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Conserved domains on  [gi|431811322|gb|AGA83729|]
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ATP synthase subunit 6 (mitochondrion) [Elminia albiventris]

Protein Classification

ATP synthase F0 subunit 6( domain architecture ID 10009573)

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 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 4.82e-106

ATP synthase F0 subunit 6; Provisional


:

Pssm-ID: 177181  Cd Length: 227  Bit Score: 304.83  E-value: 4.82e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIPLVLIALTFPALLFPTLGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  81 LLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431811322 161 LTANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 4.82e-106

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 304.83  E-value: 4.82e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIPLVLIALTFPALLFPTLGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  81 LLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431811322 161 LTANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 19-227 1.53e-45

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: 151.20  E-value: 1.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   19 LVLIALTFPALLFPTLGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFLLLINLLGLLPYTFTPTTQ 98
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   99 LSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLTANLTAGHLLIQLISTA 178
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 431811322  179 TVALSStmPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 180 LFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 90-224 1.20e-32

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


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 115.57  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  90 PYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLTANLTAGH 169
Cdd:cd00310   25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 431811322 170 LLIQLISTATVALSStmpAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310  105 LLLALLSGLVPSLLS---SVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP-synt_A pfam00119
ATP synthase A chain;
90-224 2.32e-27

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 103.72  E-value: 2.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   90 PYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSAS-LGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 431811322  169 HLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 49-225 5.71e-16

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: 73.57  E-value: 5.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  49 WLINLITKQLMTPLNKKGHKWALILTSLMIFLLLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQ-PSASLG 127
Cdd:COG0356   37 MLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLK 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322 128 HLLPEGTPtPLIPALIMIETTSLLIRPIALGVRLTANLTAGHLLIQLISTATVALSSTMPAIslltlLILFLLTILEVAV 207
Cdd:COG0356  117 HLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSL-----LLPVAWTAFELLV 190

                        170
                 ....*....|....*...
gi 431811322 208 AMIQAYVFVLLLSLYLQE 225
Cdd:COG0356  191 GFLQAYIFTMLTAVYISL 208
 
Name Accession Description Interval E-value
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 1-227 4.82e-106

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 304.83  E-value: 4.82e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIPLVLIALTFPALLFPTLGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFL 80
Cdd:MTH00120   1 MNLNFFDQFSSPELLGIPLILLAMLIPALLIPSPKNRLLTNRLTTLQLWLIKLITKQLMLPLNKKGHKWALILTSLMLLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  81 LLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVR 160
Cdd:MTH00120  81 LLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431811322 161 LTANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00120 161 LTANLTAGHLLIQLISTATLNLLPTMPTLSLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQENT 227
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 1-227 1.71e-105

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 303.72  E-value: 1.71e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIPLVLIALTFPALLFPTLGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFL 80
Cdd:MTH00132   1 MTLSFFDQFMSPTYLGIPLIALALTLPWILFPTPTSRWLNNRLLTLQGWFINRFTQQLLLPLNVGGHKWALLLTSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  81 LLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVR 160
Cdd:MTH00132  81 ITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIGMRNQPTHALGHLLPEGTPTPLIPVLIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431811322 161 LTANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00132 161 LTANLTAGHLLIQLIATAAFVLLPLMPTVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 1-227 4.88e-101

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 292.26  E-value: 4.88e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIPLVLIALTFPALLFPTLGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFL 80
Cdd:MTH00073   1 MNLSFFDQFLSPTLLGIPLIMLAMLLPWLLFPTPTNKWLNNRLSTLQIWFLQNFTKQLMLPLNTPGHKWALILTSLMVFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  81 LLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVR 160
Cdd:MTH00073  81 ITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIGLRNQPTASLGHLLPEGTPTLLIPILIIIETISLFIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431811322 161 LTANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00073 161 LTANLTAGHLLIQLISTATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQENV 227
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-226 2.85e-82

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 244.86  E-value: 2.85e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIPLVLIALTFPALLFPTLGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFL 80
Cdd:MTH00179   1 MMLSMFDQFESPSLLGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKKGHKWAVLFLSLMLFL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  81 LLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVR 160
Cdd:MTH00179  81 LTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRPLALGVR 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431811322 161 LTANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00179 161 LTANITAGHLLMHLISSAVFVLMNFMGMVALLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQEN 226
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 1-226 2.48e-78

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 234.85  E-value: 2.48e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIPLVLIALTFPALLFPTlGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFL 80
Cdd:MTH00101   1 MNENLFASFITPTILGLPIVTLIIMFPSLLFPT-PNRLINNRLISIQQWLIQLTSKQMMTIHNTKGQTWSLMLMSLILFI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  81 LLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVR 160
Cdd:MTH00101  80 GSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVR 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 431811322 161 LTANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00101 160 LTANITAGHLLIHLIGGATLALMSISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYLHDN 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 1-227 9.12e-46

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 151.66  E-value: 9.12e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIPL----VLIALTFPALLFPTlgnRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSL 76
Cdd:MTH00035   3 INNSIFGQFSPDTILFIPLtllsSVIALSWLFFINPT---NWLPSRSQSIWLTFRQEILKLIFQNTNPNTAPWAGLLTTV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  77 MIFLLLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIA 156
Cdd:MTH00035  80 FILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPIA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 431811322 157 LGVRLTANLTAGHLLIQLISTATVALSSTmPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00035 160 LGLRLAANLTAGHLLIFLLSTAIWELSNS-PLISIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQNI 229
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 19-227 1.53e-45

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: 151.20  E-value: 1.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   19 LVLIALTFPALLFPTLGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFLLLINLLGLLPYTFTPTTQ 98
Cdd:TIGR01131  20 LILLLSLLIFLISSSLSRWLIPSRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIFTLFLFILISNLLGLIPYSFTPTSH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   99 LSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLTANLTAGHLLIQLISTA 178
Cdd:TIGR01131 100 LSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLSVRLFANISAGHLLLTLLSGL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 431811322  179 TVALSStmPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:TIGR01131 180 LFSLMS--SAIFALLLLILVALIILEIFVAFIQAYVFTLLTCLYLNDAL 226
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-225 1.01e-39

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 136.07  E-value: 1.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNL-SFFDQFSSPSLlgiPLVLIALTFPALLFPTLgnRW-ITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMI 78
Cdd:MTH00157   3 TNLfSIFDPSTSFNL---SLNWLSTFLGLLFIPSS--FWlIPSRYNILWNKILKTLHKEFKTLLGPKNKGSTLIFISLFS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  79 FLLLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALG 158
Cdd:MTH00157  78 FILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 431811322 159 VRLTANLTAGHLLIQLISTATVALSSTMPAISlltLLILFLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00157 158 VRLAANMIAGHLLLTLLGNTGPSLSSMILSIL---ILIQILLLILESAVAIIQSYVFSVLSTLYSSE 221
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-226 1.81e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 125.15  E-value: 1.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIPLVL---IALTFPALLFPTlGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLM 77
Cdd:MTH00176   1 MLVDLFSSFDPPNKNIFSMISlswITLLLFLLLMPS-SVWFCPSKLQVFMLMFSTFLPEMILRSNGSYILGSASIIISLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  78 IFLLLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIAL 157
Cdd:MTH00176  80 ILVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431811322 158 GVRLTANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQEN 226
Cdd:MTH00176 160 AVRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFLLLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEH 228
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 4-225 4.92e-34

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 121.51  E-value: 4.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   4 SFFDQFSSPSLLGIPLVLIaLTFPALLFPTLGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFLLLI 83
Cdd:MTH00173   7 SSFDDHNSSFSSLSFLMWL-LSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTRSSGLNLGGFSLLLSSLFLFLISL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  84 NLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLTA 163
Cdd:MTH00173  86 NLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLTVRLLA 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 431811322 164 NLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLL-TILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00173 166 NISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGyFIFEVAVMLIQAYIFTLLIKLYSDE 228
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 90-224 1.20e-32

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


Pssm-ID: 349411 [Multi-domain]  Cd Length: 156  Bit Score: 115.57  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  90 PYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLTANLTAGH 169
Cdd:cd00310   25 PYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISELIRPLSLSVRLFANMFAGH 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 431811322 170 LLIQLISTATVALSStmpAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:cd00310  105 LLLALLSGLVPSLLS---SVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYIS 156
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 4-222 1.33e-29

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 110.21  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   4 SFFDQFSSPSLLGIPLVLIALTFPALlfptlgnrWIT-NRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFLLL 82
Cdd:MTH00005  15 SLFNNLSSTAFWAFNFSIILLLSSSF--------WITpNRLSSIMSPPKSTMHTQLSRTFGKHLKGFSSLISALFTMIIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  83 INLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLT 162
Cdd:MTH00005  87 MNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPITLSFRLA 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322 163 ANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLY 222
Cdd:MTH00005 167 ANMSAGHIVLSLIGIYAASALFSSISSTILLILTQMGYILFEVGICLIQAYIFCLLLSLY 226
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 1-227 1.26e-28

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 107.43  E-value: 1.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGI---PLVLIALTFPALLFPTlGNRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLM 77
Cdd:MTH00172   1 MSSSYFDQFNIVWLIGLtnsSIMMILVIIVVLLLFK-GIKLIPKRWQSIIEIIYNHFHGVVKDNLGNEGLKYFPFIISLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  78 IFLLLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIAL 157
Cdd:MTH00172  80 FFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAISL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322 158 GVRLTANLTAGHLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00172 160 GVRLAANLSAGHLLFAILAGFGFNMLCASGFLSLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYLADTI 229
ATP-synt_A pfam00119
ATP synthase A chain;
90-224 2.32e-27

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 103.72  E-value: 2.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   90 PYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSAS-LGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLTANLTAG 168
Cdd:pfam00119  81 PGGFTVTADINVTLALALIVFLLVHYYGIKKHGLGGyFKKLFVPPVPLPLVPLLLPIEIISEFARPVSLSLRLFGNMLAG 160

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 431811322  169 HLLIQLISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQ 224
Cdd:pfam00119 161 HLLLLLLAGLIFALLSAGFLLGVIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYIS 216
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 1-227 1.70e-26

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 102.39  E-value: 1.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322   1 MNLSFFDQFSSPSLLGIP----------------LVLIALTFPALLFptlGNRWITNRLSTLQLWLINLITKQLMTPLNK 64
Cdd:MTH00175   1 MLAAYFDQFNIIRLITIQaflgdwlvtftnssmmMVLAVIIFWLLLK---GDKLIPNRWQSIMELIYLNIRSVVHDNLGK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  65 KGHKWALILTSLMIFLLLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIM 144
Cdd:MTH00175  78 SGQKYFPFILSLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLTFKWNFLSILMPGGAPLVLAPFLVL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322 145 IETTSLLIRPIALGVRLTANLTAGHLLIQLISTATV-ALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYL 223
Cdd:MTH00175 158 IETLSYLIRAISLGVRLAANISAGHLLFAILSGFAFnMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYL 237


                 ....
gi 431811322 224 QENI 227
Cdd:MTH00175 238 GDTI 241
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 21-227 3.28e-17

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 77.67  E-value: 3.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  21 LIALTFPALLFPTLG-----NRWITNRLSTLQLWLINLITKQLMTPLNKKGHKWALILTSLMIFLLLINLLGLLPYTFTP 95
Cdd:MTH00174  37 FFMMSFAVFLFYTIGakgnnNTLVPNRILVGLELIYSHFYTVLKDNLGNKGGNYLAFVLSLFILILFGNGLGLFPYVFTP 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  96 TTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLTANLTAGHLLIQLI 175
Cdd:MTH00174 117 TVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAISLGVRLAANISSGHLLFSII 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 431811322 176 ST-ATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQENI 227
Cdd:MTH00174 197 ASfAWKMINTGILIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYLRDTV 249
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 49-225 5.71e-16

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: 73.57  E-value: 5.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  49 WLINLITKQLMTPLNKKGHKWALILTSLMIFLLLINLLGLLPYTFTPTTQLSMSLALAFPLWLATLLTGLRNQ-PSASLG 127
Cdd:COG0356   37 MLVEFVRNQVKDTIGKKGRKFAPLLLTLFLFILVSNLLGLIPGLFPPTADINVTLALALIVFVLVHYYGIKKKgLGGYLK 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322 128 HLLPEGTPtPLIPALIMIETTSLLIRPIALGVRLTANLTAGHLLIQLISTATVALSSTMPAIslltlLILFLLTILEVAV 207
Cdd:COG0356  117 HLFFPPFP-WLAPLMLPIEIISELARPLSLSLRLFGNMFAGHIILLLLAGLAPFLLLGVLSL-----LLPVAWTAFELLV 190

                        170
                 ....*....|....*...
gi 431811322 208 AMIQAYVFVLLLSLYLQE 225
Cdd:COG0356  191 GFLQAYIFTMLTAVYISL 208
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 91-225 6.66e-15

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 70.98  E-value: 6.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  91 YTFTPTTQLSMSLALAFPLWLATLLTGLRNQpsaSLGHLLPEGTPTPlIPALIMIETTSLLIRPIALGVRLTANLTAGHL 170
Cdd:PRK05815  95 LLFPPTADINVTLALALIVFVLVIYYGIKKK---GLGGYLKEFYLQP-HPLLLPIEIISEFSRPISLSLRLFGNMLAGEL 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 431811322 171 LIQLIstatVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:PRK05815 171 ILALI----ALLGGAGLLLALAPLILPVAWTIFEIFVGTLQAYIFMMLTIVYISM 221
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 90-225 8.50e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 59.22  E-value: 8.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  90 PYTFTPTTQLSMSLALAFPLWLATLLTGLRNqpSASLGHLLPEGTPTPLIP-ALIMIETTSLLIRPIALGVRLTANLTAG 168
Cdd:MTH00087  72 PYSFSPCGMVEFTFLYALVAWLSTFLSFLSK--SEKFSVYLSKGSDSFLKTfSMLFVEIVSELSRPLALTLRLTVNLMVG 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 431811322 169 HLLIQLISTatvalsstmpaISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYLQE 225
Cdd:MTH00087 150 HLISSLLNF-----------LGEKYVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 90-223 2.05e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 56.67  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  90 PYTFTPTTQLSMSLALAFPLWLATLLTGLRNQP-SASLGHLlPEGTPTPLIPALIMIETTSLLIRPIALGVRLTANLTAG 168
Cdd:PRK13419 191 PYGATATGNINVTLTLAVFTFFITQYAAIKAHGiKGYLAHL-TGGTHWSLWIIMIPIEFIGLFTKPFALTVRLFANMTAG 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 431811322 169 HLLIQLISTATVALSSTMPAISlLTLLILFLLTILEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13419 270 HIVILSLIFISFILKSYIVAVA-VSVPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 94-223 6.07e-09

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 55.28  E-value: 6.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 431811322  94 TPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIE-TTSLLIRPIALGVRLTANLTAGHLLI 172
Cdd:PRK13417 217 TVTGDISVTMTLALLTMFLIYGAGFSYQGPKFIWHSVPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHVII 296

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 431811322 173 qlISTATVALSSTMPAISLLTLLILFLLTILEVAVAMIQAYVFVLLLSLYL 223
Cdd:PRK13417 297 --LALMGFIFQFQSWGIVPVSVIGSGLIYVLEIFVAFLQAYIFVLLTSLFV 345
ATP6 MTH00050
ATP synthase F0 subunit 6; Validated
 90-168 1.90e-03

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177125  Cd Length: 170  Bit Score: 37.94  E-value: 1.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 431811322  90 PYTFTPTTQLSMSLALAFPLWLATLLTGLRNQPSASLGHLLPEGTPTPLIPALIMIETTSLLIRPIALGVRLTANLTAG 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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