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Conserved domains on  [gi|1829529719|gb|QIV68116|]
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ATP synthase F0 subunit 6 (mitochondrion) [Marsupiomonas sp. NIES 1824]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 218-354 4.43e-36

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


:

Pssm-ID: 273458  Cd Length: 226  Bit Score: 130.40  E-value: 4.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:TIGR01131  95 TPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLT 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1829529719 298 TVRGFVSALLGSATLAYcrvgrrGAVILQGVFLLETRVCVLQAYVFTRLFTIYLKDA 354
Cdd:TIGR01131 175 LLSGLLFSLMSSAIFAL------LLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
 
Name Accession Description Interval E-value
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 218-354 4.43e-36

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273458  Cd Length: 226  Bit Score: 130.40  E-value: 4.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:TIGR01131  95 TPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLT 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1829529719 298 TVRGFVSALLGSATLAYcrvgrrGAVILQGVFLLETRVCVLQAYVFTRLFTIYLKDA 354
Cdd:TIGR01131 175 LLSGLLFSLMSSAIFAL------LLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 218-352 2.61e-35

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 126.36  E-value: 2.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:cd00310    29 TPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLA 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1829529719 298 TVRGFVSALLGSATLAycrvgrrGAVILQGVFLLETRVCVLQAYVFTRLFTIYLK 352
Cdd:cd00310   109 LLSGLVPSLLSSVGLL-------PLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 218-358 3.16e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 115.49  E-value: 3.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:MTH00175  107 TPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFA 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829529719 298 TVRGFVSALLGSATLAycrVGRRGAVILQGVFLLETRVCVLQAYVFTRLFTIYLKDAKDLH 358
Cdd:MTH00175  187 ILSGFAFNMLSNGLII---LSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTIALH 244
ATP-synt_A pfam00119
ATP synthase A chain;
218-352 8.74e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 100.26  E-value: 8.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLR--FFSFFCPrGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLL 295
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHGLGgyFKKLFVP-PVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLL 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1829529719 296 LHTVRGFVSALLGSATLAYcrvgrrGAVILQGVF--LLETRVCVLQAYVFTRLFTIYLK 352
Cdd:pfam00119 164 LLLLAGLIFALLSAGFLLG------VIPPLLGVAwtLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 218-354 1.12e-20

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


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 88.98  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFF--SFFCPRGIPLAltPFIVILEMISFFFRPVSLGVRLRANMTAGHLL 295
Cdd:COG0356    82 PPTADINVTLALALIVFVLVHYYGIKKKGLGGYlkHLFFPPFPWLA--PLMLPIEIISELARPLSLSLRLFGNMFAGHII 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 296 LHTVRGFVSALLGSAtlaycrvgrrGAVILQGVF-LLETRVCVLQAYVFTRLFTIYLKDA 354
Cdd:COG0356   160 LLLLAGLAPFLLLGV----------LSLLLPVAWtAFELLVGFLQAYIFTMLTAVYISLA 209
 
Name Accession Description Interval E-value
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 218-354 4.43e-36

ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be designated ATP synthase, F0 subunit A; eukaryotic (chloroplast and mitochondrial) forms should be designated ATP synthase, F0 subunit 6. The F1/F0 ATP synthase is a multisubunit, membrane associated enzyme found in bacteria and mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. Individual subunits in each of these clusters are named differently in prokaryotes and in organelles e.g., mitochondria and chloroplast. The bacterial equivalent of subunit 6 is named subunit 'A'. It has been shown that proton is conducted though this subunit. Typically, deprotonation and reprotonation of the acidic amino acid side-chains are implicated in the process. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273458  Cd Length: 226  Bit Score: 130.40  E-value: 4.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:TIGR01131  95 TPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLT 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1829529719 298 TVRGFVSALLGSATLAYcrvgrrGAVILQGVFLLETRVCVLQAYVFTRLFTIYLKDA 354
Cdd:TIGR01131 175 LLSGLLFSLMSSAIFAL------LLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 218-352 2.61e-35

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 126.36  E-value: 2.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:cd00310    29 TPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLA 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1829529719 298 TVRGFVSALLGSATLAycrvgrrGAVILQGVFLLETRVCVLQAYVFTRLFTIYLK 352
Cdd:cd00310   109 LLSGLVPSLLSSVGLL-------PLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 218-358 3.16e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 115.49  E-value: 3.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:MTH00175  107 TPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFA 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829529719 298 TVRGFVSALLGSATLAycrVGRRGAVILQGVFLLETRVCVLQAYVFTRLFTIYLKDAKDLH 358
Cdd:MTH00175  187 ILSGFAFNMLSNGLII---LSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTIALH 244
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 218-358 4.62e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 112.06  E-value: 4.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:MTH00172   96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829529719 298 TVRGFVSALLGSATLAycrvGRRGAVILQGVFLLETRVCVLQAYVFTRLFTIYLKDAKDLH 358
Cdd:MTH00172  176 ILAGFGFNMLCASGFL----SLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTIVLH 232
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 218-350 2.95e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 101.78  E-value: 2.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:MTH00157   93 TSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLT 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1829529719 298 tvrgfvsaLLGSATLAYCRVGRRGAVILQGV-FLLETRVCVLQAYVFTRLFTIY 350
Cdd:MTH00157  173 --------LLGNTGPSLSSMILSILILIQILlLILESAVAIIQSYVFSVLSTLY 218
ATP-synt_A pfam00119
ATP synthase A chain;
218-352 8.74e-25

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 100.26  E-value: 8.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLR--FFSFFCPrGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLL 295
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGIKKHGLGgyFKKLFVP-PVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLL 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1829529719 296 LHTVRGFVSALLGSATLAYcrvgrrGAVILQGVF--LLETRVCVLQAYVFTRLFTIYLK 352
Cdd:pfam00119 164 LLLLAGLIFALLSAGFLLG------VIPPLLGVAwtLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 219-350 1.43e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 97.24  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 219 PTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLHT 298
Cdd:MTH00173   97 VTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTL 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1829529719 299 VRGFVSALLGSATLAycrVGRRGAVILQGVFLLETRVCVLQAYVFTRLFTIY 350
Cdd:MTH00173  177 IGNYLSSSLFSSSVV---SLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLY 225
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 218-351 6.96e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 95.40  E-value: 6.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:MTH00179   94 TPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRLTANITAGHLLMH 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1829529719 298 TVRGFVSALLGSATLaycrVGRRGAVILQGVFLLETRVCVLQAYVFTRLFTIYL 351
Cdd:MTH00179  174 LISSAVFVLMNFMGM----VALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYL 223
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 218-353 2.31e-22

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 93.86  E-value: 2.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLsverhGLRF-----FSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAG 292
Cdd:MTH00101   93 TPTTQLSMNLGMAIPLWAGTVIT-----GFRNktkasLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAG 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1829529719 293 HLLLHtvrgfvsaLLGSATLAYCRVGRRGA----VILQGVFLLETRVCVLQAYVFTRLFTIYLKD 353
Cdd:MTH00101  168 HLLIH--------LIGGATLALMSISTTTAlitfIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 218-353 9.22e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 92.49  E-value: 9.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:MTH00005   98 STSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLS 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1829529719 298 TVRGFVSALLGSATLAYCRVgrrgaVILQ-GVFLLETRVCVLQAYVFTRLFTIYLKD 353
Cdd:MTH00005  178 LIGIYAASALFSSISSTILL-----ILTQmGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 218-353 3.05e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 90.86  E-value: 3.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLh 297
Cdd:MTH00176   96 TSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLL- 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1829529719 298 tvrGFVSALLGSATLAYCRVGRRGAVILQGVFLLETRVCVLQAYVFTRLFTIYLKD 353
Cdd:MTH00176  175 ---GLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 218-354 1.12e-20

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


Pssm-ID: 440125 [Multi-domain]  Cd Length: 212  Bit Score: 88.98  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFF--SFFCPRGIPLAltPFIVILEMISFFFRPVSLGVRLRANMTAGHLL 295
Cdd:COG0356    82 PPTADINVTLALALIVFVLVHYYGIKKKGLGGYlkHLFFPPFPWLA--PLMLPIEIISELARPLSLSLRLFGNMFAGHII 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 296 LHTVRGFVSALLGSAtlaycrvgrrGAVILQGVF-LLETRVCVLQAYVFTRLFTIYLKDA 354
Cdd:COG0356   160 LLLLAGLAPFLLLGV----------LSLLLPVAWtAFELLVGFLQAYIFTMLTAVYISLA 209
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 218-358 6.11e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 87.69  E-value: 6.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLH 297
Cdd:MTH00174  115 TPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFS 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829529719 298 TVRGFVSALLGSATLAYCRVgrrGAVILQGVFLLETRVCVLQAYVFTRLFTIYLKDAKDLH 358
Cdd:MTH00174  195 IIASFAWKMINTGILIGSFV---PFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTVELH 252
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 218-351 1.34e-18

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 83.48  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFrrssSLfvGL-IYLSVERHGLRF-----FSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTA 291
Cdd:MTH00035   97 TSTSHISLTY----SL--GIpLWMSVNILGFYLafnsrLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTA 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1829529719 292 GHLLLH----TVRGFVSA-LLGSATLaycrvgrrgaVILQGVFLLETRVCVLQAYVFTRLFTIYL 351
Cdd:MTH00035  171 GHLLIFllstAIWELSNSpLISIITL----------IIFFLLFILEIGVACIQAYVFTALVHFYL 225
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 218-354 8.04e-18

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 81.38  E-value: 8.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLFFTFRRSSSLFVGLIYLSVERHGLRFF--SFFcprgipLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLL 295
Cdd:PRK05815   98 PPTADINVTLALALIVFVLVIYYGIKKKGLGGYlkEFY------LQPHPLLLPIEIISEFSRPISLSLRLFGNMLAGELI 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 296 LHTVRGFVSALLGSATLaycrvgrrgAVILQGVF-LLETRVCVLQAYVFTRLFTIYLKDA 354
Cdd:PRK05815  172 LALIALLGGAGLLLALA---------PLILPVAWtIFEIFVGTLQAYIFMMLTIVYISMA 222
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 218-353 1.16e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 80.78  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 218 TPTSHLfftfrrssSLFVGL---IYLSVERHGLR-----FFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANM 289
Cdd:MTH00073   94 TPTTQL--------SLNLGLavpLWLATVLIGLRnqptaSLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTANL 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1829529719 290 TAGHLLLHTVRGFVSALLGSATLaycrVGRRGAVILQGVFLLETRVCVLQAYVFTRLFTIYLKD 353
Cdd:MTH00073  166 TAGHLLIQLISTATLVLLPLMPT----VSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 255-351 1.47e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 80.69  E-value: 1.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 255 PRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLHTVRGFVSALLGSATLaycrVGRRGAVILQGVFLLETR 334
Cdd:MTH00132  131 PEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPT----VAILTATLLFLLTLLEVA 206

                          90
                  ....*....|....*..
gi 1829529719 335 VCVLQAYVFTRLFTIYL 351
Cdd:MTH00132  207 VAMIQAYVFVLLLSLYL 223
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 255-351 3.74e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 79.48  E-value: 3.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 255 PRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLHtvrgfvsaLLGSATLA----YCRVGRRGAVILQGVFL 330
Cdd:MTH00120  131 PEGTPTPLIPALILIETISLLIRPLALGVRLTANLTAGHLLIQ--------LISTATLNllptMPTLSLLTLIILLLLTI 202

                          90       100
                  ....*....|....*....|.
gi 1829529719 331 LETRVCVLQAYVFTRLFTIYL 351
Cdd:MTH00120  203 LELAVAMIQAYVFVLLLSLYL 223
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 232-346 1.42e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 58.60  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 232 SLFVGLI--YLSVERHGLRFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAGHLLLHTVRgFVSALLGS 309
Cdd:PRK13419  207 AVFTFFItqYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGHIVILSLI-FISFILKS 285

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1829529719 310 ATLAycrVGRRGAVILqGVFLLETRVCVLQAYVFTRL 346
Cdd:PRK13419  286 YIVA---VAVSVPFAI-FIYLLELFVAFLQAYIFTML 318
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 245-351 5.82e-08

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 53.74  E-value: 5.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 245 HGLRFFSFFCPRGIPLALTPFIVILEMI-SFFFRPVSLGVRLRANMTAGHLLLHTVRGFVsalLGSATLAYCRVGRRGAV 323
Cdd:PRK13417  244 QGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVIILALMGFI---FQFQSWGIVPVSVIGSG 320

                          90       100
                  ....*....|....*....|....*...
gi 1829529719 324 IlqgVFLLETRVCVLQAYVFTRLFTIYL 351
Cdd:PRK13417  321 L---IYVLEIFVAFLQAYIFVLLTSLFV 345
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 249-352 3.98e-07

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 49.98  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829529719 249 FFSFFCPRGIPLALTPF-IVILEMISFFFRPVSLGVRLRANMTAGHLLlhtvrgfvSALLGSATLAYcrvgrrgaVILQG 327
Cdd:MTH00087  105 KFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLI--------SSLLNFLGEKY--------VWLSI 168

                          90       100
                  ....*....|....*....|....*.
gi 1829529719 328 VFLL-ETRVCVLQAYVFTRLFTIYLK 352
Cdd:MTH00087  169 LAIMmECFVAFIQSYIFSRLIYLYLN 194
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 232-292 5.57e-05

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 42.95  E-value: 5.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829529719 232 SLFVGLIYLSVERhglrFFSFFCPRGIPLALTPFIVILEMISFFFRPVSLGVRLRANMTAG 292
Cdd:MTH00050   65 SLFLSRVFDSLNE----FFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
 
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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