|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00101 |
ATP synthase F0 subunit 6; Validated |
1-226 |
1.82e-123 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177163 Cd Length: 226 Bit Score: 348.87 E-value: 1.82e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGIPIVIFIIMLPSIFFHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIG 80
Cdd:MTH00101 1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1236517338 161 TANITAGHLLIHLIGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
5-225 |
1.40e-46 |
|
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: 153.90 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 5 LFASFIIP--TIVGIPIVIFIIMLPS----IFFHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILF 78
Cdd:TIGR01131 1 LFSQFDISpiTLFSLTLLSLILLLSLliflISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAV 158
Cdd:TIGR01131 81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1236517338 159 RLTANITAGHLLIHLIGGATMVLTSISptVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
65-222 |
2.40e-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: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 65 GRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIII 144
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1236517338 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSIsptVSSITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
19-223 |
2.65e-31 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 114.12 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 19 IVIFIIMLPSIFFHNPYRLIGNRLMSLQQWLIKLVLKQMMA-MHNIKGRTWSLMLMSLILFIGSTNLLGLL---PHSFTP 94
Cdd:pfam00119 7 VALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 95 TTQLSMNLGMAIPLWAAAVITGFR-HKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHL 173
Cdd:pfam00119 87 TADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1236517338 174 IGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 167 LAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
64-224 |
3.18e-19 |
|
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: 82.04 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 64 KGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHK-MKASLAHFLPQGTPIPLIPMLI 142
Cdd:COG0356 53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPWLAPLMLP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 143 IiETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSISPTVssitfIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356 133 I-EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSL-----LLPVAWTAFELLVGFLQAYIFTMLTAVYI 206
|
..
gi 1236517338 223 HD 224
Cdd:COG0356 207 SL 208
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00101 |
ATP synthase F0 subunit 6; Validated |
1-226 |
1.82e-123 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177163 Cd Length: 226 Bit Score: 348.87 E-value: 1.82e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGIPIVIFIIMLPSIFFHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIG 80
Cdd:MTH00101 1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1236517338 161 TANITAGHLLIHLIGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
|
|
| ATP6 |
MTH00120 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
5.35e-80 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177181 Cd Length: 227 Bit Score: 238.96 E-value: 5.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGIPIVIFIIMLPSIFF-HNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFI 79
Cdd:MTH00120 1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIpSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00120 81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1236517338 160 LTANITAGHLLIHLIGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
|
|
| ATP6 |
MTH00073 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
1.31e-76 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177144 Cd Length: 227 Bit Score: 230.24 E-value: 1.31e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGIPIVIFIIMLPSIFFHNPY-RLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFI 79
Cdd:MTH00073 1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTnKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00073 81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1236517338 160 LTANITAGHLLIHLIGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
|
|
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
1-225 |
6.73e-74 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 223.60 E-value: 6.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGIPIVIFIIMLPSIFFHNPY-RLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFI 79
Cdd:MTH00132 1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTsRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00132 81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1236517338 160 LTANITAGHLLIHLIGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
|
|
| ATP6 |
MTH00179 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
3.49e-63 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177230 Cd Length: 227 Bit Score: 196.32 E-value: 3.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGIPIVIFIIMLPSIFFHNPY-RLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFI 79
Cdd:MTH00179 1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTnRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00179 81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1236517338 160 LTANITAGHLLIHLIGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
5-225 |
1.40e-46 |
|
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: 153.90 E-value: 1.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 5 LFASFIIP--TIVGIPIVIFIIMLPS----IFFHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILF 78
Cdd:TIGR01131 1 LFSQFDISpiTLFSLTLLSLILLLSLliflISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAV 158
Cdd:TIGR01131 81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1236517338 159 RLTANITAGHLLIHLIGGATMVLTSISptVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
|
|
| ATP6 |
MTH00035 |
ATP synthase F0 subunit 6; Validated |
1-225 |
4.51e-41 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177110 Cd Length: 229 Bit Score: 139.72 E-value: 4.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGIPIVIF--IIMLPSIFFHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILF 78
Cdd:MTH00035 3 INNSIFGQFSPDTILFIPLTLLssVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAV 158
Cdd:MTH00035 83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1236517338 159 RLTANITAGHLLIHLIGGATMVLTSiSPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
|
|
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
1-221 |
5.77e-37 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 128.75 E-value: 5.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGIPIVIFIIMLPSIFFHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIG 80
Cdd:MTH00157 1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00157 81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1236517338 161 TANITAGHLLIHLIGGATMVLTSISptvSSITFIILILLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSMI---LSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
65-222 |
2.40e-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: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 65 GRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIII 144
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1236517338 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSIsptVSSITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
|
|
| ATP6 |
MTH00176 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
2.49e-33 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214449 Cd Length: 229 Bit Score: 119.75 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGIPIVIFIIMLPSIF---FHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLIL 77
Cdd:MTH00176 1 MLVDLFSSFDPPNKNIFSMISLSWITLLLFlllMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALA 157
Cdd:MTH00176 81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1236517338 158 VRLTANITAGHLLIHLIGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
19-223 |
2.65e-31 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 114.12 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 19 IVIFIIMLPSIFFHNPYRLIGNRLMSLQQWLIKLVLKQMMA-MHNIKGRTWSLMLMSLILFIGSTNLLGLL---PHSFTP 94
Cdd:pfam00119 7 VALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksPGGFTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 95 TTQLSMNLGMAIPLWAAAVITGFR-HKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHL 173
Cdd:pfam00119 87 TADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLLLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1236517338 174 IGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 167 LAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| ATP6 |
MTH00173 |
ATP synthase F0 subunit 6; Provisional |
25-224 |
2.21e-30 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214448 Cd Length: 231 Bit Score: 111.88 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 25 MLPSIFFHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGM 104
Cdd:MTH00173 28 LMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 105 AIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSI 184
Cdd:MTH00173 108 ALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSSSLFS 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1236517338 185 SPTVSSITFIILILL-TILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173 188 SSVVSLLLVLLIQVGyFIFEVAVMLIQAYIFTLLIKLYSDE 228
|
|
| ATP6 |
MTH00005 |
ATP synthase F0 subunit 6; Provisional |
20-226 |
2.37e-26 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 164583 Cd Length: 231 Bit Score: 101.73 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 20 VIFIIMLPSIFFHNPyrligNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLS 99
Cdd:MTH00005 30 FSIILLLSSSFWITP-----NRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 100 MNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATM 179
Cdd:MTH00005 105 FTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIYAA 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1236517338 180 VLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005 185 SALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
|
|
| ATP6 |
MTH00172 |
ATP synthase F0 subunit 6; Provisional |
1-224 |
1.20e-23 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214447 Cd Length: 232 Bit Score: 94.34 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 1 MNENLFASFIIPTIVGI---PIVIFIIMLPSIFFHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLIL 77
Cdd:MTH00172 1 MSSSYFDQFNIVWLIGLtnsSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALA 157
Cdd:MTH00172 81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1236517338 158 VRLTANITAGHLLIHLIGGATMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172 161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
|
|
| ATP6 |
MTH00175 |
ATP synthase F0 subunit 6; Provisional |
19-224 |
1.93e-21 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177228 Cd Length: 244 Bit Score: 88.91 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 19 IVIFIIMLPSIFFHNPyRLIGNRLMSLQQwLIKLVLKQMMAMH-NIKGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQ 97
Cdd:MTH00175 34 MMVLAVIIFWLLLKGD-KLIPNRWQSIME-LIYLNIRSVVHDNlGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 98 LSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIGGA 177
Cdd:MTH00175 112 IIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGF 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1236517338 178 TM-VLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175 192 AFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
64-224 |
3.18e-19 |
|
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: 82.04 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 64 KGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHK-MKASLAHFLPQGTPIPLIPMLI 142
Cdd:COG0356 53 KGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFPWLAPLMLP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 143 IiETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSISPTVssitfIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:COG0356 133 I-EIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSL-----LLPVAWTAFELLVGFLQAYIFTMLTAVYI 206
|
..
gi 1236517338 223 HD 224
Cdd:COG0356 207 SL 208
|
|
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
10-224 |
1.61e-16 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 75.22 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 10 IIPTIVGIPIVIFIIMLPSIFFHNPYRLIGNRLMSLQQWLIKLVLKQMMAMHNIKGRTWSLMLMSLILFIGSTNLLGLLP 89
Cdd:PRK05815 14 FDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 90 -HSFTPTTQLSMNLGMAIPLWAAAVITGFR-HKMKASLAHFLPQGTPIPLIPmliiiETISLFIQPMALAVRLTANITAG 167
Cdd:PRK05815 94 yLLFPPTADINVTLALALIVFVLVIYYGIKkKGLGGYLKEFYLQPHPLLLPI-----EIISEFSRPISLSLRLFGNMLAG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1236517338 168 HLLIHLIGGatmvLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815 169 ELILALIAL----LGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
|
|
| PRK13419 |
PRK13419 |
F0F1 ATP synthase subunit A; Provisional |
72-222 |
1.86e-14 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237381 Cd Length: 342 Bit Score: 70.93 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 72 LMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFR-HKMKASLAHfLPQGTPIPLIPMLIIIETISLF 150
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1236517338 151 IQPMALAVRLTANITAGHLLIHLIGGATMVLTS--ISPTVSsitFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIVILSLIFISFILKSyiVAVAVS---VPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
|
|
| ATP6 |
MTH00174 |
ATP synthase F0 subunit 6; Provisional |
64-224 |
7.54e-13 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 133799 Cd Length: 252 Bit Score: 65.73 E-value: 7.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 64 KGRTWSLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLII 143
Cdd:MTH00174 86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 144 IETISLFIQPMALAVRLTANITAGHLLIHLIGGATMVLTSISPTVSSIT-FIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174 166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVpFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245
|
..
gi 1236517338 223 HD 224
Cdd:MTH00174 246 RD 247
|
|
| ATP6 |
MTH00087 |
ATP synthase F0 subunit 6; Provisional |
74-222 |
2.08e-07 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177152 Cd Length: 195 Bit Score: 49.59 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAAAVITGFRHKMKASlaHFLPQGT-PIPLIPMLIIIETISLFIQ 152
Cdd:MTH00087 57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSdSFLKTFSMLFVEIVSELSR 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 153 PMALAVRLTANITAGHLLIHLIGgatmvltsispTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087 135 PLALTLRLTVNLMVGHLISSLLN-----------FLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
|
|
| PRK13417 |
PRK13417 |
F0F1 ATP synthase subunit A; Provisional |
93-222 |
2.32e-05 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237380 Cd Length: 352 Bit Score: 44.50 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236517338 93 TPTTQLSMNLGMAIPLWAAAVITGFRHKMKASLAHFLPQGTPIPLIPMLIIIETI-SLFIQPMALAVRLTANITAGHLLI 171
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1236517338 172 HLIGGatMVLTSISPTVSSITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417 297 LALMG--FIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
|
|
|