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Conserved domains on  [gi|2601489548|ref|WP_317449339|]
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ATP synthase F1 subunit epsilon [uncultured Sellimonas sp.]

Protein Classification

FoF1 ATP synthase subunit delta/epsilon( domain architecture ID 10187353)

The FoF1 ATP synthase subunit delta/epsilon is a component of the F1-complex catalytic core of the F-type ATPase, which synthesizes ATP from ADP in the presence of a proton gradient across the membrane

Gene Ontology:  GO:0015986|GO:0046933|GO:0045261
PubMed:  12745923|15282184
SCOP:  4004011

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F1-ATPase_delta cd12152
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
 7-129 4.73e-31

mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain. In bacteria, which is lacking a eukaryotic epsilon subunit homolog, this subunit is called the epsilon subunit.


:

Pssm-ID: 213395 [Multi-domain]  Cd Length: 123  Bit Score: 107.60  E-value: 4.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   7 FGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFALTV 86
Cdd:cd12152     1 LKLEIVTPERVFFSGEVESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVTPNRVTILADEA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2601489548  87 ERPEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMS 129
Cdd:cd12152    81 ERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 123
 
Name Accession Description Interval E-value
F1-ATPase_delta cd12152
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
 7-129 4.73e-31

mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain. In bacteria, which is lacking a eukaryotic epsilon subunit homolog, this subunit is called the epsilon subunit.


Pssm-ID: 213395 [Multi-domain]  Cd Length: 123  Bit Score: 107.60  E-value: 4.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   7 FGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFALTV 86
Cdd:cd12152     1 LKLEIVTPERVFFSGEVESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVTPNRVTILADEA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2601489548  87 ERPEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMS 129
Cdd:cd12152    81 ERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 9-137 2.19e-30

FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP synthase, epsilon subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440124 [Multi-domain]  Cd Length: 131  Bit Score: 106.04  E-value: 2.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   9 LEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFALTVER 88
Cdd:COG0355     3 LEIVTPERVLFSGEVESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPNKVTILADTAER 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2601489548  89 PEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMSRLRVTSRK 137
Cdd:COG0355    83 AEDIDVERAEEAKERAEERLEEAKDDIDYARAEAALARALARLRAAEKL 131
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 5-138 1.02e-25

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 94.06  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   5 NTFGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFAL 84
Cdd:PRK00571    2 ATLTVDIVSPEGLIYSGEVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPDKVTVLAD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2601489548  85 TVERPEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMSRLRVTSRKK 138
Cdd:PRK00571   82 SAERADDIDEARAEEAKERAEEALENKHDDVDYARAQAALARAIARLRVAEKLR 135
ATP_synt_epsi TIGR01216
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
 6-133 1.01e-19

ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five types of subunits in the F1 part of F1/F0 ATP synthases. Members of this family are designated epsilon in bacterial and chloroplast systems but designated delta in mitochondria, where the counterpart of the bacterial delta subunit is designated OSCP. In a few cases (Propionigenium modestum, Acetobacterium woodii) scoring above the trusted cutoff and designated here as exceptions, Na+ replaces H+ for translocation. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273506 [Multi-domain]  Cd Length: 130  Bit Score: 78.84  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   6 TFGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFALT 85
Cdd:TIGR01216   1 TLKLEIVTPEGEIYSGEVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPDKVTILADG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2601489548  86 VERPEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMSRLRV 133
Cdd:TIGR01216  81 AVFADDIDEAEAEKALEAAEKLLESAEDDKDLAEALLKLKKARAQLEA 128
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 9-83 1.61e-19

ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These subunits are part of the head unit of the ATP synthase. The subunit is called epsilon in bacteria and delta in mitochondria. In bacteria the delta (D) subunit is equivalent to the mitochondrial Oligomycin sensitive subunit, OSCP (pfam00213).


Pssm-ID: 460714 [Multi-domain]  Cd Length: 80  Bit Score: 76.71  E-value: 1.61e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2601489548   9 LEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFA 83
Cdd:pfam02823   3 LEIVTPERVVFSGEVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPNKVTILA 77
 
Name Accession Description Interval E-value
F1-ATPase_delta cd12152
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
 7-129 4.73e-31

mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinisic membrane domain, F1, is composed of alpha, beta, gamma, delta, and epsilon subunits with a stoichiometry of 3:3:1:1:1. Alpha and beta subunit form the globular catalytic moiety, a hexameric ring of alternating subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton translocating domain. In bacteria, which is lacking a eukaryotic epsilon subunit homolog, this subunit is called the epsilon subunit.


Pssm-ID: 213395 [Multi-domain]  Cd Length: 123  Bit Score: 107.60  E-value: 4.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   7 FGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFALTV 86
Cdd:cd12152     1 LKLEIVTPERVFFSGEVESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVTPNRVTILADEA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2601489548  87 ERPEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMS 129
Cdd:cd12152    81 ERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 9-137 2.19e-30

FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP synthase, epsilon subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440124 [Multi-domain]  Cd Length: 131  Bit Score: 106.04  E-value: 2.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   9 LEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFALTVER 88
Cdd:COG0355     3 LEIVTPERVLFSGEVESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPNKVTILADTAER 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2601489548  89 PEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMSRLRVTSRK 137
Cdd:COG0355    83 AEDIDVERAEEAKERAEERLEEAKDDIDYARAEAALARALARLRAAEKL 131
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 5-138 1.02e-25

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 94.06  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   5 NTFGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFAL 84
Cdd:PRK00571    2 ATLTVDIVSPEGLIYSGEVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPDKVTVLAD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2601489548  85 TVERPEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMSRLRVTSRKK 138
Cdd:PRK00571   82 SAERADDIDEARAEEAKERAEEALENKHDDVDYARAQAALARAIARLRVAEKLR 135
atpC PRK13450
F0F1 ATP synthase subunit epsilon; Provisional
 5-133 3.41e-22

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184059 [Multi-domain]  Cd Length: 132  Bit Score: 85.20  E-value: 3.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   5 NTFGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFAL 84
Cdd:PRK13450    2 NNIKLTILTPEKNFYIGEVKEVITEGLDGDIAILPNHVPLITYLKPTITKIIDENGEKKKIFTSSGVLKVENNEVYILCD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2601489548  85 TVERPEEIDIRRAEEAKERAEEQLRQKKSMEEYNAnQMALARAMSRLRV 133
Cdd:PRK13450   82 ASEWPEEIDIKRAENAKKRAEERLRKKDEIDVKRA-ELALFRAIARIKL 129
atpC PRK14735
F0F1 ATP synthase subunit epsilon; Provisional
 9-139 7.24e-20

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 173197 [Multi-domain]  Cd Length: 139  Bit Score: 79.66  E-value: 7.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   9 LEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDpEGNKITVAVSAGFIEVFNNRVKVFALTVER 88
Cdd:PRK14735    5 LEIVTAERVVLSDDVDMISAPTKDGRVGILPRHAPLLTILEPGELDIVK-NGVRTPFAISGGFMEVLPHRVTILADTAER 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2601489548  89 PEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMSRLRVTSRKKI 139
Cdd:PRK14735   84 ADEIDEARAEQARAEAEQRRRERQSEQDLALAEAKLRRAMVRLRVAQLHKI 134
ATP_synt_epsi TIGR01216
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
 6-133 1.01e-19

ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five types of subunits in the F1 part of F1/F0 ATP synthases. Members of this family are designated epsilon in bacterial and chloroplast systems but designated delta in mitochondria, where the counterpart of the bacterial delta subunit is designated OSCP. In a few cases (Propionigenium modestum, Acetobacterium woodii) scoring above the trusted cutoff and designated here as exceptions, Na+ replaces H+ for translocation. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273506 [Multi-domain]  Cd Length: 130  Bit Score: 78.84  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   6 TFGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFALT 85
Cdd:TIGR01216   1 TLKLEIVTPEGEIYSGEVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPDKVTILADG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2601489548  86 VERPEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMSRLRV 133
Cdd:TIGR01216  81 AVFADDIDEAEAEKALEAAEKLLESAEDDKDLAEALLKLKKARAQLEA 128
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 9-83 1.61e-19

ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These subunits are part of the head unit of the ATP synthase. The subunit is called epsilon in bacteria and delta in mitochondria. In bacteria the delta (D) subunit is equivalent to the mitochondrial Oligomycin sensitive subunit, OSCP (pfam00213).


Pssm-ID: 460714 [Multi-domain]  Cd Length: 80  Bit Score: 76.71  E-value: 1.61e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2601489548   9 LEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFA 83
Cdd:pfam02823   3 LEIVTPERVVFSGEVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPNKVTILA 77
atpC PRK13446
F0F1 ATP synthase subunit epsilon; Provisional
 26-136 2.55e-16

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184056 [Multi-domain]  Cd Length: 136  Bit Score: 69.99  E-value: 2.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548  26 ITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDpEGNKITVAVSAGFIEVFNNRVKVFALTVERPEEIDIRRAEEAKERAE 105
Cdd:PRK13446   24 VGAPGVLGEFGVLPGHAPFLTALKIGELTYKK-GGKTHYVAVNGGFAEVSNNKVTVLAETAERAEEIDVERARAALERAE 102

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2601489548 106 EQLRQKKSMEEYNANQMALARAMSRLRVTSR 136
Cdd:PRK13446  103 QRLKKLTPEDDSARAEAALERALIRLQVAGK 133
atpC PRK13442
F0F1 ATP synthase subunit epsilon; Provisional
 10-83 7.12e-14

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184055 [Multi-domain]  Cd Length: 89  Bit Score: 62.73  E-value: 7.12e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2601489548  10 EIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFA 83
Cdd:PRK13442    9 NIVAADRPVWSGEATMVVARTTEGDIGILPGHEPLLGVLESGTVTVVTPGGERISAAVDGGFISFDSNKLTVLA 82
atpE CHL00063
ATP synthase CF1 epsilon subunit
 6-138 1.09e-06

ATP synthase CF1 epsilon subunit


Pssm-ID: 214351 [Multi-domain]  Cd Length: 134  Bit Score: 44.86  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   6 TFGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDfVDPEGNKITVAVSAGFIEVFNNRVKVFALT 85
Cdd:CHL00063    2 TLNLRVLTPNRIVWDSEVEEIILPTNSGQIGVLPNHAPIATALDIGVLR-IRLNDQWLTMALMGGFARIGNNEITILVND 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2601489548  86 VERPEEIDIRRAEEAKERAEEQLRQKKSMEEYNANQMALARAMSRLRVTSRKK 138
Cdd:CHL00063   81 AEKGSDIDPQEAQQTLEIAEANLEKAEGKKQKIEANLALKRARARVEAINAIS 133
atpC PRK14736
F0F1 ATP synthase subunit epsilon; Provisional
 6-93 8.16e-06

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 173198 [Multi-domain]  Cd Length: 133  Bit Score: 42.47  E-value: 8.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601489548   6 TFGLEIYASNRQFYVGRGQSITFPVEDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKVFA-- 83
Cdd:PRK14736    3 TFHFDLVGPERTLYSGEVEAVQLPGSEGEMTVLPGHAPVLTTLKVGVITVTETTGNGKRIYVRGGFAEIGPTSVTVLAer 82

                          90
                  ....*....|...
gi 2601489548  84 -LTVER--PEEID 93
Cdd:PRK14736   83 aAPVEEltPEMID 95
alt_F1F0_F1_eps TIGR03166
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic ...
 31-81 2.22e-03

alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 epsilon subunit of this apparent second ATP synthase.


Pssm-ID: 132210 [Multi-domain]  Cd Length: 122  Bit Score: 35.79  E-value: 2.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2601489548  31 EDGEMQVLPHHEDMIAAIVPGEMDFVDPEGNKITVAVSAGFIEVFNNRVKV 81
Cdd:TIGR03166  25 ESGSFGLLPGHVDCVAALVPGILIYETADGGEHYVAVDQGILVKRGADVEV 75
atpC PRK01474
F0F1 ATP synthase subunit epsilon; Validated
 26-81 7.68e-03

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 100879  Cd Length: 112  Bit Score: 34.08  E-value: 7.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2601489548  26 ITFPVEDGEMQVLPHHEDMIAAIVPG--EMDFVDPEGNKITVAVSAGFIEVFNNRVKV 81
Cdd:PRK01474   24 VTMPGEEGMFGVLPSHVPMIVSLKAGlvQVYIDDMHKSENTYLISGGVTEVTGNYINI 81
 
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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