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Conserved domains on  [gi|1051344446|gb|AOA50229|]
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ATP synthase beta subunit, partial [Streptomyces yaanensis]

Protein Classification

F0F1 ATP synthase subunit beta( domain architecture ID 1903243)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtpD super family cl43008
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 2-165 8.20e-135

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


The actual alignment was detected with superfamily member COG0055:

Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 384.06  E-value: 8.20e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSD 81
Cdd:COG0055   120 FEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:COG0055   200 SGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 279


                  ....
gi 1051344446 162 MGLL 165
Cdd:COG0055   280 MGAL 283
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 2-165 8.20e-135

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: 384.06  E-value: 8.20e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSD 81
Cdd:COG0055   120 FEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:COG0055   200 SGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 279


                  ....
gi 1051344446 162 MGLL 165
Cdd:COG0055   280 MGAL 283
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 2-165 1.82e-118

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: 335.73  E-value: 1.82e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSD 81
Cdd:cd01133    41 FVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  82 SGVI-----DKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:cd01133   121 SGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQP 200


                  ....*....
gi 1051344446 157 NLADEMGLL 165
Cdd:cd01133   201 TLATEMGSL 209
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 2-165 5.49e-116

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: 335.92  E-value: 5.49e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSD 81
Cdd:TIGR01039 117 FEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKE 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 276


                  ....
gi 1051344446 162 MGLL 165
Cdd:TIGR01039 277 MGEL 280
atpB CHL00060
ATP synthase CF1 beta subunit
 2-165 3.63e-109

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 319.68  E-value: 3.63e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSD 81
Cdd:CHL00060  135 FIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKE 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  82 SGVID-------KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:CHL00060  215 SGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 294

                         170
                  ....*....|.
gi 1051344446 155 QPNLADEMGLL 165
Cdd:CHL00060  295 QPTLSTEMGSL 305
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 15-163 1.69e-66

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: 201.43  E-value: 1.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  15 GVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvaNNHDGVSVFAGVGERTREGNDLIEEMSDSGVIDKTALVFGQ 94
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAG-MIAR--QASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051344446  95 MDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMG 163
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 27-140 6.91e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.82  E-value: 6.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   27 KGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSDSGVIDKTalvfgqmdepPGTRLRVA 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1051344446  107 LAgltMAEYFRdvqkQDVLfFIDNIFRFTQAGSE 140
Cdd:smart00382  71 LA---LARKLK----PDVL-ILDEITSLLDAEQE 96
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 2-165 8.20e-135

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: 384.06  E-value: 8.20e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSD 81
Cdd:COG0055   120 FEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:COG0055   200 SGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 279


                  ....
gi 1051344446 162 MGLL 165
Cdd:COG0055   280 MGAL 283
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 2-165 1.82e-118

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: 335.73  E-value: 1.82e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSD 81
Cdd:cd01133    41 FVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  82 SGVI-----DKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:cd01133   121 SGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQP 200


                  ....*....
gi 1051344446 157 NLADEMGLL 165
Cdd:cd01133   201 TLATEMGSL 209
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 2-165 5.49e-116

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: 335.92  E-value: 5.49e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSD 81
Cdd:TIGR01039 117 FEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKE 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADE 161
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 276


                  ....
gi 1051344446 162 MGLL 165
Cdd:TIGR01039 277 MGEL 280
atpB CHL00060
ATP synthase CF1 beta subunit
 2-165 3.63e-109

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 319.68  E-value: 3.63e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   2 FDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSD 81
Cdd:CHL00060  135 FIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKE 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  82 SGVID-------KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:CHL00060  215 SGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 294

                         170
                  ....*....|.
gi 1051344446 155 QPNLADEMGLL 165
Cdd:CHL00060  295 QPTLSTEMGSL 305
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 7-165 2.54e-84

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: 254.75  E-value: 2.54e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   7 SKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSDSGVID 86
Cdd:TIGR03305 117 SKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLD 196

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051344446  87 KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMGLL 165
Cdd:TIGR03305 197 NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAEL 275
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 1-165 1.65e-71

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: 216.17  E-value: 1.65e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   1 NFDELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMS 80
Cdd:cd19476    40 NPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  81 DSGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLAD 160
Cdd:cd19476   120 KSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFT 198


                  ....*
gi 1051344446 161 EMGLL 165
Cdd:cd19476   199 KLATL 203
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 15-163 1.69e-66

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: 201.43  E-value: 1.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  15 GVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvaNNHDGVSVFAGVGERTREGNDLIEEMSDSGVIDKTALVFGQ 94
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAG-MIAR--QASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051344446  95 MDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEMG 163
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 9-156 6.67e-34

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: 119.97  E-value: 6.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIqEMIyrvANNHDG-VSVFAGVGERTREGNDLIEEMSDSGVIDK 87
Cdd:cd01136    48 EQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLL-GMI---ARNTDAdVNVIALIGERGREVREFIEKDLGEEGLKR 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051344446  88 TALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:cd01136   124 SVLVVATSDESPLLRVRAAYTATAIAEYFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPP 191
fliI PRK06002
flagellar protein export ATPase FliI;
12-156 3.00e-30

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 113.94  E-value: 3.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  12 FETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvANNHDGVsVFAGVGERTREGNDLIEE-MSDSgvIDKTAL 90
Cdd:PRK06002  149 LRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLA-MLAR-ADAFDTV-VIALVGERGREVREFLEDtLADN--LKKAVA 223

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1051344446  91 VFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK06002  224 VVATSDESPMMRRLAPLTATAIAEYFRD-RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPP 288
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 9-156 1.79e-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: 111.28  E-value: 1.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRVANNhDgVSVFAGVGERTREGNDLIEE------MSDS 82
Cdd:COG1157   138 TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLG-MIARNTEA-D-VNVIALIGERGREVREFIEDdlgeegLARS 214

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1051344446  83 GVIDKTAlvfgqmDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:COG1157   215 VVVVATS------DEPPLMRLRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPP 281
PRK08149 PRK08149
FliI/YscN family ATPase;
9-154 1.26e-25

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 100.84  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   9 TEMFETGVKVID-LLTPYVkGGKIGLFGGAGVGKTVLIQEMIyrvanNHDGVSVF--AGVGERTREGNDLIEEMSDSGVI 85
Cdd:PRK08149  132 REPLITGVRAIDgLLTCGV-GQRMGIFASAGCGKTSLMNMLI-----EHSEADVFviGLIGERGREVTEFVESLRASSRR 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051344446  86 DKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PRK08149  206 EKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGY 273
fliI PRK08472
flagellar protein export ATPase FliI;
10-156 4.65e-24

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 96.68  E-value: 4.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIyrVANNHDGVSVFAGVGERTREGNDLIEEMSDsGVIDKTA 89
Cdd:PRK08472  139 EVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMG-MI--VKGCLAPIKVVALIGERGREIPEFIEKNLG-GDLENTV 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1051344446  90 LVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK08472  215 IVVATSDDSPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPP 280
fliI PRK07721
flagellar protein export ATPase FliI;
10-156 1.50e-23

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 95.17  E-value: 1.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvaNNHDGVSVFAGVGERTREGNDLIE-EMSDSGvIDKT 88
Cdd:PRK07721  140 EPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMG-MIAR--NTSADLNVIALIGERGREVREFIErDLGPEG-LKRS 215

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051344446  89 ALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK07721  216 IVVVATSDQPALMRIKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTP 282
fliI PRK08927
flagellar protein export ATPase FliI;
13-156 5.14e-23

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 93.89  E-value: 5.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  13 ETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRVANNHdgVSVFAGVGERTREGNDLIEE-MSDSGvIDKTALV 91
Cdd:PRK08927  143 DLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLS-MLARNADAD--VSVIGLIGERGREVQEFLQDdLGPEG-LARSVVV 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051344446  92 FGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK08927  219 VATSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTP 282
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
9-158 4.35e-22

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 91.41  E-value: 4.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIyrVANNHDGVSVFAGVGERTREGNDLIEEMSDSGVIDKT 88
Cdd:PRK06820  144 EQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLG-ML--CADSAADVMVLALIGERGREVREFLEQVLTPEARART 220

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  89 ALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNL 158
Cdd:PRK06820  221 VVVVATSDRPALERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSV 289
fliI PRK06793
flagellar protein export ATPase FliI;
4-149 1.15e-21

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 90.04  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   4 ELESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRvaNNHDGVSVFAGVGERTREGNDLI-EEMSDS 82
Cdd:PRK06793  132 EREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLG-MIAK--NAKADINVISLVGERGREVKDFIrKELGEE 208

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1051344446  83 GvIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMP 149
Cdd:PRK06793  209 G-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELP 273
fliI PRK08972
flagellar protein export ATPase FliI;
9-156 3.22e-21

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 88.99  E-value: 3.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYR--VANnhdgVSVFAGVGERTREGNDLIEEMSDSGVID 86
Cdd:PRK08972  143 TEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLG-MMTRgtTAD----VIVVGLVGERGREVKEFIEEILGEEGRA 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  87 KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK08972  218 RSVVVAAPADTSPLMRLKGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPP 286
fliI PRK05688
flagellar protein export ATPase FliI;
10-156 1.94e-19

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 84.01  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMI-YRVANnhdgVSVFAGVGERTREGNDLIEEMSDSGVIDKT 88
Cdd:PRK05688  150 EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTrFTEAD----IIVVGLIGERGREVKEFIEHILGEEGLKRS 225

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051344446  89 ALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK05688  226 VVVASPADDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPP 292
PRK05922 PRK05922
type III secretion system ATPase; Validated
 10-154 4.71e-19

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 82.64  E-value: 4.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMiyrVANNHDGVSVFAGVGERTREGNDLIEEMSDSGVIDKTA 89
Cdd:PRK05922  139 EIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTI---AKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTI 215

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051344446  90 LVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PRK05922  216 IIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHY 279
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 9-159 9.37e-19

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: 80.70  E-value: 9.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVlIQEMIYRVANNhDGVsVFAGVGERTREGNDLIEE-------MSD 81
Cdd:cd01134    57 NVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTV-ISQSLSKWSNS-DVV-IYVGCGERGNEMAEVLEEfpelkdpITG 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051344446  82 SGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLA 159
Cdd:cd01134   134 ESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLG 210
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
13-156 1.69e-18

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 81.34  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  13 ETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNhdgVSVFAGVGERTREGNDLIE-EMSDSGvIDKTALV 91
Cdd:PRK06936  147 SLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD---VTVLALIGERGREVREFIEsDLGEEG-LRKAVLV 222

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051344446  92 FGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK06936  223 VATSDRPSMERAKAGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPP 286
fliI PRK07196
flagellar protein export ATPase FliI;
12-157 2.47e-18

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 80.71  E-value: 2.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  12 FETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRVANNHdgVSVFAGVGERTREGNDLIEEMSDSGVIDKTALV 91
Cdd:PRK07196  139 LDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLG-MITRYTQAD--VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVV 215

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1051344446  92 FGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPN 157
Cdd:PRK07196  216 AAPADESPLMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPS 280
fliI PRK07960
flagellum-specific ATP synthase FliI;
9-158 4.91e-17

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 77.13  E-value: 4.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMI-YRVANnhdgVSVFAGVGERTREGNDLIEEMSDSGVIDK 87
Cdd:PRK07960  156 EHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMArYTQAD----VIVVGLIGERGREVKDFIENILGAEGRAR 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1051344446  88 TALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNL 158
Cdd:PRK07960  232 SVVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSV 301
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 14-162 7.34e-17

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 76.35  E-value: 7.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  14 TGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQeMIYRVANNHdgVSVFAGVGERTREGNDLIEEMSDSGVIDKTALVFG 93
Cdd:PRK09099  149 TGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMG-MFARGTQCD--VNVIALIGERGREVREFIELILGEDGMARSVVVCA 225

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051344446  94 QMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQPNLADEM 162
Cdd:PRK09099  226 TSDRSSIERAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAEL 293
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
14-156 1.33e-15

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 73.06  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  14 TGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMiyrvANNHDG-VSVFAGVGERTREGNDLIEEMSDSGVIDKTALVF 92
Cdd:PRK07594  141 TGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAML----CNAPDAdSNVLVLIGERGREVREFIDFTLSEETRKRCVIVV 216

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1051344446  93 GQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGYQP 156
Cdd:PRK07594  217 ATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPP 279
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 10-154 9.71e-15

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: 69.56  E-value: 9.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGV-GKTVLIQemIYR----VANNHDGVSVFAGVGERTREGNDLIEEMSDSGV 84
Cdd:cd01135    51 EMIQTGISAIDVMNTLVRGQKLPIFSGSGLpHNELAAQ--IARqagvVGSEENFAIVFAAMGVTMEEARFFKDDFEETGA 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  85 IDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:cd01135   129 LERVVLFLNLANDPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGY 198
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 9-149 1.04e-12

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 64.55  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLiqeMIYRVANNHDG--VSVFAGVGERTREGNDLIEEMSDSGVID 86
Cdd:PRK13343  143 TEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAI---AIDAIINQKDSdvICVYVAIGQKASAVARVIETLREHGALE 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1051344446  87 KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMP 149
Cdd:PRK13343  220 YTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPP 281
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 9-159 1.38e-11

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 61.34  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   9 TEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEmiyrVANNHDG-VSVFAGVGERTREGNDLIEE---MSD--S 82
Cdd:PRK04192  208 VEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQ----LAKWADAdIVIYVGCGERGNEMTEVLEEfpeLIDpkT 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  83 G--VIDKTALVFGQMDEPpgtrlrVAlA-------GLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVG 153
Cdd:PRK04192  284 GrpLMERTVLIANTSNMP------VA-AreasiytGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPGEEG 355


                  ....*.
gi 1051344446 154 YQPNLA 159
Cdd:PRK04192  356 YPAYLA 361
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 10-154 4.14e-10

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 56.97  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVGktvlIQEMIYRVANNHDG-VSVFAGVGERTREGNDLIEEMSDSGVIDKT 88
Cdd:PRK02118  122 EMIRTGIPMIDVFNTLVESQKIPIFSVSGEP----YNALLARIALQAEAdIIILGGMGLTFDDYLFFKDTFENAGALDRT 197

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1051344446  89 ALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PRK02118  198 VMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGY 263
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 6-149 6.15e-10

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: 56.03  E-value: 6.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   6 ESKTEMFETGVKVIDLLTPYVKGGKIGLFGGAGVGKT-VLIQEMIYRVANNHdgVSVFAGVGERTREGNDLIEEMSDSGV 84
Cdd:cd01132    47 QSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaIAIDTIINQKGKKV--YCIYVAIGQKRSTVAQIVKTLEEHGA 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051344446  85 IDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMP 149
Cdd:cd01132   125 MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 59-163 9.33e-10

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 56.18  E-value: 9.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   59 VSVFAGVGERTREGNDLIEEM-------SDSGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVqKQDVLFFIDNI 131
Cdd:PRK14698   684 VVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMADST 762

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1051344446  132 FRFTQAGSEVSTLLGRMPSAVGYQPNLADEMG 163
Cdd:PRK14698   763 SRWAEALREISGRLEEMPGEEGYPAYLASKLA 794
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 10-154 1.91e-08

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 52.14  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAGVgKTVLIQEMIYRVANNHDGVS----VFAGVGERTREGNDLIEEMSDSGVI 85
Cdd:PRK04196  125 EFIQTGISAIDGLNTLVRGQKLPIFSGSGL-PHNELAAQIARQAKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGAL 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1051344446  86 DKTALVFGQMDEPPGTRL---RVAlagLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PRK04196  204 ERSVVFLNLADDPAIERIltpRMA---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGY 272
PRK12608 PRK12608
transcription termination factor Rho; Provisional
 16-137 1.24e-06

transcription termination factor Rho; Provisional


Pssm-ID: 237150 [Multi-domain]  Cd Length: 380  Bit Score: 47.00  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  16 VKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAG-VGERTREGNDLIEEMSdsgvidktALVFGQ 94
Cdd:PRK12608  121 MRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYAS 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1051344446  95 -MDEPPgtRLRVALAGLTMAEYFRDV-QKQDVLFFIDNIFRFTQA 137
Cdd:PRK12608  193 tFDRPP--DEHIRVAELVLERAKRLVeQGKDVVILLDSLTRLARA 235
rho TIGR00767
transcription termination factor Rho; This RNA helicase, the transcription termination factor ...
 5-150 2.14e-06

transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]


Pssm-ID: 162030 [Multi-domain]  Cd Length: 415  Bit Score: 46.22  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   5 LESKTEMFETgvKVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNH-DGVSVFAGVGERTREGNDLIEEMsDSG 83
Cdd:TIGR00767 147 LETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHpEVELIVLLIDERPEEVTDMQRSV-KGE 223

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051344446  84 VIDKTalvfgqMDEPPGTRLRVALAGLTMAEyfRDV-QKQDVLFFIDNIFRFTQAGSEVSTLLGRMPS 150
Cdd:TIGR00767 224 VVAST------FDEPASRHVQVAEMVIEKAK--RLVeHKKDVVILLDSITRLARAYNTVTPASGKVLS 283
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 10-154 6.01e-06

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: 45.10  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  10 EMFETGVKVIDLLTPYVKGGKIGLFGGAG----------VGKTVLIQEMIYRVANNHDG--VSVFAGVGERTREGNDLIE 77
Cdd:TIGR01040 123 EMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaaqiCRQAGLVKLPTKDVHDGHEDnfAIVFAAMGVNMETARFFKQ 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1051344446  78 EMSDSGVIDKTALVFGQMDEPPGTRLRVALAGLTMAEYFRDVQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:TIGR01040 203 DFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGF 279
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 14-154 8.90e-06

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 44.65  E-value: 8.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  14 TGVKVIDLLTPYVKGGKIGLFGGAGVGKT-VLIQEMIYRVANNHD------GVSVFAGVGERTREGNDLIEEMSDSGVID 86
Cdd:PTZ00185  175 TGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINQVRINQQilsknaVISIYVSIGQRCSNVARIHRLLRSYGALR 254

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051344446  87 KTALVFGQMDEPPGTRLRVALAGLTMAEYFRDvQKQDVLFFIDNIFRFTQAGSEVSTLLGRMPSAVGY 154
Cdd:PTZ00185  255 YTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAY 321
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 17-150 1.64e-05

C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.


Pssm-ID: 410872 [Multi-domain]  Cd Length: 249  Bit Score: 43.35  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446  17 KVIDLLTPYVKGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAG-VGERTREGNDLIEEMsDSGVIDKTalvfgqM 95
Cdd:cd01128     5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTDMRRSV-KGEVVAST------F 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1051344446  96 DEPPGTRLRVALAGLTMAEyfRDV-QKQDVLFFIDNIFRFTQAGSEVSTLLGRMPS 150
Cdd:cd01128    78 DEPPERHVQVAEMVIEKAK--RLVeHGKDVVILLDSITRLARAYNTVVPSSGKTLS 131
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 27-140 6.91e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 40.82  E-value: 6.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051344446   27 KGGKIGLFGGAGVGKTVLIQEMIYRVANNHDGVSVFAGVGERTREGNDLIEEMSDSGVIDKTalvfgqmdepPGTRLRVA 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1051344446  107 LAgltMAEYFRdvqkQDVLfFIDNIFRFTQAGSE 140
Cdd:smart00382  71 LA---LARKLK----PDVL-ILDEITSLLDAEQE 96
 
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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