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Conserved domains on  [gi|2554484949|ref|YP_010886822|]
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hypothetical protein Q6B14_mgp31 (mitochondrion) [Paralagenidium karlingii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-140 2.10e-30

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: 107.10  E-value: 2.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:cd00310    23 LIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFA 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIAhfipliLLVILIGLEFAVAIIQAYVFTILTCMYIN 140
Cdd:cd00310   103 GHLLLALLSGLVPSLLSSVGLLPLL------LPVALTLLELFVAFIQAYVFTLLTAVYIS 156
 
Name Accession Description Interval E-value
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-140 2.10e-30

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: 107.10  E-value: 2.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:cd00310    23 LIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFA 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIAhfipliLLVILIGLEFAVAIIQAYVFTILTCMYIN 140
Cdd:cd00310   103 GHLLLALLSGLVPSLLSSVGLLPLL------LPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 1-143 2.63e-30

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: 108.83  E-value: 2.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:TIGR01131  89 LIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISA 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIahfipLILLVILIGLEFAVAIIQAYVFTILTCMYINDAL 143
Cdd:TIGR01131 169 GHLLLTLLSGLLFSLMSSAIFALL-----LLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 3-146 5.53e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 98.16  E-value: 5.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   3 PYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMAGH 82
Cdd:MTH00175  103 PYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGH 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2554484949  83 TLLKVIAGFAWSMLnVNGFIFIAHFiPLILLVILIGLEFAVAIIQAYVFTILTCMYINDALNLH 146
Cdd:MTH00175  183 LLFAILSGFAFNML-SNGLIILSLF-PMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTIALH 244
ATP-synt_A pfam00119
ATP synthase A chain;
3-140 1.06e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 94.09  E-value: 1.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   3 PYSFTLTSQLIVTFTLALTIYIGFNIIGIKKH--KKHFLNLLLPSGSsIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHglGGYFKKLFVPPVP-LPLVPLLLPIEIISEFARPVSLSLRLFGNMLA 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIAHFiplILLVILIGLEFAVAIIQAYVFTILTCMYIN 140
Cdd:pfam00119 160 GHLLLLLLAGLIFALLSAGFLLGVIPP---LLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 1-144 4.32e-22

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: 87.05  E-value: 4.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKH--KKHFLNLLLPSGssIFLVPLLVPLELISYIFRVISLPVRLFANM 78
Cdd:COG0356    76 LIPGLFPPTADINVTLALALIVFVLVHYYGIKKKglGGYLKHLFFPPF--PWLAPLMLPIEIISELARPLSLSLRLFGNM 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2554484949  79 MAGHTLLKVIAGFAWSMLNVNGFIFIAhfiplillVILIGLEFAVAIIQAYVFTILTCMYINDALN 144
Cdd:COG0356   154 FAGHIILLLLAGLAPFLLLGVLSLLLP--------VAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211
 
Name Accession Description Interval E-value
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-140 2.10e-30

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: 107.10  E-value: 2.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:cd00310    23 LIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFA 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIAhfipliLLVILIGLEFAVAIIQAYVFTILTCMYIN 140
Cdd:cd00310   103 GHLLLALLSGLVPSLLSSVGLLPLL------LPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 1-143 2.63e-30

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: 108.83  E-value: 2.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:TIGR01131  89 LIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISA 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIahfipLILLVILIGLEFAVAIIQAYVFTILTCMYINDAL 143
Cdd:TIGR01131 169 GHLLLTLLSGLLFSLMSSAIFALL-----LLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 3-146 5.53e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 98.16  E-value: 5.53e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   3 PYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMAGH 82
Cdd:MTH00175  103 PYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGH 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2554484949  83 TLLKVIAGFAWSMLnVNGFIFIAHFiPLILLVILIGLEFAVAIIQAYVFTILTCMYINDALNLH 146
Cdd:MTH00175  183 LLFAILSGFAFNML-SNGLIILSLF-PMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGDTIALH 244
ATP-synt_A pfam00119
ATP synthase A chain;
3-140 1.06e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 94.09  E-value: 1.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   3 PYSFTLTSQLIVTFTLALTIYIGFNIIGIKKH--KKHFLNLLLPSGSsIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHglGGYFKKLFVPPVP-LPLVPLLLPIEIISEFARPVSLSLRLFGNMLA 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIAHFiplILLVILIGLEFAVAIIQAYVFTILTCMYIN 140
Cdd:pfam00119 160 GHLLLLLLAGLIFALLSAGFLLGVIPP---LLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 3-146 6.09e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 92.41  E-value: 6.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   3 PYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMAGH 82
Cdd:MTH00172   92 PYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGH 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2554484949  83 TLLKVIAGFAWSMLNVNGFifiAHFIPLILLVILIGLEFAVAIIQAYVFTILTCMYINDALNLH 146
Cdd:MTH00172  172 LLFAILAGFGFNMLCASGF---LSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTIVLH 232
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-141 7.08e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 89.46  E-value: 7.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00157   87 LFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIA 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIahfiplILLVILIGLEFAVAIIQAYVFTILTCMYIND 141
Cdd:MTH00157  167 GHLLLTLLGNTGPSLSSMILSILI------LIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 1-144 4.32e-22

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: 87.05  E-value: 4.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKH--KKHFLNLLLPSGssIFLVPLLVPLELISYIFRVISLPVRLFANM 78
Cdd:COG0356    76 LIPGLFPPTADINVTLALALIVFVLVHYYGIKKKglGGYLKHLFFPPF--PWLAPLMLPIEIISELARPLSLSLRLFGNM 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2554484949  79 MAGHTLLKVIAGFAWSMLNVNGFIFIAhfiplillVILIGLEFAVAIIQAYVFTILTCMYINDALN 144
Cdd:COG0356   154 FAGHIILLLLAGLAPFLLLGVLSLLLP--------VAWTAFELLVGFLQAYIFTMLTAVYISLAVE 211
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 1-146 7.56e-19

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 79.07  E-value: 7.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIP-YSFTLTSQLIVTFTLALTIYIGFNIIGIKKHK-KHFLNLLLPSGSSIFLVPLLvplelISYIFRVISLPVRLFANM 78
Cdd:PRK05815   91 LIPyLLFPPTADINVTLALALIVFVLVIYYGIKKKGlGGYLKEFYLQPHPLLLPIEI-----ISEFSRPISLSLRLFGNM 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2554484949  79 MAGHTLLKVIAGFAWSMLNVNGFIFIAHFiplillvILIGLEFAVAIIQAYVFTILTCMYINDALNLH 146
Cdd:PRK05815  166 LAGELILALIALLGGAGLLLALAPLILPV-------AWTIFEIFVGTLQAYIFMMLTIVYISMAVEEE 226
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-141 2.36e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 77.77  E-value: 2.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00176   90 LIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSA 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFiahFIPLILLVILIGLEFAVAIIQAYVFTILTCMYIND 141
Cdd:MTH00176  170 GHLLLGLLGAAMWGLLPVSPLIG---FLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 1-146 6.38e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 77.29  E-value: 6.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00174  109 LFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISS 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNgfIFIAHFIPLILLVILIGLEFAVAIIQAYVFTILTCMYINDALNLH 146
Cdd:MTH00174  189 GHLLFSIIASFAWKMINTG--ILIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTVELH 252
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-143 2.73e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 74.98  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00179   88 LLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRLTANITA 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFiahFIPLILLVILIGLEFAVAIIQAYVFTILTCMYINDAL 143
Cdd:MTH00179  168 GHLLMHLISSAVFVLMNFMGMVA---LLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-141 2.91e-16

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 72.29  E-value: 2.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00101   87 LLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITA 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNgfiFIAHFIPLILLVILIGLEFAVAIIQAYVFTILTCMYIND 141
Cdd:MTH00101  167 GHLLIHLIGGATLALMSIS---TTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-141 1.19e-14

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 67.97  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00173   90 LLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISA 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIahFIPLILLVILIGLEFAVAIIQAYVFTILTCMYIND 141
Cdd:MTH00173  170 GHIVLTLIGNYLSSSLFSSSVVSL--LLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-138 3.05e-14

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 66.77  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00120   88 LLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTANLTA 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIahfIPLILLVILIGLEFAVAIIQAYVFTILTCMY 138
Cdd:MTH00120  168 GHLLIQLISTATLNLLPTMPTLSL---LTLIILLLLTILELAVAMIQAYVFVLLLSLY 222
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-138 9.01e-14

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 65.66  E-value: 9.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00132   88 LLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTA 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIahfIPLILLVILIGLEFAVAIIQAYVFTILTCMY 138
Cdd:MTH00132  168 GHLLIQLIATAAFVLLPLMPTVAI---LTATLLFLLTLLEVAVAMIQAYVFVLLLSLY 222
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-139 7.80e-13

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 63.07  E-value: 7.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00035   91 LFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTA 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIahfiPLILLVILIGLEFAVAIIQAYVFTILTCMYI 139
Cdd:MTH00035  171 GHLLIFLLSTAIWELSNSPLISII----TLIIFFLLFILEIGVACIQAYVFTALVHFYL 225
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-141 2.85e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 61.67  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00005   92 LLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSA 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIahfIPLILLVILIGLEFAVAIIQAYVFTILTCMYIND 141
Cdd:MTH00005  172 GHIVLSLIGIYAASALFSSISSTI---LLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-139 3.99e-12

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 61.14  E-value: 3.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELISYIFRVISLPVRLFANMMA 80
Cdd:MTH00073   88 LLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTANLTA 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2554484949  81 GHTLLKVIAGFAWSMLNVNGFIFIAHFiplILLVILIGLEFAVAIIQAYVFTILTCMYI 139
Cdd:MTH00073  168 GHLLIQLISTATLVLLPLMPTVSILTM---IVLFLLTLLEIAVAMIQAYVFVLLLSLYL 223
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 1-143 6.40e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 44.35  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   1 MIPYSFTLTSQLIVTFTLAL-----TIYIGFNIIGIKKHKKHflnllLPSGSSIFLVPLLVPLELISYIFRVISLPVRLF 75
Cdd:PRK13419  189 LVPYGATATGNINVTLTLAVftffiTQYAAIKAHGIKGYLAH-----LTGGTHWSLWIIMIPIEFIGLFTKPFALTVRLF 263

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2554484949  76 ANMMAGHTLLkviagfawsmLNVNGFIFI------AHFIPLILLVILIGLEFAVAIIQAYVFTILTCMYINDAL 143
Cdd:PRK13419  264 ANMTAGHIVI----------LSLIFISFIlksyivAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFIGLAT 327
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 7-146 3.27e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 36.41  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554484949   7 TLTSQLIVTFTLALTIYIGFNIIGIKKHKKHFLNLLLPSGSSIFLVPLLVPLELI-SYIFRVISLPVRLFANMMAGHTLL 85
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554484949  86 KVIAGFAWsMLNVNGFIFIAhfipLILLVILIGLEFAVAIIQAYVFTILTCMYINDALNLH 146
Cdd:PRK13417  297 LALMGFIF-QFQSWGIVPVS----VIGSGLIYVLEIFVAFLQAYIFVLLTSLFVGLSMHRH 352
 
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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