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Conserved domains on  [gi|937627152|gb|ALI87180|]
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H+-transporter, partial [Lactobacillus delbrueckii subsp. bulgaricus]

Protein Classification

F0F1 ATP synthase subunit beta( domain architecture ID 1903243)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtpD super family cl43008
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-130 7.54e-117

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


The actual alignment was detected with superfamily member COG0055:

Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 336.68  E-value: 7.54e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   1 HNIAQEHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFID 80
Cdd:COG0055  168 HNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFID 247

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 937627152  81 NIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:COG0055  248 NIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITS 297
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-130 7.54e-117

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: 336.68  E-value: 7.54e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   1 HNIAQEHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFID 80
Cdd:COG0055  168 HNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFID 247

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 937627152  81 NIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:COG0055  248 NIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITS 297
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-130 2.07e-105

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: 301.06  E-value: 2.07e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   1 HNIAQEHNGISVFTGVGERTREGNDLYFEMKASGV-----LDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDV 75
Cdd:cd01133   89 NNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEEGQDV 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 937627152  76 LLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:cd01133  169 LLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITS 223
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-130 1.88e-101

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: 297.40  E-value: 1.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152    1 HNIAQEHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFID 80
Cdd:TIGR01039 165 NNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFID 244

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 937627152   81 NIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:TIGR01039 245 NIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITS 294
atpB CHL00060
ATP synthase CF1 beta subunit
 2-130 3.60e-96

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 285.01  E-value: 3.60e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   2 NIAQEHNGISVFTGVGERTREGNDLYFEMKASGVLD-------KTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQD 74
Cdd:CHL00060 184 NIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQD 263

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 937627152  75 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:CHL00060 264 VLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITS 319
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 1-130 1.29e-56

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: 174.85  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152    1 HNIA-QEHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFI 79
Cdd:pfam00006  32 GMIArQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIM 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 937627152   80 DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITST--KKGSITS 130
Cdd:pfam00006 111 DSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkgKGGSITA 163
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-130 7.54e-117

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: 336.68  E-value: 7.54e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   1 HNIAQEHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFID 80
Cdd:COG0055  168 HNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFID 247

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 937627152  81 NIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:COG0055  248 NIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITS 297
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 1-130 2.07e-105

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: 301.06  E-value: 2.07e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   1 HNIAQEHNGISVFTGVGERTREGNDLYFEMKASGV-----LDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDV 75
Cdd:cd01133   89 NNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEEGQDV 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 937627152  76 LLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:cd01133  169 LLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITS 223
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-130 1.88e-101

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: 297.40  E-value: 1.88e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152    1 HNIAQEHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFID 80
Cdd:TIGR01039 165 NNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFID 244

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 937627152   81 NIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:TIGR01039 245 NIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITS 294
atpB CHL00060
ATP synthase CF1 beta subunit
 2-130 3.60e-96

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 285.01  E-value: 3.60e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   2 NIAQEHNGISVFTGVGERTREGNDLYFEMKASGVLD-------KTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQD 74
Cdd:CHL00060 184 NIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQD 263

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 937627152  75 VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:CHL00060 264 VLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITS 319
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 1-130 3.08e-70

alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.


Pssm-ID: 132348 [Multi-domain]  Cd Length: 449  Bit Score: 217.00  E-value: 3.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152    1 HNIAQEHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFID 80
Cdd:TIGR03305 160 HNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLID 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 937627152   81 NIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:TIGR03305 240 NIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITS 289
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 2-130 2.83e-60

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: 186.12  E-value: 2.83e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   2 NIAQEHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDN 81
Cdd:cd19476   90 NQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-NGQHVLLIIDD 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 937627152  82 IFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTK--KGSITS 130
Cdd:cd19476  169 ISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITA 219
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 1-130 1.29e-56

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: 174.85  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152    1 HNIA-QEHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFI 79
Cdd:pfam00006  32 GMIArQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIM 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 937627152   80 DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITST--KKGSITS 130
Cdd:pfam00006 111 DSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkgKGGSITA 163
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 10-129 3.14e-22

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.


Pssm-ID: 410880 [Multi-domain]  Cd Length: 265  Bit Score: 88.00  E-value: 3.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAG 89
Cdd:cd01136   95 VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-QGKKVLLLMDSLTRFAMAQ 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 937627152  90 SEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSIT 129
Cdd:cd01136  174 REVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSIT 213
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
12-129 4.12e-19

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 81.40  E-value: 4.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  12 VFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSE 91
Cdd:PRK06820 193 VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAARE 271

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 937627152  92 VSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSIT 129
Cdd:PRK06820 272 IGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSIT 309
fliI PRK06002
flagellar protein export ATPase FliI;
16-129 4.93e-18

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 78.50  E-value: 4.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  16 VGERTREGNDlYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSAL 95
Cdd:PRK06002 199 VGERGREVRE-FLEDTLADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD-RGENVLLIVDSVTRFAHAAREVALA 276

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 937627152  96 LGRIPSAVGYQPTLATEMGQLQERI--TSTKKGSIT 129
Cdd:PRK06002 277 AGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSIT 312
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 48-129 2.05e-17

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: 76.61  E-value: 2.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  48 EPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGS 127
Cdd:COG1157  223 EPPLMRLRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGS 301


                 ..
gi 937627152 128 IT 129
Cdd:COG1157  302 IT 303
PRK08149 PRK08149
FliI/YscN family ATPase;
16-129 2.38e-17

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 76.57  E-value: 2.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  16 VGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSAL 95
Cdd:PRK08149 185 IGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALA 263

                         90       100       110
                 ....*....|....*....|....*....|....
gi 937627152  96 LGRIPSAVGYQPTLATEMGQLQERITSTKKGSIT 129
Cdd:PRK08149 264 AGELPARRGYPASVFDSLPRLLERPGATLAGSIT 297
fliI PRK08927
flagellar protein export ATPase FliI;
10-129 3.00e-16

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 73.47  E-value: 3.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTRE-----GNDLYFEMKASGVLdktamVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFR 84
Cdd:PRK08927 186 VSVIGLIGERGREvqeflQDDLGPEGLARSVV-----VVATSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTR 259

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 937627152  85 FTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERI--TSTKKGSIT 129
Cdd:PRK08927 260 FAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTIT 306
fliI PRK08472
flagellar protein export ATPase FliI;
10-130 7.53e-16

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 72.41  E-value: 7.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTREGNDlYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAG 89
Cdd:PRK08472 185 IKVVALIGERGREIPE-FIEKNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQ 262

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 937627152  90 SEVSALLGRIPSAVGYQPTLATEMGQLQERITSTK-KGSITS 130
Cdd:PRK08472 263 REIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITA 304
fliI PRK07721
flagellar protein export ATPase FliI;
3-129 3.76e-15

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 70.14  E-value: 3.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   3 IAQEHNG-ISVFTGVGERTREGND-LYFEMKASGvLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFID 80
Cdd:PRK07721 178 IARNTSAdLNVIALIGERGREVREfIERDLGPEG-LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRD-QGLNVMLMMD 255

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 937627152  81 NIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSIT 129
Cdd:PRK07721 256 SVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSIT 304
fliI PRK05688
flagellar protein export ATPase FliI;
10-130 1.48e-14

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 68.60  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAG 89
Cdd:PRK05688 196 IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQ 274

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 937627152  90 SEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKK--GSITS 130
Cdd:PRK05688 275 REIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggGSITA 317
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
10-130 1.80e-14

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 68.24  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTREGND-LYFEMKASGvLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQA 88
Cdd:PRK06936 190 VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRD-QGKRVLLLMDSVTRFARA 267

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 937627152  89 GSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:PRK06936 268 QREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITA 309
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 1-119 1.95e-14

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 68.51  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152    1 HNIAQEHN-------GISVFTGVGERTREGNDLYFEM-------KASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEY 66
Cdd:PRK14698  668 HNTVTQHQlakwsdaQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEY 747

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 937627152   67 FRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQER 119
Cdd:PRK14698  748 FRDM-GYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYER 799
fliI PRK08972
flagellar protein export ATPase FliI;
16-130 2.59e-14

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 67.80  E-value: 2.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  16 VGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSAL 95
Cdd:PRK08972 196 VGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALA 274

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 937627152  96 LGRIPSAVGYQPTLATEMGQLQERI--TSTKKGSITS 130
Cdd:PRK08972 275 VGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITA 311
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 10-119 2.46e-13

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 64.52  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERtreGND----------LYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVeGQDVLLFI 79
Cdd:cd01134  104 VVIYVGCGER---GNEmaevleefpeLKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMA 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 937627152  80 DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQER 119
Cdd:cd01134  180 DSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYER 219
fliI PRK06793
flagellar protein export ATPase FliI;
10-129 2.67e-13

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 65.00  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAG 89
Cdd:PRK06793 184 INVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADAR 262

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 937627152  90 SEVSALLGRIPSAvGYQPTLATEMGQLQERITSTKKGSIT 129
Cdd:PRK06793 263 RSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSIT 301
PRK05922 PRK05922
type III secretion system ATPase; Validated
 10-130 5.94e-13

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 64.15  E-value: 5.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTREGNDlYFEMKASGVLD-KTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQA 88
Cdd:PRK05922 185 INVIALIGERGREVRE-YIEQHKEGLAAqRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAA 262

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 937627152  89 GSEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:PRK05922 263 LQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITA 304
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 10-130 2.07e-11

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 59.78  E-value: 2.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAG 89
Cdd:PRK09099 191 VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQ 269

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 937627152  90 SEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:PRK09099 270 REIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITA 310
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 6-129 2.74e-11

V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.


Pssm-ID: 410879 [Multi-domain]  Cd Length: 282  Bit Score: 58.77  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   6 EHNGISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRF 85
Cdd:cd01135   99 EENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNY 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 937627152  86 TQAGSEVSALLGRIPSAVGYQPTLATEMGQLQER--ITSTKKGSIT 129
Cdd:cd01135  179 AEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSIT 224
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
10-130 6.13e-11

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 58.43  E-value: 6.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAG 89
Cdd:PRK07594 183 SNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAA 261

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 937627152  90 SEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKGSITS 130
Cdd:PRK07594 262 REIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITA 302
fliI PRK07196
flagellar protein export ATPase FliI;
16-118 3.29e-10

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 56.05  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  16 VGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSAL 95
Cdd:PRK07196 189 IGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALS 267

                         90       100
                 ....*....|....*....|...
gi 937627152  96 LGRIPSAVGYQPTLATEMGQLQE 118
Cdd:PRK07196 268 LGEPPATKGYPPSAFSIIPRLAE 290
fliI PRK07960
flagellum-specific ATP synthase FliI;
16-130 2.94e-09

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 53.63  E-value: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  16 VGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSAL 95
Cdd:PRK07960 209 IGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALA 287

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 937627152  96 LGRIPSAVGYQPTLATEMGQLQERITS--TKKGSITS 130
Cdd:PRK07960 288 IGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITA 324
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 12-129 7.22e-09

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 52.14  E-value: 7.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  12 VFTGVGERTREGNdlYF--EMKASGVLDKTAMVFGQMNEPPGARM---RVAltgLTIAEYFRDVEGQDVLLFIDNIFRFT 86
Cdd:PRK04196 179 VFAAMGITFEEAN--FFmeDFEETGALERSVVFLNLADDPAIERIltpRMA---LTAAEYLAFEKGMHVLVILTDMTNYC 253

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 937627152  87 QAGSEVSALLGRIPSAVGYQPTLATEMGQLQER--ITSTKKGSIT 129
Cdd:PRK04196 254 EALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSIT 298
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 59-129 2.49e-08

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 50.94  E-value: 2.49e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937627152  59 TGLTIAEYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGQLQER----IT-STKKGSIT 129
Cdd:PRK04192 311 TGITIAEYYRDM-GYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVT 385
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 3-100 3.46e-08

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 50.30  E-value: 3.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   3 IAQEHNG-ISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDN 81
Cdd:PRK13343 184 INQKDSDvICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDD 262

                         90
                 ....*....|....*....
gi 937627152  82 IFRFTQAGSEVSALLGRIP 100
Cdd:PRK13343 263 LSKHAAAYRELSLLLRRPP 281
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 26-129 2.23e-07

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 48.11  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  26 LYF--EMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAV 103
Cdd:PRK02118 182 LFFkdTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNR 261

                         90       100
                 ....*....|....*....|....*..
gi 937627152 104 GYQPTLATEMGQLQERITSTKK-GSIT 129
Cdd:PRK02118 262 GYPGSLYSDLASRYEKAVDFEDgGSIT 288
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 3-100 1.47e-05

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: 42.55  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   3 IAQEHNG-ISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDN 81
Cdd:cd01132   91 INQKGKKvYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD-NGKHALIIYDD 169

                         90
                 ....*....|....*....
gi 937627152  82 IFRFTQAGSEVSALLGRIP 100
Cdd:cd01132  170 LSKQAVAYRQMSLLLRRPP 188
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 10-126 4.88e-04

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 38.48  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152  10 ISVFTGVGERTREGNDLYFEMKASGVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAG 89
Cdd:PTZ00185 227 ISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAY 305

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 937627152  90 SEVSALLGRIPSAVGYQPTLATEMGQLQERITSTKKG 126
Cdd:PTZ00185 306 RQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPG 342
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 34-129 3.58e-03

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: 35.85  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937627152   34 GVLDKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEM 113
Cdd:TIGR01040 208 GSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDL 287

                          90
                  ....*....|....*...
gi 937627152  114 GQLQERI--TSTKKGSIT 129
Cdd:TIGR01040 288 ATIYERAgrVEGRNGSIT 305
 
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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