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Conserved domains on  [gi|1904806547|ref|YP_009919796|]
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Atp6 (mitochondrion) [Metschnikowia agaves]

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 ...
50-243 2.45e-45

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: 151.20  E-value: 2.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  50 KLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTML 129
Cdd:TIGR01131  38 WLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTIS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 130 GFVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIGfslgfIP 209
Cdd:TIGR01131 118 GFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSSAIFA-----LL 192
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1904806547 210 IMGVIAIVILEFAISMIQAYVFCITLSGYLKDAI 243
Cdd:TIGR01131 193 LLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
 
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 ...
50-243 2.45e-45

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: 151.20  E-value: 2.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  50 KLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTML 129
Cdd:TIGR01131  38 WLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTIS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 130 GFVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIGfslgfIP 209
Cdd:TIGR01131 118 GFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSSAIFA-----LL 192
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1904806547 210 IMGVIAIVILEFAISMIQAYVFCITLSGYLKDAI 243
Cdd:TIGR01131 193 LLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
1-246 7.15e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 142.84  E-value: 7.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547   1 MMNSPLEQFEMKSLLTMNNMYMFSMSNYVLYLMLVSMMMMMYMVSLSKTKLMYNRWGLVMLSMYDTMLNMMKSQMGMRGG 80
Cdd:MTH00175    1 MLAAYFDQFNIIRLITIQAFLGDWLVTFTNSSMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  81 YYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVLIET 160
Cdd:MTH00175   81 KYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIET 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 161 LSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIgfSLGFIPIMGVIAIVILEFAISMIQAYVFCITLSGYLK 240
Cdd:MTH00175  161 LSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNGLI--ILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLG 238

                  ....*.
gi 1904806547 241 DAIYLH 246
Cdd:MTH00175  239 DTIALH 244
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
82-240 3.85e-33

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: 117.50  E-value: 3.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  82 YFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVLIETL 161
Cdd:cd00310     4 YLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELI 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904806547 162 SYSSRAISLGLRLSSNILAGHLTMLILGSLilslmnSSLIGFSLGFIPIMGVIAIVILEFAISMIQAYVFCITLSGYLK 240
Cdd:cd00310    84 SELIRPLSLSVRLFANMFAGHLLLALLSGL------VPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
54-240 1.01e-31

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 115.66  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  54 NRWGLVMLSMYDTMLNMMKSQMGMRGGY-YFPLMFTLFNFMLMANLMSMM---PYTFAMSAQMVFMMSLSLTLWLGLTML 129
Cdd:pfam00119  28 GRLQNFVEMLVEFVDNIVKDNIGKKKGRkFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 130 GFVNHGLN--FFSLFVPtGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNsslIGFSLGF 207
Cdd:pfam00119 108 GIKKHGLGgyFKKLFVP-PVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLS---AGFLLGV 183
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1904806547 208 IPIMGVIAIVILEFAISMIQAYVFCITLSGYLK 240
Cdd:pfam00119 184 IPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
48-243 3.84e-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: 90.52  E-value: 3.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  48 KTKLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLT 127
Cdd:COG0356    23 KLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVH 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 128 MLGFVNHGLNFF--SLFVPTGTPLAlvPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSlmnssligFSL 205
Cdd:COG0356   103 YYGIKKKGLGGYlkHLFFPPFPWLA--PLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPF--------LLL 172
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1904806547 206 GFIPIMGVIAIVILEFAISMIQAYVFCITLSGYLKDAI 243
Cdd:COG0356   173 GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAV 210
 
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 ...
50-243 2.45e-45

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: 151.20  E-value: 2.45e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  50 KLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTML 129
Cdd:TIGR01131  38 WLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTIS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 130 GFVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIGfslgfIP 209
Cdd:TIGR01131 118 GFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSSAIFA-----LL 192
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1904806547 210 IMGVIAIVILEFAISMIQAYVFCITLSGYLKDAI 243
Cdd:TIGR01131 193 LLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
1-246 7.15e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 142.84  E-value: 7.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547   1 MMNSPLEQFEMKSLLTMNNMYMFSMSNYVLYLMLVSMMMMMYMVSLSKTKLMYNRWGLVMLSMYDTMLNMMKSQMGMRGG 80
Cdd:MTH00175    1 MLAAYFDQFNIIRLITIQAFLGDWLVTFTNSSMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  81 YYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVLIET 160
Cdd:MTH00175   81 KYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIET 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 161 LSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIgfSLGFIPIMGVIAIVILEFAISMIQAYVFCITLSGYLK 240
Cdd:MTH00175  161 LSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNGLI--ILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLG 238

                  ....*.
gi 1904806547 241 DAIYLH 246
Cdd:MTH00175  239 DTIALH 244
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
49-246 1.55e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 136.71  E-value: 1.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  49 TKLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTM 128
Cdd:MTH00172   38 IKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 129 LGFVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIgfsLGFI 208
Cdd:MTH00172  118 AGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNMLCASGF---LSLF 194
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1904806547 209 PIMGVIAIVILEFAISMIQAYVFCITLSGYLKDAIYLH 246
Cdd:MTH00172  195 PLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTIVLH 232
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
82-240 3.85e-33

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: 117.50  E-value: 3.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  82 YFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVLIETL 161
Cdd:cd00310     4 YLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELI 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904806547 162 SYSSRAISLGLRLSSNILAGHLTMLILGSLilslmnSSLIGFSLGFIPIMGVIAIVILEFAISMIQAYVFCITLSGYLK 240
Cdd:cd00310    84 SELIRPLSLSVRLFANMFAGHLLLALLSGL------VPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
54-240 1.01e-31

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 115.66  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  54 NRWGLVMLSMYDTMLNMMKSQMGMRGGY-YFPLMFTLFNFMLMANLMSMM---PYTFAMSAQMVFMMSLSLTLWLGLTML 129
Cdd:pfam00119  28 GRLQNFVEMLVEFVDNIVKDNIGKKKGRkFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 130 GFVNHGLN--FFSLFVPtGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNsslIGFSLGF 207
Cdd:pfam00119 108 GIKKHGLGgyFKKLFVP-PVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLS---AGFLLGV 183
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1904806547 208 IPIMGVIAIVILEFAISMIQAYVFCITLSGYLK 240
Cdd:pfam00119 184 IPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
54-239 4.03e-27

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 104.28  E-value: 4.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  54 NRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVN 133
Cdd:MTH00035   44 SRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 134 HGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIgfslGFIPIMGV 213
Cdd:MTH00035  124 AFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAIWELSNSPLI----SIITLIIF 199
                         170       180
                  ....*....|....*....|....*.
gi 1904806547 214 IAIVILEFAISMIQAYVFCITLSGYL 239
Cdd:MTH00035  200 FLLFILEIGVACIQAYVFTALVHFYL 225
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
19-246 5.39e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 104.25  E-value: 5.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  19 NMYMFSMSNYVLYLMLVSMMMMMYMVSLSKTKLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANL 98
Cdd:MTH00174   27 NGEFFCFTNTFFMMSFAVFLFYTIGAKGNNNTLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  99 MSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNI 178
Cdd:MTH00174  107 LGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANI 186
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904806547 179 LAGHLTMLILGSLILSLMNSSLIGFSlgFIPIMGVIAIVILEFAISMIQAYVFCITLSGYLKDAIYLH 246
Cdd:MTH00174  187 SSGHLLFSIIASFAWKMINTGILIGS--FVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTVELH 252
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
51-238 3.75e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 101.40  E-value: 3.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  51 LMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLG 130
Cdd:MTH00157   37 LIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFG 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 131 FVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIGFslgfipI 210
Cdd:MTH00157  117 WINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSMILSIL------I 190
                         170       180
                  ....*....|....*....|....*...
gi 1904806547 211 MGVIAIVILEFAISMIQAYVFCITLSGY 238
Cdd:MTH00157  191 LIQILLLILESAVAIIQSYVFSVLSTLY 218
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
50-239 6.88e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 100.79  E-value: 6.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  50 KLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTML 129
Cdd:MTH00179   37 RWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLY 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 130 GFVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIgfsLGFIP 209
Cdd:MTH00179  117 GLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRLTANITAGHLLMHLISSAVFVLMNFMGM---VALLT 193
                         170       180       190
                  ....*....|....*....|....*....|
gi 1904806547 210 IMGVIAIVILEFAISMIQAYVFCITLSGYL 239
Cdd:MTH00179  194 LLVLFLLTLLEVAVAMIQAYVFVLLLSLYL 223
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
84-241 8.26e-23

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 92.87  E-value: 8.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  84 PLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVLIETLSY 163
Cdd:MTH00005   75 SLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISI 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904806547 164 SSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIGFSLGFIPIMGVIaivILEFAISMIQAYVFCITLSGYLKD 241
Cdd:MTH00005  155 LVRPITLSFRLAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYI---LFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
85-241 1.31e-22

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 91.94  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  85 LMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYS 164
Cdd:MTH00101   71 MLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLF 150
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1904806547 165 SRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIGFSLGFIPImgvIAIVILEFAISMIQAYVFCITLSGYLKD 241
Cdd:MTH00101  151 IQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTALITFIIL---ILLTILEFAVALIQAYVFTLLVSLYLHD 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
48-243 3.84e-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: 90.52  E-value: 3.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  48 KTKLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLT 127
Cdd:COG0356    23 KLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVH 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 128 MLGFVNHGLNFF--SLFVPTGTPLAlvPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSlmnssligFSL 205
Cdd:COG0356   103 YYGIKKKGLGGYlkHLFFPPFPWLA--PLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPF--------LLL 172
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1904806547 206 GFIPIMGVIAIVILEFAISMIQAYVFCITLSGYLKDAI 243
Cdd:COG0356   173 GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAV 210
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
79-239 1.01e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 89.93  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  79 GGYYFPLMFT-LFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVL 157
Cdd:MTH00132   65 GGHKWALLLTsLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLII 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 158 IETLSYSSRAISLGLRLSSNILAGHLTMLILgslilslmnsSLIGFSLgfIPIMGVIAIV---------ILEFAISMIQA 228
Cdd:MTH00132  145 IETISLFIRPLALGVRLTANLTAGHLLIQLI----------ATAAFVL--LPLMPTVAILtatllflltLLEVAVAMIQA 212
                         170
                  ....*....|.
gi 1904806547 229 YVFCITLSGYL 239
Cdd:MTH00132  213 YVFVLLLSLYL 223
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
48-246 1.91e-21

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 89.08  E-value: 1.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  48 KTKLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMP-YTFAMSAQMVFMMSLSLTLWLGL 126
Cdd:PRK05815   38 KLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 127 TMLGFVNHGL-NFFSLFVPTGTPLalvpvLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILslmnsslIGFSL 205
Cdd:PRK05815  118 IYYGIKKKGLgGYLKEFYLQPHPL-----LLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGG-------AGLLL 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1904806547 206 GFIPIMGVIAIVILEFAISMIQAYVFCITLSGYLKDAIYLH 246
Cdd:PRK05815  186 ALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEE 226
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
51-232 2.92e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 88.77  E-value: 2.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  51 LMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLG 130
Cdd:MTH00173   40 VSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 131 FVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIGFSLGFIPI 210
Cdd:MTH00173  120 LFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLI 199
                         170       180
                  ....*....|....*....|..
gi 1904806547 211 MGViaIVILEFAISMIQAYVFC 232
Cdd:MTH00173  200 QVG--YFIFEVAVMLIQAYIFT 219
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
58-241 3.11e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 88.55  E-value: 3.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  58 LVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLN 137
Cdd:MTH00176   47 VFMLMFSTFLPEMILRSNGSYILGSASIIISLFILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 138 FFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIGFSLGFIPimgVIAIV 217
Cdd:MTH00176  127 RLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIV---QILYF 203
                         170       180
                  ....*....|....*....|....
gi 1904806547 218 ILEFAISMIQAYVFCITLSGYLKD 241
Cdd:MTH00176  204 MFEIAVCMIQAYVFTLLLSLYLDE 227
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
48-239 4.62e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 87.96  E-value: 4.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  48 KTKLMYNRWGLVMLSMYDTMLNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLT 127
Cdd:MTH00120   35 KNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 128 MLGFVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLigfSLGF 207
Cdd:MTH00120  115 LTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTANLTAGHLLIQLISTATLNLLPTMP---TLSL 191
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1904806547 208 IPIMGVIAIVILEFAISMIQAYVFCITLSGYL 239
Cdd:MTH00120  192 LTLIILLLLTILELAVAMIQAYVFVLLLSLYL 223
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
80-241 2.67e-20

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 85.79  E-value: 2.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  80 GYYFPLMFT-LFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVLI 158
Cdd:MTH00073   66 GHKWALILTsLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIII 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 159 ETLSYSSRAISLGLRLSSNILAGHLTMLILGSLILSLMNSSLIGFSLGFIPImgvIAIVILEFAISMIQAYVFCITLSGY 238
Cdd:MTH00073  146 ETISLFIRPLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVL---FLLTLLEIAVAMIQAYVFVLLLSLY 222

                  ...
gi 1904806547 239 LKD 241
Cdd:MTH00073  223 LQE 225
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
68-231 1.87e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 47.82  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  68 LNMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMPYTFAMSAQMVFMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGT 147
Cdd:PRK13419  156 LDVAKSNIGHGYEKFLPYLLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGT 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 148 PLALVPVLVLIETLSYSSRAISLGLRLSSNILAGHLTMLilgslilslmnsSLIGFSlgFI---PIMGV-------IAIV 217
Cdd:PRK13419  236 HWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGHIVIL------------SLIFIS--FIlksYIVAVavsvpfaIFIY 301
                         170
                  ....*....|....
gi 1904806547 218 ILEFAISMIQAYVF 231
Cdd:PRK13419  302 LLELFVAFLQAYIF 315
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
51-181 2.47e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 46.42  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  51 LMYNRWGLVMLSMYDTMLNMMKSQMgmrggYYFPLMFTLFNFMLManlmsMMPYTFAMSAQMVFMMSLSLTLWLGLTMLG 130
Cdd:MTH00050    1 MFVNDFSSLFSLIYKLILGGSVSYY-----YSVVLFIVLFLFLLY-----RLPYIYSPFLFVVFLFVVVFPLFISLFLSR 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1904806547 131 FVNHGLNFFSLFVPTGTPLALVPVLVLIETLSYSSRAISLGLRLSSNILAG 181
Cdd:MTH00050   71 VFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
69-246 2.49e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 44.50  E-value: 2.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547  69 NMMKSQMGMRGGYYFPLMFTLFNFMLMANLMSMMP----------------------------YTFA-------MSAQMV 113
Cdd:PRK13417  144 DIVDESMHGHGHSYYHYIFTLFFFILFCNLMGLVPsvgeltvvasdygglvalgvmdhtphalPTFAkvwsgitVTGDIS 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806547 114 FMMSLSLTLWLGLTMLGFVNHGLNFFSLFVPTGTPLALVPVLVLIE-TLSYSSRAISLGLRLSSNILAGHLTMLILGSLI 192
Cdd:PRK13417  224 VTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVIILALMGFI 303
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1904806547 193 LSLMNSSLIGFSlgfipIMGVIAIVILEFAISMIQAYVFCITLSGYLKDAIYLH 246
Cdd:PRK13417  304 FQFQSWGIVPVS-----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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