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Conserved domains on  [gi|21360628|gb|AAM49628|]
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ATP synthase alpha subunit, partial [Enterococcus faecium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtpA super family cl43009
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 1-184 4.22e-143

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


The actual alignment was detected with superfamily member COG0056:

Pssm-ID: 439826 [Multi-domain]  Cd Length: 504  Bit Score: 407.12  E-value: 4.22e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:COG0056  74 VLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAI 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:COG0056 154 DAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAP 233

                       170       180
                ....*....|....*....|....
gi 21360628 161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:COG0056 234 LQYIAPYAGCAMGEYFMDQGKDVL 257
 
Name Accession Description Interval E-value
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 1-184 4.22e-143

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


Pssm-ID: 439826 [Multi-domain]  Cd Length: 504  Bit Score: 407.12  E-value: 4.22e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:COG0056  74 VLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAI 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:COG0056 154 DAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAP 233

                       170       180
                ....*....|....*....|....
gi 21360628 161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:COG0056 234 LQYIAPYAGCAMGEYFMDQGKDVL 257
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 1-184 5.76e-143

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 406.76  E-value: 5.76e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:PRK09281  74 VILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAI 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:PRK09281 154 DAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAP 233

                        170       180
                 ....*....|....*....|....
gi 21360628  161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:PRK09281 234 LQYLAPYAGCAMGEYFMDNGKDAL 257
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
 1-184 2.50e-115

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


Pssm-ID: 273365 [Multi-domain]  Cd Length: 501  Bit Score: 336.67  E-value: 2.50e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628     1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:TIGR00962  73 VIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAI 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:TIGR00962 153 DAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSAS 232

                         170       180
                  ....*....|....*....|....
gi 21360628   161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:TIGR00962 233 LQYLAPYTGCTMGEYFRDNGKHAL 256
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 21-184 2.23e-108

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: 310.64  E-value: 2.23e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  21 IMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKT 100
Cdd:cd01132   1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628 101 GKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNG 180
Cdd:cd01132  81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160


                ....
gi 21360628 181 KHVL 184
Cdd:cd01132 161 KHAL 164
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 76-184 5.59e-46

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: 150.20  E-value: 5.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    76 GLKAIDALVPIGRGQRELVIGDRKTGKTSIAiDTIINQKGQDmICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGA 155
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78

                          90       100
                  ....*....|....*....|....*....
gi 21360628   156 SQPAPLLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:pfam00006  79 DEPPLARYRAPYTALTIAEYFRDQGKDVL 107
 
Name Accession Description Interval E-value
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 1-184 4.22e-143

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


Pssm-ID: 439826 [Multi-domain]  Cd Length: 504  Bit Score: 407.12  E-value: 4.22e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:COG0056  74 VLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAI 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:COG0056 154 DAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAP 233

                       170       180
                ....*....|....*....|....
gi 21360628 161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:COG0056 234 LQYIAPYAGCAMGEYFMDQGKDVL 257
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 1-184 5.76e-143

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 406.76  E-value: 5.76e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:PRK09281  74 VILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAI 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:PRK09281 154 DAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAP 233

                        170       180
                 ....*....|....*....|....
gi 21360628  161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:PRK09281 234 LQYLAPYAGCAMGEYFMDNGKDAL 257
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
 1-184 2.50e-115

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


Pssm-ID: 273365 [Multi-domain]  Cd Length: 501  Bit Score: 336.67  E-value: 2.50e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628     1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:TIGR00962  73 VIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAI 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:TIGR00962 153 DAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSAS 232

                         170       180
                  ....*....|....*....|....
gi 21360628   161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:TIGR00962 233 LQYLAPYTGCTMGEYFRDNGKHAL 256
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 1-184 5.29e-110

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 323.02  E-value: 5.29e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:PRK13343  74 VLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVV 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:PRK13343 154 DALIPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPG 233

                        170       180
                 ....*....|....*....|....
gi 21360628  161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:PRK13343 234 LQYLAPFAGCAIAEYFRDQGQDAL 257
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 21-184 2.23e-108

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: 310.64  E-value: 2.23e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  21 IMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKT 100
Cdd:cd01132   1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628 101 GKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNG 180
Cdd:cd01132  81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160


                ....
gi 21360628 181 KHVL 184
Cdd:cd01132 161 KHAL 164
atpA CHL00059
ATP synthase CF1 alpha subunit
 1-184 7.81e-102

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 301.50  E-value: 7.81e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:CHL00059  53 VLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAI 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:CHL00059 133 DSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPAT 212

                        170       180
                 ....*....|....*....|....
gi 21360628  161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:CHL00059 213 LQYLAPYTGAALAEYFMYRGRHTL 236
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 24-184 1.31e-52

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: 168.79  E-value: 1.31e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  24 VPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKT 103
Cdd:cd19476   2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628 104 SIAIDTIINQKGQD-MICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKH 182
Cdd:cd19476  82 VLAMQLARNQAKAHaGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161


                ..
gi 21360628 183 VL 184
Cdd:cd19476 162 VL 163
PRK07165 PRK07165
ATP F0F1 synthase subunit alpha;
60-179 2.85e-46

ATP F0F1 synthase subunit alpha;


Pssm-ID: 235951 [Multi-domain]  Cd Length: 507  Bit Score: 158.21  E-value: 2.85e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   60 APGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETL 139
Cdd:PRK07165 114 AHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETL 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 21360628  140 KKYGAMDYTIVVNAGASQPAPlLYIAPYAGTAMGEEFMYN 179
Cdd:PRK07165 194 KEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENISYN 232
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 76-184 5.59e-46

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: 150.20  E-value: 5.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    76 GLKAIDALVPIGRGQRELVIGDRKTGKTSIAiDTIINQKGQDmICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGA 155
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78

                          90       100
                  ....*....|....*....|....*....
gi 21360628   156 SQPAPLLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:pfam00006  79 DEPPLARYRAPYTALTIAEYFRDQGKDVL 107
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 1-184 8.30e-46

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 158.28  E-value: 8.30e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDgLGEIVTDKAR--------PVEAMAPGVMQRKSVNEP 72
Cdd:PTZ00185  94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRALleseqtlgKVDAGAPNIVSRSPVNYN 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   73 MQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQ--------KGQDMICIYVAIGQKDSTVRTQVETLKKYGA 144
Cdd:PTZ00185 173 LLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSNVARIHRLLRSYGA 252

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 21360628  145 MDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:PTZ00185 253 LRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCL 292
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 3-91 2.78e-33

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: 122.45  E-value: 2.78e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   3 LGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDA 82
Cdd:COG1157  71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150


                ....*....
gi 21360628  83 LVPIGRGQR 91
Cdd:COG1157 151 LLTVGRGQR 159
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 23-184 3.44e-30

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: 111.11  E-value: 3.44e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  23 EVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGK 102
Cdd:cd01136   1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628 103 TSIaIDTIINQKGQDMICIyVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKH 182
Cdd:cd01136  81 STL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158


                ..
gi 21360628 183 VL 184
Cdd:cd01136 159 VL 160
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 4-184 3.89e-25

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 100.61  E-value: 3.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    4 GDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDAL 83
Cdd:PRK09099  78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   84 VPIGRGQRELVIGDRKTGKTsiaidTIINQKGQDMIC---IYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCdvnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSI 232

                        170       180
                 ....*....|....*....|....
gi 21360628  161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:PRK09099 233 ERAKAAYVATAIAEYFRDRGLRVL 256
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
3-184 1.39e-23

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 95.97  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    3 LGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGlGEIVTDKAR-PVEAMAPGVMQRKSVNEPMQTGLKAID 81
Cdd:PRK06936  76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDG-GHPPEPAAWyPVYADAPAPMSRRLIETPLSLGVRVID 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   82 ALVPIGRGQRELVIGDRKTGKTSIaIDTIINQKGQDmICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPL 161
Cdd:PRK06936 155 GLLTCGEGQRMGIFAAAGGGKSTL-LASLIRSAEVD-VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSME 232

                        170       180
                 ....*....|....*....|...
gi 21360628  162 LYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:PRK06936 233 RAKAGFVATSIAEYFRDQGKRVL 255
fliI PRK07721
flagellar protein export ATPase FliI;
1-184 4.68e-23

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 94.79  E-value: 4.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    1 IILGDFESIRE---GDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGL 77
Cdd:PRK07721  67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   78 KAIDALVPIGRGQRELVIGDRKTGKTSIaIDTIINQKGQDMICIYVaIGQKDSTVRTQVET------LKKygamdyTIVV 151
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADLNVIAL-IGERGREVREFIERdlgpegLKR------SIVV 218

                        170       180       190
                 ....*....|....*....|....*....|...
gi 21360628  152 NAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:PRK07721 219 VATSDQPALMRIKGAYTATAIAEYFRDQGLNVM 251
PRK08149 PRK08149
FliI/YscN family ATPase;
15-184 8.32e-23

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 93.91  E-value: 8.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   15 VKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTD----KARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQ 90
Cdd:PRK08149  73 LKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVgpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQ 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   91 RELVIGDRKTGKTSIaIDTIINQKGQDmicIYVA--IGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYA 168
Cdd:PRK08149 153 RMGIFASAGCGKTSL-MNMLIEHSEAD---VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALV 228

                        170
                 ....*....|....*.
gi 21360628  169 GTAMGEEFMYNGKHVL 184
Cdd:PRK08149 229 ATTVAEYFRDQGKRVV 244
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-89 2.41e-20

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: 87.07  E-value: 2.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:COG0055  58 IAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVI 137


                ....*....
gi 21360628  81 DALVPIGRG 89
Cdd:COG0055 138 DLLAPYAKG 146
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
9-184 8.46e-20

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 85.64  E-value: 8.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    9 IREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGlGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGR 88
Cdd:PRK06820  84 LRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   89 GQRELVIGDRKTGKTSIaIDTIINQKGQDMIcIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYA 168
Cdd:PRK06820 163 GQRIGIFAAAGVGKSTL-LGMLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLST 240

                        170
                 ....*....|....*.
gi 21360628  169 GTAMGEEFMYNGKHVL 184
Cdd:PRK06820 241 ATTIAEYFRDRGKKVL 256
PRK05922 PRK05922
type III secretion system ATPase; Validated
 24-184 9.74e-20

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 85.34  E-value: 9.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   24 VPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKT 103
Cdd:PRK05922  92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  104 SIAidTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHV 183
Cdd:PRK05922 172 SLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRV 249


                 .
gi 21360628  184 L 184
Cdd:PRK05922 250 L 250
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
12-184 2.99e-19

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 83.85  E-value: 2.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   12 GDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLgEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQR 91
Cdd:PRK07594  79 GQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQR 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   92 ELVIGDRKTGKTSIaIDTIINQKGQDmICIYVAIGQKDSTVRTQVE-TLKKYGAMDYTIVVnAGASQPAPLLYIAPYAGT 170
Cdd:PRK07594 158 VGIFSAPGVGKSTL-LAMLCNAPDAD-SNVLVLIGERGREVREFIDfTLSEETRKRCVIVV-ATSDRPALERVRALFVAT 234

                        170
                 ....*....|....
gi 21360628  171 AMGEEFMYNGKHVL 184
Cdd:PRK07594 235 TIAEFFRDNGKRVV 248
fliI PRK08472
flagellar protein export ATPase FliI;
7-91 5.04e-19

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 83.20  E-value: 5.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    7 ESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPI 86
Cdd:PRK08472  75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154


                 ....*
gi 21360628   87 GRGQR 91
Cdd:PRK08472 155 GKGQK 159
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-112 4.50e-17

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: 77.84  E-value: 4.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628     1 IILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAI 80
Cdd:TIGR01039  55 IAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVI 134

                          90       100       110
                  ....*....|....*....|....*....|..
gi 21360628    81 DALVPIGRGQRELVIGDRKTGKTSIAIDTIIN 112
Cdd:TIGR01039 135 DLLAPYAKGGKIGLFGGAGVGKTVLIQELINN 166
fliI PRK08972
flagellar protein export ATPase FliI;
12-91 1.28e-16

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 76.66  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   12 GDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQR 91
Cdd:PRK08972  85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 21-184 1.95e-16

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: 74.95  E-value: 1.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  21 IMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQR--------- 91
Cdd:cd01135   1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKlpifsgsgl 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  92 ---ELVIgdrktgktSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYA 168
Cdd:cd01135  81 phnELAA--------QIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152

                       170
                ....*....|....*..
gi 21360628 169 GTAMGEEFMY-NGKHVL 184
Cdd:cd01135 153 ALTTAEYLAYeKGKHVL 169
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 23-112 3.27e-16

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: 74.18  E-value: 3.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  23 EVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGK 102
Cdd:cd01133   1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80

                        90
                ....*....|
gi 21360628 103 TSIAIDTIIN 112
Cdd:cd01133  81 TVLIMELINN 90
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 11-91 5.32e-16

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 74.86  E-value: 5.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   11 EGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPV--EAMAPgvMQRKSVNEPMQTGLKAIDALVPIGR 88
Cdd:PRK04196  65 KDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDIngAPINP--VAREYPEEFIQTGISAIDGLNTLVR 142


                 ...
gi 21360628   89 GQR 91
Cdd:PRK04196 143 GQK 145
fliI PRK06002
flagellar protein export ATPase FliI;
12-184 1.01e-15

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 73.88  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   12 GDKVKRTGKiMEVPVGEALIGRVVNPLGQPIDGLGEIVT-DKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQ 90
Cdd:PRK06002  88 GDAVFRKGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQ 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   91 RELVIGDRKTGKTSI--------AIDTIInqkgqdmiciyVA-IGQKDSTVRTQVE-TLKkyGAMDYTIVVNAGASQPAP 160
Cdd:PRK06002 167 RIGIFAGSGVGKSTLlamlaradAFDTVV-----------IAlVGERGREVREFLEdTLA--DNLKKAVAVVATSDESPM 233

                        170       180
                 ....*....|....*....|....
gi 21360628  161 LLYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:PRK06002 234 MRRLAPLTATAIAEYFRDRGENVL 257
fliI PRK08927
flagellar protein export ATPase FliI;
4-184 4.12e-15

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 72.32  E-value: 4.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    4 GDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVT-DKARPVEAMAPGVMQRKSVNEPMQTGLKAIDA 82
Cdd:PRK08927  72 GPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   83 LVPIGRGQRELVIGDRKTGKtSIAIDTIINQKGQDMICIYVaIGQKDSTVRTQVE-TLKKYGaMDYTIVVNAGASQPAPL 161
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGK-SVLLSMLARNADADVSVIGL-IGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALM 228

                        170       180
                 ....*....|....*....|...
gi 21360628  162 LYIAPYAGTAMGEEFMYNGKHVL 184
Cdd:PRK08927 229 RRQAAYLTLAIAEYFRDQGKDVL 251
atpB CHL00060
ATP synthase CF1 beta subunit
 7-112 1.64e-13

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 67.76  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    7 ESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPI 86
Cdd:CHL00060  79 DGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPY 158

                         90       100
                 ....*....|....*....|....*.
gi 21360628   87 GRGQRELVIGDRKTGKTSIAIDTIIN 112
Cdd:CHL00060 159 RRGGKIGLFGGAGVGKTVLIMELINN 184
fliI PRK05688
flagellar protein export ATPase FliI;
3-184 8.58e-13

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 65.52  E-value: 8.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    3 LGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDA 82
Cdd:PRK05688  82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   83 LVPIGRGQRELVIGDRKTGKtSIAIDTIINQKGQDMICIYVaIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQpAPL- 161
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGK-SVLLGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVVASPADD-APLm 238

                        170       180
                 ....*....|....*....|....
gi 21360628  162 -LYIAPYAgTAMGEEFMYNGKHVL 184
Cdd:PRK05688 239 rLRAAMYC-TRIAEYFRDKGKNVL 261
fliI PRK07960
flagellum-specific ATP synthase FliI;
23-184 1.65e-12

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 64.80  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   23 EVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGK 102
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628  103 tSIAIDTIINQKGQDMICIYVaIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQpAPLLYI--APYAgTAMGEEFMYNG 180
Cdd:PRK07960 189 -SVLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVIAAPADV-SPLLRMqgAAYA-TRIAEDFRDRG 264


                 ....
gi 21360628  181 KHVL 184
Cdd:PRK07960 265 QHVL 268
fliI PRK07196
flagellar protein export ATPase FliI;
23-164 3.49e-12

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 63.76  E-value: 3.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   23 EVPVGEALIGRVVNPLGQPIDGLGEIVTDKarPVEAMAPGV--MQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKT 100
Cdd:PRK07196  89 ELLIGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGV 166

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21360628  101 GKtSIAIDTIINQKGQDMICIYVaIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQpAPLLYI 164
Cdd:PRK07196 167 GK-SVLLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPADE-SPLMRI 227
fliI PRK06793
flagellar protein export ATPase FliI;
7-184 1.93e-10

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 58.84  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    7 ESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPI 86
Cdd:PRK06793  74 EKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTI 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   87 GRGQRELVIGDRKTGKTSIAidTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAP 166
Cdd:PRK06793 154 GIGQKIGIFAGSGVGKSTLL--GMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAA 231

                        170
                 ....*....|....*...
gi 21360628  167 YAGTAMGEEFMYNGKHVL 184
Cdd:PRK06793 232 KLATSIAEYFRDQGNNVL 249
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 7-184 1.60e-08

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 53.11  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    7 ESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDkarPVEAMAPGV--MQRKSVNEPMQTGLKAIDALV 84
Cdd:PRK02118  59 RGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPSVnpVKRIVPREMIRTGIPMIDVFN 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628   85 PIGRGQRELVIGDrkTGKTSIAI-DTIINQKGQDMIcIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLY 163
Cdd:PRK02118 136 TLVESQKIPIFSV--SGEPYNALlARIALQAEADII-ILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECL 212

                        170       180
                 ....*....|....*....|..
gi 21360628  164 IAPYAGTAMGEEFMYNG-KHVL 184
Cdd:PRK02118 213 LVPDMALAVAEKFALEGkKKVL 234
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 14-184 8.94e-08

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: 50.88  E-value: 8.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    14 KVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQREL 93
Cdd:TIGR01040  66 TCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21360628    94 VIGD-------------RKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 160
Cdd:TIGR01040 146 IFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTI 225

                         170       180
                  ....*....|....*....|....*
gi 21360628   161 LLYIAPYAGTAMGEEFMYN-GKHVL 184
Cdd:TIGR01040 226 ERIITPRLALTTAEYLAYQcEKHVL 250
rho PRK09376
transcription termination factor Rho; Provisional
 80-105 5.56e-03

transcription termination factor Rho; Provisional


Pssm-ID: 236490 [Multi-domain]  Cd Length: 416  Bit Score: 36.66  E-value: 5.56e-03
                         10        20
                 ....*....|....*....|....*.
gi 21360628   80 IDALVPIGRGQRELVIGDRKTGKTSI 105
Cdd:PRK09376 160 IDLIAPIGKGQRGLIVAPPKAGKTVL 185
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 78-114 5.89e-03

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: 36.41  E-value: 5.89e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 21360628  78 KAIDALVPIGRGQRELVIGDRKTGKT----SIAIDTIINQK 114
Cdd:cd01128   5 RVIDLIAPIGKGQRGLIVAPPKAGKTtllqNIANAIAKNHP 45
ATP-synt_F1_alpha_N cd18116
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ...
 1-20 6.65e-03

F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, in 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 alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.


Pssm-ID: 349740 [Multi-domain]  Cd Length: 67  Bit Score: 33.97  E-value: 6.65e-03
                        10        20
                ....*....|....*....|
gi 21360628   1 IILGDFESIREGDKVKRTGK 20
Cdd:cd18116  48 VLLGDYKLIKEGDSVKRTGR 67
 
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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