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Conserved domains on  [gi|41152365|ref|NP_956262|]
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ATP synthase subunit delta, mitochondrial [Danio rerio]

Protein Classification

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, ...
 29-153 4.05e-35

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: 118.77  E-value: 4.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365  29 MSFTFASPTEVFFKEAsVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNaDSSVQLLAE 108
Cdd:cd12152   1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVT-PNRVTILAD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 41152365 109 EAFPLESLDVAAAKANLEKAQSELVSASDEATRAEVLISIEANEA 153
Cdd:cd12152  79 EAERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 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, ...
 29-153 4.05e-35

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: 118.77  E-value: 4.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365  29 MSFTFASPTEVFFKEAsVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNaDSSVQLLAE 108
Cdd:cd12152   1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVT-PNRVTILAD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 41152365 109 EAFPLESLDVAAAKANLEKAQSELVSASDEATRAEVLISIEANEA 153
Cdd:cd12152  79 EAERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 29-159 6.04e-24

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: 90.25  E-value: 6.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365  29 MSFTFASPTEVFFKEAsVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNADsSVQLLAE 108
Cdd:COG0355   1 LKLEIVTPERVLFSGE-VESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPN-KVTILAD 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 41152365 109 EAFPLESLDVAAAKANLEKAQSELVSASDEATRAEVLISIEANEAIVKALE 159
Cdd:COG0355  79 TAERAEDIDVERAEEAKERAEERLEEAKDDIDYARAEAALARALARLRAAE 129
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 27-159 4.76e-18

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 75.18  E-value: 4.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   27 AQMSFTFASPTEVFFkEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNADsSVQLL 106
Cdd:PRK00571   2 ATLTVDIVSPEGLIY-SGEVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPD-KVTVL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152365  107 AEEAFPLESLDVAAAKANLEKAQSELVSASDEATRAEVLISIEANEAIVKALE 159
Cdd:PRK00571  80 ADSAERADDIDEARAEEAKERAEEALENKHDDVDYARAQAALARAIARLRVAE 132
ATP_synt_epsi TIGR01216
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
 35-159 1.22e-17

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: 74.21  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365    35 SPTEVFFkEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNADsSVQLLAEEAFPLE 114
Cdd:TIGR01216   8 TPEGEIY-SGEVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPD-KVTILADGAVFAD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 41152365   115 SLDVAAAKANLEKAQSELVSASDEATRAEVLISIEANEAIVKALE 159
Cdd:TIGR01216  86 DIDEAEAEKALEAAEKLLESAEDDKDLAEALLKLKKARAQLEALE 130
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 29-110 1.07e-15

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: 67.46  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365    29 MSFTFASPTEVFFkEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNADsSVQLLAE 108
Cdd:pfam02823   1 LKLEIVTPERVVF-SGEVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPN-KVTILAD 78


                  ..
gi 41152365   109 EA 110
Cdd:pfam02823  79 SA 80
 
Name Accession Description Interval E-value
F1-ATPase_delta cd12152
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
 29-153 4.05e-35

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: 118.77  E-value: 4.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365  29 MSFTFASPTEVFFKEAsVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNaDSSVQLLAE 108
Cdd:cd12152   1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVT-PNRVTILAD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 41152365 109 EAFPLESLDVAAAKANLEKAQSELVSASDEATRAEVLISIEANEA 153
Cdd:cd12152  79 EAERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 29-159 6.04e-24

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: 90.25  E-value: 6.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365  29 MSFTFASPTEVFFKEAsVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNADsSVQLLAE 108
Cdd:COG0355   1 LKLEIVTPERVLFSGE-VESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPN-KVTILAD 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 41152365 109 EAFPLESLDVAAAKANLEKAQSELVSASDEATRAEVLISIEANEAIVKALE 159
Cdd:COG0355  79 TAERAEDIDVERAEEAKERAEERLEEAKDDIDYARAEAALARALARLRAAE 129
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 27-159 4.76e-18

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 75.18  E-value: 4.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   27 AQMSFTFASPTEVFFkEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNADsSVQLL 106
Cdd:PRK00571   2 ATLTVDIVSPEGLIY-SGEVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPD-KVTVL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 41152365  107 AEEAFPLESLDVAAAKANLEKAQSELVSASDEATRAEVLISIEANEAIVKALE 159
Cdd:PRK00571  80 ADSAERADDIDEARAEEAKERAEEALENKHDDVDYARAQAALARAIARLRVAE 132
ATP_synt_epsi TIGR01216
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
 35-159 1.22e-17

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: 74.21  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365    35 SPTEVFFkEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNADsSVQLLAEEAFPLE 114
Cdd:TIGR01216   8 TPEGEIY-SGEVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPD-KVTILADGAVFAD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 41152365   115 SLDVAAAKANLEKAQSELVSASDEATRAEVLISIEANEAIVKALE 159
Cdd:TIGR01216  86 DIDEAEAEKALEAAEKLLESAEDDKDLAEALLKLKKARAQLEALE 130
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 29-110 1.07e-15

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: 67.46  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365    29 MSFTFASPTEVFFkEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNADsSVQLLAE 108
Cdd:pfam02823   1 LKLEIVTPERVVF-SGEVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPN-KVTILAD 78


                  ..
gi 41152365   109 EA 110
Cdd:pfam02823  79 SA 80
atpC PRK14736
F0F1 ATP synthase subunit epsilon; Provisional
 27-148 9.43e-12

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 173198 [Multi-domain]  Cd Length: 133  Bit Score: 59.04  E-value: 9.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   27 AQMSFTFASPTEVFFkEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNAdSSVQLL 106
Cdd:PRK14736   2 ATFHFDLVGPERTLY-SGEVEAVQLPGSEGEMTVLPGHAPVLTTLKVGVITVTETTGNGKRIYVRGGFAEIGP-TSVTVL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 41152365  107 AEEAFPLESLDVAAAKANLEKAQSELVSASDEATRAEVLISI 148
Cdd:PRK14736  80 AERAAPVEELTPEMIDREIEAVEMERDATQDLDKREALNAQI 121
atpC PRK13450
F0F1 ATP synthase subunit epsilon; Provisional
 41-143 9.54e-12

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184059 [Multi-domain]  Cd Length: 132  Bit Score: 58.62  E-value: 9.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   41 FKEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNaDSSVQLLAEEAFPLESLDVAA 120
Cdd:PRK13450  15 FYIGEVKEVITEGLDGDIAILPNHVPLITYLKPTITKIIDENGEKKKIFTSSGVLKVE-NNEVYILCDASEWPEEIDIKR 93

                         90       100
                 ....*....|....*....|....*
gi 41152365  121 AKANLEKAQSELvSASDE--ATRAE 143
Cdd:PRK13450  94 AENAKKRAEERL-RKKDEidVKRAE 117
atpC PRK13448
F0F1 ATP synthase subunit epsilon; Provisional
 27-142 1.11e-11

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 139579 [Multi-domain]  Cd Length: 135  Bit Score: 58.63  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   27 AQMSFTFASPTEVFFkEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNddGSSKKYFVSSGSVTVNADSSVQLL 106
Cdd:PRK13448   2 ATFHFDLVSPEKLAF-SGEVDQVDIPGVEGDFGVLAGHAPVVAVIRPGILTVTA--GGNQQKIVVLGGLAEVSEKGLTVL 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 41152365  107 AEEAFPLESLDVAAAKANLEKAQSELVS-ASDEATRA 142
Cdd:PRK13448  79 ADVATSVADLDLAQFAATIAEMEAQLAGkVGDELDRA 115
atpC PRK13446
F0F1 ATP synthase subunit epsilon; Provisional
 46-143 1.30e-11

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184056 [Multi-domain]  Cd Length: 136  Bit Score: 58.43  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   46 VKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTvFNDDGSSKKYFVSSGSVTVnADSSVQLLAEEAFPLESLDVAAAKANL 125
Cdd:PRK13446  21 VDEVGAPGVLGEFGVLPGHAPFLTALKIGELT-YKKGGKTHYVAVNGGFAEV-SNNKVTVLAETAERAEEIDVERARAAL 98

                         90       100
                 ....*....|....*....|
gi 41152365  126 EKAQSELVSAS--DEATRAE 143
Cdd:PRK13446  99 ERAEQRLKKLTpeDDSARAE 118
atpC PRK13443
F0F1 ATP synthase subunit epsilon; Provisional
 29-144 5.02e-09

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 237388 [Multi-domain]  Cd Length: 136  Bit Score: 51.85  E-value: 5.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   29 MSFTFASPtEVFFKEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSkKYFVSSGSVTVNADsSVQLLAE 108
Cdd:PRK13443   5 LQFDLVSP-ERRLASFQATAVQIPGADGDMTAMEGHAPTITTLRPGILRAHGPSGTQ-EYAVTGGFAEINAT-SISVLAE 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 41152365  109 EAFPLESLDVAAAKANLEKAQSELVSASDEATRAEV 144
Cdd:PRK13443  82 KAIPVEELTGAVLDEFIAEARELASVALPENEPGDV 117
atpC PRK13449
ATP synthase F1 subunit epsilon;
27-110 5.64e-09

ATP synthase F1 subunit epsilon;


Pssm-ID: 184058 [Multi-domain]  Cd Length: 88  Bit Score: 50.54  E-value: 5.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   27 AQMSFTFASPTEVFFKEaSVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYF-VSSGSVTVNADsSVQL 105
Cdd:PRK13449   2 AKLHFELVTPERLLRSG-EVDMVVVPGTEGDFGVLAGHAPFMTTLREGEVTVYSSDGAAPEVFhVQGGFAEVNEK-GLTI 79


                 ....*
gi 41152365  106 LAEEA 110
Cdd:PRK13449  80 LAEHA 84
PRK13447 PRK13447
F0F1 ATP synthase subunit epsilon; Provisional
 29-141 1.34e-08

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184057 [Multi-domain]  Cd Length: 136  Bit Score: 50.39  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   29 MSFTFASPTEVFFKEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVNADSSVQLLAE 108
Cdd:PRK13447   1 LRLTIATPLAVVVDELDIVSLRAEDASGGFGILPGHADFLTVLRASVVRWRRADGATHYCAVRGGVLRVTGGARVEIACR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 41152365  109 EAFPLESLDV--AAAKANLEKAQSELVSASDEATR 141
Cdd:PRK13447  81 EAVLGEDLARleAVVRAVRAAQLDAARRARVEQTR 115
atpE CHL00063
ATP synthase CF1 epsilon subunit
 36-157 1.63e-07

ATP synthase CF1 epsilon subunit


Pssm-ID: 214351 [Multi-domain]  Cd Length: 134  Bit Score: 47.55  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   36 PTEVFFkEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTV-FNDDGSSkkyFVSSGSVTVNADSSVQLLAEEAFPLE 114
Cdd:CHL00063  10 PNRIVW-DSEVEEIILPTNSGQIGVLPNHAPIATALDIGVLRIrLNDQWLT---MALMGGFARIGNNEITILVNDAEKGS 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 41152365  115 SLDVAAAKANLEKAQSELVSAsdEATRAEvlisIEANEAIVKA 157
Cdd:CHL00063  86 DIDPQEAQQTLEIAEANLEKA--EGKKQK----IEANLALKRA 122
atpC PRK01474
F0F1 ATP synthase subunit epsilon; Validated
 35-131 7.06e-07

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 100879  Cd Length: 112  Bit Score: 45.63  E-value: 7.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   35 SPTEVFFKEASvKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDD--GSSKKYFVSSGsVTVNADSSVQLLAEEAFP 112
Cdd:PRK01474  11 TPLSIAFEKQA-KMVTMPGEEGMFGVLPSHVPMIVSLKAGLVQVYIDDmhKSENTYLISGG-VTEVTGNYINIATETAIN 88

                         90       100
                 ....*....|....*....|..
gi 41152365  113 LESL---DVAAAKANLEKAQSE 131
Cdd:PRK01474  89 VTNLseaEIATKLLDLQKTLSD 110
atpC PRK14735
F0F1 ATP synthase subunit epsilon; Provisional
 46-144 9.66e-07

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 173197 [Multi-domain]  Cd Length: 139  Bit Score: 45.76  E-value: 9.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   46 VKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNdDGSSKKYFVSSG-------SVTVNADSsvqllAEEAFPLESLDV 118
Cdd:PRK14735  19 VDMISAPTKDGRVGILPRHAPLLTILEPGELDIVK-NGVRTPFAISGGfmevlphRVTILADT-----AERADEIDEARA 92

                         90       100
                 ....*....|....*....|....*.
gi 41152365  119 AAAKANLEKAQSELVSASDEAtRAEV 144
Cdd:PRK14735  93 EQARAEAEQRRRERQSEQDLA-LAEA 117
atpC PRK13444
F0F1 ATP synthase subunit epsilon; Provisional
 26-138 2.81e-06

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 139576 [Multi-domain]  Cd Length: 127  Bit Score: 44.10  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365   26 SAQMSFTFASPTEVFFKeASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVfNDDGSSKKYFVSSGSVTVNaDSSVQL 105
Cdd:PRK13444   3 AKKLTVSVISPEKILYK-GEVDSLIVPGSEGFFGILPNHAPLVATLGIGLLEI-RKGEKLKRISVEGGFCEVK-DNQISI 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 41152365  106 LAEEAFPLESLDVAAAKANLekAQSELVSASDE 138
Cdd:PRK13444  80 LTDHGALKEDIDHEHEKKLL--AEAEKLPPSDS 110
atpC PRK13442
F0F1 ATP synthase subunit epsilon; Provisional
 34-110 3.58e-06

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184055 [Multi-domain]  Cd Length: 89  Bit Score: 43.08  E-value: 3.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152365   34 ASPTEVFFKEAsvKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDGSSKKYFVSSGSVTVnADSSVQLLAEEA 110
Cdd:PRK13442  12 AADRPVWSGEA--TMVVARTTEGDIGILPGHEPLLGVLESGTVTVVTPGGERISAAVDGGFISF-DSNKLTVLAERA 85
alt_F1F0_F1_eps TIGR03166
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic ...
 32-142 6.21e-05

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: 40.41  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152365    32 TFASPTEVFFKEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVtVFNDDGSSKKYFVSSGSVTVNADSSVQLLAEEAF 111
Cdd:TIGR03166   3 KILTPFRVFLDKLPVTRIVAETESGSFGLLPGHVDCVAALVPGIL-IYETADGGEHYVAVDQGILVKRGADVEVSVRNAV 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 41152365   112 PLESLdvaaakANLEKAQSELVSASDEATRA 142
Cdd:TIGR03166  82 GGTEL------EELEEAVRQEFLTLDEQERS 106
PRK06228 PRK06228
F0F1 ATP synthase subunit epsilon; Validated
 27-83 3.98e-04

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 235750 [Multi-domain]  Cd Length: 131  Bit Score: 38.37  E-value: 3.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 41152365   27 AQMSFTFASPTEVFFKEASVKQIDVPTLTGAFGILPAHVPTLQVLRPGVVTVFNDDG 83
Cdd:PRK06228   1 ASMNLKILLPFEVFAEKKGVTRIVAETREGSFGLLPHRLDCVAALVPGILVYETEAE 57
 
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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