVAqhlGENTVRTIaMDGTEGL-IRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEE-----MKSSIHAD 92
Cdd:TIGR01040  41 VLEVS---GNKAVVQV-FEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEdyldiNGQPINPY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999   93 APEFVEmnvkqEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRLIMELINNVA--------NAHGG-----CSVFAGVG 159
Cdd:TIGR01040 117 ARIYPE-----EMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvklptkDVHDGhednfAIVFAAMG 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  160 ERTREGNDLYHEMIQSGVISlkddksKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSE 239
Cdd:TIGR01040 192 VNMETARFFKQDFEENGSME------RVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALRE 265

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  240 VSALLGRIPSAVGYQPTLATDMGTMQERI--TTTQKGSITSVQAVFVPADDLTDPAPATT 297
Cdd:TIGR01040 266 VSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLT 325
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 38-297 1.82e-17

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 82.00  E-value: 1.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  38 GTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDeRGPVGEEmkSSIHADAPEF--VEMNVKQEILVTGIKVVDL 115
Cdd:PRK02118  57 GTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPID-GGPELEG--EPIEIGGPSVnpVKRIVPREMIRTGIPMIDV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 116 LAPYAKGGKIGLFGRAGvgrRLIMELINNVAN-AHGGCSVFAGVGERTREGNDLYHEMIQSGVISlkddksKVALVYGQM 194
Cdd:PRK02118 134 FNTLVESQKIPIFSVSG---EPYNALLARIALqAEADIIILGGMGLTFDDYLFFKDTFENAGALD------RTVMFIHTA 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 195 NEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQER-ITTTQK 273
Cdd:PRK02118 205 SDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDG 284

                        250       260
                 ....*....|....*....|....
gi 387165999 274 GSITSVQAVFVPADDLTDPAPATT 297
Cdd:PRK02118 285 GSITIIAVTTMPGDDVTHPVPDNT 308
fliI PRK07960
flagellum-specific ATP synthase FliI;
49-302 4.80e-17

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 80.98  E-value: 4.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  49 NDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLF 128
Cdd:PRK07960 102 EGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLF 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 129 GRAGVGRRLIMELINNVANAHggCSVFAGVGERTREGNDLYHEMI------QSGVISLKDDKSkvalvygqmnepPGARA 202
Cdd:PRK07960 182 AGSGVGKSVLLGMMARYTQAD--VIVVGLIGERGREVKDFIENILgaegraRSVVIAAPADVS------------PLLRM 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 203 RVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITT--TQKGSITSVQ 280
Cdd:PRK07960 248 QGAAYATRIAEDFRDR-GQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFY 326

                        250       260
                 ....*....|....*....|..
gi 387165999 281 AVFVPADDLTDPAPATTFAHLD 302
Cdd:PRK07960 327 TVLTEGDDQQDPIADSARAILD 348
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 19-248 1.28e-14

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


Pssm-ID: 439826 [Multi-domain]  Cd Length: 504  Bit Score: 73.92  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  19 VLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVE 98
Cdd:COG0056   59 VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVID 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  99 -MNVKqEILVTGIKVVDLLAPyakggkIglfGRagvGRRlimELInnvanahggcsvfagVGERtregndlyhemiQSG- 176
Cdd:COG0056  139 rQPVH-EPLQTGIKAIDAMIP------I---GR---GQR---ELI---------------IGDR------------QTGk 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 177 -------VISLKDD------------KSKVALV------YGQM----------NEPPGARARVALTGLTVAEYFRDQeGQ 221
Cdd:COG0056  176 taiaidtIINQKGKdviciyvaigqkASTVAQVvetleeHGAMeytivvaataSDPAPLQYIAPYAGCAMGEYFMDQ-GK 254

                        250       260
                 ....*....|....*....|....*..
gi 387165999 222 DVLLFIDNIFRFTQAGSEVSALLGRIP 248
Cdd:COG0056  255 DVLIVYDDLSKHAVAYRELSLLLRRPP 281
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 55-248 5.00e-14

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: 70.67  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  55 IKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGRAGVG 134
Cdd:cd01132    2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 135 RRLImeLINNVANAHGG--CSVFAGVGERTREGNDLYHEMIQSGVIslkdDKSKValVYGQMNEPPGARARVALTGLTVA 212
Cdd:cd01132   82 KTAI--AIDTIINQKGKkvYCIYVAIGQKRSTVAQIVKTLEEHGAM----EYTIV--VAATASDPAPLQYLAPYAGCAMG 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 387165999 213 EYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIP 248
Cdd:cd01132  154 EYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 19-248 8.17e-14

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 71.25  E-value: 8.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  19 VLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVE 98
Cdd:PRK09281  59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  99 MNVKQEILVTGIKVVDLLAPyakggkIglfGRagvGRRlimELInnvanahggcsvfagVGERtregndlyhemiQSG-- 176
Cdd:PRK09281 139 RKSVHEPLQTGIKAIDAMIP------I---GR---GQR---ELI---------------IGDR------------QTGkt 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 177 ------VISLKDDK------------SKVALV------YGQM----------NEPPGARARVALTGLTVAEYFRDQeGQD 222
Cdd:PRK09281 177 aiaidtIINQKGKDviciyvaigqkaSTVAQVvrkleeHGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMDN-GKD 255

                        250       260
                 ....*....|....*....|....*.
gi 387165999 223 VLLFIDNIFRFTQAGSEVSALLGRIP 248
Cdd:PRK09281 256 ALIVYDDLSKQAVAYRQLSLLLRRPP 281
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 154-298 9.47e-14

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 71.59  E-value: 9.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  154 VFAGVGERTREGNDLYHEMIQsgvisLKDDKS------KVALVYGQMNEPPGARARVALTGLTVAEYFRDQeGQDVLLFI 227
Cdd:PRK14698  686 IYIGCGERGNEMTDVLEEFPK-----LKDPKTgkplmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMA 759

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387165999  228 DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI-------TTTQKGSITSVQAVFVPADDLTDPAPATTF 298
Cdd:PRK14698  760 DSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTL 837
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 2-52 1.61e-10

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


Pssm-ID: 427029 [Multi-domain]  Cd Length: 69  Bit Score: 56.01  E-value: 1.61e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 387165999    2 LPPILNSLEVE-NRKPRLVLEVAQHLGENTVRTIAMDGTEGLIRGQVCNDTG 52
Cdd:pfam02874  18 LPGLLNALEVElVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 104-292 3.86e-10

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 60.57  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 104 EILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRLIMELINNVANAHggCSVFAGVGERtreGNdlyhEMIQsgVIS---- 179
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWADAD--IVIYVGCGER---GN----EMTE--VLEefpe 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 180 LKDDKSKVALvygqM----------NEPPGAR-ARVaLTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIP 248
Cdd:PRK04192 278 LIDPKTGRPL----MertvliantsNMPVAAReASI-YTGITIAEYYRDM-GYDVLLMADSTSRWAEALREISGRLEEMP 351

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 387165999 249 SAVGYQPTLATDMGTMQER---ITT--TQKGSITSVQAVFVPADDLTDP 292
Cdd:PRK04192 352 GEEGYPAYLASRLAEFYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEP 400
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 34-290 4.14e-09

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 57.36  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  34 IAMDGTEGLIRGQVCNDTGSPIKIPVGPKTLGRIINVIGEPIdergPVG-----------EEMKSSIHADAPEFVEMNVK 102
Cdd:PTZ00185  94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGlltrsrallesEQTLGKVDAGAPNIVSRSPV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 103 QEILVTGIKVVDLLAPYAKGGKIGLFGRAGVGRRLIM--ELINNVA------NAHGGCSVFAGVGERTREGNDLYHEMIQ 174
Cdd:PTZ00185 170 NYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvsTIINQVRinqqilSKNAVISIYVSIGQRCSNVARIHRLLRS 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 175 SGVISLKDDKSKVALvygqmnEPPGARARVALTGLTVAEYFRDQeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQ 254
Cdd:PTZ00185 250 YGALRYTTVMAATAA------EPAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYP 322

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 387165999 255 PTLATDMGTMQERITTTQK----GSITSVQAVFVPADDLT 290
Cdd:PTZ00185 323 GDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVT 362
atpA CHL00059
ATP synthase CF1 alpha subunit
 51-248 2.70e-07

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 51.50  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999  51 TGSPIKIPVGPKTLGRIINVIGEPIDERGPVGEEMKSSIHADAPEFVEMNVKQEILVTGIKVVDLLAPYAKGGKIGLFGR 130
Cdd:CHL00059  70 TGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387165999 131 AGVGRRLI-MELINNVANAHGGCsVFAGVGERTREgndlyhemIQSGVISLKDdksKVALVY----GQMNEPPGARARVA 205
Cdd:CHL00059 150 RQTGKTAVaTDTILNQKGQNVIC-VYVAIGQKASS--------VAQVVTTLQE---RGAMEYtivvAETADSPATLQYLA 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 387165999 206 -LTGLTVAEYFRdQEGQDVLLFIDNIFRFTQAGSEVSALLGRIP 248
Cdd:CHL00059 218 pYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
 
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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