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Conserved domains on  [gi|1181491985|ref|YP_009353878|]
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ATP synthase F0 subunit 6 (mitochondrion) [Tropidomya abbreviata]

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 ...
 1-224 7.14e-35

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 MTH00173:

Pssm-ID: 469762  Cd Length: 231  Bit Score: 123.82  E-value: 7.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985   1 MSTDLFSSFDDINFCL-WGSHMNYFISAVPMFIFVFGVGYFSGGVYRFMFSLLDSLTKKSF------LSGVELMMPCLFI 73
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFsSLSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTrssglnLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  74 FMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPLFLG 153
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1181491985 154 MRLTVNMMVGQVILGLSGSILSSLIVSGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDEYSV 224
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEHPV 231
 
Name Accession Description Interval E-value
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-224 7.14e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 123.82  E-value: 7.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985   1 MSTDLFSSFDDINFCL-WGSHMNYFISAVPMFIFVFGVGYFSGGVYRFMFSLLDSLTKKSF------LSGVELMMPCLFI 73
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFsSLSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTrssglnLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  74 FMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPLFLG 153
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1181491985 154 MRLTVNMMVGQVILGLSGSILSSLIVSGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDEYSV 224
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEHPV 231
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-221 2.67e-29

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: 109.22  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985   5 LFSSFDDINFCLWGSHMNYFISAVPMFIFVF-----------GVGYFSGGVYRFMFSLLDSLTKKSFLSGVELMMpCLFI 73
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLIssslsrwlipsRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  74 FMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPLFLG 153
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1181491985 154 MRLTVNMMVGQVILGLSGSILSSLIVSGYFvgsGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDE 221
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSAIF---ALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-219 1.15e-27

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: 102.86  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  66 LMMPCLFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSN 145
Cdd:cd00310     6 PLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1181491985 146 LARPLFLGMRLTVNMMVGQVILGlsgsILSSLIVSGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:cd00310    86 LIRPLSLSVRLFANMFAGHLLLA----LLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP-synt_A pfam00119
ATP synthase A chain;
71-219 1.65e-18

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 80.23  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLI---PYGFSWTSHFAITYGLAIPFWLGLIMSSV-LWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNL 146
Cdd:pfam00119  64 LFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIkKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEF 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1181491985 147 ARPLFLGMRLTVNMMVGQVILGLSGSILSSLIVSGYFVGsGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:pfam00119 144 ARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG-VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYI 215
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 71-219 1.76e-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: 72.03  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLIPYGFSWTSHFAITYGLAipfwlglIMSSVLWNW-SLVSSGLLPY------GVKGLLAVMMVWVEIV 143
Cdd:COG0356    64 LFLFILVSNLLGLIPGLFPPTADINVTLALA-------LIVFVLVHYyGIKKKGLGGYlkhlffPPFPWLAPLMLPIEII 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1181491985 144 SNLARPLFLGMRLTVNMMVGQVILGLsgsiLSSLIvsGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:COG0356   137 SELARPLSLSLRLFGNMFAGHIILLL----LAGLA--PFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206
 
Name Accession Description Interval E-value
ATP6 MTH00173
ATP synthase F0 subunit 6; Provisional
 1-224 7.14e-35

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214448  Cd Length: 231  Bit Score: 123.82  E-value: 7.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985   1 MSTDLFSSFDDINFCL-WGSHMNYFISAVPMFIFVFGVGYFSGGVYRFMFSLLDSLTKKSF------LSGVELMMPCLFI 73
Cdd:MTH00173    1 MMVDLFSSFDDHNSSFsSLSFLMWLLSLMSLFFFSSSVWVSSSNLSSVFKLFVLTVSSQVTrssglnLGGFSLLLSSLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  74 FMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPLFLG 153
Cdd:MTH00173   81 FLISLNLSGLLPFVFSVTSHLAFTFSLALPLWLSLILSGLFYNPSKSLAGLVPAGAPAGLNPFLVLIETVSILIRPLTLT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1181491985 154 MRLTVNMMVGQVILGLSGSILSSLIVSGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDEYSV 224
Cdd:MTH00173  161 VRLLANISAGHIVLTLIGNYLSSSLFSSSVVSLLLVLLIQVGYFIFEVAVMLIQAYIFTLLIKLYSDEHPV 231
ATP6 MTH00176
ATP synthase F0 subunit 6; Provisional
 1-223 2.11e-33

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214449  Cd Length: 229  Bit Score: 119.75  E-value: 2.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985   1 MSTDLFSSFDDINFCLWGSHMNYFISA-VPMFIFVFGVGYFSGGVYRFMFSLLD------SLTKKSFLSGVELMMPCLFI 73
Cdd:MTH00176    1 MLVDLFSSFDPPNKNIFSMISLSWITLlLFLLLMPSSVWFCPSKLQVFMLMFSTflpemiLRSNGSYILGSASIIISLFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  74 FMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPLFLG 153
Cdd:MTH00176   81 LVMSLNLSGLIPYVFTSTSHLVITLSLALPLWLGVILSGFINNFYSRLSHLVPQGTPPLLNPFLVLIELVSLLIRPLTLA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985 154 MRLTVNMMVGQVILGLSGSILSSLIVSGYFVGSGiVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDEYS 223
Cdd:MTH00176  161 VRLAANLSAGHLLLGLLGAAMWGLLPVSPLIGFL-LLIVQILYFMFEIAVCMIQAYVFTLLLSLYLDEHP 229
ATP6 MTH00157
ATP synthase F0 subunit 6; Provisional
 1-222 8.90e-30

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214441  Cd Length: 223  Bit Score: 110.26  E-value: 8.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985   1 MSTDLFSSFDDINFCLWgsHMNYFISAVPMFIFVFGVGYFSGGVYRFMFSLLDSLTK------KSFLSGVELMMPCLFIF 74
Cdd:MTH00157    1 MMTNLFSIFDPSTSFNL--SLNWLSTFLGLLFIPSSFWLIPSRYNILWNKILKTLHKefktllGPKNKGSTLIFISLFSF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  75 MLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPLFLGM 154
Cdd:MTH00157   79 ILFNNFLGLFPYIFTSTSHLSLTLSLALPLWLSFMLFGWINNTNHMFAHLVPQGTPPILMPFMVLIETISNLIRPGTLAV 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1181491985 155 RLTVNMMVGQVILGLSGSILSSLIVSGYFvgsgIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDEY 222
Cdd:MTH00157  159 RLAANMIAGHLLLTLLGNTGPSLSSMILS----ILILIQILLLILESAVAIIQSYVFSVLSTLYSSEV 222
ATP_synt_6_or_A TIGR01131
ATP synthase subunit 6 (eukaryotes),also subunit A (prokaryotes); Bacterial forms should be ...
 5-221 2.67e-29

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: 109.22  E-value: 2.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985   5 LFSSFDDINFCLWGSHMNYFISAVPMFIFVF-----------GVGYFSGGVYRFMFSLLDSLTKKSFLSGVELMMpCLFI 73
Cdd:TIGR01131   1 LFSQFDISPITLFSLTLLSLILLLSLLIFLIssslsrwlipsRWQNLMESIYEFVLSIVKSQIGGKKGKFFPLIF-TLFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  74 FMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPLFLG 153
Cdd:TIGR01131  80 FILISNLLGLIPYSFTPTSHLSFTLGLALPLWLGLTISGFRKHPKGFLAHLVPSGTPLPLIPFLVIIETISYLARPISLS 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1181491985 154 MRLTVNMMVGQVILGLSGSILSSLIVSGYFvgsGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDE 221
Cdd:TIGR01131 160 VRLFANISAGHLLLTLLSGLLFSLMSSAIF---ALLLLILVALIILEIFVAFIQAYVFTLLTCLYLND 224
ATP-synt_Fo_a_6 cd00310
ATP synthase Fo complex, subunit 6 (eukaryotes) and subunit a (prokaryotes); Bacterial forms ...
 66-219 1.15e-27

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: 102.86  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  66 LMMPCLFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSN 145
Cdd:cd00310     6 PLLGTLFLFILFSNLLGLIPYSFTPTSHLNVTLALALIVFLGVHILGIKKHGLGFFLHFLPPGTPLPLAPLMVPIELISE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1181491985 146 LARPLFLGMRLTVNMMVGQVILGlsgsILSSLIVSGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:cd00310    86 LIRPLSLSVRLFANMFAGHLLLA----LLSGLVPSLLSSVGLLPLLLPVALTLLELFVAFIQAYVFTLLTAVYI 155
ATP6 MTH00005
ATP synthase F0 subunit 6; Provisional
 1-223 4.10e-27

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 164583  Cd Length: 231  Bit Score: 103.66  E-value: 4.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985   1 MSTDLFSSFDDINFCLWGSHMN-YFISAVPMFIFVFGVGY---------FSGGVYRFMFSLLdSLTKKSFLSGVELMMPC 70
Cdd:MTH00005    1 MLTDIFSSFDPATNSLFNNLSStAFWAFNFSIILLLSSSFwitpnrlssIMSPPKSTMHTQL-SRTFGKHLKGFSSLISA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPL 150
Cdd:MTH00005   80 LFTMIILMNLSGLLPYVFSTSSHLIFTLTLGLPLWLSLIMSSVTFSPKKFAAHLLPGGAPDWLNPFLVLIETISILVRPI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1181491985 151 FLGMRLTVNMMVGQVILGLSGSILSSLIVSGYFvGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDEYS 223
Cdd:MTH00005  160 TLSFRLAANMSAGHIVLSLIGIYAASALFSSIS-STILLILTQMGYILFEVGICLIQAYIFCLLLSLYSDDHP 231
ATP6 MTH00179
ATP synthase F0 subunit 6; Provisional
 1-221 4.11e-24

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177230  Cd Length: 227  Bit Score: 95.40  E-value: 4.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985   1 MSTDLFSSFDDINFclwgshMNYFISAVPMFIFVFGVGYFSGGVYRFMFSLLDSLTKKSFLSGVELMMPC---------- 70
Cdd:MTH00179    1 MMLSMFDQFESPSL------LGIPLLALALLLPWLLFPSLTNRWLNNRLSTLQSWFFGSFTFQLMQPINKkghkwavlfl 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 -LFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARP 149
Cdd:MTH00179   75 sLMLFLLTLNLLGLLPYTFTPTTQLSLNLGLALPLWLGTVLYGLFNQPTIALAHLLPEGTPTPLIPMLVWIETISLLIRP 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1181491985 150 LFLGMRLTVNMMVGQVILGLSGSILSSLIVSGYFVGsGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDE 221
Cdd:MTH00179  155 LALGVRLTANITAGHLLMHLISSAVFVLMNFMGMVA-LLTLLVLFLLTLLEVAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00035
ATP synthase F0 subunit 6; Validated
 71-221 6.56e-21

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177110  Cd Length: 229  Bit Score: 86.95  E-value: 6.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPL 150
Cdd:MTH00035   79 VFILILSINVLGLFPYAFTSTSHISLTYSLGIPLWMSVNILGFYLAFNSRLSHLVPQGTPSFLIPLMVWIETLSLFAQPI 158

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1181491985 151 FLGMRLTVNMMVGQVILGLSGSILSSLIVSGYFvgSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDE 221
Cdd:MTH00035  159 ALGLRLAANLTAGHLLIFLLSTAIWELSNSPLI--SIITLIIFFLLFILEIGVACIQAYVFTALVHFYLEQ 227
ATP-synt_A pfam00119
ATP synthase A chain;
71-219 1.65e-18

ATP synthase A chain;


Pssm-ID: 459679 [Multi-domain]  Cd Length: 216  Bit Score: 80.23  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLI---PYGFSWTSHFAITYGLAIPFWLGLIMSSV-LWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNL 146
Cdd:pfam00119  64 LFFFILVSNLLGLIpksPGGFTVTADINVTLALALIVFLLVHYYGIkKHGLGGYFKKLFVPPVPLPLVPLLLPIEIISEF 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1181491985 147 ARPLFLGMRLTVNMMVGQVILGLSGSILSSLIVSGYFVGsGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:pfam00119 144 ARPVSLSLRLFGNMLAGHLLLLLLAGLIFALLSAGFLLG-VIPPLLGVAWTLFELLVAFIQAYVFTMLTAVYI 215
ATP6 MTH00120
ATP synthase F0 subunit 6; Provisional
 71-221 5.63e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177181  Cd Length: 227  Bit Score: 79.10  E-value: 5.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPL 150
Cdd:MTH00120   76 LMLLLLLINLLGLLPYTFTPTTQLSMNMALAIPLWLATVLTGLRNQPTTSLAHLLPEGTPTPLIPALILIETISLLIRPL 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1181491985 151 FLGMRLTVNMMVGQVILGLSGSILSSLIVSGYFVgSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDE 221
Cdd:MTH00120  156 ALGVRLTANLTAGHLLIQLISTATLNLLPTMPTL-SLLTLIILLLLTILELAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00073
ATP synthase F0 subunit 6; Provisional
 66-221 7.02e-18

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177144  Cd Length: 227  Bit Score: 78.86  E-value: 7.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  66 LMMPCLFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSvLWNWSLVSSG-LLPYGVKGLLAVMMVWVEIVS 144
Cdd:MTH00073   71 LILTSLMVFLITMNLLGLLPYTFTPTTQLSLNLGLAVPLWLATVLIG-LRNQPTASLGhLLPEGTPTLLIPILIIIETIS 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1181491985 145 NLARPLFLGMRLTVNMMVGQVILGLSgSILSSLIVSGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDE 221
Cdd:MTH00073  150 LFIRPLALGVRLTANLTAGHLLIQLI-STATLVLLPLMPTVSILTMIVLFLLTLLEIAVAMIQAYVFVLLLSLYLQE 225
ATP6 MTH00132
ATP synthase F0 subunit 6; Provisional
 66-221 1.91e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177190  Cd Length: 227  Bit Score: 74.91  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  66 LMMPCLFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSvLWNWSLVSSG-LLPYGVKGLLAVMMVWVEIVS 144
Cdd:MTH00132   71 LLLTSLMLFLITLNMLGLLPYTFTPTTQLSLNMGLAVPLWLATVIIG-MRNQPTHALGhLLPEGTPTPLIPVLIIIETIS 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985 145 NLARPLFLGMRLTVNMMVGQVILglsgsilsSLIVSGYFV-------GSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTV 217
Cdd:MTH00132  150 LFIRPLALGVRLTANLTAGHLLI--------QLIATAAFVllplmptVAILTATLLFLLTLLEVAVAMIQAYVFVLLLSL 221


                  ....
gi 1181491985 218 YIDE 221
Cdd:MTH00132  222 YLQE 225
ATP6 MTH00172
ATP synthase F0 subunit 6; Provisional
 71-219 2.66e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 214447  Cd Length: 232  Bit Score: 74.69  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPL 150
Cdd:MTH00172   78 LFFFIVFLNLLGLFPYVFTPTTHIVVTLGLSFSIIIGVTLAGFWRFKWDFFSILMPSGAPLGLAPLLVLIETVSYISRAI 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985 151 FLGMRLTVNMMVGQVILG-LSGSILSSLIVSGYFvgSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:MTH00172  158 SLGVRLAANLSAGHLLFAiLAGFGFNMLCASGFL--SLFPLLIMVFITLLEIAVAVIQAYVFCLLTTIYL 225
ATP6 MTH00175
ATP synthase F0 subunit 6; Provisional
 70-219 3.27e-16

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177228  Cd Length: 244  Bit Score: 74.66  E-value: 3.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  70 CLFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVL-WNWSLVSSgLLPYGVKGLLAVMMVWVEIVSNLAR 148
Cdd:MTH00175   88 SLFLFIAILNILGLFPYVFTPTAHIIITFGLSLSIIIAVTLLGFLtFKWNFLSI-LMPGGAPLVLAPFLVLIETLSYLIR 166

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1181491985 149 PLFLGMRLTVNMMVGQVILGLSGSILSSLIVSGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:MTH00175  167 AISLGVRLAANISAGHLLFAILSGFAFNMLSNGLIILSLFPMLIMIFITLLEMAVAVIQAYVFCLLTTIYL 237
AtpB COG0356
FoF1-type ATP synthase, membrane subunit a [Energy production and conversion]; FoF1-type ATP ...
 71-219 1.76e-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: 72.03  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLIPYGFSWTSHFAITYGLAipfwlglIMSSVLWNW-SLVSSGLLPY------GVKGLLAVMMVWVEIV 143
Cdd:COG0356    64 LFLFILVSNLLGLIPGLFPPTADINVTLALA-------LIVFVLVHYyGIKKKGLGGYlkhlffPPFPWLAPLMLPIEII 136

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1181491985 144 SNLARPLFLGMRLTVNMMVGQVILGLsgsiLSSLIvsGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:COG0356   137 SELARPLSLSLRLFGNMFAGHIILLL----LAGLA--PFLLLGVLSLLLPVAWTAFELLVGFLQAYIFTMLTAVYI 206
ATP6 MTH00101
ATP synthase F0 subunit 6; Validated
 66-219 6.19e-14

ATP synthase F0 subunit 6; Validated


Pssm-ID: 177163  Cd Length: 226  Bit Score: 68.06  E-value: 6.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  66 LMMPCLFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSN 145
Cdd:MTH00101   70 LMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGTVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISL 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1181491985 146 LARPLFLGMRLTVNMMVGQVILGLSGSILSSLIvSGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:MTH00101  150 FIQPMALAVRLTANITAGHLLIHLIGGATLALM-SISTTTALITFIILILLTILEFAVALIQAYVFTLLVSLYL 222
PRK13419 PRK13419
F0F1 ATP synthase subunit A; Provisional
 42-219 3.86e-12

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237381  Cd Length: 342  Bit Score: 64.38  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  42 GGVYRFMFSLLD----SLTKKSFLSGVELMMPCL---FIFMLFMNLSGLIPYGFSWTSHFAITYGLAI-PFWLGLImssv 113
Cdd:PRK13419  141 KGLANAMEALVEfirlDVAKSNIGHGYEKFLPYLltvFFFILVCNLLGLVPYGATATGNINVTLTLAVfTFFITQY---- 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985 114 lwnwslvsSGLLPYGVKGLLA-----------VMMVWVEIVSNLARPLFLGMRLTVNMMVGQ-VILGLsgsILSSLIVSG 181
Cdd:PRK13419  217 --------AAIKAHGIKGYLAhltggthwslwIIMIPIEFIGLFTKPFALTVRLFANMTAGHiVILSL---IFISFILKS 285

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1181491985 182 YFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:PRK13419  286 YIVAVAVSVPFAIFIYLLELFVAFLQAYIFTMLSALFI 323
ATP6 MTH00174
ATP synthase F0 subunit 6; Provisional
 71-219 1.63e-11

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 133799  Cd Length: 252  Bit Score: 61.88  E-value: 1.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLIMSSVLWNWSLVSSGLLPYGVKGLLAVMMVWVEIVSNLARPL 150
Cdd:MTH00174   97 LFILILFGNGLGLFPYVFTPTVHMVITLGLSFAIIVGTTLAGLITFRFNFFSILMPQGAPLALAPLLTIIETLSYISRAI 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1181491985 151 FLGMRLTVNMMVGQVILGLSGSILSSLIVSGYFVGSGIVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:MTH00174  177 SLGVRLAANISSGHLLFSIIASFAWKMINTGILIGSFVPFAILIFVTILEMAVAIIQAYVFTLLTIVYL 245
PRK05815 PRK05815
F0F1 ATP synthase subunit A; Validated
 71-219 6.41e-11

F0F1 ATP synthase subunit A; Validated


Pssm-ID: 235617  Cd Length: 227  Bit Score: 59.81  E-value: 6.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLIPYG-FSWTSHFAITYGLAIpfwlgliMSSVLWN-WSLVSSGLLPYGVKGLLA--VMMVWVEIVSNL 146
Cdd:PRK05815   79 LFLFILLMNLLGLIPYLlFPPTADINVTLALAL-------IVFVLVIyYGIKKKGLGGYLKEFYLQphPLLLPIEIISEF 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1181491985 147 ARPLFLGMRLTVNMMVGQVILGLSGSILSSLIVSGYFvgsgiVLVVMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:PRK05815  152 SRPISLSLRLFGNMLAGELILALIALLGGAGLLLALA-----PLILPVAWTIFEIFVGTLQAYIFMMLTIVYI 219
ATP6 MTH00087
ATP synthase F0 subunit 6; Provisional
 30-221 1.25e-05

ATP synthase F0 subunit 6; Provisional


Pssm-ID: 177152  Cd Length: 195  Bit Score: 44.20  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  30 MFIFVFGVGYFSGGVYRFMFSLLDSLTKKSFLSGVELMMPCLFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIPFWLGLI 109
Cdd:MTH00087   17 QYLLYFKESMLNVLVKKFFGLLIIVFSYSNKLPLSSVISFFTFIVLLLFCFGGLFPYSFSPCGMVEFTFLYALVAWLSTF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985 110 MSSVlwNWSLVSSGLLPYGVKGLL-AVMMVWVEIVSNLARPLFLGMRLTVNMMVGQVILGLsgsilssLIVSGYFvgsgi 188
Cdd:MTH00087   97 LSFL--SKSEKFSVYLSKGSDSFLkTFSMLFVEIVSELSRPLALTLRLTVNLMVGHLISSL-------LNFLGEK----- 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1181491985 189 VLVVMLLLIVLEIGVAVIQAYLFCFLLTVYIDE 221
Cdd:MTH00087  163 YVWLSILAIMMECFVAFIQSYIFSRLIYLYLNE 195
PRK13420 PRK13420
F0F1 ATP synthase subunit A; Provisional
 71-219 4.61e-04

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237382 [Multi-domain]  Cd Length: 226  Bit Score: 40.11  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985  71 LFIFMLFMNLSGLIPYGFSWTSHFAITYGLAIpfwlgLIMSSVLWnWSLVSSGLLPYGVKGLL-AVMMVWVEIVSNLARP 149
Cdd:PRK13420   81 LWIFILVANLIGLIPGFHSPTADLSVTAALAL-----LVFFSVHW-FGIRAEGLREYLKHYLSpSPFLLPFHLISEITRT 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985 150 LFLGMRLTVNMMVGQVILGLsgsilsSLIVSGYFVgsgivlvvMLLLIVLEIGVAVIQAYLFCFLLTVYI 219
Cdd:PRK13420  155 LALAVRLFGNIMSLELAALL------VLLVAGFLV--------PVPILMLHIIEALVQAYIFGMLALIYI 210
PRK13417 PRK13417
F0F1 ATP synthase subunit A; Provisional
 125-219 2.40e-03

F0F1 ATP synthase subunit A; Provisional


Pssm-ID: 237380  Cd Length: 352  Bit Score: 38.33  E-value: 2.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1181491985 125 LPYGVKGLLAVMMVWVE-IVSNLARPLFLGMRLTVNMMVGQV-ILGLSGSILSS---LIVSGYFVGSGIVLVVmlllivl 199
Cdd:PRK13417  253 VPNGVPLLLYPIMWPLEfIVSPMAKTFALTVRLLANMTAGHViILALMGFIFQFqswGIVPVSVIGSGLIYVL------- 325

                          90       100
                  ....*....|....*....|
gi 1181491985 200 EIGVAVIQAYLFCFLLTVYI 219
Cdd:PRK13417  326 EIFVAFLQAYIFVLLTSLFV 345
 
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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