|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
1.79e-123 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 349.17 E-value: 1.79e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00132 1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00132 81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
6-227 |
8.48e-50 |
|
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: 161.99 E-value: 8.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 6 FDQFLSP--TILGIPLIMLSLILP--WLLYPTSPNRWL-SNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:TIGR01131 2 FSQFDISpiTLFSLTLLSLILLLSllIFLISSSLSRWLiPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:TIGR01131 82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
66-224 |
2.33e-37 |
|
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: 127.90 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 66 GHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVI 145
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313666483 146 ETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVmptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQ 224
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
66-224 |
4.67e-32 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 116.05 E-value: 4.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 66 GHKWAAILTSLMILLISINLLGLL---PYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTS-IGHLLPE*TPNLLIPA 141
Cdd:pfam00119 54 GRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 142 LVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTL 221
Cdd:pfam00119 134 LLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAV 213
|
...
gi 313666483 222 YLQ 224
Cdd:pfam00119 214 YIS 216
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
61-225 |
8.63e-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: 94.37 E-value: 8.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 61 PINQQGHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTS-IGHLLPE*TPnLLI 139
Cdd:COG0356 49 TIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 140 PALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALltytvLFLLTILELAVAMIQAYVFVLLL 219
Cdd:COG0356 128 PLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL-----PVAWTAFELLVGFLQAYIFTMLT 202
|
....*.
gi 313666483 220 TLYLQE 225
Cdd:COG0356 203 AVYISL 208
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
1.79e-123 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 349.17 E-value: 1.79e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00132 1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00132 81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
|
|
| ATP6 |
MTH00073 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
5.62e-113 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177144 Cd Length: 227 Bit Score: 322.69 E-value: 5.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00073 1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00073 81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
|
|
| ATP6 |
MTH00120 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
2.44e-106 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177181 Cd Length: 227 Bit Score: 305.60 E-value: 2.44e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00120 1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00120 81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
|
|
| ATP6 |
MTH00179 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
6.26e-89 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177230 Cd Length: 227 Bit Score: 261.81 E-value: 6.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00179 1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00179 81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
|
|
| ATP6 |
MTH00101 |
ATP synthase F0 subunit 6; Validated |
1-226 |
5.99e-80 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177163 Cd Length: 226 Bit Score: 238.70 E-value: 5.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTsPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:MTH00101 1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPT-PNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:MTH00101 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
|
|
| ATP6 |
MTH00035 |
ATP synthase F0 subunit 6; Validated |
4-227 |
1.46e-51 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177110 Cd Length: 229 Bit Score: 166.69 E-value: 1.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 4 SFFDQFLSPTILGIPLIMLSLI--LPWLLYPTSPNrWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILLI 81
Cdd:MTH00035 6 SIFGQFSPDTILFIPLTLLSSViaLSWLFFINPTN-WLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFILIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 82 SINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVRL 161
Cdd:MTH00035 85 SINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313666483 162 TANLTAGHLLMQLIATAVFFLASVmPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00035 165 AANLTAGHLLIFLLSTAIWELSNS-PLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
6-227 |
8.48e-50 |
|
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: 161.99 E-value: 8.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 6 FDQFLSP--TILGIPLIMLSLILP--WLLYPTSPNRWL-SNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILL 80
Cdd:TIGR01131 2 FSQFDISpiTLFSLTLLSLILLLSllIFLISSSLSRWLiPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 81 ISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVR 160
Cdd:TIGR01131 82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313666483 161 LTANLTAGHLLMQLIATAVFFLASVMptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMSSA--IFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
|
|
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
1-225 |
4.74e-42 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 141.84 E-value: 4.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSpnRWLS-NRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMIL 79
Cdd:MTH00157 1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSS--FWLIpSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 80 LISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGV 159
Cdd:MTH00157 79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313666483 160 RLTANLTAGHLLMQLIATAVFFLASVMPTIALLTytvLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:MTH00157 159 RLAANMIAGHLLLTLLGNTGPSLSSMILSILILI---QILLLILESAVAIIQSYVFSVLSTLYSSE 221
|
|
| ATP6 |
MTH00176 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
7.41e-40 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214449 Cd Length: 229 Bit Score: 136.70 E-value: 7.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGIPLIMLSLILPWLLYPTSPNRW--LSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMI 78
Cdd:MTH00176 1 MLVDLFSSFDPPNKNIFSMISLSWITLLLFLLLMPSSVwfCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 79 LLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALG 158
Cdd:MTH00176 81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313666483 159 VRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQEN 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
|
|
| ATP6 |
MTH00173 |
ATP synthase F0 subunit 6; Provisional |
4-225 |
9.47e-40 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214448 Cd Length: 231 Bit Score: 136.53 E-value: 9.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 4 SFFDQFLSPTILGIPLIMLSLILPWLLYPtSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILLISI 83
Cdd:MTH00173 7 SSFDDHNSSFSSLSFLMWLLSLMSLFFFS-SSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 84 NLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVRLTA 163
Cdd:MTH00173 86 NLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313666483 164 NLTAGHLLMQLIATAV-FFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQE 225
Cdd:MTH00173 166 NISAGHIVLTLIGNYLsSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
66-224 |
2.33e-37 |
|
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: 127.90 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 66 GHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVI 145
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313666483 146 ETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVmptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQ 224
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSS---VGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
66-224 |
4.67e-32 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 116.05 E-value: 4.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 66 GHKWAAILTSLMILLISINLLGLL---PYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTS-IGHLLPE*TPNLLIPA 141
Cdd:pfam00119 54 GRKFFPLLLTLFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 142 LVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTL 221
Cdd:pfam00119 134 LLPIEIISEFARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAV 213
|
...
gi 313666483 222 YLQ 224
Cdd:pfam00119 214 YIS 216
|
|
| ATP6 |
MTH00005 |
ATP synthase F0 subunit 6; Provisional |
70-222 |
7.55e-31 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 164583 Cd Length: 231 Bit Score: 113.29 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 70 AAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETIS 149
Cdd:MTH00005 74 SSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETIS 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 313666483 150 LFIRPLALGVRLTANLTAGHLLMQLIA--TAVFFLASVMPTIALLTYTVLFLLtiLELAVAMIQAYVFVLLLTLY 222
Cdd:MTH00005 154 ILVRPITLSFRLAANMSAGHIVLSLIGiyAASALFSSISSTILLILTQMGYIL--FEVGICLIQAYIFCLLLSLY 226
|
|
| ATP6 |
MTH00172 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
3.32e-30 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214447 Cd Length: 232 Bit Score: 111.67 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGI--PLIMLSLILPWLLYPTSPNRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMI 78
Cdd:MTH00172 1 MSSSYFDQFNIVWLIGLtnSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 79 LLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALG 158
Cdd:MTH00172 81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313666483 159 VRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00172 161 VRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
|
|
| ATP6 |
MTH00175 |
ATP synthase F0 subunit 6; Provisional |
1-227 |
6.79e-29 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177228 Cd Length: 244 Bit Score: 108.56 E-value: 6.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 1 MTLSFFDQFLSPTILGIP---------------LIMLSLILPWLLYPTS---PNRWLSNRLLTLENwfifrttAQLMVPI 62
Cdd:MTH00175 1 MLAAYFDQFNIIRLITIQaflgdwlvtftnssmMMVLAVIIFWLLLKGDkliPNRWQSIMELIYLN-------IRSVVHD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 63 N--QQGHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIP 140
Cdd:MTH00175 74 NlgKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 141 ALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVF-FLASVMPTIALLTYTVLFLLTILELAVAMIQAYVFVLLL 219
Cdd:MTH00175 154 FLVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLT 233
|
....*...
gi 313666483 220 TLYLQENI 227
Cdd:MTH00175 234 TIYLGDTI 241
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
61-225 |
8.63e-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: 94.37 E-value: 8.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 61 PINQQGHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTS-IGHLLPE*TPnLLI 139
Cdd:COG0356 49 TIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 140 PALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALltytvLFLLTILELAVAMIQAYVFVLLL 219
Cdd:COG0356 128 PLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSLLL-----PVAWTAFELLVGFLQAYIFTMLT 202
|
....*.
gi 313666483 220 TLYLQE 225
Cdd:COG0356 203 AVYISL 208
|
|
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
62-225 |
2.54e-20 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 85.62 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 62 INQQGHKWAAILTSLMILLISINLLGLLP-YTFTPTTQLSMNMGFAVPMWLATVLIGLRNQpttSIGHLLPE*TPNLlIP 140
Cdd:PRK05815 65 IGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 141 ALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALLTytvlFLLTILELAVAMIQAYVFVLLLT 220
Cdd:PRK05815 141 LLLPIEIISEFSRPISLSLRLFGNMLAGELILALIALLGGAGLLLALAPLILP----VAWTIFEIFVGTLQAYIFMMLTI 216
|
....*
gi 313666483 221 LYLQE 225
Cdd:PRK05815 217 VYISM 221
|
|
| ATP6 |
MTH00174 |
ATP synthase F0 subunit 6; Provisional |
36-227 |
3.13e-20 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 133799 Cd Length: 252 Bit Score: 85.76 E-value: 3.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 36 NRWLSNRLLTLENWFIFRTTAQLMVPINQQGHKWAAILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVL 115
Cdd:MTH00174 57 NTLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 116 IGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLFIRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTI-ALLTY 194
Cdd:MTH00174 137 AGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPF 216
|
170 180 190
....*....|....*....|....*....|...
gi 313666483 195 TVLFLLTILELAVAMIQAYVFVLLLTLYLQENI 227
Cdd:MTH00174 217 AILIFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
|
|
| PRK13419 |
PRK13419 |
F0F1 ATP synthase subunit A; Provisional |
72-223 |
6.44e-14 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237381 Cd Length: 342 Bit Score: 69.39 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 72 ILTSLMILLIsINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETISLF 151
Cdd:PRK13419 174 LLTVFFFILV-CNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLF 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313666483 152 IRPLALGVRLTANLTAGHLLMQLIATAVFFLASVMPTIALltyTVLFLLTI--LELAVAMIQAYVFVLLLTLYL 223
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIVILSLIFISFILKSYIVAVAV---SVPFAIFIylLELFVAFLQAYIFTMLSALFI 323
|
|
| ATP6 |
MTH00087 |
ATP synthase F0 subunit 6; Provisional |
75-225 |
1.91e-11 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177152 Cd Length: 195 Bit Score: 60.76 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 75 SLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSigHLLPE*TPNLLIP-ALVVIETISLFIR 153
Cdd:MTH00087 57 FTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTfSMLFVEIVSELSR 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313666483 154 PLALGVRLTANLTAGHLLMQLIATAVFFlasvmptialltYTVLFLLTIL-ELAVAMIQAYVFVLLLTLYLQE 225
Cdd:MTH00087 135 PLALTLRLTVNLMVGHLISSLLNFLGEK------------YVWLSILAIMmECFVAFIQSYIFSRLIYLYLNE 195
|
|
| PRK13417 |
PRK13417 |
F0F1 ATP synthase subunit A; Provisional |
94-223 |
4.80e-09 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237380 Cd Length: 352 Bit Score: 55.28 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 94 TPTTQLSMNMGFAVPMWLATVLIGLRNQPTTSIGHLLPE*TPNLLIPALVVIETI-SLFIRPLALGVRLTANLTAGHLLM 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 313666483 173 QLIATAVFFLASVMptIALLTYTVLFLLTILELAVAMIQAYVFVLLLTLYL 223
Cdd:PRK13417 297 LALMGFIFQFQSWG--IVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
|
|
| PRK13420 |
PRK13420 |
F0F1 ATP synthase subunit A; Provisional |
75-223 |
2.71e-04 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237382 [Multi-domain] Cd Length: 226 Bit Score: 40.88 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 75 SLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTsiGHLLPE*TPNlliPALVVIETISLFIRP 154
Cdd:PRK13420 80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVFFSVHWFGIRAEGLR--EYLKHYLSPS---PFLLPFHLISEITRT 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313666483 155 LALGVRLTANLTAghllMQLIATAVFFLASVMPTIALLtytvlfLLTILElavAMIQAYVFVLLLTLYL 223
Cdd:PRK13420 155 LALAVRLFGNIMS----LELAALLVLLVAGFLVPVPIL------MLHIIE---ALVQAYIFGMLALIYI 210
|
|
| PRK13421 |
PRK13421 |
F0F1 ATP synthase subunit A; Provisional |
71-218 |
3.51e-03 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237383 Cd Length: 223 Bit Score: 37.37 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313666483 71 AILTSLMILLISINLLGLLPYTFTPTTQLSMNMGFAVPMWLATVLIGLRNQPTTsiGHLLPE*TPNLLIPALVVIETISl 150
Cdd:PRK13421 79 ALIGTLFLFVLVANWSSLVPGVEPPTAHLETDAALALIVFLATIYYGVRARGVR--GYLATFAEPTWVMIPLNLVEQLT- 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 313666483 151 fiRPLALGVRLTANLTAGhllmqliataVFFLASVMPTIALLtytVLFLLTILELAVAMIQAYVFVLL 218
Cdd:PRK13421 156 --RTFSLIVRLFGNVMSG----------VFVIGIVLSLAGLL---VPIPLMALDLLTGAVQAYIFAVL 208
|
|
|