|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
4.35e-112 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 320.28 E-value: 4.35e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFL 80
Cdd:MTH00132 1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 81 ISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVR 160
Cdd:MTH00132 81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18138244 161 LTANLTAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
2-226 |
1.96e-47 |
|
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: 155.83 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 2 ILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTNRWVI-NRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFL 80
Cdd:TIGR01131 2 FSQFDISPITLFSLTLLSLILLLSLLIFLISSSLSRWLIpSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 81 ISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVR 160
Cdd:TIGR01131 82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18138244 161 LTANLTAGHLLMQLIATAVFYLLTtlPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
66-224 |
3.32e-36 |
|
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: 124.82 E-value: 3.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 66 GHKWAAILTTMLIFLISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVII 145
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18138244 146 ETISLFIRPIALGVRLTANLTAGHLLMQLIATAVFYLLTtlpSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQ 224
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLS---SVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
14-224 |
9.92e-33 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 117.59 E-value: 9.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 14 LLGMPLIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSP-GHKWAAILTTMLIFLI---SLNLLGLL 89
Cdd:pfam00119 1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKkGRKFFPLLLTLFFFILvsnLLGLIPKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 90 PYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTS-LGHLLPEGTPTLLIPALVIIETISLFIRPIALGVRLTANLTAG 168
Cdd:pfam00119 81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18138244 169 HLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
19-225 |
6.38e-23 |
|
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: 92.06 E-value: 6.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 19 LIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFLISLNLLGLLPYTFTPTTQ 98
Cdd:COG0356 7 WLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 99 LSMNVSLAIPMWLATVLIGLRNQPTTS-LGHLLPEGTPtLLIPALVIIETISLFIRPIALGVRLTANLTAGHLLMQLIAT 177
Cdd:COG0356 87 INVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18138244 178 AVFYLLTtlpsiAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:COG0356 166 LAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
4.35e-112 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 320.28 E-value: 4.35e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFL 80
Cdd:MTH00132 1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 81 ISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVR 160
Cdd:MTH00132 81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18138244 161 LTANLTAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
|
|
| ATP6 |
MTH00073 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
2.01e-107 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177144 Cd Length: 227 Bit Score: 308.43 E-value: 2.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFL 80
Cdd:MTH00073 1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 81 ISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVR 160
Cdd:MTH00073 81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18138244 161 LTANLTAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQENT 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
|
|
| ATP6 |
MTH00120 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
1.18e-104 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177181 Cd Length: 227 Bit Score: 301.36 E-value: 1.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFL 80
Cdd:MTH00120 1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 81 ISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVR 160
Cdd:MTH00120 81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18138244 161 LTANLTAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQENT 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
|
|
| ATP6 |
MTH00179 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
6.13e-86 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177230 Cd Length: 227 Bit Score: 254.10 E-value: 6.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFL 80
Cdd:MTH00179 1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 81 ISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVR 160
Cdd:MTH00179 81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18138244 161 LTANLTAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQENT 227
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
|
|
| ATP6 |
MTH00101 |
ATP synthase F0 subunit 6; Validated |
6-227 |
2.82e-80 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177163 Cd Length: 226 Bit Score: 239.47 E-value: 2.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 6 FDQFLSPTLLGMPLIILAIVFPWILYPSqTNRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFLISLNL 85
Cdd:MTH00101 6 FASFITPTILGLPIVTLIIMFPSLLFPT-PNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIGSTNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 86 LGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVRLTANL 165
Cdd:MTH00101 85 LGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18138244 166 TAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQENT 227
Cdd:MTH00101 165 TAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
|
|
| ATP6 |
MTH00035 |
ATP synthase F0 subunit 6; Validated |
1-226 |
5.09e-51 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177110 Cd Length: 229 Bit Score: 165.15 E-value: 5.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGMPLIILAIVFP--WILYPSQTNrWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLI 78
Cdd:MTH00035 3 INNSIFGQFSPDTILFIPLTLLSSVIAlsWLFFINPTN-WLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 79 FLISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALG 158
Cdd:MTH00035 82 LILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18138244 159 VRLTANLTAGHLLMQLIATAVfYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:MTH00035 162 LRLAANLTAGHLLIFLLSTAI-WELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
2-226 |
1.96e-47 |
|
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: 155.83 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 2 ILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTNRWVI-NRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFL 80
Cdd:TIGR01131 2 FSQFDISPITLFSLTLLSLILLLSLLIFLISSSLSRWLIpSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 81 ISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVR 160
Cdd:TIGR01131 82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18138244 161 LTANLTAGHLLMQLIATAVFYLLTtlPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
|
|
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
90-225 |
2.97e-40 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 137.22 E-value: 2.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 90 PYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVRLTANLTAGH 169
Cdd:MTH00157 89 PYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGH 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 18138244 170 LLMQLIATAVFYLLTTLPSIailTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:MTH00157 169 LLLTLLGNTGPSLSSMILSI---LILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
|
|
| ATP6 |
MTH00176 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
2.68e-37 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214449 Cd Length: 229 Bit Score: 130.15 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGMPLIILAIVFPWI-LYPSQTNRWVI-NRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLI 78
Cdd:MTH00176 1 MLVDLFSSFDPPNKNIFSMISLSWITLLLfLLLMPSSVWFCpSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 79 FLISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALG 158
Cdd:MTH00176 81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18138244 159 VRLTANLTAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQENT 227
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
|
|
| ATP6 |
MTH00173 |
ATP synthase F0 subunit 6; Provisional |
2-225 |
3.64e-37 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214448 Cd Length: 231 Bit Score: 129.60 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 2 ILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTnRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFLI 81
Cdd:MTH00173 5 LFSSFDDHNSSFSSLSFLMWLLSLMSLFFFSSSV-WVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 82 SLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVRL 161
Cdd:MTH00173 84 SLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18138244 162 TANLTAGHLLMQLIATAVFYLLTTLPS-IAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:MTH00173 164 LANISAGHIVLTLIGNYLSSSLFSSSVvSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
66-224 |
3.32e-36 |
|
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: 124.82 E-value: 3.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 66 GHKWAAILTTMLIFLISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVII 145
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18138244 146 ETISLFIRPIALGVRLTANLTAGHLLMQLIATAVFYLLTtlpSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQ 224
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLS---SVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
14-224 |
9.92e-33 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 117.59 E-value: 9.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 14 LLGMPLIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSP-GHKWAAILTTMLIFLI---SLNLLGLL 89
Cdd:pfam00119 1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKkGRKFFPLLLTLFFFILvsnLLGLIPKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 90 PYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTS-LGHLLPEGTPTLLIPALVIIETISLFIRPIALGVRLTANLTAG 168
Cdd:pfam00119 81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18138244 169 HLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| ATP6 |
MTH00005 |
ATP synthase F0 subunit 6; Provisional |
2-227 |
1.06e-29 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 164583 Cd Length: 231 Bit Score: 110.21 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 2 ILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTNRWVI-NRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFL 80
Cdd:MTH00005 5 IFSSFDPATNSLFNNLSSTAFWAFNFSIILLLSSSFWITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 81 ISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVR 160
Cdd:MTH00005 85 ILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18138244 161 LTANLTAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQENT 227
Cdd:MTH00005 165 LAANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
|
|
| ATP6 |
MTH00172 |
ATP synthase F0 subunit 6; Provisional |
1-223 |
2.02e-29 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214447 Cd Length: 232 Bit Score: 109.75 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGM--PLIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLI 78
Cdd:MTH00172 1 MSSSYFDQFNIVWLIGLtnSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 79 FLISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALG 158
Cdd:MTH00172 81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18138244 159 VRLTANLTAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYL 223
Cdd:MTH00172 161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
|
|
| ATP6 |
MTH00175 |
ATP synthase F0 subunit 6; Provisional |
1-223 |
2.94e-29 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177228 Cd Length: 244 Bit Score: 109.71 E-value: 2.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGMP---------------LIILAIVFPWILYpsQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSP 65
Cdd:MTH00175 1 MLAAYFDQFNIIRLITIQaflgdwlvtftnssmMMVLAVIIFWLLL--KGDKLIPNRWQSIMELIYLNIRSVVHDNLGKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 66 GHKWAAILTTMLIFLISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVII 145
Cdd:MTH00175 79 GQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18138244 146 ETISLFIRPIALGVRLTANLTAGHLLMQLIATAVFYLLTT-LPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYL 223
Cdd:MTH00175 159 ETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYL 237
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
19-225 |
6.38e-23 |
|
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: 92.06 E-value: 6.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 19 LIILAIVFPWILYPSQTNRWVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFLISLNLLGLLPYTFTPTTQ 98
Cdd:COG0356 7 WLAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 99 LSMNVSLAIPMWLATVLIGLRNQPTTS-LGHLLPEGTPtLLIPALVIIETISLFIRPIALGVRLTANLTAGHLLMQLIAT 177
Cdd:COG0356 87 INVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18138244 178 AVFYLLTtlpsiAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:COG0356 166 LAPFLLL-----GVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
|
|
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
1-225 |
1.59e-18 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 80.61 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 1 MILSFFDQFLSPTLLGMPLIILAIVFPWILYPSQTNRwVINRLSSIQNWLVLLVTKQLLQPVNSPGHKWAAILTTMLIFL 80
Cdd:PRK05815 5 LIIGFGGFNFDSLLLSVLLGVLILLLFALVATRKLSG-VPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 81 ISLNLLGLLP-YTFTPTTQLSMNVSLAIPMWLATVLIGLRNQpttSLGHLLPEGTPTLlIPALVIIETISLFIRPIALGV 159
Cdd:PRK05815 84 LLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18138244 160 RLTANLTAGHLLMQLIATAVFYLLTtlpsIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:PRK05815 160 RLFGNMLAGELILALIALLGGAGLL----LALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
|
|
| ATP6 |
MTH00174 |
ATP synthase F0 subunit 6; Provisional |
66-225 |
2.77e-18 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 133799 Cd Length: 252 Bit Score: 80.75 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 66 GHKWAAILTTMLIFLISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVII 145
Cdd:MTH00174 87 GGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTII 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 146 ETISLFIRPIALGVRLTANLTAGHLLMQLIATAVFYLLTTLPSI-AILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQ 224
Cdd:MTH00174 167 ETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLR 246
|
.
gi 18138244 225 E 225
Cdd:MTH00174 247 D 247
|
|
| PRK13419 |
PRK13419 |
F0F1 ATP synthase subunit A; Provisional |
73-223 |
3.89e-12 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237381 Cd Length: 342 Bit Score: 64.38 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 73 LTTMLIFLISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFI 152
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFT 253
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18138244 153 RPIALGVRLTANLTAGHLLMQLIATAVFYLLTTLPSIAILTFIVLFLLtILELAVAMIQAYVFVLLLTLYL 223
Cdd:PRK13419 254 KPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVSVPFAIFIY-LLELFVAFLQAYIFTMLSALFI 323
|
|
| PRK13417 |
PRK13417 |
F0F1 ATP synthase subunit A; Provisional |
94-223 |
2.51e-10 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237380 Cd Length: 352 Bit Score: 59.13 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 94 TPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETI-SLFIRPIALGVRLTANLTAGHLLm 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVI- 295
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 18138244 173 qLIATAVFYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYL 223
Cdd:PRK13417 296 -ILALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
|
|
| ATP6 |
MTH00087 |
ATP synthase F0 subunit 6; Provisional |
90-225 |
1.21e-09 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177152 Cd Length: 195 Bit Score: 55.75 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 90 PYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSlgHLLPEGTPTLLIP-ALVIIETISLFIRPIALGVRLTANLTAG 168
Cdd:MTH00087 72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 18138244 169 HLLMQLIAtavfyllttlpSIAILTFIVLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:MTH00087 150 HLISSLLN-----------FLGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
|
|
| ATP6 |
MTH00050 |
ATP synthase F0 subunit 6; Validated |
90-214 |
1.15e-03 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177125 Cd Length: 170 Bit Score: 38.33 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 90 PYTFTPTTQLSMNVSLAIPMWLATVLIGLRNQPTTSLGHLLPEGTPTLLIPALVIIETISLFIRPIALGVRLTANLTAGH 169
Cdd:MTH00050 43 PYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGC 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 18138244 170 LLMqliatavfYLLTTLPSIAILTFIVLFLLTILELAVAMIQAYV 214
Cdd:MTH00050 123 FGG--------VALGNLCFISYWWFLVLFFLFFYEVFVALVHWFI 159
|
|
| PRK13421 |
PRK13421 |
F0F1 ATP synthase subunit A; Provisional |
42-218 |
6.47e-03 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237383 Cd Length: 223 Bit Score: 36.60 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 42 RLSSIQNWLVLLVT---KQLLQPVNSPGHKWAAILTTMLIFLISLNLLGLLPYTFTPTTQLSMNVSLAIPMWLATVLIGL 118
Cdd:PRK13421 47 APGRLQSVLELVVTtidAQIRDTMQTDPAPYRALIGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18138244 119 RNQPTTslGHLLPEGTPTLLIPALVIIETISlfiRPIALGVRLTANLTAGHLLMQlIATAVFYLLTTLPSIAiltfivlf 198
Cdd:PRK13421 127 RARGVR--GYLATFAEPTWVMIPLNLVEQLT---RTFSLIVRLFGNVMSGVFVIG-IVLSLAGLLVPIPLMA-------- 192
|
170 180
....*....|....*....|
gi 18138244 199 lltiLELAVAMIQAYVFVLL 218
Cdd:PRK13421 193 ----LDLLTGAVQAYIFAVL 208
|
|
|