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Conserved domains on  [gi|443609819|gb|AGC95263|]
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ATP synthase alpha subunit, partial (mitochondrion) [Actinidia deliciosa x Actinidia arguta]

Protein Classification

F0F1 ATP synthase subunit alpha( domain architecture ID 1000038)

F0F1 ATP synthase subunit alpha is part of the catalytic core of the F-ATPase that uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient and is found in bacterial, mitochondrial, and chloroplast membranes

CATH:  1.20.150.20|3.40.50.300
Gene Ontology:  GO:0015986|GO:0046933|GO:0045261
PubMed:  8905099|12887009|11479684
SCOP:  4002275|4004011|3000684

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09281 super family cl35802
F0F1 ATP synthase subunit alpha; Validated
 1-133 7.88e-93

F0F1 ATP synthase subunit alpha; Validated


The actual alignment was detected with superfamily member PRK09281:

Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 276.95  E-value: 7.88e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAP 80
Cdd:PRK09281  55 FPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAP 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 443609819  81 GIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQK 133
Cdd:PRK09281 135 GVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQK 187
 
Name Accession Description Interval E-value
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 1-133 7.88e-93

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 276.95  E-value: 7.88e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAP 80
Cdd:PRK09281  55 FPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAP 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 443609819  81 GIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQK 133
Cdd:PRK09281 135 GVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQK 187
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 1-133 9.64e-93

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: 276.53  E-value: 9.64e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAP 80
Cdd:COG0056   55 FPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAP 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 443609819  81 GIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQK 133
Cdd:COG0056  135 GVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQK 187
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
 1-134 1.78e-75

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: 232.28  E-value: 1.78e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819    1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAP 80
Cdd:TIGR00962  54 FEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAP 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 443609819   81 GIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQ 134
Cdd:TIGR00962 134 GVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKD 187
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 40-136 1.26e-61

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: 190.08  E-value: 1.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  40 IVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQT 119
Cdd:cd01132    1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80

                         90
                 ....*....|....*..
gi 443609819 120 GKTAIAIDTILNQKQMN 136
Cdd:cd01132   81 GKTAIAIDTIINQKGKK 97
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 95-132 1.23e-13

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: 64.69  E-value: 1.23e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 443609819   95 GLKAVDSLVPIGRGQRELIIGDRQTGKTAIAiDTILNQ 132
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQ 37
 
Name Accession Description Interval E-value
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 1-133 7.88e-93

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 276.95  E-value: 7.88e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAP 80
Cdd:PRK09281  55 FPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAP 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 443609819  81 GIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQK 133
Cdd:PRK09281 135 GVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQK 187
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 1-133 9.64e-93

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: 276.53  E-value: 9.64e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAP 80
Cdd:COG0056   55 FPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAP 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 443609819  81 GIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQK 133
Cdd:COG0056  135 GVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQK 187
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
 1-134 1.78e-75

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: 232.28  E-value: 1.78e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819    1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAP 80
Cdd:TIGR00962  54 FEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAP 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 443609819   81 GIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQ 134
Cdd:TIGR00962 134 GVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKD 187
atpA CHL00059
ATP synthase CF1 alpha subunit
 1-136 2.47e-71

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 221.38  E-value: 2.47e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAP 80
Cdd:CHL00059  34 FEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAP 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 443609819  81 GIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMN 136
Cdd:CHL00059 114 GIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQN 169
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 1-136 1.02e-67

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 212.47  E-value: 1.02e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAP 80
Cdd:PRK13343  55 FEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAP 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 443609819  81 GIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMN 136
Cdd:PRK13343 135 AIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSD 190
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 40-136 1.26e-61

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: 190.08  E-value: 1.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  40 IVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQT 119
Cdd:cd01132    1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80

                         90
                 ....*....|....*..
gi 443609819 120 GKTAIAIDTILNQKQMN 136
Cdd:cd01132   81 GKTAIAIDTIINQKGKK 97
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 42-134 1.75e-32

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: 115.25  E-value: 1.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  42 DVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGK 121
Cdd:cd19476    1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80

                         90
                 ....*....|...
gi 443609819 122 TAIAIDTILNQKQ 134
Cdd:cd19476   81 TVLAMQLARNQAK 93
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 7-138 4.31e-27

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 104.74  E-value: 4.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   7 GIALNLENEN-VGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLG--VPI---DGKGSLSDHERR--RVEVK 78
Cdd:PTZ00185  80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGheVPVgllTRSRALLESEQTlgKVDAG 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  79 APGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSR 138
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQ 219
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 22-110 3.71e-25

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: 98.56  E-value: 3.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  22 FGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDS 101
Cdd:COG1157   71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150


                 ....*....
gi 443609819 102 LVPIGRGQR 110
Cdd:COG1157  151 LLTVGRGQR 159
PRK07165 PRK07165
ATP F0F1 synthase subunit alpha;
78-136 8.30e-24

ATP F0F1 synthase subunit alpha;


Pssm-ID: 235951 [Multi-domain]  Cd Length: 507  Bit Score: 95.43  E-value: 8.30e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 443609819  78 KAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMN 136
Cdd:PRK07165 113 LAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTN 171
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 43-110 1.68e-18

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: 78.37  E-value: 1.68e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443609819  43 VPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQR 110
Cdd:cd01136    2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQR 69
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 31-108 3.18e-17

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: 76.67  E-value: 3.18e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443609819  31 GDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRG 108
Cdd:COG0055   69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 22-124 1.25e-16

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 74.80  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  22 FGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDS 101
Cdd:PRK09099  77 FGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDG 156

                         90       100
                 ....*....|....*....|...
gi 443609819 102 LVPIGRGQRELIIGDRQTGKTAI 124
Cdd:PRK09099 157 LMTLGEGQRMGIFAPAGVGKSTL 179
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
3-124 2.52e-15

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 71.00  E-value: 2.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   3 SGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGkGSLSDHERRRVEVKAPGI 82
Cdd:PRK06820  59 QGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSP 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 443609819  83 IERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAI 124
Cdd:PRK06820 138 LTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL 179
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
34-124 7.16e-15

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 69.78  E-value: 7.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  34 VKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELI 113
Cdd:PRK06936  88 VSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGI 167

                         90
                 ....*....|.
gi 443609819 114 IGDRQTGKTAI 124
Cdd:PRK06936 168 FAAAGGGKSTL 178
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 8-131 1.81e-14

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: 68.59  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819    8 IALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKS 87
Cdd:TIGR01039  43 VAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQST 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 443609819   88 VHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILN 131
Cdd:TIGR01039 123 KVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINN 166
fliI PRK07721
flagellar protein export ATPase FliI;
14-122 5.30e-14

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 67.44  E-value: 5.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  14 NENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQ 93
Cdd:PRK07721  64 DEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPME 143

                         90       100
                 ....*....|....*....|....*....
gi 443609819  94 TGLKAVDSLVPIGRGQRELIIGDRQTGKT 122
Cdd:PRK07721 144 VGVRAIDSLLTVGKGQRVGIFAGSGVGKS 172
ATP-synt_F1_alpha_N cd18116
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ...
 1-38 8.56e-14

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: 61.70  E-value: 8.56e-14
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 443609819   1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTG 38
Cdd:cd18116   29 FPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTG 66
fliI PRK08972
flagellar protein export ATPase FliI;
43-110 1.11e-13

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 66.26  E-value: 1.11e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443609819  43 VPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQR 110
Cdd:PRK08972  97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 95-132 1.23e-13

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: 64.69  E-value: 1.23e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 443609819   95 GLKAVDSLVPIGRGQRELIIGDRQTGKTAIAiDTILNQ 132
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQ 37
fliI PRK06002
flagellar protein export ATPase FliI;
31-122 1.33e-12

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 63.48  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  31 GDLVKRTGSIVDVPAgKAMLGRVVDGLGVPIDGKGSLSDHERRR-VEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQ 109
Cdd:PRK06002  88 GDAVFRKGPLRIRPD-PSWKGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQ 166

                         90
                 ....*....|...
gi 443609819 110 RELIIGDRQTGKT 122
Cdd:PRK06002 167 RIGIFAGSGVGKS 179
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
43-124 2.07e-12

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 62.66  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  43 VPAGKAMLGRVVDGLGVPIDGKgSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKT 122
Cdd:PRK07594  91 VPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS 169


                 ..
gi 443609819 123 AI 124
Cdd:PRK07594 170 TL 171
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 43-131 2.12e-12

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: 62.24  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  43 VPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKT 122
Cdd:cd01133    2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81


                 ....*....
gi 443609819 123 AIAIDTILN 131
Cdd:cd01133   82 VLIMELINN 90
fliI PRK08472
flagellar protein export ATPase FliI;
7-122 3.64e-12

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 62.01  E-value: 3.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   7 GIALNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVeVKAP-GIIER 85
Cdd:PRK08472  56 GMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPI-MKAPiAAMKR 134

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 443609819  86 KSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKT 122
Cdd:PRK08472 135 GLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKS 171
PRK05922 PRK05922
type III secretion system ATPase; Validated
 43-124 1.60e-11

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 60.30  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  43 VPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKT 122
Cdd:PRK05922  92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171


                 ..
gi 443609819 123 AI 124
Cdd:PRK05922 172 SL 173
fliI PRK05688
flagellar protein export ATPase FliI;
43-110 1.84e-11

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 60.13  E-value: 1.84e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  43 VPAGKAMLGRVVDGLGVPIDGKGSLSDHErrRVEVKAPGI--IERKSVHEPMQTGLKAVDSLVPIGRGQR 110
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPMKAED--WVPMDGPTInpLNRHPISEPLDVGIRSINGLLTVGRGQR 170
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 6-110 1.84e-10

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 57.14  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819   6 KGIALNLENENVGIVVFGSDTYIK-EGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIE 84
Cdd:PRK04196  40 RGQVLEVSEDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVA 119

                         90       100
                 ....*....|....*....|....*.
gi 443609819  85 RKSVHEPMQTGLKAVDSLVPIGRGQR 110
Cdd:PRK04196 120 REYPEEFIQTGISAIDGLNTLVRGQK 145
fliI PRK08927
flagellar protein export ATPase FliI;
47-110 4.70e-10

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 56.14  E-value: 4.70e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 443609819  47 KAMLGRVVDGLGVPIDGKGSLSDHERRRVeVKA--PGIIERKSVHEPMQTGLKAVDSLVPIGRGQR 110
Cdd:PRK08927  96 RAWLGRVVNALGEPIDGKGPLPQGPVPYP-LRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQR 160
atpB CHL00060
ATP synthase CF1 beta subunit
 28-131 7.39e-10

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 55.43  E-value: 7.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  28 IKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIE---RKSVHEpmqTGLKAVDSLVP 104
Cdd:CHL00060  81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQldtKLSIFE---TGIKVVDLLAP 157

                         90       100
                 ....*....|....*....|....*..
gi 443609819 105 IGRGQRELIIGDRQTGKTAIAIDTILN 131
Cdd:CHL00060 158 YRRGGKIGLFGGAGVGKTVLIMELINN 184
fliI PRK07196
flagellar protein export ATPase FliI;
46-124 1.20e-09

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 54.90  E-value: 1.20e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 443609819  46 GKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAI 124
Cdd:PRK07196  93 GDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171
PRK08149 PRK08149
FliI/YscN family ATPase;
33-122 3.79e-08

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 50.38  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  33 LVKRTGSIVDVPAGKAMLGRVVDGLGVpIDGK-----GSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGR 107
Cdd:PRK08149  72 VLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGV 150

                         90
                 ....*....|....*
gi 443609819 108 GQRELIIGDRQTGKT 122
Cdd:PRK08149 151 GQRMGIFASAGCGKT 165
fliI PRK06793
flagellar protein export ATPase FliI;
10-124 4.00e-08

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 50.36  E-value: 4.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  10 LNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVH 89
Cdd:PRK06793  58 IAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEIT 137

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 443609819  90 EPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAI 124
Cdd:PRK06793 138 DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTL 172
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 43-110 7.93e-08

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: 49.53  E-value: 7.93e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443609819  43 VPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQR 110
Cdd:cd01135    4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQK 71
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 1-38 1.84e-07

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


Pssm-ID: 427029 [Multi-domain]  Cd Length: 69  Bit Score: 45.23  E-value: 1.84e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 443609819    1 FASGVKGIALNLENENVGIVVFGSDTYIKEGDLVKRTG 38
Cdd:pfam02874  32 FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
fliI PRK07960
flagellum-specific ATP synthase FliI;
43-110 9.14e-07

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 46.70  E-value: 9.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 443609819  43 VPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQR 110
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQR 177
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 37-110 2.32e-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: 45.48  E-value: 2.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 443609819   37 TGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQR 110
Cdd:TIGR01040  70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQK 143
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 10-100 2.55e-06

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 45.41  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 443609819  10 LNLENENVGIVVFGSDTYIKEGDLVKRTGSIVDVPAGKAMLGRVVDGLGVPIDGKGSLSDHErrrVEVKAPGI--IERKS 87
Cdd:PRK02118  43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEP---IEIGGPSVnpVKRIV 119

                         90
                 ....*....|...
gi 443609819  88 VHEPMQTGLKAVD 100
Cdd:PRK02118 120 PREMIRTGIPMID 132
 
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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