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Conserved domains on  [gi|619727289|gb|AHY03860|]
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ATPase subunit 6, partial (mitochondrion) [Cinnyris chloropygius]

Protein Classification

FoF1 ATP synthase subunit a( domain architecture ID 116)

FoF1 ATP synthase subunit a is part of the membrane proton channel (Fo complex) of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane; it plays a direct role in the translocation of protons across the membrane

Gene Ontology:  GO:0045263|GO:0015078|GO:0015986
PubMed:  11533110|12370007|30901262

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_a_6 super family cl00413
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-120 2.08e-55

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.


The actual alignment was detected with superfamily member MTH00132:

Pssm-ID: 469762  Cd Length: 227  Bit Score: 171.98  E-value: 2.08e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00132  90 PYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGH 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:MTH00132 170 LLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAM 209
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-120 2.08e-55

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 171.98  E-value: 2.08e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00132  90 PYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGH 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:MTH00132 170 LLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAM 209
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 1-120 2.81e-30

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: 107.68  E-value: 2.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289    1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:TIGR01131  91 PYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGH 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 619727289   81 LLIQLISTATMALFStmPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:TIGR01131 171 LLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAF 208
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-101 1.31e-26

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: 96.31  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:cd00310   25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104

                         90       100
                 ....*....|....*....|.
gi 619727289  81 LLIQLISTATMALFSTMPVVS 101
Cdd:cd00310  105 LLLALLSGLVPSLLSSVGLLP 125
ATP-synt_A pfam00119
ATP synthase A chain;
1-120 3.73e-21

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 84.08  E-value: 3.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289    1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVS-LGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAG 79
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 619727289   80 HLLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAF 201
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 1-100 1.78e-11

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: 58.16  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVS-LGHLLPEGTPtPLIPALIMIETTSLLIRPLALGVRLTANLTAG 79
Cdd:COG0356   78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156

                         90       100
                 ....*....|....*....|.
gi 619727289  80 HLLIQLISTATMALFSTMPVV 100
Cdd:COG0356  157 HIILLLLAGLAPFLLLGVLSL 177
 
Name Accession Description Interval E-value
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-120 2.08e-55

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 171.98  E-value: 2.08e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00132  90 PYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVRLTANLTAGH 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:MTH00132 170 LLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAM 209
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-120 3.40e-55

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 171.55  E-value: 3.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00120  90 PYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVRLTANLTAGH 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:MTH00120 170 LLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAM 209
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-120 2.84e-53

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 166.68  E-value: 2.84e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00073  90 PYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVRLTANLTAGH 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:MTH00073 170 LLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAM 209
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-120 2.56e-43

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 141.24  E-value: 2.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00179  90 PYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVRLTANITAGH 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:MTH00179 170 LLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAM 209
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-120 4.22e-42

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 138.16  E-value: 4.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00101  89 PHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGH 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:MTH00101 169 LLIHLIGGATLALMSISTTTALITFIILILLTILEFAVAL 208
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-97 1.88e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 107.95  E-value: 1.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00157  89 PYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAVRLAANMIAGH 168

                         90
                 ....*....|....*..
gi 619727289  81 LLIQLISTATMALFSTM 97
Cdd:MTH00157 169 LLLTLLGNTGPSLSSMI 185
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 1-120 2.81e-30

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: 107.68  E-value: 2.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289    1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:TIGR01131  91 PYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGH 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 619727289   81 LLIQLISTATMALFStmPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:TIGR01131 171 LLLTLLSGLLFSLMS--SAIFALLLLILVALIILEIFVAF 208
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-119 2.92e-29

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 105.06  E-value: 2.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00035  93 PYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIALGLRLAANLTAGH 172

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 619727289  81 LLIQLISTATMALFSTmPVVSLLTLLVLFLLTILEVAVA 119
Cdd:MTH00035 173 LLIFLLSTAIWELSNS-PLISIITLIIFFLLFILEIGVA 210
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 1-101 1.31e-26

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: 96.31  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:cd00310   25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104

                         90       100
                 ....*....|....*....|.
gi 619727289  81 LLIQLISTATMALFSTMPVVS 101
Cdd:cd00310  105 LLLALLSGLVPSLLSSVGLLP 125
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-101 1.02e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 96.09  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00173  92 PFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLANISAGH 171

                         90       100
                 ....*....|....*....|.
gi 619727289  81 LLIQLISTATMALFSTMPVVS 101
Cdd:MTH00173 172 IVLTLIGNYLSSSLFSSSVVS 192
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-120 2.39e-25

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 95.10  E-value: 2.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00176  92 PYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLAVRLAANLSAGH 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:MTH00176 172 LLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCM 211
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-96 2.14e-21

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 84.78  E-value: 2.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00005  94 PYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLAANMSAGH 173

                         90
                 ....*....|....*..
gi 619727289  81 LLIQLISTATM-ALFST 96
Cdd:MTH00005 174 IVLSLIGIYAAsALFSS 190
ATP-synt_A pfam00119
ATP synthase A chain;
1-120 3.73e-21

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 84.08  E-value: 3.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289    1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVS-LGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAG 79
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 619727289   80 HLLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAF 201
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-120 1.35e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 77.39  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00172  92 PYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISLGVRLAANLSAGH 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFSTMPVVSLLTLLVLFLLTILEVAVAM 120
Cdd:MTH00172 172 LLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAV 211
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 1-119 3.38e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 71.58  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00175 103 PYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVLIETLSYLIRAISLGVRLAANISAGH 182

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 619727289  81 LLIQLISTATMALFST-MPVVSLLTLLVLFLLTILEVAVA 119
Cdd:MTH00175 183 LLFAILSGFAFNMLSNgLIILSLFPMLIMIFITLLEMAVA 222
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 1-96 9.24e-13

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 62.26  E-value: 9.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:MTH00174 111 PYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGH 190

                         90
                 ....*....|....*.
gi 619727289  81 LLIQLISTATMALFST 96
Cdd:MTH00174 191 LLFSIIASFAWKMINT 206
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 1-100 1.78e-11

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: 58.16  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVS-LGHLLPEGTPtPLIPALIMIETTSLLIRPLALGVRLTANLTAG 79
Cdd:COG0356   78 PGLFPPTADINVTLALALIVFVLVHYYGIKKKGLGGyLKHLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAG 156

                         90       100
                 ....*....|....*....|.
gi 619727289  80 HLLIQLISTATMALFSTMPVV 100
Cdd:COG0356  157 HIILLLLAGLAPFLLLGVLSL 177
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 2-99 7.70e-11

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 56.73  E-value: 7.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   2 YTFTPTTQLSMNLALAFPLWLATLLTGLRNQpsvSLGHLLPEGTPTPlIPALIMIETTSLLIRPLALGVRLTANLTAGHL 81
Cdd:PRK05815  95 LLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170

                         90
                 ....*....|....*...
gi 619727289  82 LIQLISTATMALFSTMPV 99
Cdd:PRK05815 171 ILALIALLGGAGLLLALA 188
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 1-88 2.81e-10

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 54.98  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNqpSVSLGHLLPEGTPTPLIP-ALIMIETTSLLIRPLALGVRLTANLTAG 79
Cdd:MTH00087  72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149


                 ....*....
gi 619727289  80 HLLIQLIST 88
Cdd:MTH00087 150 HLISSLLNF 158
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 5-83 6.71e-06

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 43.34  E-value: 6.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   5 TPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIE-TTSLLIRPLALGVRLTANLTAGHLLI 83
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVII 296
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 1-83 1.24e-05

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 42.81  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAGH 80
Cdd:PRK13419 191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHGIKGYLAHLTGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAGH 270


                 ...
gi 619727289  81 LLI 83
Cdd:PRK13419 271 IVI 273
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 1-79 4.79e-04

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 37.56  E-value: 4.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 619727289   1 PYTFTPTTQLSMNLALAFPLWLATLLTGLRNQPSVSLGHLLPEGTPTPLIPALIMIETTSLLIRPLALGVRLTANLTAG 79
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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