NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1860557302|gb|QKX44897|]
View 

ATP synthase beta subunit, partial (chloroplast) [Acmella repens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
atpB super family cl33325
ATP synthase CF1 beta subunit
 1-231 0e+00

ATP synthase CF1 beta subunit


The actual alignment was detected with superfamily member CHL00060:

Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 565.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:CHL00060  264 VLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 160
Cdd:CHL00060  344 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 423

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860557302 161 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEMESNLKK 231
Cdd:CHL00060  424 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVESKLKK 494
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 1-231 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 565.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:CHL00060  264 VLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 160
Cdd:CHL00060  344 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 423

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860557302 161 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEMESNLKK 231
Cdd:CHL00060  424 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVESKLKK 494
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-227 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: 515.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:COG0055   242 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLD 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 160
Cdd:COG0055   322 ATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKI 401

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860557302 161 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEMES 227
Cdd:COG0055   402 QRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-223 9.18e-162

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: 455.33  E-value: 9.18e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:TIGR01039 239 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLD 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 160
Cdd:TIGR01039 319 ATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRI 398

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860557302 161 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNL 223
Cdd:TIGR01039 399 QRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-110 1.91e-90

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: 267.55  E-value: 1.91e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:cd01133   168 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLD 247

                          90       100       110
                  ....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 110
Cdd:cd01133   248 ATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 1-105 8.37e-49

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: 159.06  E-value: 8.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE--GSITSIQAVYVPADDLTDPAPATTFAH 78
Cdd:pfam00006 106 VLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGkgGSITALPTVLVPGDDITDPIPDNTRSI 185

                          90       100
                  ....*....|....*....|....*..
gi 1860557302  79 LDATTVLSRGLAAKGIYPAVDPLDSTS 105
Cdd:pfam00006 186 LDGQIVLSRDLAEKGHYPAIDVLASVS 212
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 1-231 0e+00

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 565.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:CHL00060  264 VLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 160
Cdd:CHL00060  344 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 423

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1860557302 161 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEMESNLKK 231
Cdd:CHL00060  424 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVESKLKK 494
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-227 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: 515.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:COG0055   242 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLD 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 160
Cdd:COG0055   322 ATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKI 401

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1860557302 161 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLEMES 227
Cdd:COG0055   402 QRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-223 9.18e-162

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: 455.33  E-value: 9.18e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:TIGR01039 239 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLD 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 160
Cdd:TIGR01039 319 ATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRI 398

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1860557302 161 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNL 223
Cdd:TIGR01039 399 QRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 1-216 1.12e-111

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: 327.55  E-value: 1.12e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI 160
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1860557302 161 ERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEA 216
Cdd:TIGR03305 394 ERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-110 1.91e-90

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: 267.55  E-value: 1.91e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:cd01133   168 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLD 247

                          90       100       110
                  ....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 110
Cdd:cd01133   248 ATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
ATP-synt_F1_beta_C cd18110
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ...
 112-219 1.40e-78

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: 231.21  E-value: 1.40e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302 112 IVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGF 191
Cdd:cd18110     1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80

                          90       100
                  ....*....|....*....|....*...
gi 1860557302 192 QLILSGELDGLPEQAFYLVGNIDEATAK 219
Cdd:cd18110    81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 1-107 7.17e-54

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: 174.18  E-value: 7.17e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK--EGSITSIQAVYVPADDLTDPAPATTFAH 78
Cdd:cd19476   162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNTFAI 241

                          90       100
                  ....*....|....*....|....*....
gi 1860557302  79 LDATTVLSRGLAAKGIYPAVDPLDSTSTM 107
Cdd:cd19476   242 LDGQIVLSRELARKGIYPAINVLDSTSRV 270
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 1-105 8.37e-49

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: 159.06  E-value: 8.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE--GSITSIQAVYVPADDLTDPAPATTFAH 78
Cdd:pfam00006 106 VLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGkgGSITALPTVLVPGDDITDPIPDNTRSI 185

                          90       100
                  ....*....|....*....|....*..
gi 1860557302  79 LDATTVLSRGLAAKGIYPAVDPLDSTS 105
Cdd:pfam00006 186 LDGQIVLSRDLAEKGHYPAIDVLASVS 212
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 1-195 9.82e-29

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: 111.66  E-value: 9.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:COG1157   249 VLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILD 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPRIVGDEHYETAQQVKQTLQRYKELQDIIAIlG---------LDElseed 150
Cdd:COG1157   329 GHIVLSRKLAERGHYPAIDVLASISrVM--PDIVSPEHRALARRLRRLLARYEENEDLIRI-GayqpgsdpeLDE----- 400

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1860557302 151 rlTVARARKIERFLSQpffvaevftgSPGKYVGLAETIRGFQLIL 195
Cdd:COG1157   401 --AIALIPAIEAFLRQ----------GMDERVSFEESLAQLAELL 433
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
1-166 4.80e-25

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 101.81  E-value: 4.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:PRK06820  255 VLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLD 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGDEHYETAQQVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVAR 156
Cdd:PRK06820  335 GHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQR 410

                         170
                  ....*....|
gi 1860557302 157 ARKIERFLSQ 166
Cdd:PRK06820  411 YPAICAFLQQ 420
fliI PRK05688
flagellar protein export ATPase FliI;
1-166 1.99e-24

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 100.19  E-value: 1.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEG--SITSIQAVYVPADDLTDPAPATTFAH 78
Cdd:PRK05688  260 VLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGV 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  79 LDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGDEHYETAQQVKQTLQRYKELQDIIAI----LGLDelsEEDRLTV 154
Cdd:PRK05688  340 LDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAI 415

                         170
                  ....*....|..
gi 1860557302 155 ARARKIERFLSQ 166
Cdd:PRK05688  416 ARFPHLVQFLRQ 427
fliI PRK08972
flagellar protein export ATPase FliI;
1-140 4.91e-24

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 99.00  E-value: 4.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT--STKEGSITSIQAVYVPADDLTDPAPATTFAH 78
Cdd:PRK08972  254 VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSITAFYTVLTEGDDLQDPIADASRAI 333

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1860557302  79 LDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGDEHYETAQQVKQTLQRYKELQDIIAI 140
Cdd:PRK08972  334 LDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
1-166 1.38e-23

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 97.90  E-value: 1.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:PRK06936  254 VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILD 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGDEHYETAQQVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVAR 156
Cdd:PRK06936  334 GHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ---AIER 409

                         170
                  ....*....|
gi 1860557302 157 ARKIERFLSQ 166
Cdd:PRK06936  410 IGAIRGFLRQ 419
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 1-105 5.42e-22

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: 91.08  E-value: 5.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:cd01136   159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSILD 238

                          90       100
                  ....*....|....*....|....*
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTS 105
Cdd:cd01136   239 GHIVLSRRLAERGHYPAIDVLASIS 263
fliI PRK07721
flagellar protein export ATPase FliI;
1-140 2.25e-21

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 91.32  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:PRK07721  250 VMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILD 329

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGDEHYETAQQVKQTLQRYKELQDIIAI 140
Cdd:PRK07721  330 GHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 1-167 2.97e-21

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 91.37  E-value: 2.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:PRK09099  255 VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILD 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGDEHYETAQQVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVAR 156
Cdd:PRK09099  335 GHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AIAK 410

                         170
                  ....*....|.
gi 1860557302 157 ARKIERFLSQP 167
Cdd:PRK09099  411 IDAIRDFLSQR 421
fliI PRK06002
flagellar protein export ATPase FliI;
1-142 3.96e-21

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 90.83  E-value: 3.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE--GSITSIQAVYVPADDLTDPAPATTFAH 78
Cdd:PRK06002  256 VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVADSIRGT 335

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860557302  79 LDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGDEHyETAQQVKQTLQRYKELQDIIAILG 142
Cdd:PRK06002  336 LDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQR-KLVSRLKSMIARFEETRDLRLIGG 398
fliI PRK06793
flagellar protein export ATPase FliI;
1-166 6.09e-21

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 90.42  E-value: 6.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAvGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:PRK06793  248 VLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILD 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGDEHYETAQQVKQTLQRYKElQDIIAILGLDELSEEDRLTVARARKI 160
Cdd:PRK06793  327 GHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKV 404


                  ....*....
gi 1860557302 161 E---RFLSQ 166
Cdd:PRK06793  405 EginTFLKQ 413
fliI PRK07196
flagellar protein export ATPase FliI;
1-185 7.65e-21

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 89.95  E-value: 7.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-TSTKEGSITSIQAVYVPADDLTDPAPATTFAHL 79
Cdd:PRK07196  247 VLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVL 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  80 DATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGDEHYETAQQVKQTLQRYKELQDIIA----ILGLDELSEEdrlTVA 155
Cdd:PRK07196  327 DGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIPlggyVAGADPMADQ---AVH 402

                         170       180       190
                  ....*....|....*....|....*....|
gi 1860557302 156 RARKIERFLSQPFFVAEVFTGSPGKYVGLA 185
Cdd:PRK07196  403 YYPAITQFLRQEVGHPALFSASVEQLTGMF 432
fliI PRK08472
flagellar protein export ATPase FliI;
1-166 4.02e-20

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 87.82  E-value: 4.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-EGSITSIQAVYVPADDLTDPAPATTFAHL 79
Cdd:PRK08472  248 VLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVEGDDMSDPIADQSRSIL 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  80 DATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGDEHYETAQQVKQTLQRYKELQDIIAI----LGLD-ELSEedrlTV 154
Cdd:PRK08472  328 DGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGNDkELDE----AI 402

                         170
                  ....*....|..
gi 1860557302 155 ARARKIERFLSQ 166
Cdd:PRK08472  403 SKKEFMEQFLKQ 414
PRK08149 PRK08149
FliI/YscN family ATPase;
1-168 1.31e-19

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 86.59  E-value: 1.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:PRK08149  243 VVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILD 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGDEHYETAQQVKQTLQRYKELQDIIAiLG---LDELSEEDRlTVARA 157
Cdd:PRK08149  323 GHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKR 399

                         170
                  ....*....|.
gi 1860557302 158 RKIERFLSQPF 168
Cdd:PRK08149  400 PALEAFLKQDV 410
ATP-synt_F1_V1_A1_AB_FliI_C cd01429
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
 117-180 1.02e-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: 77.10  E-value: 1.02e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860557302 117 HYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGK 180
Cdd:cd01429     1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
fliI PRK07960
flagellum-specific ATP synthase FliI;
1-169 3.54e-18

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 82.52  E-value: 3.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS--TKEGSITSIQAVYVPADDLTDPAPATTFAH 78
Cdd:PRK07960  267 VLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAI 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  79 LDATTVLSRGLAAKGIYPAVDPLDSTSTMLQpRIVGDEHYETAQQVKQTLQRYKELQDIIAI----LGLDELSEEdrlTV 154
Cdd:PRK07960  347 LDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSDPMLDK---AI 422

                         170
                  ....*....|....*
gi 1860557302 155 ARARKIERFLSQPFF 169
Cdd:PRK07960  423 ALWPQLEAFLQQGIF 437
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 17-168 4.29e-18

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 82.18  E-value: 4.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  17 EVSALLGRMPSAVGYQPTLSTEMGSLQER--ITSTKEGSITSIQAVYVPADDLTDPAPattfahlDAT-------TVLSR 87
Cdd:PRK04196  258 EISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSR 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  88 GLAAKGIYPAVDPLDSTSTMLQPRIvG-----DEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIE- 161
Cdd:PRK04196  331 ELHRKGIYPPIDVLPSLSRLMKDGI-GegktrEDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFEr 409


                  ....*..
gi 1860557302 162 RFLSQPF 168
Cdd:PRK04196  410 EFVNQGF 416
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
1-140 4.58e-18

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 81.92  E-value: 4.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLD 80
Cdd:PRK07594  247 VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLD 326

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  81 ATTVLSRGLAAKGIYPAVDPLDSTSTMLqPRIVGDEHYETAQQVKQTLQRYKELQDIIAI 140
Cdd:PRK07594  327 GHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLIRI 385
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 1-166 5.84e-16

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 76.36  E-value: 5.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER----IT-STKEGSITSIQAVYVPADDLTDPapaTT 75
Cdd:PRK04192  326 VLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSEP---VT 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  76 FAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQP---RIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDEL 146
Cdd:PRK04192  403 QNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPwweENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDAL 482

                         170       180
                  ....*....|....*....|.
gi 1860557302 147 SEEDRLTVARARKI-ERFLSQ 166
Cdd:PRK04192  483 PEEDRLILEVARLIrEDFLQQ 503
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 1-178 1.22e-12

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 66.58  E-value: 1.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302    1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPA 73
Cdd:PRK14698   755 VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQ 834

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   74 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP------RIVGDEHYETAQQVKQTLQRYKELQDIIAILGLDELS 147
Cdd:PRK14698   835 NTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALP 914

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1860557302  148 EEDRLTVARARKI-ERFLSQPFFvAEVFTGSP 178
Cdd:PRK14698   915 ERERAILLVARMLrEDYLQQDAF-DEVDTYCP 945
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 1-109 3.41e-11

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: 61.47  E-value: 3.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER--ITSTKEGSITSIQAVYVPADDLTDPAPATTFAH 78
Cdd:cd01135   168 VLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDDITHPIPDLTGYI 247

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1860557302  79 LDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 109
Cdd:cd01135   248 TEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 1-166 7.35e-11

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: 61.28  E-value: 7.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI--TSTKEGSITSIQAVYVPADDLTDPAPATTFAH 78
Cdd:TIGR01040 249 VLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYI 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  79 LDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRI----VGDEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTV 154
Cdd:TIGR01040 329 TEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYL 408

                         170
                  ....*....|...
gi 1860557302 155 ARARKIER-FLSQ 166
Cdd:TIGR01040 409 EFLDKFEKnFIAQ 421
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 1-105 2.56e-10

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: 58.74  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPA 73
Cdd:cd01134   175 VSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQ 254

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1860557302  74 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 105
Cdd:cd01134   255 ATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
PRK05922 PRK05922
type III secretion system ATPase; Validated
 1-198 7.32e-07

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 49.13  E-value: 7.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302   1 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAV-YVP--ADDLTDPAPATTFA 77
Cdd:PRK05922  249 VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDG 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1860557302  78 HLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQpRIVGDEHYETAQQVKQTLQRYKELQDIIAiLGLDELSEEDRL--TVA 155
Cdd:PRK05922  329 HFFLTPQ-GKALAS----PPIDILTSLSRSAR-QLALPHHYAAAEELRSLLKAYHEALDIIQ-LGAYVPGQDAHLdrAVK 401

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1860557302 156 RARKIERFLSQPFfvaevftgspGKYVGLAETIRGFQLILSGE 198
Cdd:PRK05922  402 LLPSIKQFLSQPL----------SSYCALHNTLKQLEALLKHE 434
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 ...
 122-166 2.60e-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: 39.29  E-value: 2.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1860557302 122 QQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 166
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 ...
 132-166 3.40e-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: 38.57  E-value: 3.40e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1860557302 132 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 166
Cdd:cd18112    22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
T3SS_ATPase_C pfam18269
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ...
 113-167 5.02e-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: 37.41  E-value: 5.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1860557302 113 VGDEHYETAQQVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 167
Cdd:pfam18269   1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH