|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
34-267 |
3.67e-79 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 238.54 E-value: 3.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 34 SFWNVHIDSLFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:PRK05815 8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 114 VMDLVPIdflpypaehwlgipyLKVVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELALHPFnhPLMIPfnllIE 193
Cdd:PRK05815 88 LLGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLP----IE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503999423 194 VVSLLAKPLSLGMRLFGNMFAGEVVFILC-----AAMLPWYLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHED 267
Cdd:PRK05815 147 IISEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEE 225
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
41-267 |
9.96e-75 |
|
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: 226.49 E-value: 9.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 41 DSLFFSWFTGLIFLGIFYKVAKRTtAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLvpi 120
Cdd:COG0356 1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 121 dflpypaehwlgIPYLKvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELALHPFnhPLMIPFNLLIEVVSLLAK 200
Cdd:COG0356 77 ------------IPGLF-PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--PWLAPLMLPIEIISELAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503999423 201 PLSLGMRLFGNMFAGEVVFILCAAMLPW----YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHED 267
Cdd:COG0356 142 PLSLSLRLFGNMFAGHIILLLLAGLAPFlllgVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
43-262 |
2.06e-61 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 193.09 E-value: 2.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 43 LFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRN-PLIAPLALTIFCWVFLMNVMDLVPId 121
Cdd:pfam00119 1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 122 fLPYPAEhwlgipylkvvPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELaLHPFNHPLMIPFNLLIEVVSLLAKP 201
Cdd:pfam00119 80 -SPGGFT-----------VTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKL-FVPPVPLPLVPLLLPIEIISEFARP 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 202 LSLGMRLFGNMFAGEVVFILCAAMLPW---------YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLS 262
Cdd:pfam00119 147 VSLSLRLFGNMLAGHLLLLLLAGLIFAllsagfllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
33-262 |
2.82e-37 |
|
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: 131.17 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 33 TSFWNVHIDSLFFSWFTGLIFLGIFYKVAKRttaGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLM 112
Cdd:TIGR01131 8 SPITLFSLTLLSLILLLSLLIFLISSSLSRW---LIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILIS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 113 NVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAkELALHPFNHPLmIPFNLLI 192
Cdd:TIGR01131 85 NLLGLIPYSF----------------TPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLA-HLVPSGTPLPL-IPFLVII 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503999423 193 EVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPW-------YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLS 262
Cdd:TIGR01131 147 ETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSlmssaifALLLLILVALIILEIFVAFIQAYVFTLLTCLYLN 223
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
99-262 |
7.15e-32 |
|
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: 115.19 E-value: 7.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 99 APLALTIFCWVFLMNVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELalh 178
Cdd:cd00310 5 LPLLGTLFLFILFSNLLGLIPYSF----------------TPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 179 PFNHPL-MIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAI------FHILVITIQAF 251
Cdd:cd00310 66 PPGTPLpLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLpvaltlLELFVAFIQAY 145
|
170
....*....|.
gi 503999423 252 VFMMLTIVYLS 262
Cdd:cd00310 146 VFTLLTAVYIS 156
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
34-267 |
3.67e-79 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 238.54 E-value: 3.67e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 34 SFWNVHIDSLFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:PRK05815 8 GFGGFNFDSLLLSVLLGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 114 VMDLVPIdflpypaehwlgipyLKVVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELALHPFnhPLMIPfnllIE 193
Cdd:PRK05815 88 LLGLIPY---------------LLFPPTADINVTLALALIVFVLVIYYGIKKKGLGGYLKEFYLQPH--PLLLP----IE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503999423 194 VVSLLAKPLSLGMRLFGNMFAGEVVFILC-----AAMLPWYLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHED 267
Cdd:PRK05815 147 IISEFSRPISLSLRLFGNMLAGELILALIallggAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISMAVEE 225
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
41-267 |
9.96e-75 |
|
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: 226.49 E-value: 9.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 41 DSLFFSWFTGLIFLGIFYKVAKRTtAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLvpi 120
Cdd:COG0356 1 DTVLMSWLAMLLLLLLFLLATRKL-KLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 121 dflpypaehwlgIPYLKvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELALHPFnhPLMIPFNLLIEVVSLLAK 200
Cdd:COG0356 77 ------------IPGLF-PPTADINVTLALALIVFVLVHYYGIKKKGLGGYLKHLFFPPF--PWLAPLMLPIEIISELAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503999423 201 PLSLGMRLFGNMFAGEVVFILCAAMLPW----YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHED 267
Cdd:COG0356 142 PLSLSLRLFGNMFAGHIILLLLAGLAPFlllgVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISLAVEE 212
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
43-262 |
2.06e-61 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 193.09 E-value: 2.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 43 LFFSWFTGLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRN-PLIAPLALTIFCWVFLMNVMDLVPId 121
Cdd:pfam00119 1 LLMSLIVALILLLFLLLATRKTKKLVPGRLQNFVEMLVEFVDNIVKDNIGKKKgRKFFPLLLTLFFFILVSNLLGLIPK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 122 fLPYPAEhwlgipylkvvPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELaLHPFNHPLMIPFNLLIEVVSLLAKP 201
Cdd:pfam00119 80 -SPGGFT-----------VTADINVTLALALIVFLLVHYYGIKKHGLGGYFKKL-FVPPVPLPLVPLLLPIEIISEFARP 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 202 LSLGMRLFGNMFAGEVVFILCAAMLPW---------YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLS 262
Cdd:pfam00119 147 VSLSLRLFGNMLAGHLLLLLLAGLIFAllsagfllgVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
33-262 |
2.82e-37 |
|
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: 131.17 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 33 TSFWNVHIDSLFFSWFTGLIFLGIFYKVAKRttaGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLM 112
Cdd:TIGR01131 8 SPITLFSLTLLSLILLLSLLIFLISSSLSRW---LIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILIS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 113 NVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAkELALHPFNHPLmIPFNLLI 192
Cdd:TIGR01131 85 NLLGLIPYSF----------------TPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLA-HLVPSGTPLPL-IPFLVII 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503999423 193 EVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPW-------YLQWMGSLPWAIFHILVITIQAFVFMMLTIVYLS 262
Cdd:TIGR01131 147 ETISYLARPISLSVRLFANISAGHLLLTLLSGLLFSlmssaifALLLLILVALIILEIFVAFIQAYVFTLLTCLYLN 223
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
99-262 |
7.15e-32 |
|
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: 115.19 E-value: 7.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 99 APLALTIFCWVFLMNVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELalh 178
Cdd:cd00310 5 LPLLGTLFLFILFSNLLGLIPYSF----------------TPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFL--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 179 PFNHPL-MIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAI------FHILVITIQAF 251
Cdd:cd00310 66 PPGTPLpLAPLMVPIELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSVGLLPLLLpvaltlLELFVAFIQAY 145
|
170
....*....|.
gi 503999423 252 VFMMLTIVYLS 262
Cdd:cd00310 146 VFTLLTAVYIS 156
|
|
| PRK13419 |
PRK13419 |
F0F1 ATP synthase subunit A; Provisional |
51-270 |
2.07e-18 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237381 Cd Length: 342 Bit Score: 83.25 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 51 LIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNV--KDTFHGRNPLIaPLALTIFCWVFLMNVMDLVPidflpYPAe 128
Cdd:PRK13419 122 VVFLAAGRKYKKMTKSQAPKGLANAMEALVEFIRLDVakSNIGHGYEKFL-PYLLTVFFFILVCNLLGLVP-----YGA- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 129 hwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKEL--ALHPFNHPLMIPfnllIEVVSLLAKPLSLGM 206
Cdd:PRK13419 195 ----------TATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLtgGTHWSLWIIMIP----IEFIGLFTKPFALTV 260
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503999423 207 RLFGNMFAGEVV-----FILCAAMLPWYLQWMgSLPWAIF----HILVITIQAFVFMMLTIVY--LSMAHEDPDH 270
Cdd:PRK13419 261 RLFANMTAGHIVilsliFISFILKSYIVAVAV-SVPFAIFiyllELFVAFLQAYIFTMLSALFigLATAHEGHDE 334
|
|
| PRK13421 |
PRK13421 |
F0F1 ATP synthase subunit A; Provisional |
51-270 |
1.83e-16 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237383 Cd Length: 223 Bit Score: 75.89 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 51 LIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPidflpypaehw 130
Cdd:PRK13421 30 MAVLAAGSALATRRLSLAPGRLQSVLELVVTTIDAQIRDTMQTDPAPYRALIGTLFLFVLVANWSSLVP----------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 131 lGIPylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELAlHPfnHPLMIPFNLlievVSLLAKPLSLGMRLFG 210
Cdd:PRK13421 99 -GVE----PPTAHLETDAALALIVFLATIYYGVRARGVRGYLATFA-EP--TWVMIPLNL----VEQLTRTFSLIVRLFG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503999423 211 NMFAGEVV--FILCAAMLpwylqwMGSLPWAIFHILVITIQAFVFMMLTIVYLSMAHEDPDH 270
Cdd:PRK13421 167 NVMSGVFVigIVLSLAGL------LVPIPLMALDLLTGAVQAYIFAVLAMVFIGAAVSDDEA 222
|
|
| PRK13420 |
PRK13420 |
F0F1 ATP synthase subunit A; Provisional |
41-262 |
2.68e-14 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237382 [Multi-domain] Cd Length: 226 Bit Score: 70.16 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 41 DSLFFSWFTgLIFLGIFYKVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPi 120
Cdd:PRK13420 18 ESVLTTWGI-MIVLVLASWLTTRRLSLDPGRFQVALEGVVSTIEDAIKEVLPRHARLVLPFVGTLWIFILVANLIGLIP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 121 dflpypAEHwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELaLHPFnhPLMIPFNLLIEVVSLLAk 200
Cdd:PRK13420 96 ------GFH---------SPTADLSVTAALALLVFFSVHWFGIRAEGLREYLKHY-LSPS--PFLLPFHLISEITRTLA- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503999423 201 plsLGMRLFGNM----FAGEVVFILCAAMLPwylqwmgsLPWAIFHILVITIQAFVFMMLTIVYLS 262
Cdd:PRK13420 157 ---LAVRLFGNImsleLAALLVLLVAGFLVP--------VPILMLHIIEALVQAYIFGMLALIYIA 211
|
|
| atpI |
CHL00046 |
ATP synthase CF0 A subunit |
38-260 |
3.58e-10 |
|
ATP synthase CF0 A subunit
Pssm-ID: 176987 Cd Length: 228 Bit Score: 58.41 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 38 VHIDSLFFSWFTGLIFLGIFYkVAKRTTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLI-APLALTIFCWVFLMN-VM 115
Cdd:CHL00046 21 VHGQVLITSWVVIAILLGSAL-LATRNLQTIPTGGQNFFEYVLEFIRDLAKTQIGEEEYRPwVPFIGTMFLFIFVSNwSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 116 DLVPIDFLPYPaEHWLGipylkvVPSADVNITMAMALGVfALMIFYS-IKVKGLGGFAKelALHPFnhPLMIPFNLLIEv 194
Cdd:CHL00046 100 ALLPWKLIELP-HGELA------APTNDINTTVALALLT-SVAYFYAgLSKKGLGYFGK--YIQPT--PILLPINILED- 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503999423 195 vslLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLqwmgSLPWAIFHILVITIQAFVFMMLTIVY 260
Cdd:CHL00046 167 ---FTKPLSLSFRLFGNILADELVVAVLVSLVPLVV----PIPVMFLGLFTSGIQALIFATLAAAY 225
|
|
| ATP6 |
MTH00175 |
ATP synthase F0 subunit 6; Provisional |
68-262 |
2.11e-07 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177228 Cd Length: 244 Bit Score: 50.78 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 68 VPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPIDFlpypaehwlgipylkvVPSADVNIT 147
Cdd:MTH00175 52 IPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVF----------------TPTAHIIIT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 148 MAMALGvfalmIFYSIKVKGLGGFAKEL--ALHPFNHPLMI-PFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAA 224
Cdd:MTH00175 116 FGLSLS-----IIIAVTLLGFLTFKWNFlsILMPGGAPLVLaPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSG 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503999423 225 ----MLPWYLQWMGSLPW------AIFHILVITIQAFVFMMLTIVYLS 262
Cdd:MTH00175 191 fafnMLSNGLIILSLFPMlimifiTLLEMAVAVIQAYVFCLLTTIYLG 238
|
|
| ATP6 |
MTH00172 |
ATP synthase F0 subunit 6; Provisional |
68-261 |
2.62e-07 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214447 Cd Length: 232 Bit Score: 50.04 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 68 VPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMNVMDLVPIDFLPypaehwlgipylkvvpsaDVNIT 147
Cdd:MTH00172 41 IPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNLLGLFPYVFTP------------------TTHIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 148 MAMALGVFalmIFYSIKVKGLGGFAKELA--LHPFNHPLMI-PFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVF----- 219
Cdd:MTH00172 103 VTLGLSFS---IIIGVTLAGFWRFKWDFFsiLMPSGAPLGLaPLLVLIETVSYISRAISLGVRLAANLSAGHLLFailag 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503999423 220 ----ILCAAMLPWYLQWMGSLPWAIFHILVITIQAFVFMMLTIVYL 261
Cdd:MTH00172 180 fgfnMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
|
|
| ATP6 |
MTH00176 |
ATP synthase F0 subunit 6; Provisional |
183-262 |
4.78e-07 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214449 Cd Length: 229 Bit Score: 49.26 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 183 PLMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLpWYLQWMGSLPWA----------IFHILVITIQAFV 252
Cdd:MTH00176 138 PLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGHLLLGLLGAAM-WGLLPVSPLIGFlllivqilyfMFEIAVCMIQAYV 216
|
90
....*....|
gi 503999423 253 FMMLTIVYLS 262
Cdd:MTH00176 217 FTLLLSLYLD 226
|
|
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
33-262 |
1.84e-06 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 47.47 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 33 TSFWNVHIDslFFSWFTGLIFLGIFYKVakrttagVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLM 112
Cdd:MTH00157 12 STSFNLSLN--WLSTFLGLLFIPSSFWL-------IPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 113 NVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGV-FALMIFYSIKvkglggFAKELALH--PFNHPLM-IPF 188
Cdd:MTH00157 83 NFLGLFPYIF----------------TSTSHLSLTLSLALPLwLSFMLFGWIN------NTNHMFAHlvPQGTPPIlMPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 189 NLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFIL---CAAMLPWYLQWMGSLPWAIFHIL---VITIQAFVFMMLTIVYLS 262
Cdd:MTH00157 141 MVLIETISNLIRPGTLAVRLAANMIAGHLLLTLlgnTGPSLSSMILSILILIQILLLILesaVAIIQSYVFSVLSTLYSS 220
|
|
| PRK13417 |
PRK13417 |
F0F1 ATP synthase subunit A; Provisional |
47-264 |
7.49e-06 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237380 Cd Length: 352 Bit Score: 46.42 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 47 WFTGLIFLGIFYKVAK---RTTAGVPGKLQCAVEMIVEFVADNVKD-TFHGRNPLIAPLALTIFCWVFLMNVMDLVP--- 119
Cdd:PRK13417 102 WIVAFFLFLIFIPAANiiaKNPLKVQSRFANTVEVFVNFLRKDIVDeSMHGHGHSYYHYIFTLFFFILFCNLMGLVPsvg 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 120 -----------------IDFLPYpAEHWLGIPYLKVVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKEL--ALHPF 180
Cdd:PRK13417 182 eltvvasdygglvalgvMDHTPH-ALPTFAKVWSGITVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVpnGVPLL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 181 NHPLMIPFNLlieVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQW-------MGSLPWAIFHILVITIQAFVF 253
Cdd:PRK13417 261 LYPIMWPLEF---IVSPMAKTFALTVRLLANMTAGHVIILALMGFIFQFQSWgivpvsvIGSGLIYVLEIFVAFLQAYIF 337
|
250
....*....|.
gi 503999423 254 MMLTIVYLSMA 264
Cdd:PRK13417 338 VLLTSLFVGLS 348
|
|
| ATP6 |
MTH00035 |
ATP synthase F0 subunit 6; Validated |
183-262 |
8.09e-06 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177110 Cd Length: 229 Bit Score: 45.73 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 183 PLMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLpWYLqwMGSLPWA-----------IFHILVITIQAF 251
Cdd:MTH00035 139 SFLIPLMVWIETLSLFAQPIALGLRLAANLTAGHLLIFLLSTAI-WEL--SNSPLISiitliiffllfILEIGVACIQAY 215
|
90
....*....|.
gi 503999423 252 VFMMLTIVYLS 262
Cdd:MTH00035 216 VFTALVHFYLE 226
|
|
| ATP6 |
MTH00120 |
ATP synthase F0 subunit 6; Provisional |
184-261 |
3.02e-05 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177181 Cd Length: 227 Bit Score: 44.04 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 184 LMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA----AMLPWYLQwMGSLPWAIFHIL------VITIQAFVF 253
Cdd:MTH00120 137 PLIPALILIETISLLIRPLALGVRLTANLTAGHLLIQLIStatlNLLPTMPT-LSLLTLIILLLLtilelaVAMIQAYVF 215
|
....*...
gi 503999423 254 MMLTIVYL 261
Cdd:MTH00120 216 VLLLSLYL 223
|
|
| ATP6 |
MTH00173 |
ATP synthase F0 subunit 6; Provisional |
34-260 |
3.40e-05 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214448 Cd Length: 231 Bit Score: 44.09 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 34 SFWNVHIDSLFFSWFTGLIFLGIFYKVakrtTAGVPGKLQCAVEMIVEFVADNVKDTFHGRNPLIAPLALTIFCWVFLMN 113
Cdd:MTH00173 11 DHNSSFSSLSFLMWLLSLMSLFFFSSS----VWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 114 VMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIkVKGLGGFAKELAlhPFNHPLM-IPFNLLI 192
Cdd:MTH00173 87 LSGLLPFVF----------------SVTSHLAFTFSLALPLWLSLILSGL-FYNPSKSLAGLV--PAGAPAGlNPFLVLI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503999423 193 EVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLP---WYLQWMGSLP-------WAIFHILVITIQAFVFMMLTIVY 260
Cdd:MTH00173 148 ETVSILIRPLTLTVRLLANISAGHIVLTLIGNYLSsslFSSSVVSLLLvlliqvgYFIFEVAVMLIQAYIFTLLIKLY 225
|
|
| ATP6 |
MTH00073 |
ATP synthase F0 subunit 6; Provisional |
184-261 |
1.16e-04 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177144 Cd Length: 227 Bit Score: 42.26 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 184 LMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA----AMLPW-----YLQWMGSLPWAIFHILVITIQAFVFM 254
Cdd:MTH00073 137 LLIPILIIIETISLFIRPLALGVRLTANLTAGHLLIQLIStatlVLLPLmptvsILTMIVLFLLTLLEIAVAMIQAYVFV 216
|
....*..
gi 503999423 255 MLTIVYL 261
Cdd:MTH00073 217 LLLSLYL 223
|
|
| ATP6 |
MTH00179 |
ATP synthase F0 subunit 6; Provisional |
101-261 |
2.60e-04 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177230 Cd Length: 227 Bit Score: 41.09 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 101 LALTIFCWVFLMNVMDLVPIDFlpypaehwlgipylkvVPSADVNITMAMALGVFALMIFYSIKVKGLGGFAKELalhPF 180
Cdd:MTH00179 72 LFLSLMLFLLTLNLLGLLPYTF----------------TPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLL---PE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 181 NHP-LMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCAAMLPWYLQWMGSLPWAIFHIL---------VITIQA 250
Cdd:MTH00179 133 GTPtPLIPMLVWIETISLLIRPLALGVRLTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLflltllevaVAMIQA 212
|
170
....*....|.
gi 503999423 251 FVFMMLTIVYL 261
Cdd:MTH00179 213 YVFVLLLSLYL 223
|
|
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
183-261 |
4.00e-04 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 40.63 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 183 PLMIPFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA----AMLP-----WYLQWMGSLPWAIFHILVITIQAFVF 253
Cdd:MTH00132 136 TPLIPVLIIIETISLFIRPLALGVRLTANLTAGHLLIQLIAtaafVLLPlmptvAILTATLLFLLTLLEVAVAMIQAYVF 215
|
....*...
gi 503999423 254 MMLTIVYL 261
Cdd:MTH00132 216 VLLLSLYL 223
|
|
| ATP6 |
MTH00005 |
ATP synthase F0 subunit 6; Provisional |
187-260 |
6.43e-03 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 164583 Cd Length: 231 Bit Score: 37.02 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999423 187 PFNLLIEVVSLLAKPLSLGMRLFGNMFAGEVVFILCA--AMLPWYLQWMGSLPWAIFHILVI-------TIQAFVFMMLT 257
Cdd:MTH00005 144 PFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGiyAASALFSSISSTILLILTQMGYIlfevgicLIQAYIFCLLL 223
|
...
gi 503999423 258 IVY 260
Cdd:MTH00005 224 SLY 226
|
|
|