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Conserved domains on  [gi|1593549712|ref|YP_009561234|]
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ATP synthase F0 subunit 6 (mitochondrion) [Geochelone elegans]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009577)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-225 2.82e-102

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177190  Cd Length: 227  Bit Score: 295.24  E-value: 2.82e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGIPLITLALLAPSLIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAML 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593549712 161 LTANLTAGHLLIQLTSTAALTLTP-MTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQEN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPlMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-225 2.82e-102

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 295.24  E-value: 2.82e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGIPLITLALLAPSLIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAML 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593549712 161 LTANLTAGHLLIQLTSTAALTLTP-MTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQEN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPlMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
6-225 3.42e-43

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: 145.04  E-value: 3.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   6 FDQFMSPQ--ILGIPLITLALLAPS---LIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAML 80
Cdd:TIGR01131   2 FSQFDISPitLFSLTLLSLILLLSLlifLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1593549712 161 LTANLTAGHLLIQLTSTAALTLTPMtTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQEN 225
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMSS-AIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
90-223 6.02e-30

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 108.64  E-value: 6.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310    25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1593549712 170 LLIQLTSTAALTLtpMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQ 223
Cdd:cd00310   105 LLLALLSGLVPSL--LSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
90-223 7.83e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 94.48  E-value: 7.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1593549712 169 HLLIQLTSTAALTLTPMTTLFILTTIILLLLTILE-LAVAMIQAYVFVLLLSLYLQ 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFeLLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
90-224 1.57e-15

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: 72.41  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLLPVGTPtPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356    78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1593549712 169 HLLIQLtstaALTLTPMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQE 224
Cdd:COG0356   157 HIILLL----LAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
1-225 2.82e-102

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 295.24  E-value: 2.82e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGIPLITLALLAPSLIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAML 80
Cdd:MTH00132    1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00132   81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593549712 161 LTANLTAGHLLIQLTSTAALTLTP-MTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQEN 225
Cdd:MTH00132  161 LTANLTAGHLLIQLIATAAFVLLPlMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
1-226 4.01e-100

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 289.80  E-value: 4.01e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGIPLITLALLAPSLIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAML 80
Cdd:MTH00120    1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00120   81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1593549712 161 LTANLTAGHLLIQLTSTAALTLTP-MTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 226
Cdd:MTH00120  161 LTANLTAGHLLIQLISTATLNLLPtMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
1-226 5.48e-99

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 287.25  E-value: 5.48e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGIPLITLALLAPSLIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAML 80
Cdd:MTH00073    1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00073   81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1593549712 161 LTANLTAGHLLIQLTSTAALTLTPMTTLFILTTIILLLLTILE-LAVAMIQAYVFVLLLSLYLQENT 226
Cdd:MTH00073  161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLeIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
1-226 1.10e-78

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 235.61  E-value: 1.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGIPLITLALLAPSLIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAML 80
Cdd:MTH00179    1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00179   81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1593549712 161 LTANLTAGHLLIQLTSTAALTLTP-MTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 226
Cdd:MTH00179  161 LTANITAGHLLMHLISSAVFVLMNfMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQENL 227
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
1-226 1.36e-71

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 217.51  E-value: 1.36e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGIPLITLALLAPSLIFPTqNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAML 80
Cdd:MTH00101    1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPT-PNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:MTH00101   80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1593549712 161 LTANLTAGHLLIQLTSTAALTLTPMTTLFILTTIILLLLTILE-LAVAMIQAYVFVLLLSLYLQENT 226
Cdd:MTH00101  160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILeFAVALIQAYVFTLLVSLYLHDNT 226
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
6-225 3.42e-43

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: 145.04  E-value: 3.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   6 FDQFMSPQ--ILGIPLITLALLAPS---LIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAML 80
Cdd:TIGR01131   2 FSQFDISPitLFSLTLLSLILLLSLlifLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  81 LMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVR 160
Cdd:TIGR01131  82 LISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVR 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1593549712 161 LTANLTAGHLLIQLTSTAALTLTPMtTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQEN 225
Cdd:TIGR01131 162 LFANISAGHLLLTLLSGLLFSLMSS-AIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDA 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
1-225 2.55e-41

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 140.49  E-value: 2.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGIPLITLAL-LAPSLIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAM 79
Cdd:MTH00035    3 INNSIFGQFSPDTILFIPLTLLSSvIALSWLFFINPTNWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTVFIL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  80 LLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGV 159
Cdd:MTH00035   83 ILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593549712 160 RLTANLTAGHLLIQLTSTAALTLTPMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQEN 225
Cdd:MTH00035  163 RLAANLTAGHLLIFLLSTAIWELSNSPLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQN 228
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
39-224 2.27e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 122.20  E-value: 2.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  39 LTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGL 118
Cdd:MTH00157   38 IPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFSFILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGW 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712 119 RNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGHLLIQLTSTAALTLTPMttLFILTTIILLL 198
Cdd:MTH00157  118 INNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGHLLLTLLGNTGPSLSSM--ILSILILIQIL 195
                         170       180
                  ....*....|....*....|....*.
gi 1593549712 199 LTILELAVAMIQAYVFVLLLSLYLQE 224
Cdd:MTH00157  196 LLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
1-226 6.60e-32

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 115.90  E-value: 6.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGIPLITLA---LLAPSLIFPTQNNRWLTNRLSTLQSWaVNLFTKQLMTPINKTGHKWSIILTSLM 77
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSwitLLLFLLLMPSSVWFCPSKLQVFMLMF-STFLPEMILRSNGSYILGSASIIISLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  78 AMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLAL 157
Cdd:MTH00176   80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712 158 GVRLTANLTAGHLLIQLTSTAALTLTPMTTLFILTTIILLLLTILE-LAVAMIQAYVFVLLLSLYLQENT 226
Cdd:MTH00176  160 AVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFeIAVCMIQAYVFTLLLSLYLDEHP 229
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
90-223 6.02e-30

ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms are designated as ATP synthase, Fo complex, subunit a; eukaryotic (chloroplast and mitochondrial) forms are designated as ATP synthase, Fo complex, subunit 6. The F-ATP synthases (also called FoF1-ATPases) consist of two structural domains: F1 (factor one) complex containing the soluble catalytic core, and Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. F-ATP synthase has also been found in the archaea Methanosarcina acetivorans. F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis.


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 108.64  E-value: 6.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGH 169
Cdd:cd00310    25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1593549712 170 LLIQLTSTAALTLtpMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQ 223
Cdd:cd00310   105 LLLALLSGLVPSL--LSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
38-224 1.42e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 107.26  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  38 WLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTG 117
Cdd:MTH00173   40 VSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712 118 LRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGHLLIQLTS--TAALTLTPMTTLFILTTII 195
Cdd:MTH00173  120 LFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGHIVLTLIGnyLSSSLFSSSVVSLLLVLLI 199
                         170       180
                  ....*....|....*....|....*....
gi 1593549712 196 LLLLTILELAVAMIQAYVFVLLLSLYLQE 224
Cdd:MTH00173  200 QVGYFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
28-226 2.69e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 96.34  E-value: 2.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  28 SLIFPTQNNRWLT-NRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAMLLMINLLGLLPYTFTPTTQLSMNMGLA 106
Cdd:MTH00005   31 SIILLLSSSFWITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIILMNLSGLLPYVFSTSSHLIFTLTLG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712 107 IPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGHLLIQLTST-AALTLTPM 185
Cdd:MTH00005  111 LPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGHIVLSLIGIyAASALFSS 190
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1593549712 186 TTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 226
Cdd:MTH00005  191 ISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP-synt_A pfam00119
ATP synthase A chain;
90-223 7.83e-24

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 94.48  E-value: 7.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHgLGGYFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1593549712 169 HLLIQLTSTAALTLTPMTTLFILTTIILLLLTILE-LAVAMIQAYVFVLLLSLYLQ 223
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFeLLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
1-222 2.31e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 88.56  E-value: 2.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712   1 MNLTFFDQFMSPQILGI--PLITLALLAPSLIFPTQNNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMA 78
Cdd:MTH00172    1 MSSSYFDQFNIVWLIGLtnSSIMMILVIIVVLLLFKGIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  79 MLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALG 158
Cdd:MTH00172   81 FIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1593549712 159 VRLTANLTAGHLLIQ-LTSTAALTLTPMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYL 222
Cdd:MTH00172  161 VRLAANLSAGHLLFAiLAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
62-222 2.80e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 80.44  E-value: 2.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  62 INKTGHKWSIILTSLMAMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPI 141
Cdd:MTH00175   75 LGKSGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPF 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712 142 LIMIETISLFIRPLALGVRLTANLTAGHLLIQLTSTAALTL--TPMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLS 219
Cdd:MTH00175  155 LVLIETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFNMlsNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTT 234

                  ...
gi 1593549712 220 LYL 222
Cdd:MTH00175  235 IYL 237
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
90-224 1.57e-15

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: 72.41  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLLPVGTPtPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:COG0356    78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1593549712 169 HLLIQLtstaALTLTPMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQE 224
Cdd:COG0356   157 HIILLL----LAGLAPFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYISL 208
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
35-224 4.60e-15

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 71.89  E-value: 4.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  35 NNRWLTNRLSTLQSWAVNLFTKQLMTPINKTGHKWSIILTSLMAMLLMINLLGLLPYTFTPTTQLSMNMGLAIPMWMATV 114
Cdd:MTH00174   56 NNTLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTT 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712 115 LTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAGHLLIQLTSTAALTL--TPMTTLFILT 192
Cdd:MTH00174  136 LAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSIIASFAWKMinTGILIGSFVP 215
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1593549712 193 TIILLLLTILELAVAMIQAYVFVLLLSLYLQE 224
Cdd:MTH00174  216 FAILIFVTILEMAVAIIQAYVFTLLTIVYLRD 247
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
91-224 1.11e-12

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 64.82  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  91 YTFTPTTQLSMNMGLAIPMWMATVLTGLRNQlttSLGHLLPVGTPTPlIPILIMIETISLFIRPLALGVRLTANLTAGHL 170
Cdd:PRK05815   95 LLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1593549712 171 LIQLtstAALTLTPMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYLQE 224
Cdd:PRK05815  171 ILAL---IALLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
90-222 2.89e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 55.90  E-value: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQ-LTTSLGHLlPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:PRK13419  191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHgIKGYLAHL-TGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAG 269
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1593549712 169 HLLIQLTSTAALTLTPMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYL 222
Cdd:PRK13419  270 HIVILSLIFISFILKSYIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
90-224 3.65e-09

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 54.60  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSlgHLLPVGTPTPLIP-ILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:MTH00087   72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSKSEKFS--VYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1593549712 169 HLLIQLTSTAALtltpmttlfiLTTIILLLLTILELAVAMIQAYVFVLLLSLYLQE 224
Cdd:MTH00087  150 HLISSLLNFLGE----------KYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
94-222 1.13e-07

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 51.43  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593549712  94 TPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETI-SLFIRPLALGVRLTANLTAGHLLI 172
Cdd:PRK13417  217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEFIvSPMAKTFALTVRLLANMTAGHVII 296
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1593549712 173 qLTSTAALTLTPMTTLFILTTIILLLLTILELAVAMIQAYVFVLLLSLYL 222
Cdd:PRK13417  297 -LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
90-168 1.25e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 41.02  E-value: 1.25e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1593549712  90 PYTFTPTTQLSMNMGLAIPMWMATVLTGLRNQLTTSLGHLLPVGTPTPLIPILIMIETISLFIRPLALGVRLTANLTAG 168
Cdd:MTH00050   43 PYIYSPFLFVVFLFVVVFPLFISLFLSRVFDSLNEFFSSFVPVGTPLYICPFVCIAETISYIIRPVVLILRPFINISLG 121
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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