|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
1-224 |
1.21e-102 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 295.92 E-value: 1.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 1 MMSNLFSVFDPSTSiMNYSFNWLSTFLGVLMIPLSYWLLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTLL 80
Cdd:MTH00157 1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 81 LYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAVR 160
Cdd:MTH00157 80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770691071 161 LAANMIAGHLLLTLLGNTGPYLNSSSLSILILAQLALLTLECAVSIIQAYVFAILITLYASEVN 224
Cdd:MTH00157 160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
5-224 |
8.79e-48 |
|
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: 156.60 E-value: 8.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 5 LFSVFDPSTSIM-NYSFNWLSTFLGVLMI----PLSYWLLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTL 79
Cdd:TIGR01131 1 LFSQFDISPITLfSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 80 LLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAV 159
Cdd:TIGR01131 81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770691071 160 RLAANMIAGHLLLTLLGNTGPYLNSSSL-SILILAQLALLTLECAVSIIQAYVFAILITLYASEVN 224
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIfALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
72-219 |
1.30e-39 |
|
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: 133.29 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 72 IFISLFTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTM 151
Cdd:cd00310 7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770691071 152 IRPGTLAVRLAANMIAGHLLLTLLGNTGPYLNSSSLSILILAQLALLTLECAVSIIQAYVFAILITLY 219
Cdd:cd00310 87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVY 154
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
22-219 |
2.41e-25 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 98.33 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 22 WLSTFLGVLMIPLSYW----LLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFI-SLFTLLLYNNFLGLL---PYVF 93
Cdd:pfam00119 5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPGGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 94 TSSSHLSMTLALALPLWLSFMLFGWINY-TQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAVRLAANMIAGHLLL 172
Cdd:pfam00119 85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1770691071 173 TLLGNTGPYLNSSSLSILILAQLALLTL---ECAVSIIQAYVFAILITLY 219
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPPLLGVAWtlfELLVAFIQAYVFTMLTAVY 214
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
24-219 |
5.79e-20 |
|
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440125 [Multi-domain] Cd Length: 212 Bit Score: 83.97 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 24 STFLGVLMIPLSYW------LLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTLLLYNNFLGLLPYVFTSSS 97
Cdd:COG0356 6 SWLAMLLLLLLFLLatrklkLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 98 HLSMTLALALPLWLSFMLF-----GWINYTQHMFAHLVPqgtpaALMPFMVCIETISTMIRPGTLAVRLAANMIAGHLLL 172
Cdd:COG0356 86 DINVTLALALIVFVLVHYYgikkkGLGGYLKHLFFPPFP-----WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1770691071 173 TLLGNTGPYLNSSSLSilILAQLALLTLECAVSIIQAYVFAILITLY 219
Cdd:COG0356 161 LLLAGLAPFLLLGVLS--LLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
1-224 |
1.21e-102 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 295.92 E-value: 1.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 1 MMSNLFSVFDPSTSiMNYSFNWLSTFLGVLMIPLSYWLLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTLL 80
Cdd:MTH00157 1 MMTNLFSIFDPSTS-FNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 81 LYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAVR 160
Cdd:MTH00157 80 LFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770691071 161 LAANMIAGHLLLTLLGNTGPYLNSSSLSILILAQLALLTLECAVSIIQAYVFAILITLYASEVN 224
Cdd:MTH00157 160 LAANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
|
|
| ATP6 |
MTH00176 |
ATP synthase F0 subunit 6; Provisional |
1-223 |
1.29e-50 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214449 Cd Length: 229 Bit Score: 164.05 E-value: 1.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 1 MMSNLFSVFDPSTSIM--NYSFNWLSTFLGVLMIPLSYWLLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFT 78
Cdd:MTH00176 1 MLVDLFSSFDPPNKNIfsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 79 LLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLA 158
Cdd:MTH00176 81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770691071 159 VRLAANMIAGHLLLTLLGNTGPYLNSSS---LSILILAQLALLTLECAVSIIQAYVFAILITLYASEV 223
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSpliGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
5-224 |
8.79e-48 |
|
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: 156.60 E-value: 8.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 5 LFSVFDPSTSIM-NYSFNWLSTFLGVLMI----PLSYWLLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTL 79
Cdd:TIGR01131 1 LFSQFDISPITLfSLTLLSLILLLSLLIFlissSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 80 LLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAV 159
Cdd:TIGR01131 81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770691071 160 RLAANMIAGHLLLTLLGNTGPYLNSSSL-SILILAQLALLTLECAVSIIQAYVFAILITLYASEVN 224
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIfALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
|
|
| ATP6 |
MTH00005 |
ATP synthase F0 subunit 6; Provisional |
1-222 |
2.86e-45 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 164583 Cd Length: 231 Bit Score: 150.65 E-value: 2.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 1 MMSNLFSVFDPSTSIMNYSFN----WLSTFLGVLMIPLSYWLLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISL 76
Cdd:MTH00005 1 MLTDIFSSFDPATNSLFNNLSstafWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 77 FTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGT 156
Cdd:MTH00005 81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770691071 157 LAVRLAANMIAGHLLLTLLG---NTGPYLNSSSLSILILAQLALLTLECAVSIIQAYVFAILITLYASE 222
Cdd:MTH00005 161 LSFRLAANMSAGHIVLSLIGiyaASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
|
|
| ATP6 |
MTH00173 |
ATP synthase F0 subunit 6; Provisional |
1-222 |
6.42e-42 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214448 Cd Length: 231 Bit Score: 141.93 E-value: 6.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 1 MMSNLFSVFDPSTSIM--NYSFNWLSTFLGVLMIPLSYWLLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFT 78
Cdd:MTH00173 1 MMVDLFSSFDDHNSSFssLSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 79 LLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLA 158
Cdd:MTH00173 81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770691071 159 VRLAANMIAGHLLLTLLGN--TGPYLNSSSLSILILAQLAL--LTLECAVSIIQAYVFAILITLYASE 222
Cdd:MTH00173 161 VRLLANISAGHIVLTLIGNylSSSLFSSSVVSLLLVLLIQVgyFIFEVAVMLIQAYIFTLLIKLYSDE 228
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
72-219 |
1.30e-39 |
|
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: 133.29 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 72 IFISLFTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTM 151
Cdd:cd00310 7 LLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISEL 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770691071 152 IRPGTLAVRLAANMIAGHLLLTLLGNTGPYLNSSSLSILILAQLALLTLECAVSIIQAYVFAILITLY 219
Cdd:cd00310 87 IRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVY 154
|
|
| ATP6 |
MTH00120 |
ATP synthase F0 subunit 6; Provisional |
1-222 |
8.62e-37 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177181 Cd Length: 227 Bit Score: 128.40 E-value: 8.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 1 MMSNLFSVFDpSTSIMNYSFNWLSTFLGVLMIPL-SYWLLPSRFTffwTSISNTLHNEFKTLLGPSLKGG---TFIFISL 76
Cdd:MTH00120 1 MNLNFFDQFS-SPELLGIPLILLAMLIPALLIPSpKNRLLTNRLT---TLQLWLIKLITKQLMLPLNKKGhkwALILTSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 77 FTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGT 156
Cdd:MTH00120 77 MLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770691071 157 LAVRLAANMIAGHLLLTLLGNTGPYLNSSSLSILILAQLALL---TLECAVSIIQAYVFAILITLYASE 222
Cdd:MTH00120 157 LGVRLTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLlltILELAVAMIQAYVFVLLLSLYLQE 225
|
|
| ATP6 |
MTH00179 |
ATP synthase F0 subunit 6; Provisional |
1-222 |
1.02e-36 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177230 Cd Length: 227 Bit Score: 128.14 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 1 MMSNLFSVFDpSTSIMNYSFNWLSTFLGVLMIPLSY-WLLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTL 79
Cdd:MTH00179 1 MMLSMFDQFE-SPSLLGIPLLALALLLPWLLFPSLTnRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 80 LLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAV 159
Cdd:MTH00179 80 LLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770691071 160 RLAANMIAGHLLLTLLGNTGPYLNSSSLSILILAQL---ALLTLECAVSIIQAYVFAILITLYASE 222
Cdd:MTH00179 160 RLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLvlfLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
|
|
| ATP6 |
MTH00035 |
ATP synthase F0 subunit 6; Validated |
3-222 |
6.42e-34 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177110 Cd Length: 229 Bit Score: 121.23 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 3 SNLFSVFDPSTsIMNYSFNWLSTFLGVLMIPLSY---WLlPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTL 79
Cdd:MTH00035 5 NSIFGQFSPDT-ILFIPLTLLSSVIALSWLFFINptnWL-PSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 80 LLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAV 159
Cdd:MTH00035 83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770691071 160 RLAANMIAGHLLLTLLGNTGPYLNSSSL--SILILAQLALLTLECAVSIIQAYVFAILITLYASE 222
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTAIWELSNSPLisIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
|
|
| ATP6 |
MTH00101 |
ATP synthase F0 subunit 6; Validated |
1-219 |
1.91e-32 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177163 Cd Length: 226 Bit Score: 117.36 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 1 MMSNLFSVFDPSTsIMNYSFNWLSTFLGVLMIPLSYWLLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTLL 80
Cdd:MTH00101 1 MNENLFASFITPT-ILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 81 LYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAVR 160
Cdd:MTH00101 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770691071 161 LAANMIAGHLLLTLLGNTGPYLNSSSLSILILAQLALL---TLECAVSIIQAYVFAILITLY 219
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILIlltILEFAVALIQAYVFTLLVSLY 221
|
|
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
72-222 |
6.62e-32 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 115.74 E-value: 6.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 72 IFISLFTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTM 151
Cdd:MTH00132 72 LLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLF 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770691071 152 IRPGTLAVRLAANMIAGHLLLTLLGNTG----PYLNSSSLsILILAQLALLTLECAVSIIQAYVFAILITLYASE 222
Cdd:MTH00132 152 IRPLALGVRLTANLTAGHLLIQLIATAAfvllPLMPTVAI-LTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
|
|
| ATP6 |
MTH00073 |
ATP synthase F0 subunit 6; Provisional |
71-222 |
4.32e-30 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177144 Cd Length: 227 Bit Score: 111.21 E-value: 4.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 71 FIFISLFTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETIST 150
Cdd:MTH00073 71 LILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISL 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770691071 151 MIRPGTLAVRLAANMIAGHLLLTLLGNTGPYLNSSSLSILILAQLALL---TLECAVSIIQAYVFAILITLYASE 222
Cdd:MTH00073 151 FIRPLALGVRLTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFlltLLEIAVAMIQAYVFVLLLSLYLQE 225
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
22-219 |
2.41e-25 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 98.33 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 22 WLSTFLGVLMIPLSYW----LLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFI-SLFTLLLYNNFLGLL---PYVF 93
Cdd:pfam00119 5 LIVALILLLFLLLATRktkkLVPGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPGGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 94 TSSSHLSMTLALALPLWLSFMLFGWINY-TQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAVRLAANMIAGHLLL 172
Cdd:pfam00119 85 TVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1770691071 173 TLLGNTGPYLNSSSLSILILAQLALLTL---ECAVSIIQAYVFAILITLY 219
Cdd:pfam00119 165 LLLAGLIFALLSAGFLLGVIPPLLGVAWtlfELLVAFIQAYVFTMLTAVY 214
|
|
| ATP6 |
MTH00172 |
ATP synthase F0 subunit 6; Provisional |
15-219 |
1.02e-24 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214447 Cd Length: 232 Bit Score: 97.03 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 15 IMNYSFNWLSTFLGVLMIPLSYWLLPSRFTFFWTSISNTLHNEFKTLLGP-SLKGGTFIfISLFTLLLYNNFLGLLPYVF 93
Cdd:MTH00172 17 LTNSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNeGLKYFPFI-ISLFFFIVFLNLLGLFPYVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 94 TSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAVRLAANMIAGHLLLT 173
Cdd:MTH00172 96 TPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1770691071 174 LLGNTGPYLNSSSLSILILAQLAL---LTLECAVSIIQAYVFAILITLY 219
Cdd:MTH00172 176 ILAGFGFNMLCASGFLSLFPLLIMvfiTLLEIAVAVIQAYVFCLLTTIY 224
|
|
| ATP6 |
MTH00175 |
ATP synthase F0 subunit 6; Provisional |
37-219 |
2.76e-21 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177228 Cd Length: 244 Bit Score: 88.53 E-value: 2.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 37 WLLPSRftffWTSISNTLHNEFKTL----LGPSLKGGTFIFISLFTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLS 112
Cdd:MTH00175 50 KLIPNR----WQSIMELIYLNIRSVvhdnLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 113 FMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAVRLAANMIAGHLLLTLLGNTGPYLNSSSLSILIL 192
Cdd:MTH00175 126 VTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSL 205
|
170 180 190
....*....|....*....|....*....|.
gi 1770691071 193 AQLALLT----LECAVSIIQAYVFAILITLY 219
Cdd:MTH00175 206 FPMLIMIfitlLEMAVAVIQAYVFCLLTTIY 236
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
24-219 |
5.79e-20 |
|
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440125 [Multi-domain] Cd Length: 212 Bit Score: 83.97 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 24 STFLGVLMIPLSYW------LLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTLLLYNNFLGLLPYVFTSSS 97
Cdd:COG0356 6 SWLAMLLLLLLFLLatrklkLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 98 HLSMTLALALPLWLSFMLF-----GWINYTQHMFAHLVPqgtpaALMPFMVCIETISTMIRPGTLAVRLAANMIAGHLLL 172
Cdd:COG0356 86 DINVTLALALIVFVLVHYYgikkkGLGGYLKHLFFPPFP-----WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1770691071 173 TLLGNTGPYLNSSSLSilILAQLALLTLECAVSIIQAYVFAILITLY 219
Cdd:COG0356 161 LLLAGLAPFLLLGVLS--LLLPVAWTAFELLVGFLQAYIFTMLTAVY 205
|
|
| ATP6 |
MTH00174 |
ATP synthase F0 subunit 6; Provisional |
38-219 |
3.06e-16 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 133799 Cd Length: 252 Bit Score: 74.98 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 38 LLPSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFG 117
Cdd:MTH00174 59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 118 WINYTQHMFAHLVPQGTPAALMPFMVCIETISTMIRPGTLAVRLAANMIAGHLLLTLLGNTGPYLNSSSL----SILILA 193
Cdd:MTH00174 139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGIligsFVPFAI 218
|
170 180
....*....|....*....|....*.
gi 1770691071 194 QLALLTLECAVSIIQAYVFAILITLY 219
Cdd:MTH00174 219 LIFVTILEMAVAIIQAYVFTLLTIVY 244
|
|
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
23-219 |
1.74e-13 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 67.13 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 23 LSTFLGVLMIPLSYWLL-------PSRFTFFWTSISNTLHNEFKTLLGPSLKGGTFIFISLFTLLLYNNFLGLLP-YVFT 94
Cdd:PRK05815 19 LSVLLGVLILLLFALVAtrklsgvPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 95 SSSHLSMTLALALPLWLSFMLFG-WINYTQHMFAHLVPQgtpaaLMPFMVCIETISTMIRPGTLAVRLAANMIAGHLLLT 173
Cdd:PRK05815 99 PTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1770691071 174 LLGNTGPYLNSSSLsILILAQLALLTLECAVSIIQAYVFAILITLY 219
Cdd:PRK05815 174 LIALLGGAGLLLAL-APLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
|
|
| PRK13419 |
PRK13419 |
F0F1 ATP synthase subunit A; Provisional |
74-219 |
6.80e-10 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237381 Cd Length: 342 Bit Score: 57.83 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 74 ISLFTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWL-----SFMLFGWINYTQHMFAhlvpqGTPAALMPFMVCIETI 148
Cdd:PRK13419 175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFitqyaAIKAHGIKGYLAHLTG-----GTHWSLWIIMIPIEFI 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770691071 149 STMIRPGTLAVRLAANMIAGHLLLTLLGNTGPYLNSSSLSILIL--AQLALLTLECAVSIIQAYVFAILITLY 219
Cdd:PRK13419 250 GLFTKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAVSvpFAIFIYLLELFVAFLQAYIFTMLSALF 322
|
|
| ATP6 |
MTH00087 |
ATP synthase F0 subunit 6; Provisional |
71-222 |
2.78e-06 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177152 Cd Length: 195 Bit Score: 46.12 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 71 FIFISLFTLLLYNNFLGLLPYVFTSSSHLSMTLALALPLWLSFMLFGWINytQHMFAHLVPQGTPAALMPF-MVCIETIS 149
Cdd:MTH00087 53 VISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTFsMLFVEIVS 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770691071 150 TMIRPGTLAVRLAANMIAGHLLLTLLGNTGpylnssslSILILAQLALLTLECAVSIIQAYVFAILITLYASE 222
Cdd:MTH00087 131 ELSRPLALTLRLTVNLMVGHLISSLLNFLG--------EKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
|
|
| PRK13417 |
PRK13417 |
F0F1 ATP synthase subunit A; Provisional |
94-219 |
1.50e-04 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237380 Cd Length: 352 Bit Score: 41.80 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 94 TSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETIST-MIRPGTLAVRLAANMIAGHLL- 171
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIVSpMAKTFALTVRLLANMTAGHVIi 296
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1770691071 172 LTLLGNTGPYLNSSSLSILILAQLALLTLECAVSIIQAYVFAILITLY 219
Cdd:PRK13417 297 LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLF 344
|
|
| PRK13420 |
PRK13420 |
F0F1 ATP synthase subunit A; Provisional |
23-219 |
1.25e-03 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237382 [Multi-domain] Cd Length: 226 Bit Score: 38.57 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 23 LSTFLGVLMIPLSYWLLPSRFTFFWTSISNTLHNEFKTLLgPSLKGGTFIFI-SLFTLLLYNNFLGLLPYVFTSSSHLSM 101
Cdd:PRK13420 28 IVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVL-PRHARLVLPFVgTLWIFILVANLIGLIPGFHSPTADLSV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 102 TLALALPLWLSFMLFG-----WINYTQHmfaHLVPQgtpaalmPFMVCIETISTMIRPGTLAVRLAANMIAGHLLLTLLG 176
Cdd:PRK13420 107 TAALALLVFFSVHWFGiraegLREYLKH---YLSPS-------PFLLPFHLISEITRTLALAVRLFGNIMSLELAALLVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1770691071 177 NTGPYLNSSSLsililaqlalLTLECAVSIIQAYVFAILITLY 219
Cdd:PRK13420 177 LVAGFLVPVPI----------LMLHIIEALVQAYIFGMLALIY 209
|
|
| ATP6 |
MTH00050 |
ATP synthase F0 subunit 6; Validated |
72-168 |
1.32e-03 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177125 Cd Length: 170 Bit Score: 38.33 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770691071 72 IFISLFTLLLYNnflglLPYVFTSSSHLSMTLALALPLWLSFMLFGWINYTQHMFAHLVPQGTPAALMPFMVCIETISTM 151
Cdd:MTH00050 30 LFIVLFLFLLYR-----LPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYI 104
|
90
....*....|....*..
gi 1770691071 152 IRPGTLAVRLAANMIAG 168
Cdd:MTH00050 105 IRPVVLILRPFINISLG 121
|
|
|