|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00101 |
ATP synthase F0 subunit 6; Validated |
1-226 |
1.68e-143 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177163 Cd Length: 226 Bit Score: 399.71 E-value: 1.68e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIG 80
Cdd:MTH00101 1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 722489951 161 TANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
15-225 |
7.50e-55 |
|
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: 174.70 E-value: 7.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 15 MGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFTP 94
Cdd:TIGR01131 17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 95 TTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLI 174
Cdd:TIGR01131 97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 722489951 175 GEATLVLMSISPATafITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
65-222 |
1.28e-42 |
|
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.
Pssm-ID: 349411 [Multi-domain] Cd Length: 156 Bit Score: 141.38 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 65 GQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIII 144
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 722489951 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGEATLVLMSISpatAFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
14-223 |
1.20e-39 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 135.70 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 14 MMGFPIVILIIMFPSIMFPTPnRLINNRLVAIQQWLIQLISKQMMA-IHNQKGQTWTLMLISLILFIGSTNLLGLL---P 89
Cdd:pfam00119 3 MSLIVALILLLFLLLATRKTK-KLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 90 HSFTPTTQLSMNLGMAIPLWAGTVISGFR-HKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGH 168
Cdd:pfam00119 82 GGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 722489951 169 LLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
19-224 |
1.83e-26 |
|
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: 101.30 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 19 IVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:COG0356 8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 99 SMNLGMAIPLWAGTVISGFRHK-TKASLAHFLPQGTPlPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIgea 177
Cdd:COG0356 88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL--- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 722489951 178 tlVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356 164 --AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ATP6 |
MTH00101 |
ATP synthase F0 subunit 6; Validated |
1-226 |
1.68e-143 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177163 Cd Length: 226 Bit Score: 399.71 E-value: 1.68e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIG 80
Cdd:MTH00101 1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPTPNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00101 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 722489951 161 TANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00101 161 TANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDNT 226
|
|
| ATP6 |
MTH00120 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
2.68e-92 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177181 Cd Length: 227 Bit Score: 270.16 E-value: 2.68e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTP-NRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFI 79
Cdd:MTH00120 1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPkNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00120 81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 722489951 160 LTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
|
|
| ATP6 |
MTH00073 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
4.15e-89 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177144 Cd Length: 227 Bit Score: 262.21 E-value: 4.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTP-NRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFI 79
Cdd:MTH00073 1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPtNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00073 81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 722489951 160 LTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
|
|
| ATP6 |
MTH00132 |
ATP synthase F0 subunit 6; Provisional |
1-225 |
7.91e-89 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177190 Cd Length: 227 Bit Score: 261.35 E-value: 7.91e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTP-NRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFI 79
Cdd:MTH00132 1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPtSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00132 81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 722489951 160 LTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
|
|
| ATP6 |
MTH00179 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
1.02e-76 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177230 Cd Length: 227 Bit Score: 230.61 E-value: 1.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTP-NRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFI 79
Cdd:MTH00179 1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLtNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVR 159
Cdd:MTH00179 81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 722489951 160 LTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
|
|
| ATP_synt_6_or_A |
TIGR01131 |
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ... |
15-225 |
7.50e-55 |
|
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: 174.70 E-value: 7.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 15 MGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFTP 94
Cdd:TIGR01131 17 LLSLILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 95 TTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLI 174
Cdd:TIGR01131 97 TSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 722489951 175 GEATLVLMSISPATafITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:TIGR01131 177 SGLLFSLMSSAIFA--LLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
|
|
| ATP6 |
MTH00157 |
ATP synthase F0 subunit 6; Provisional |
1-221 |
4.16e-50 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214441 Cd Length: 223 Bit Score: 162.64 E-value: 4.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 1 MNENLFASFATPTMMGFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIG 80
Cdd:MTH00157 1 MMTNLFSIFDPSTSFNLSLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 81 STNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRL 160
Cdd:MTH00157 81 FNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 722489951 161 TANITAGHLLIHLIGEATLVLMSIspaTAFITFIILVMLTILEFAVALIQAYVFTLLVSLY 221
Cdd:MTH00157 161 AANMIAGHLLLTLLGNTGPSLSSM---ILSILILIQILLLILESAVAIIQSYVFSVLSTLY 218
|
|
| ATP6 |
MTH00035 |
ATP synthase F0 subunit 6; Validated |
1-225 |
7.38e-50 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177110 Cd Length: 229 Bit Score: 162.06 E-value: 7.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 1 MNENLFASFATPTMMGFPIVIL--IIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILF 78
Cdd:MTH00035 3 INNSIFGQFSPDTILFIPLTLLssVIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 79 IGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAV 158
Cdd:MTH00035 83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 722489951 159 RLTANITAGHLLIHLIGEATLVLMSiSPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDN 225
Cdd:MTH00035 163 RLAANLTAGHLLIFLLSTAIWELSN-SPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
|
|
| ATP-synt_Fo_a_6 |
cd00310 |
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ... |
65-222 |
1.28e-42 |
|
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.
Pssm-ID: 349411 [Multi-domain] Cd Length: 156 Bit Score: 141.38 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 65 GQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIII 144
Cdd:cd00310 1 GKKYLPLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 722489951 145 ETISLFIQPMALAVRLTANITAGHLLIHLIGEATLVLMSISpatAFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:cd00310 81 ELISELIRPLSLSVRLFANMFAGHLLLALLSGLVPSLLSSV---GLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
|
|
| ATP6 |
MTH00173 |
ATP synthase F0 subunit 6; Provisional |
5-224 |
3.19e-41 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214448 Cd Length: 231 Bit Score: 140.00 E-value: 3.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 5 LFASFATPTMMGFPIVILIIMFPS---IMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGS 81
Cdd:MTH00173 5 LFSSFDDHNSSFSSLSFLMWLLSLmslFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLIS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 82 TNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLT 161
Cdd:MTH00173 85 LNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 722489951 162 ANITAGHLLIHLIGEA-TLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00173 165 ANISAGHIVLTLIGNYlSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
|
|
| ATP6 |
MTH00176 |
ATP synthase F0 subunit 6; Provisional |
1-226 |
1.24e-40 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214449 Cd Length: 229 Bit Score: 138.63 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 1 MNENLFASFATPTMMGFPIVILI---IMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLIL 77
Cdd:MTH00176 1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 78 FIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALA 157
Cdd:MTH00176 81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 722489951 158 VRLTANITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00176 161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
|
|
| ATP-synt_A |
pfam00119 |
ATP synthase A chain; |
14-223 |
1.20e-39 |
|
ATP synthase A chain;
Pssm-ID: 459679 [Multi-domain] Cd Length: 216 Bit Score: 135.70 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 14 MMGFPIVILIIMFPSIMFPTPnRLINNRLVAIQQWLIQLISKQMMA-IHNQKGQTWTLMLISLILFIGSTNLLGLL---P 89
Cdd:pfam00119 3 MSLIVALILLLFLLLATRKTK-KLVPGRLQNFVEMLVEFVDNIVKDnIGKKKGRKFFPLLLTLFFFILVSNLLGLIpksP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 90 HSFTPTTQLSMNLGMAIPLWAGTVISGFR-HKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGH 168
Cdd:pfam00119 82 GGFTVTADINVTLALALIVFLLVHYYGIKkHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAGH 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 722489951 169 LLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLH 223
Cdd:pfam00119 162 LLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
|
|
| ATP6 |
MTH00172 |
ATP synthase F0 subunit 6; Provisional |
5-224 |
4.80e-33 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 214447 Cd Length: 232 Bit Score: 118.99 E-value: 4.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 5 LFASFATPTMMGFPIVILIIMFPSimfptpNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNL 84
Cdd:MTH00172 14 LIGLTNSSIMMILVIIVVLLLFKG------IKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFFFIVFLNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 85 LGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANI 164
Cdd:MTH00172 88 LGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 165 TAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00172 168 SAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLAD 227
|
|
| ATP6 |
MTH00005 |
ATP synthase F0 subunit 6; Provisional |
4-226 |
5.92e-33 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 164583 Cd Length: 231 Bit Score: 118.68 E-value: 5.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 4 NLFASFATPTMMGFPIVILIIMFPSIMFPTPNRLInnrlvAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTN 83
Cdd:MTH00005 14 NSLFNNLSSTAFWAFNFSIILLLSSSFWITPNRLS-----SIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 84 LLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTAN 163
Cdd:MTH00005 89 LSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAAN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 722489951 164 ITAGHLLIHLIGEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHDNT 226
Cdd:MTH00005 169 MSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
|
|
| ATP6 |
MTH00175 |
ATP synthase F0 subunit 6; Provisional |
14-224 |
8.26e-31 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177228 Cd Length: 244 Bit Score: 113.56 E-value: 8.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 14 MMGFPIVILIIMFPSimfptpNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFT 93
Cdd:MTH00175 34 MMVLAVIIFWLLLKG------DKLIPNRWQSIMELIYLNIRSVVHDNLGKSGQKYFPFILSLFLFIAILNILGLFPYVFT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 94 PTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHL 173
Cdd:MTH00175 108 PTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGHLLFAI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 722489951 174 I-GEATLVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:MTH00175 188 LsGFAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYLGD 239
|
|
| AtpB |
COG0356 |
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ... |
19-224 |
1.83e-26 |
|
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: 101.30 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 19 IVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQL 98
Cdd:COG0356 8 LAMLLLLLLFLLATRKLKLVPGGLQNFVEMLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 99 SMNLGMAIPLWAGTVISGFRHK-TKASLAHFLPQGTPlPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIgea 177
Cdd:COG0356 88 NVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLL--- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 722489951 178 tlVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:COG0356 164 --AGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
|
|
| PRK05815 |
PRK05815 |
F0F1 ATP synthase subunit A; Validated |
19-224 |
2.07e-23 |
|
F0F1 ATP synthase subunit A; Validated
Pssm-ID: 235617 Cd Length: 227 Bit Score: 93.71 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 19 IVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLISKQMMAIHNQKGQTWTLMLISLILFIGSTNLLGLLP-HSFTPTTQ 97
Cdd:PRK05815 23 LGVLILLLFALVATRKLSGVPGGLQNFVEMIVEFVRGQVKDNIGGKGKKFAPLAFTLFLFILLMNLLGLIPyLLFPPTAD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 98 LSMNLGMAIPLWAGTVISGFRHKtkaSLAHFLPQGTPLPlIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIGea 177
Cdd:PRK05815 103 INVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGELILALIA-- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 722489951 178 tlVLMSISPATAFITFIILVMLTILEFAVALIQAYVFTLLVSLYLHD 224
Cdd:PRK05815 177 --LLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
|
|
| ATP6 |
MTH00174 |
ATP synthase F0 subunit 6; Provisional |
64-224 |
2.25e-22 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 133799 Cd Length: 252 Bit Score: 91.54 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 64 KGQTWTLMLISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASLAHFLPQGTPLPLIPMLII 143
Cdd:MTH00174 86 KGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 144 IETISLFIQPMALAVRLTANITAGHLLIHLIGEATLVLMSISPAT-AFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00174 166 IETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMINTGILIgSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245
|
..
gi 722489951 223 HD 224
Cdd:MTH00174 246 RD 247
|
|
| PRK13419 |
PRK13419 |
F0F1 ATP synthase subunit A; Provisional |
72-222 |
8.03e-19 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237381 Cd Length: 342 Bit Score: 83.25 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 72 LISLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFR-HKTKASLAHfLPQGTPLPLIPMLIIIETISLF 150
Cdd:PRK13419 174 LLTVFFFILVCNLLGLVPYGATATGNINVTLTLAVFTFFITQYAAIKaHGIKGYLAH-LTGGTHWSLWIIMIPIEFIGLF 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 722489951 151 IQPMALAVRLTANITAGHLLI-HLIGEATLVLMSISPATAFITFIILVMLtiLEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13419 253 TKPFALTVRLFANMTAGHIVIlSLIFISFILKSYIVAVAVSVPFAIFIYL--LELFVAFLQAYIFTMLSALFI 323
|
|
| ATP6 |
MTH00087 |
ATP synthase F0 subunit 6; Provisional |
71-222 |
3.11e-11 |
|
ATP synthase F0 subunit 6; Provisional
Pssm-ID: 177152 Cd Length: 195 Bit Score: 60.38 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 71 MLISLILFigstNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVISGFRHKTKASlaHFLPQGTPLPLIPM-LIIIETISL 149
Cdd:MTH00087 58 TFIVLLLF----CFGGLFPYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTFsMLFVEIVSE 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 722489951 150 FIQPMALAVRLTANITAGHLLIHLIGEATlvlmsispataFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:MTH00087 132 LSRPLALTLRLTVNLMVGHLISSLLNFLG-----------EKYVWLSILAIMMECFVAFIQSYIFSRLIYLYL 193
|
|
| PRK13417 |
PRK13417 |
F0F1 ATP synthase subunit A; Provisional |
65-222 |
1.15e-09 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237380 Cd Length: 352 Bit Score: 57.21 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 65 GQTWTLMLISLILFIGSTNLLGLLP----------------------------HSF-------TPTTQLSMNLGMAIPLW 109
Cdd:PRK13417 154 GHSYYHYIFTLFFFILFCNLMGLVPsvgeltvvasdygglvalgvmdhtphalPTFakvwsgiTVTGDISVTMTLALLTM 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 110 AGTVISGFRHKTKASLAHFLPQGTPLPLIPMLIIIETI-SLFIQPMALAVRLTANITAGHLLIhlIGEATLVLMSISPAT 188
Cdd:PRK13417 234 FLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII--LALMGFIFQFQSWGI 311
|
170 180 190
....*....|....*....|....*....|....
gi 722489951 189 AFITFIILVMLTILEFAVALIQAYVFTLLVSLYL 222
Cdd:PRK13417 312 VPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
|
|
| PRK13420 |
PRK13420 |
F0F1 ATP synthase subunit A; Provisional |
74-222 |
2.15e-04 |
|
F0F1 ATP synthase subunit A; Provisional
Pssm-ID: 237382 [Multi-domain] Cd Length: 226 Bit Score: 40.88 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 74 SLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPL-----WAGTVISGFRhktkASLAHFLPQGtplpliPMLIIIETIS 148
Cdd:PRK13420 80 TLWIFILVANLIGLIPGFHSPTADLSVTAALALLVffsvhWFGIRAEGLR----EYLKHYLSPS------PFLLPFHLIS 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 722489951 149 LFIQPMALAVRLTANITAGHLLihligeATLVLMsispATAFITFIILVMLTILEfavALIQAYVFTLLVSLYL 222
Cdd:PRK13420 150 EITRTLALAVRLFGNIMSLELA------ALLVLL----VAGFLVPVPILMLHIIE---ALVQAYIFGMLALIYI 210
|
|
| CYP5A1 |
cd20649 |
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ... |
6-64 |
5.78e-03 |
|
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; Cytochrome P450 5A1 (CYP5A1), also called thromboxane-A synthase (EC 5.3.99.5) or thromboxane synthetase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid that has been implicated in stroke, asthma, and various cardiovascular diseases, due to its acute and chronic effects in promoting platelet aggregation, vasoconstriction, bronchoconstriction, and proliferation. CYP5A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.
Pssm-ID: 410742 [Multi-domain] Cd Length: 457 Bit Score: 37.13 E-value: 5.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 722489951 6 FASFATPtmmgFPIVILIIMFPSIMFPTPNRLINNRLVAIQQWLIQLIsKQMMAIHNQK 64
Cdd:cd20649 144 FFEFSFF----RPILILFLAFPFIMIPLARILPNKSRDELNSFFTQCI-RNMIAFRDQQ 197
|
|
| ATP6 |
MTH00050 |
ATP synthase F0 subunit 6; Validated |
126-215 |
8.31e-03 |
|
ATP synthase F0 subunit 6; Validated
Pssm-ID: 177125 Cd Length: 170 Bit Score: 36.02 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 722489951 126 AHFLPQGTPLPLIPMLIIIETISLFIQPMALAVRLTANITAGHLLIHLIGeaTLVLMSispataFITFIILVMLTILEFA 205
Cdd:MTH00050 80 SSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLGCFGGVALG--NLCFIS------YWWFLVLFFLFFYEVF 151
|
90
....*....|
gi 722489951 206 VALIQAYVFT 215
Cdd:MTH00050 152 VALVHWFIVS 161
|
|
|