|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
1-223 |
2.00e-88 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 260.10 E-value: 2.00e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIM 80
Cdd:MTH00157 1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRL 160
Cdd:MTH00157 81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811917422 161 AANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEIN 223
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
5-223 |
1.48e-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: 153.52 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 5 LFSSFDPSTSNSLSINWLSTLLFIMLVPMTF------WLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFII 78
Cdd:TIGR01131 1 LFSQFDISPITLFSLTLLSLILLLSLLIFLIssslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 79 IMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAI 158
Cdd:TIGR01131 81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811917422 159 RLAANMIAGHLLLTLLGNTGNKLSEIMLIGM-LTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEIN 223
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
65-220 |
4.60e-42 |
|
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: 139.84 E-value: 4.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 65 NKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCI 144
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811917422 145 ETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSS 220
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
21-220 |
9.16e-28 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 104.88 E-value: 9.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 21 WLSTLLFIMLVPMTFWLIK----SRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFI-SLFIIIMINNVMGLF---PYIF 92
Cdd:pfam00119 5 LIVALILLLFLLLATRKTKklvpGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPGGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 93 TSSSHMVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLL 171
Cdd:pfam00119 85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1811917422 172 TLLGNTGNKLSEIML---IGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSS 220
Cdd:pfam00119 165 LLLAGLIFALLSAGFllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
21-218 |
4.08e-22 |
|
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440125 [Multi-domain] Cd Length: 212 Bit Score: 89.75 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 21 WLSTLLFIMLVPMTFWLIKSRPN---MLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSH 97
Cdd:COG0356 7 WLAMLLLLLLFLLATRKLKLVPGglqNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 98 MVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSGTPAMlMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGN 176
Cdd:COG0356 87 INVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPWL-APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1811917422 177 TGNKLSEIMLIGMLTMQMMLlvLESAVSLIQAYVFSVLTTLY 218
Cdd:COG0356 166 LAPFLLLGVLSLLLPVAWTA--FELLVGFLQAYIFTMLTAVY 205
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
1-223 |
2.00e-88 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 260.10 E-value: 2.00e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIM 80
Cdd:MTH00157 1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRL 160
Cdd:MTH00157 81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1811917422 161 AANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEIN 223
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
5-223 |
1.48e-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: 153.52 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 5 LFSSFDPSTSNSLSINWLSTLLFIMLVPMTF------WLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFII 78
Cdd:TIGR01131 1 LFSQFDISPITLFSLTLLSLILLLSLLIFLIssslsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 79 IMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAI 158
Cdd:TIGR01131 81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811917422 159 RLAANMIAGHLLLTLLGNTGNKLSEIMLIGM-LTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEIN 223
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
|
|
| ATP6 |
MTH00176 |
ATP synthase F0 subunit 6; Provisional |
1-221 |
1.37e-45 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214449 Cd Length: 229 Bit Score: 151.34 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 1 MMTNLFSSFDPSTSN---SLSINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFI 77
Cdd:MTH00176 1 MLVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 78 IIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLA 157
Cdd:MTH00176 81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811917422 158 IRLAANMIAGHLLLT---LLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00176 161 VRLAANLSAGHLLLGllgAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
65-220 |
4.60e-42 |
|
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: 139.84 E-value: 4.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 65 NKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCI 144
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1811917422 145 ETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSS 220
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
|
|
| ATP6 |
MTH00005 |
ATP synthase F0 subunit 6; Provisional |
1-221 |
1.12e-41 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 164583 Cd Length: 231 Bit Score: 141.41 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 1 MMTNLFSSFDPSTSNSL-----SINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISL 75
Cdd:MTH00005 1 MLTDIFSSFDPATNSLFnnlssTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 76 FIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGT 155
Cdd:MTH00005 81 FTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPIT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811917422 156 LAIRLAANMIAGHLLLTLLGNTGNKL---SEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00005 161 LSFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
|
|
| ATP6 |
MTH00173 |
ATP synthase F0 subunit 6; Provisional |
1-222 |
4.60e-38 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214448 Cd Length: 231 Bit Score: 131.91 E-value: 4.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 1 MMTNLFSSFDPSTSNSLSIN---WLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFI 77
Cdd:MTH00173 1 MMVDLFSSFDDHNSSFSSLSflmWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 78 IIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLA 157
Cdd:MTH00173 81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1811917422 158 IRLAANMIAGHLLLT----LLGNTGNKLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSSEI 222
Cdd:MTH00173 161 VRLLANISAGHIVLTlignYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
|
|
| ATP6 |
MTH00179 |
ATP synthase F0 subunit 6; Provisional |
1-221 |
8.13e-36 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177230 Cd Length: 227 Bit Score: 125.83 E-value: 8.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPM-TFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIII 79
Cdd:MTH00179 1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSlTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 80 MINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIR 159
Cdd:MTH00179 81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811917422 160 LAANMIAGHLLLTLLGNTGNKLSEIM-LIGMLT--MQMMLLVLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMgMVALLTllVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
|
|
| ATP6 |
MTH00035 |
ATP synthase F0 subunit 6; Validated |
3-221 |
9.67e-36 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177110 Cd Length: 229 Bit Score: 125.86 E-value: 9.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 3 TNLFSSFDPSTSNSLSINWLST---LLFIMLVPMTFWLIkSRPNMLMEILTKNMnyeFNNILNNKNKGS---TLLFISLF 76
Cdd:MTH00035 5 NSIFGQFSPDTILFIPLTLLSSviaLSWLFFINPTNWLP-SRSQSIWLTFRQEI---LKLIFQNTNPNTapwAGLLTTVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 77 IIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTL 156
Cdd:MTH00035 81 ILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811917422 157 AIRLAANMIAGHLLLTLLGNTGNKLSEIMLIGMLTMQM--MLLVLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00035 161 GLRLAANLTAGHLLIFLLSTAIWELSNSPLISIITLIIffLLFILEIGVACIQAYVFTALVHFYLEQ 227
|
|
| ATP6 |
MTH00120 |
ATP synthase F0 subunit 6; Provisional |
1-221 |
7.39e-35 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177181 Cd Length: 227 Bit Score: 123.40 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVP-MTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIII 79
Cdd:MTH00120 1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPsPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 80 MINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIR 159
Cdd:MTH00120 81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811917422 160 LAANMIAGHLLLTLLGNTGNKLSEIM-LIGMLTMQMMLL--VLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMpTLSLLTLIILLLltILELAVAMIQAYVFVLLLSLYLQE 225
|
|
| ATP6 |
MTH00101 |
ATP synthase F0 subunit 6; Validated |
1-218 |
1.49e-31 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177163 Cd Length: 226 Bit Score: 115.05 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIM 80
Cdd:MTH00101 1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 81 INNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRL 160
Cdd:MTH00101 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1811917422 161 AANMIAGHLLLTLLGNTGNKLSEIMLIGML---TMQMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALitfIILILLTILEFAVALIQAYVFTLLVSLY 221
|
|
| ATP6 |
MTH00073 |
ATP synthase F0 subunit 6; Provisional |
1-221 |
4.57e-31 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177144 Cd Length: 227 Bit Score: 113.52 E-value: 4.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 1 MMTNLFSSFDPSTSNSLSINWLSTLLFIMLVPM-TFWLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIII 79
Cdd:MTH00073 1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTpTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 80 MINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIR 159
Cdd:MTH00073 81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811917422 160 LAANMIAGHLLLTLLGNTGNKLSEIM-LIGMLTMQMMLL--VLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMpTVSILTMIVLFLltLLEIAVAMIQAYVFVLLLSLYLQE 225
|
|
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
70-221 |
1.16e-30 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 112.66 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 70 LLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETIST 149
Cdd:MTH00132 71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISL 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811917422 150 LIRPGTLAIRLAANMIAGHLLLTLLGNTGNKLSEIM-LIGMLTMQMMLL--VLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00132 151 FIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMpTVAILTATLLFLltLLEVAVAMIQAYVFVLLLSLYLQE 225
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
21-220 |
9.16e-28 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 104.88 E-value: 9.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 21 WLSTLLFIMLVPMTFWLIK----SRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFI-SLFIIIMINNVMGLF---PYIF 92
Cdd:pfam00119 5 LIVALILLLFLLLATRKTKklvpGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPGGF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 93 TSSSHMVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLL 171
Cdd:pfam00119 85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1811917422 172 TLLGNTGNKLSEIML---IGMLTMQMMLLVLESAVSLIQAYVFSVLTTLYSS 220
Cdd:pfam00119 165 LLLAGLIFALLSAGFllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| ATP6 |
MTH00175 |
ATP synthase F0 subunit 6; Provisional |
36-218 |
4.69e-27 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177228 Cd Length: 244 Bit Score: 103.55 E-value: 4.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 36 WLIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLF 115
Cdd:MTH00175 50 KLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 116 GWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKL--SEIMLIGMLTMQ 193
Cdd:MTH00175 130 GFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMlsNGLIILSLFPML 209
|
170 180
....*....|....*....|....*..
gi 1811917422 194 MMLLV--LESAVSLIQAYVFSVLTTLY 218
Cdd:MTH00175 210 IMIFItlLEMAVAVIQAYVFCLLTTIY 236
|
|
| ATP6 |
MTH00172 |
ATP synthase F0 subunit 6; Provisional |
37-218 |
1.74e-24 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214447 Cd Length: 232 Bit Score: 96.65 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 37 LIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFG 116
Cdd:MTH00172 40 LIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 117 WINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNK-LSEIMLIGMLTMQMM 195
Cdd:MTH00172 120 FWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAGFGFNmLCASGFLSLFPLLIM 199
|
170 180
....*....|....*....|....*
gi 1811917422 196 LLV--LESAVSLIQAYVFSVLTTLY 218
Cdd:MTH00172 200 VFItlLEIAVAVIQAYVFCLLTTIY 224
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
21-218 |
4.08e-22 |
|
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit a is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440125 [Multi-domain] Cd Length: 212 Bit Score: 89.75 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 21 WLSTLLFIMLVPMTFWLIKSRPN---MLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSH 97
Cdd:COG0356 7 WLAMLLLLLLFLLATRKLKLVPGglqNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 98 MVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSGTPAMlMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGN 176
Cdd:COG0356 87 INVTLALALIVFVLVHYYGiKKKGLGGYLKHLFFPPFPWL-APLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1811917422 177 TGNKLSEIMLIGMLTMQMMLlvLESAVSLIQAYVFSVLTTLY 218
Cdd:COG0356 166 LAPFLLLGVLSLLLPVAWTA--FELLVGFLQAYIFTMLTAVY 205
|
|
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
21-218 |
2.07e-19 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 82.92 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 21 WLSTLLFIMLVPMTFWLIKSRPN---MLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFP-YIFTSSS 96
Cdd:PRK05815 22 LLGVLILLLFALVATRKLSGVPGglqNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 97 HMVMTLSLALPMWLSFNLFG-WINKTNHMFEHMVPSgtpamLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLG 175
Cdd:PRK05815 102 DINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1811917422 176 NTGNkLSEIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:PRK05815 177 LLGG-AGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVY 218
|
|
| ATP6 |
MTH00174 |
ATP synthase F0 subunit 6; Provisional |
37-218 |
5.75e-18 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 133799 Cd Length: 252 Bit Score: 79.60 E-value: 5.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 37 LIKSRPNMLMEILTKNMNYEFNNILNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFG 116
Cdd:MTH00174 59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 117 WINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKL-SEIMLIGMLTMQMM 195
Cdd:MTH00174 139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMiNTGILIGSFVPFAI 218
|
170 180
....*....|....*....|....*.
gi 1811917422 196 LL---VLESAVSLIQAYVFSVLTTLY 218
Cdd:MTH00174 219 LIfvtILEMAVAIIQAYVFTLLTIVY 244
|
|
| PRK13419 |
PRK13419 |
F0F1 ATP synthase subunit A; Provisional |
73-218 |
1.40e-10 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237381 Cd Length: 342 Bit Score: 59.76 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 73 ISLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALpmwlsFNLFgwINKTNHMFEHMV-------PSGTPAMLMPFMVCIE 145
Cdd:PRK13419 175 LTVFFFILVCNLLGLVPYGATATGNINVTLTLAV-----FTFF--ITQYAAIKAHGIkgylahlTGGTHWSLWIIMIPIE 247
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1811917422 146 TISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNKL-SEIMLIGM-LTMQMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:PRK13419 248 FIGLFTKPFALTVRLFANMTAGHIVILSLIFISFILkSYIVAVAVsVPFAIFIYLLELFVAFLQAYIFTMLSALF 322
|
|
| PRK13417 |
PRK13417 |
F0F1 ATP synthase subunit A; Provisional |
93-218 |
7.64e-07 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237380 Cd Length: 352 Bit Score: 48.73 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 93 TSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAMLMPFMVCIETISTLI-RPGTLAIRLAANMIAGHLLL 171
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIVSPMaKTFALTVRLLANMTAGHVII 296
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1811917422 172 TLLGNTGNkLSEIMLIGMLTM--QMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:PRK13417 297 LALMGFIF-QFQSWGIVPVSVigSGLIYVLEIFVAFLQAYIFVLLTSLF 344
|
|
| ATP6 |
MTH00087 |
ATP synthase F0 subunit 6; Provisional |
22-221 |
1.46e-06 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177152 Cd Length: 195 Bit Score: 46.90 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 22 LSTLLFIMLVPMTFWLIKSRPNMLMEILTKNMNYEFNniLNNKNKGSTLLFISLFIIIMINNVMGLFPYIFTSSSHMVMT 101
Cdd:MTH00087 7 LDVFMFVFLLQYLLYFKESMLNVLVKKFFGLLIIVFS--YSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 102 LSLALPMWLSFNLFGWINKTnhMFEHMVPSGTPAMLMPF-MVCIETISTLIRPGTLAIRLAANMIAGHLLLTLLGNTGNK 180
Cdd:MTH00087 85 FLYALVAWLSTFLSFLSKSE--KFSVYLSKGSDSFLKTFsMLFVEIVSELSRPLALTLRLTVNLMVGHLISSLLNFLGEK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1811917422 181 LSEIMLIgmltmqmmLLVLESAVSLIQAYVFSVLTTLYSSE 221
Cdd:MTH00087 163 YVWLSIL--------AIMMECFVAFIQSYIFSRLIYLYLNE 195
|
|
| ATP6 |
MTH00050 |
ATP synthase F0 subunit 6; Validated |
57-167 |
4.04e-06 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177125 Cd Length: 170 Bit Score: 45.26 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 57 FNNILNNkNKGSTLLFISLFIIIMINnVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINKTNHMFEHMVPSGTPAM 136
Cdd:MTH00050 13 IYKLILG-GSVSYYYSVVLFIVLFLF-LLYRLPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLY 90
|
90 100 110
....*....|....*....|....*....|.
gi 1811917422 137 LMPFMVCIETISTLIRPGTLAIRLAANMIAG 167
Cdd:MTH00050 91 ICPFVCIAETISYIIRPVVLILRPFINISLG 121
|
|
| PRK13420 |
PRK13420 |
F0F1 ATP synthase subunit A; Provisional |
74-218 |
2.03e-04 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237382 [Multi-domain] Cd Length: 226 Bit Score: 41.27 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1811917422 74 SLFIIIMINNVMGLFPYIFTSSSHMVMTLSLALPMWLSFNLFGWINK--TNHMFEHMVPSgtpAMLMPFMVcietISTLI 151
Cdd:PRK13420 80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEglREYLKHYLSPS---PFLLPFHL----ISEIT 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1811917422 152 RPGTLAIRLAANMIAGHLLLTLlgntgnklseIMLIGMLTMQMMLLVLESAVSLIQAYVFSVLTTLY 218
Cdd:PRK13420 153 RTLALAVRLFGNIMSLELAALL----------VLLVAGFLVPVPILMLHIIEALVQAYIFGMLALIY 209
|
|
|