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Conserved domains on  [gi|440655389|gb|AGC22287|]
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ATP synthase F0 subunit 6 (mitochondrion) [Trachytettix bufo]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009593)

ATP synthase F0 subunit 6 is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-222 2.33e-94

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 214441  Cd Length: 223  Bit Score: 275.12  E-value: 2.33e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   1 MTNLFSSFDPSTSTSTSLNWMSMWLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMI 80
Cdd:MTH00157   2 MTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  81 NNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLA 160
Cdd:MTH00157  82 NNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655389 161 ANMIAGHMLLALLGNTGSKINEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLYTSEIN 222
Cdd:MTH00157 162 ANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-222 2.33e-94

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 275.12  E-value: 2.33e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   1 MTNLFSSFDPSTSTSTSLNWMSMWLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMI 80
Cdd:MTH00157   2 MTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  81 NNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLA 160
Cdd:MTH00157  82 NNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655389 161 ANMIAGHMLLALLGNTGSKINEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLYTSEIN 222
Cdd:MTH00157 162 ANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 4-222 1.18e-52

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: 168.92  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389    4 LFSSFDPSTSTSTSLNWMSMWLF----MFLIPSSF--WLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFIL 77
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLlsllIFLISSSLsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   78 IMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAI 157
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440655389  158 RLAANMIAGHMLLALLGNTGSKINEMLLMGM-LSVQTLLLMLESAVAIIQAYVFSVLMTLYTSEIN 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 64-219 1.82e-46

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: 151.01  E-value: 1.82e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  64 NKGTTLLMISLFILIMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCI 143
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440655389 144 ETISNTIRPMTLAIRLAANMIAGHMLLALLGNTGSKINEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLYTS 219
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
20-219 4.21e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 110.66  E-value: 4.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   20 WMSMWLFMFLIPSSFWLIK----SRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMI-SLFILIMINNTMGLI---PYVF 91
Cdd:pfam00119   5 LIVALILLLFLLLATRKTKklvpGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   92 TSTSHMAMTLSLALPLWMGLNLYG-WINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLAANMIAGHMLL 170
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 440655389  171 ALLGN-TGSKINEMLLMGMLSV--QTLLLMLESAVAIIQAYVFSVLMTLYTS 219
Cdd:pfam00119 165 LLLAGlIFALLSAGFLLGVIPPllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 23-220 8.61e-24

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: 93.98  E-value: 8.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  23 MWLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMINNTMGLIPYVFTSTSHMAMTLS 102
Cdd:COG0356   13 LLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389 103 LALPLWMGLNLYG-WINTTNNMFAHLVPSGTPnILMPFMVCIETISNTIRPMTLAIRLAANMIAGHMLLALLGNTGSKIN 181
Cdd:COG0356   93 LALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL 171

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 440655389 182 EMLLMGMLSVqtLLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:COG0356  172 LGVLSLLLPV--AWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-222 2.33e-94

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 275.12  E-value: 2.33e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   1 MTNLFSSFDPSTSTSTSLNWMSMWLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMI 80
Cdd:MTH00157   2 MTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  81 NNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLA 160
Cdd:MTH00157  82 NNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 440655389 161 ANMIAGHMLLALLGNTGSKINEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLYTSEIN 222
Cdd:MTH00157 162 ANMIAGHLLLTLLGNTGPSLSSMILSILILIQILLLILESAVAIIQSYVFSVLSTLYSSEVN 223
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 4-222 1.18e-52

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: 168.92  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389    4 LFSSFDPSTSTSTSLNWMSMWLF----MFLIPSSF--WLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFIL 77
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLlsllIFLISSSLsrWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   78 IMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAI 157
Cdd:TIGR01131  81 ILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440655389  158 RLAANMIAGHMLLALLGNTGSKINEMLLMGM-LSVQTLLLMLESAVAIIQAYVFSVLMTLYTSEIN 222
Cdd:TIGR01131 161 RLFANISAGHLLLTLLSGLLFSLMSSAIFALlLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-220 1.76e-50

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 163.67  E-value: 1.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   1 MTNLFSSFDPSTST---STSLNWMSMWLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFIL 77
Cdd:MTH00176   2 LVDLFSSFDPPNKNifsMISLSWITLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  78 IMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAI 157
Cdd:MTH00176  82 VMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAV 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440655389 158 RLAANMIAGHMLLALLGNTGSK---INEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:MTH00176 162 RLAANLSAGHLLLGLLGAAMWGllpVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDE 227
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 64-219 1.82e-46

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: 151.01  E-value: 1.82e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  64 NKGTTLLMISLFILIMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCI 143
Cdd:cd00310    1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440655389 144 ETISNTIRPMTLAIRLAANMIAGHMLLALLGNTGSKINEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLYTS 219
Cdd:cd00310   81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-221 1.09e-44

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 148.86  E-value: 1.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   1 MTNLFSSFDPSTSTSTSLnWMSMWLF----MFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFI 76
Cdd:MTH00173   2 MVDLFSSFDDHNSSFSSL-SFLMWLLslmsLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  77 LIMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLA 156
Cdd:MTH00173  81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 440655389 157 IRLAANMIAGHMLLALLGNT-GSKINEMLLMGMLS---VQTLLLMLESAVAIIQAYVFSVLMTLYTSEI 221
Cdd:MTH00173 161 VRLLANISAGHIVLTLIGNYlSSSLFSSSVVSLLLvllIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEH 229
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-220 1.92e-42

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 143.33  E-value: 1.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   1 MTNLFSSFDPSTST-----STSLNWMSMWLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLF 75
Cdd:MTH00005   2 LTDIFSSFDPATNSlfnnlSSTAFWAFNFSIILLLSSSFWITPNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  76 ILIMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTL 155
Cdd:MTH00005  82 TMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 440655389 156 AIRLAANMIAGHMLLALLGNTGSKI---NEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:MTH00005 162 SFRLAANMSAGHIVLSLIGIYAASAlfsSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDD 229
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 2-220 1.19e-41

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 140.88  E-value: 1.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   2 TNLFSSFDPSTSTSTSLNWMSMWL---FMFLIPSSFWLIkSRPMTIMTTItkkLNNEFDTILNSKNKGT---TLLMISLF 75
Cdd:MTH00035   5 NSIFGQFSPDTILFIPLTLLSSVIalsWLFFINPTNWLP-SRSQSIWLTF---RQEILKLIFQNTNPNTapwAGLLTTVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  76 ILIMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTL 155
Cdd:MTH00035  81 ILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIAL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440655389 156 AIRLAANMIAGHMLLALLGNTGSKINEMLLMGM--LSVQTLLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:MTH00035 161 GLRLAANLTAGHLLIFLLSTAIWELSNSPLISIitLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-220 1.43e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 135.46  E-value: 1.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   1 MTNLFSSFDPSTSTSTSLNWMSM-WLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIM 79
Cdd:MTH00179   2 MLSMFDQFESPSLLGIPLLALALlLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  80 INNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRL 159
Cdd:MTH00179  82 TLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440655389 160 AANMIAGHMLLALLGntGSKINEMLLMGMLSVQT-----LLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:MTH00179 162 TANITAGHLLMHLIS--SAVFVLMNFMGMVALLTllvlfLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 3-217 7.83e-39

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 133.54  E-value: 7.83e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   3 NLFSSFDPSTSTSTSLNWMSMWLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMINN 82
Cdd:MTH00101   4 NLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIGSTN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  83 TMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLAAN 162
Cdd:MTH00101  84 LLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTAN 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 440655389 163 MIAGHMLLALLGNTG---SKINEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLY 217
Cdd:MTH00101 164 ITAGHLLIHLIGGATlalMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLY 221
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-220 1.65e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 124.94  E-value: 1.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   1 MTNLFSSFDPSTSTSTSLNWMSMWL-FMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIM 79
Cdd:MTH00120   2 NLNFFDQFSSPELLGIPLILLAMLIpALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  80 INNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRL 159
Cdd:MTH00120  82 LINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440655389 160 AANMIAGHMLLALLGNTG---SKINEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:MTH00120 162 TANLTAGHLLIQLISTATlnlLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-220 2.70e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 119.30  E-value: 2.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   1 MTNLFSSFDPSTSTSTSLNWMSMWLFMFLI--PSSFWLiKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILI 78
Cdd:MTH00073   2 NLSFFDQFLSPTLLGIPLIMLAMLLPWLLFptPTNKWL-NNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  79 MINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIR 158
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 440655389 159 LAANMIAGHMLLALLGNTGSKIneMLLMGMLSVQT-----LLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVL--LPLMPTVSILTmivlfLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 27-220 4.01e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 118.82  E-value: 4.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  27 MFLIPSSFWLiKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMINNTMGLIPYVFTSTSHMAMTLSLALP 106
Cdd:MTH00132  30 LFPTPTSRWL-NNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389 107 LWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLAANMIAGHMLLALLGNTGSKINEMLLM 186
Cdd:MTH00132 109 LWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIATAAFVLLPLMPT 188

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 440655389 187 GMLSVQTLLLM---LESAVAIIQAYVFSVLMTLYTSE 220
Cdd:MTH00132 189 VAILTATLLFLltlLEVAVAMIQAYVFVLLLSLYLQE 225
ATP-synt_A pfam00119
ATP synthase A chain;
20-219 4.21e-30

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 110.66  E-value: 4.21e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   20 WMSMWLFMFLIPSSFWLIK----SRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMI-SLFILIMINNTMGLI---PYVF 91
Cdd:pfam00119   5 LIVALILLLFLLLATRKTKklvpGRLQNFVEMLVEFVDNIVKDNIGKKKGRKFFPLLlTLFFFILVSNLLGLIpksPGGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   92 TSTSHMAMTLSLALPLWMGLNLYG-WINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLAANMIAGHMLL 170
Cdd:pfam00119  85 TVTADINVTLALALIVFLLVHYYGiKKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 440655389  171 ALLGN-TGSKINEMLLMGMLSV--QTLLLMLESAVAIIQAYVFSVLMTLYTS 219
Cdd:pfam00119 165 LLLAGlIFALLSAGFLLGVIPPllGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 12-217 2.45e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 109.71  E-value: 2.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  12 TSTSTSLNWMSMWLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMINNTMGLIPYVF 91
Cdd:MTH00175  27 TFTNSSMMMVLAVIIFWLLLKGDKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  92 TSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLAANMIAGHMLLA 171
Cdd:MTH00175 107 TPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFA 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 440655389 172 LLgnTGSKINeMLLMGM--LSVQTLLLM-----LESAVAIIQAYVFSVLMTLY 217
Cdd:MTH00175 187 IL--SGFAFN-MLSNGLiiLSLFPMLIMifitlLEMAVAVIQAYVFCLLTTIY 236
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 69-217 2.47e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 106.66  E-value: 2.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  69 LLMISLFILIMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISN 148
Cdd:MTH00172  73 PFIISLFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSY 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440655389 149 TIRPMTLAIRLAANMIAGHMLLALLGNTGskINEMLLMGMLSVQTLLLM-----LESAVAIIQAYVFSVLMTLY 217
Cdd:MTH00172 153 ISRAISLGVRLAANLSAGHLLFAILAGFG--FNMLCASGFLSLFPLLIMvfitlLEIAVAVIQAYVFCLLTTIY 224
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 23-220 8.61e-24

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: 93.98  E-value: 8.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  23 MWLFMFLIPSSFWLIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMINNTMGLIPYVFTSTSHMAMTLS 102
Cdd:COG0356   13 LLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389 103 LALPLWMGLNLYG-WINTTNNMFAHLVPSGTPnILMPFMVCIETISNTIRPMTLAIRLAANMIAGHMLLALLGNTGSKIN 181
Cdd:COG0356   93 LALIVFVLVHYYGiKKKGLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLL 171

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 440655389 182 EMLLMGMLSVqtLLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:COG0356  172 LGVLSLLLPV--AWTAFELLVGFLQAYIFTMLTAVYISL 208
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 36-217 7.16e-22

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 90.00  E-value: 7.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  36 LIKSRPMTIMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYG 115
Cdd:MTH00174  59 LVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAG 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389 116 WINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLAANMIAGHMLLALLGNTGSK-INEMLLMGM---LSV 191
Cdd:MTH00174 139 LITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKmINTGILIGSfvpFAI 218

                        170       180
                 ....*....|....*....|....*.
gi 440655389 192 QTLLLMLESAVAIIQAYVFSVLMTLY 217
Cdd:MTH00174 219 LIFVTILEMAVAIIQAYVFTLLTIVY 244
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 21-220 3.21e-20

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 85.23  E-value: 3.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  21 MSMWLFMFLIpSSFWLIKSRPMT--------IMTTITKKLNNEFDTILNSKNKGTTLLMISLFILIMINNTMGLIP-YVF 91
Cdd:PRK05815  19 LSVLLGVLIL-LLFALVATRKLSgvpgglqnFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  92 TSTSHMAMTLSLALPLWMGLNLYG-WINTTNNMFAHLVPSgtpniLMPFMVCIETISNTIRPMTLAIRLAANMIAGHMLL 170
Cdd:PRK05815  98 PPTADINVTLALALIVFVLVIYYGiKKKGLGGYLKEFYLQ-----PHPLLLPIEIISEFSRPISLSLRLFGNMLAGELIL 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 440655389 171 ALLGNTGSkINEMLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:PRK05815 173 ALIALLGG-AGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 71-217 3.59e-13

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 67.46  E-value: 3.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  71 MISLFILIMINNTMGLIPYVFTSTSHMAMTLSLALPLW----------MGLNLYgwinttnnmFAHLVpSGTPNILMPFM 140
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFfitqyaaikaHGIKGY---------LAHLT-GGTHWSLWIIM 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389 141 VCIETISNTIRPMTLAIRLAANMIAGHM-LLALLGNTGSKINEMLLMGMlSV--QTLLLMLESAVAIIQAYVFSVLMTLY 217
Cdd:PRK13419 244 IPIEFIGLFTKPFALTVRLFANMTAGHIvILSLIFISFILKSYIVAVAV-SVpfAIFIYLLELFVAFLQAYIFTMLSALF 322
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 8-217 6.89e-10

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 57.98  E-value: 6.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389   8 FDPSTSTSTSLNWM-SMWLFMFLIPSSFwLIKSRPMTIMTTITKKL--------NNEFDTILNSKNKGTTLLMISLFILI 78
Cdd:PRK13417  90 FDMHITKRVTMMWIvAFFLFLIFIPAAN-IIAKNPLKVQSRFANTVevfvnflrKDIVDESMHGHGHSYYHYIFTLFFFI 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  79 MINNTMGLIPYV-----------------------------------FTSTSHMAMTLSLALPLWMGLNLYGWINTTNNM 123
Cdd:PRK13417 169 LFCNLMGLVPSVgeltvvasdygglvalgvmdhtphalptfakvwsgITVTGDISVTMTLALLTMFLIYGAGFSYQGPKF 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389 124 FAHLVPSGTPNILMPFMVCIETI-SNTIRPMTLAIRLAANMIAGH-MLLALLGNTGSKINEMLLMGMLSVQTLLLMLESA 201
Cdd:PRK13417 249 IWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHvIILALMGFIFQFQSWGIVPVSVIGSGLIYVLEIF 328

                        250
                 ....*....|....*.
gi 440655389 202 VAIIQAYVFSVLMTLY 217
Cdd:PRK13417 329 VAFLQAYIFVLLTSLF 344
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 73-220 2.62e-08

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 51.90  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  73 SLFILIMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYgwINTTNNMFAHLVPSGTPNILMPF-MVCIETISNTIR 151
Cdd:MTH00087  57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLS--FLSKSEKFSVYLSKGSDSFLKTFsMLFVEIVSELSR 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 440655389 152 PMTLAIRLAANMIAGHMLLALLGNTGSKINEMLLmgmlsvqtLLLMLESAVAIIQAYVFSVLMTLYTSE 220
Cdd:MTH00087 135 PLALTLRLTVNLMVGHLISSLLNFLGEKYVWLSI--------LAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 70-217 1.54e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 50.13  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  70 LMISLFILIMINNTMGLIPYVFTSTSHMAMTLSLALPL-----WMGLNLYGWintTNNMFAHLVPSgtpNILMPFMVcie 144
Cdd:PRK13420  77 FVGTLWIFILVANLIGLIPGFHSPTADLSVTAALALLVffsvhWFGIRAEGL---REYLKHYLSPS---PFLLPFHL--- 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440655389 145 tISNTIRPMTLAIRLAANMIAGHMLLALLgntgskinemLLMGMLSVQTLLLMLESAVAIIQAYVFSVLMTLY 217
Cdd:PRK13420 148 -ISEITRTLALAVRLFGNIMSLELAALLV----------LLVAGFLVPVPILMLHIIEALVQAYIFGMLALIY 209
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 87-175 1.63e-06

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 46.42  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  87 IPYVFTSTSHMAMTLSLALPLWMGLNLYGWINTTNNMFAHLVPSGTPNILMPFMVCIETISNTIRPMTLAIRLAANMIAG 166
Cdd:MTH00050  42 LPYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121


                 ....*....
gi 440655389 167 HMLLALLGN 175
Cdd:MTH00050 122 CFGGVALGN 130
PRK13421 PRK13421
F0F1 ATP synthase subunit A; Provisional
 70-213 1.47e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237383  Cd Length: 223  Bit Score: 38.52  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440655389  70 LMISLFILIMINNTMGLIPYVFTSTSHMAMTLSLALPLWMGLNLYGWinTTNNMFAHLVPSGTPNILMPFMVCIETISnt 149
Cdd:PRK13421  80 LIGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGV--RARGVRGYLATFAEPTWVMIPLNLVEQLT-- 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 440655389 150 iRPMTLAIRLAANMIAGHMLLALLgntgskineMLLMGMLsVQTLLLMLESAVAIIQAYVFSVL 213
Cdd:PRK13421 156 -RTFSLIVRLFGNVMSGVFVIGIV---------LSLAGLL-VPIPLMALDLLTGAVQAYIFAVL 208
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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