|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
38-271 |
1.07e-75 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 229.68 E-value: 1.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 38 FWTINIDSMFFSVVLGLLFLVLFRSVAKKATSGVPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNL 117
Cdd:PRK05815 9 FGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 118 MDLLPIdllpyiaehvlglpaLRVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQPFnhWAFIPVNLIleg 197
Cdd:PRK05815 89 LGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLPIEII--- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699825 198 vSLLSKPVSLGLRLFGNMYAGELIFILI-----AGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH 271
Cdd:PRK05815 149 -SEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEE 226
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
44-270 |
1.73e-69 |
|
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: 213.40 E-value: 1.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 44 DSMFFSVVLGLLFLVLFRSVAKKAtSGVPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPi 123
Cdd:COG0356 1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 124 dllpyiaehvlGLpalrVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQPFnhWAFIPVNLILEGVSLLSK 203
Cdd:COG0356 79 -----------GL----FPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--PWLAPLMLPIEIISELAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699825 204 PVSLGLRLFGNMYAGELIFILIAGLLPWWS----QWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEE 270
Cdd:COG0356 142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLlgvlSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
63-265 |
3.49e-56 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 179.61 E-value: 3.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 63 VAKKATSGVPGKFQTAIELVIGFVNGSVKDMYHGKS-KLIAPLALTIFVWVFLMNLMDLLPIdlLPYIAEhvlglpalrv 141
Cdd:pfam00119 18 ATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK--SPGGFT---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 142 vPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLqPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELI 221
Cdd:pfam00119 86 -VTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFV-PPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1447699825 222 FILIAGLLPW---------WSQWILNVPWAIFHILIITLQAFIFMVLTIVYLS 265
Cdd:pfam00119 164 LLLLAGLIFAllsagfllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
35-265 |
8.74e-31 |
|
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: 114.23 E-value: 8.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 35 PATFWTINIDSMFFSVVLGLLFLVLFRSVAKKAtsgVPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFL 114
Cdd:TIGR01131 7 ISPITLFSLTLLSLILLLSLLIFLISSSLSRWL---IPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 115 MNLMDLLPidllpyiaehvlglpaLRVVPSADVNVTLSMALGVFILILFYSIKMKGIGgFTKELTLQPFNHWaFIPVNLI 194
Cdd:TIGR01131 84 SNLLGLIP----------------YSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKG-FLAHLVPSGTPLP-LIPFLVI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699825 195 LEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQ-------WILNVPWAIFHILIITLQAFIFMVLTIVYLS 265
Cdd:TIGR01131 146 IETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSsaifallLLILVALIILEIFVAFIQAYVFTLLTCLYLN 223
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
99-265 |
3.13e-30 |
|
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: 110.95 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 99 KLIAPLALTIFVWVFLMNLMDLLPidllpyiaehvlglpaLRVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKEL 178
Cdd:cd00310 2 KKYLPLLGTLFLFILFSNLLGLIP----------------YSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 179 TLQPFnhWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQW------ILNVPWAIFHILIITLQ 252
Cdd:cd00310 66 PPGTP--LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSvgllplLLPVALTLLELFVAFIQ 143
|
170
....*....|...
gi 1447699825 253 AFIFMVLTIVYLS 265
Cdd:cd00310 144 AYVFTLLTAVYIS 156
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
38-271 |
1.07e-75 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 229.68 E-value: 1.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 38 FWTINIDSMFFSVVLGLLFLVLFRSVAKKATSGVPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNL 117
Cdd:PRK05815 9 FGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 118 MDLLPIdllpyiaehvlglpaLRVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQPFnhWAFIPVNLIleg 197
Cdd:PRK05815 89 LGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLPIEII--- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1447699825 198 vSLLSKPVSLGLRLFGNMYAGELIFILI-----AGLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH 271
Cdd:PRK05815 149 -SEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEEE 226
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
44-270 |
1.73e-69 |
|
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: 213.40 E-value: 1.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 44 DSMFFSVVLGLLFLVLFRSVAKKAtSGVPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPi 123
Cdd:COG0356 1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 124 dllpyiaehvlGLpalrVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQPFnhWAFIPVNLILEGVSLLSK 203
Cdd:COG0356 79 -----------GL----FPPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--PWLAPLMLPIEIISELAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699825 204 PVSLGLRLFGNMYAGELIFILIAGLLPWWS----QWILNVPWAIFHILIITLQAFIFMVLTIVYLSMASEE 270
Cdd:COG0356 142 PLSLSLRLFGNMFAGHIILLLLAGLAPFLLlgvlSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
63-265 |
3.49e-56 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 179.61 E-value: 3.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 63 VAKKATSGVPGKFQTAIELVIGFVNGSVKDMYHGKS-KLIAPLALTIFVWVFLMNLMDLLPIdlLPYIAEhvlglpalrv 141
Cdd:pfam00119 18 ATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK--SPGGFT---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 142 vPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLqPFNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELI 221
Cdd:pfam00119 86 -VTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKLFV-PPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGHLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1447699825 222 FILIAGLLPW---------WSQWILNVPWAIFHILIITLQAFIFMVLTIVYLS 265
Cdd:pfam00119 164 LLLLAGLIFAllsagfllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
35-265 |
8.74e-31 |
|
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: 114.23 E-value: 8.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 35 PATFWTINIDSMFFSVVLGLLFLVLFRSVAKKAtsgVPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFL 114
Cdd:TIGR01131 7 ISPITLFSLTLLSLILLLSLLIFLISSSLSRWL---IPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 115 MNLMDLLPidllpyiaehvlglpaLRVVPSADVNVTLSMALGVFILILFYSIKMKGIGgFTKELTLQPFNHWaFIPVNLI 194
Cdd:TIGR01131 84 SNLLGLIP----------------YSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKG-FLAHLVPSGTPLP-LIPFLVI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1447699825 195 LEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQ-------WILNVPWAIFHILIITLQAFIFMVLTIVYLS 265
Cdd:TIGR01131 146 IETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSLMSsaifallLLILVALIILEIFVAFIQAYVFTLLTCLYLN 223
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
99-265 |
3.13e-30 |
|
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: 110.95 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 99 KLIAPLALTIFVWVFLMNLMDLLPidllpyiaehvlglpaLRVVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKEL 178
Cdd:cd00310 2 KKYLPLLGTLFLFILFSNLLGLIP----------------YSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 179 TLQPFnhWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLPWWSQW------ILNVPWAIFHILIITLQ 252
Cdd:cd00310 66 PPGTP--LPLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSvgllplLLPVALTLLELFVAFIQ 143
|
170
....*....|...
gi 1447699825 253 AFIFMVLTIVYLS 265
Cdd:cd00310 144 AYVFTLLTAVYIS 156
|
|
| PRK13419 |
PRK13419 |
F0F1 ATP synthase subunit A; Provisional |
61-271 |
2.91e-20 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237381 Cd Length: 342 Bit Score: 88.65 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 61 RSVAKKATSGVPGKFQTAIELVIGFVNGSV--KDMYHGKSKLIaPLALTIFVWVFLMNLmdllpIDLLPYIAehvlglpa 138
Cdd:PRK13419 129 RKYKKMTKSQAPKGLANAMEALVEFIRLDVakSNIGHGYEKFL-PYLLTVFFFILVCNL-----LGLVPYGA-------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 139 lrvVPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQpfNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAG 218
Cdd:PRK13419 195 ---TATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGG--THWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAG 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699825 219 E-----LIFILIAgLLPWWSQWILNVPWAIF----HILIITLQAFIFMVLTIVYLSMASEEH 271
Cdd:PRK13419 270 HivilsLIFISFI-LKSYIVAVAVSVPFAIFiyllELFVAFLQAYIFTMLSALFIGLATAHE 330
|
|
| PRK13421 |
PRK13421 |
F0F1 ATP synthase subunit A; Provisional |
71-270 |
1.36e-16 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237383 Cd Length: 223 Bit Score: 76.27 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 71 VPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPidllpyiaehvlGLPAlrvvPSADVNVT 150
Cdd:PRK13421 47 APGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVANWSSLVP------------GVEP----PTAHLETD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 151 LSMALGVFILILFYSIKMKGIGGFtkeltLQPFNH--WAFIPVNLilegVSLLSKPVSLGLRLFGNMYAGEL---IFILI 225
Cdd:PRK13421 111 AALALIVFLATIYYGVRARGVRGY-----LATFAEptWVMIPLNL----VEQLTRTFSLIVRLFGNVMSGVFvigIVLSL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1447699825 226 AGLLpwwsqwiLNVPWAIFHILIITLQAFIFMVLTIVYLSMASEE 270
Cdd:PRK13421 182 AGLL-------VPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSD 219
|
|
| PRK13420 |
PRK13420 |
F0F1 ATP synthase subunit A; Provisional |
72-271 |
1.88e-16 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237382 [Multi-domain] Cd Length: 226 Bit Score: 75.93 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 72 PGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPidllpyiaehvlGLPAlrvvPSADVNVTL 151
Cdd:PRK13420 45 PGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIP------------GFHS----PTADLSVTA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 152 SMALGVFILILFYSIKMKGIGGFTKE-LTLQPFnhwaFIPVNLILEgvslLSKPVSLGLRLFGNMYAGE---LIFILIAG 227
Cdd:PRK13420 109 ALALLVFFSVHWFGIRAEGLREYLKHyLSPSPF----LLPFHLISE----ITRTLALAVRLFGNIMSLElaaLLVLLVAG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1447699825 228 LLpwwsqwiLNVPWAIFHILIITLQAFIFMVLTIVYLSMASEEH 271
Cdd:PRK13420 181 FL-------VPVPILMLHIIEALVQAYIFGMLALIYIAGGIQAH 217
|
|
| atpI |
CHL00046 |
ATP synthase CF0 A subunit |
71-263 |
5.80e-08 |
|
ATP synthase CF0 A subunit
Pssm-ID: 176987 Cd Length: 228 Bit Score: 52.24 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 71 VPGKFQTAIELVIGFVNGSVKD-MYHGKSKLIAPLALTIFVWVFLMNLMD-LLPIDLLPyiaehvlgLPALRVV-PSADV 147
Cdd:CHL00046 50 IPTGGQNFFEYVLEFIRDLAKTqIGEEEYRPWVPFIGTMFLFIFVSNWSGaLLPWKLIE--------LPHGELAaPTNDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 148 NVTLSMALGVFILILFYSIKMKGIGGFTKELTLQPFnhwaFIPVNlILEGvslLSKPVSLGLRLFGNMYAGELIFILIAG 227
Cdd:CHL00046 122 NTTVALALLTSVAYFYAGLSKKGLGYFGKYIQPTPI----LLPIN-ILED---FTKPLSLSFRLFGNILADELVVAVLVS 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 1447699825 228 LLPwwsqwiLNVPWAIFHILIIT--LQAFIFMVLTIVY 263
Cdd:CHL00046 194 LVP------LVVPIPVMFLGLFTsgIQALIFATLAAAY 225
|
|
| ATP6 |
MTH00176 |
ATP synthase F0 subunit 6; Provisional |
72-265 |
1.98e-06 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214449 Cd Length: 229 Bit Score: 47.72 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 72 PGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPidllpyiaeHVLGlpalrvvPSADVNVTL 151
Cdd:MTH00176 42 PSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFILVMSLNLSGLIP---------YVFT-------STSHLVITL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 152 SMALGVFILILFYSIKMKGIGGFTKELTLQpfNHWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIA----- 226
Cdd:MTH00176 106 SLALPLWLGVILSGFINNFYSRLSHLVPQG--TPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLGaamwg 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1447699825 227 ----GLLPWWSQWILNVPWAIFHILIITLQAFIFMVLTIVYLS 265
Cdd:MTH00176 184 llpvSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLD 226
|
|
| ATP6 |
MTH00172 |
ATP synthase F0 subunit 6; Provisional |
71-264 |
3.01e-06 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214447 Cd Length: 232 Bit Score: 46.96 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 71 VPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPIDLLPyiaehvlglpalrvvpsaDVNVT 150
Cdd:MTH00172 41 IPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTP------------------TTHIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 151 LSMALGVFILIlfySIKMKGIGGFTKEL--TLQPFNH-WAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAG 227
Cdd:MTH00172 103 VTLGLSFSIII---GVTLAGFWRFKWDFfsILMPSGApLGLAPLLVLIETVSYISRAISLGVRLAANLSAGHLLFAILAG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1447699825 228 LLpwWSQWILNVPWAIFHILI---ITL--------QAFIFMVLTIVYL 264
Cdd:MTH00172 180 FG--FNMLCASGFLSLFPLLImvfITLleiavaviQAYVFCLLTTIYL 225
|
|
| ATP6 |
MTH00175 |
ATP synthase F0 subunit 6; Provisional |
71-265 |
1.06e-05 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177228 Cd Length: 244 Bit Score: 45.38 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 71 VPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLmdllpIDLLPYIaehvlglpalrVVPSADVNVT 150
Cdd:MTH00175 52 IPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNI-----LGLFPYV-----------FTPTAHIIIT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 151 LSMALGVFILIL----------FYSIKMKGiggfTKELTLQPFNhwafipvnLILEGVSLLSKPVSLGLRLFGNMYAGEL 220
Cdd:MTH00175 116 FGLSLSIIIAVTllgfltfkwnFLSILMPG----GAPLVLAPFL--------VLIETLSYLIRAISLGVRLAANISAGHL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699825 221 IFILIAG-----------LLPWWSQWILnVPWAIFHILIITLQAFIFMVLTIVYLS 265
Cdd:MTH00175 184 LFAILSGfafnmlsngliILSLFPMLIM-IFITLLEMAVAVIQAYVFCLLTTIYLG 238
|
|
| PRK13417 |
PRK13417 |
F0F1 ATP synthase subunit A; Provisional |
71-271 |
1.76e-05 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237380 Cd Length: 352 Bit Score: 45.27 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 71 VPGKFQTAIELVIGFVNGSVKD-MYHGKSKLIAPLALTIFVWVFLMNLMDLLP-IDLLPYIAEHVLGLPALRV------- 141
Cdd:PRK13417 126 VQSRFANTVEVFVNFLRKDIVDeSMHGHGHSYYHYIFTLFFFILFCNLMGLVPsVGELTVVASDYGGLVALGVmdhtpha 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 142 -----------VPSADVNVTLSMALGVFILILFYSIKMKGIGGFTKELTLQ-PFNHWAFI-PVNLIlegVSLLSKPVSLG 208
Cdd:PRK13417 206 lptfakvwsgiTVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGvPLLLYPIMwPLEFI---VSPMAKTFALT 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699825 209 LRLFGNMYAGELIFILIAGLLPWWSQWILnVPWAI--------FHILIITLQAFIFMVLTIVYLSMASEEH 271
Cdd:PRK13417 283 VRLLANMTAGHVIILALMGFIFQFQSWGI-VPVSVigsgliyvLEIFVAFLQAYIFVLLTSLFVGLSMHRH 352
|
|
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
71-265 |
6.90e-05 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 42.85 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 71 VPGKFQTAIELVIGFVNGSVKDMYHGKSKLIAPLALTIFVWVFLMNLMDLLPidllpYIaehvlglpalrVVPSADVNVT 150
Cdd:MTH00157 38 IPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFP-----YI-----------FTSTSHLSLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 151 LSMALGVFILILFYSIKMKgiggftkelTLQPFNHW-------AFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFI 223
Cdd:MTH00157 102 LSLALPLWLSFMLFGWINN---------TNHMFAHLvpqgtppILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1447699825 224 LIAGLLPWWSQWILNVPWaIFHILIITL-------QAFIFMVLTIVYLS 265
Cdd:MTH00157 173 LLGNTGPSLSSMILSILI-LIQILLLILesavaiiQSYVFSVLSTLYSS 220
|
|
| ATP6 |
MTH00173 |
ATP synthase F0 subunit 6; Provisional |
185-271 |
1.03e-03 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214448 Cd Length: 231 Bit Score: 39.46 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 185 HWAFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLLP---WWSQW-------ILNVPWAIFHILIITLQAF 254
Cdd:MTH00173 137 PAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSsslFSSSVvslllvlLIQVGYFIFEVAVMLIQAY 216
|
90
....*....|....*..
gi 1447699825 255 IFMVLTIVYlsmaSEEH 271
Cdd:MTH00173 217 IFTLLIKLY----SDEH 229
|
|
| ATP6 |
MTH00174 |
ATP synthase F0 subunit 6; Provisional |
187-271 |
4.04e-03 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 133799 Cd Length: 252 Bit Score: 38.00 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699825 187 AFIPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIAGLL-PWWSQWILNVPWAIFHILIIT---------LQAFIF 256
Cdd:MTH00174 158 ALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAwKMINTGILIGSFVPFAILIFVtilemavaiIQAYVF 237
|
90
....*....|....*
gi 1447699825 257 MVLTIVYLSMASEEH 271
Cdd:MTH00174 238 TLLTIVYLRDTVELH 252
|
|
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
189-226 |
5.99e-03 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 37.16 E-value: 5.99e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1447699825 189 IPVNLILEGVSLLSKPVSLGLRLFGNMYAGELIFILIA 226
Cdd:MTH00132 139 IPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIA 176
|
|
|