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Conserved domains on  [gi|1937931316|ref|NP_620806|]
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ATP synthase subunit delta, mitochondrial precursor [Rattus norvegicus]

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, ...
 38-162 1.78e-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: 119.92  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTFASPTQVFFDGAnVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNaDSSVQLLAE 117
Cdd:cd12152     1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVT-PNRVTILAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1937931316 118 EVVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEA 162
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, ...
 38-162 1.78e-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: 119.92  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTFASPTQVFFDGAnVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNaDSSVQLLAE 117
Cdd:cd12152     1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVT-PNRVTILAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1937931316 118 EVVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEA 162
Cdd:cd12152    79 EAERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 38-168 4.22e-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: 91.02  E-value: 4.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTFASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNADsSVQLLAE 117
Cdd:COG0355     1 LKLEIVTPERVLFSG-EVESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPN-KVTILAD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937931316 118 EVVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 168
Cdd:COG0355    79 TAERAEDIDVERAEEAKERAEERLEEAKDDIDYARAEAALARALARLRAAE 129
ATP_synt_epsi TIGR01216
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
 44-168 5.52e-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: 72.67  E-value: 5.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  44 SPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNADSsVQLLAEEVVTLD 123
Cdd:TIGR01216   8 TPEGEIYSG-EVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPDK-VTILADGAVFAD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1937931316 124 MLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 168
Cdd:TIGR01216  86 DIDEAEAEKALEAAEKLLESAEDDKDLAEALLKLKKARAQLEALE 130
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 38-168 8.95e-17

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 72.10  E-value: 8.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTF--ASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNADsSVQLL 115
Cdd:PRK00571    2 ATLTVdiVSPEGLIYSG-EVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPD-KVTVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1937931316 116 AEEVVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 168
Cdd:PRK00571   80 ADSAERADDIDEARAEEAKERAEEALENKHDDVDYARAQAALARAIARLRVAE 132
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 38-118 4.63e-14

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: 63.61  E-value: 4.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTFASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNADsSVQLLAE 117
Cdd:pfam02823   1 LKLEIVTPERVVFSG-EVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPN-KVTILAD 78


                  .
gi 1937931316 118 E 118
Cdd:pfam02823  79 S 79
 
Name Accession Description Interval E-value
F1-ATPase_delta cd12152
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
 38-162 1.78e-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: 119.92  E-value: 1.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTFASPTQVFFDGAnVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNaDSSVQLLAE 117
Cdd:cd12152     1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVT-PNRVTILAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1937931316 118 EVVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEA 162
Cdd:cd12152    79 EAERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 38-168 4.22e-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: 91.02  E-value: 4.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTFASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNADsSVQLLAE 117
Cdd:COG0355     1 LKLEIVTPERVLFSG-EVESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPN-KVTILAD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937931316 118 EVVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 168
Cdd:COG0355    79 TAERAEDIDVERAEEAKERAEERLEEAKDDIDYARAEAALARALARLRAAE 129
ATP_synt_epsi TIGR01216
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
 44-168 5.52e-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: 72.67  E-value: 5.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  44 SPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNADSsVQLLAEEVVTLD 123
Cdd:TIGR01216   8 TPEGEIYSG-EVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPDK-VTILADGAVFAD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1937931316 124 MLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 168
Cdd:TIGR01216  86 DIDEAEAEKALEAAEKLLESAEDDKDLAEALLKLKKARAQLEALE 130
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 38-168 8.95e-17

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 72.10  E-value: 8.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTF--ASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNADsSVQLL 115
Cdd:PRK00571    2 ATLTVdiVSPEGLIYSG-EVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPD-KVTVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1937931316 116 AEEVVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 168
Cdd:PRK00571   80 ADSAERADDIDEARAEEAKERAEEALENKHDDVDYARAQAALARAIARLRVAE 132
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 38-118 4.63e-14

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: 63.61  E-value: 4.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTFASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNADsSVQLLAE 117
Cdd:pfam02823   1 LKLEIVTPERVVFSG-EVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPN-KVTILAD 78


                  .
gi 1937931316 118 E 118
Cdd:pfam02823  79 S 79
atpC PRK13448
F0F1 ATP synthase subunit epsilon; Provisional
 40-151 1.76e-12

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 139579 [Multi-domain]  Cd Length: 135  Bit Score: 60.94  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  40 FTFASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAedGTTTKYFVSSGSVTVNADSSVQLLAEEV 119
Cdd:PRK13448    6 FDLVSPEKLAFSG-EVDQVDIPGVEGDFGVLAGHAPVVAVIRPGILTVTA--GGNQQKIVVLGGLAEVSEKGLTVLADVA 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1937931316 120 VTLDMLDLGAARANLEKAQSELSG-AADEAARA 151
Cdd:PRK13448   83 TSVADLDLAQFAATIAEMEAQLAGkVGDELDRA 115
atpC PRK13443
F0F1 ATP synthase subunit epsilon; Provisional
 36-150 2.05e-10

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 237388 [Multi-domain]  Cd Length: 136  Bit Score: 55.70  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  36 GQMSFTFASPTQVFFDGAnVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGtTTKYFVSSGSVTVNADsSVQLL 115
Cdd:PRK13443    3 GTLQFDLVSPERRLASFQ-ATAVQIPGADGDMTAMEGHAPTITTLRPGILRAHGPSG-TQEYAVTGGFAEINAT-SISVL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1937931316 116 AEEVVTLDMLD-------LGAARANLEKAQSELS-GAADEAAR 150
Cdd:PRK13443   80 AEKAIPVEELTgavldefIAEARELASVALPENEpGDVDDAAK 122
atpC PRK13446
F0F1 ATP synthase subunit epsilon; Provisional
 55-158 4.54e-10

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184056 [Multi-domain]  Cd Length: 136  Bit Score: 54.58  E-value: 4.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  55 VRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHaEDGTTTKYFVSSGSVTVnADSSVQLLAEEVVTLDMLDLGAARANL 134
Cdd:PRK13446   21 VDEVGAPGVLGEFGVLPGHAPFLTALKIGELTYK-KGGKTHYVAVNGGFAEV-SNNKVTVLAETAERAEEIDVERARAAL 98

                          90       100
                  ....*....|....*....|....
gi 1937931316 135 EKAQSELSGAADEAARAEIQIRIE 158
Cdd:PRK13446   99 ERAEQRLKKLTPEDDSARAEAALE 122
atpC PRK14736
F0F1 ATP synthase subunit epsilon; Provisional
 40-163 7.00e-10

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 173198 [Multi-domain]  Cd Length: 133  Bit Score: 54.03  E-value: 7.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  40 FTFASPTQVFFDGAnVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNAdSSVQLLAEEV 119
Cdd:PRK14736    6 FDLVGPERTLYSGE-VEAVQLPGSEGEMTVLPGHAPVLTTLKVGVITVTETTGNGKRIYVRGGFAEIGP-TSVTVLAERA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1937931316 120 VTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRI----EANEAL 163
Cdd:PRK14736   84 APVEELTPEMIDREIEAVEMERDATQDLDKREALNAQIvqmqEAKATL 131
atpC PRK13449
ATP synthase F1 subunit epsilon;
36-120 3.56e-09

ATP synthase F1 subunit epsilon;


Pssm-ID: 184058 [Multi-domain]  Cd Length: 88  Bit Score: 51.31  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  36 GQMSFTFASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYF-VSSGSVTVNADsSVQL 114
Cdd:PRK13449    2 AKLHFELVTPERLLRSG-EVDMVVVPGTEGDFGVLAGHAPFMTTLREGEVTVYSSDGAAPEVFhVQGGFAEVNEK-GLTI 79


                  ....*.
gi 1937931316 115 LAEEVV 120
Cdd:PRK13449   80 LAEHAV 85
atpE CHL00063
ATP synthase CF1 epsilon subunit
 45-166 5.92e-08

ATP synthase CF1 epsilon subunit


Pssm-ID: 214351 [Multi-domain]  Cd Length: 134  Bit Score: 49.09  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  45 PTQVFFDgANVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTkyFVSSGSVTVNADSSVQLLAEEVVTLDM 124
Cdd:CHL00063   10 PNRIVWD-SEVEEIILPTNSGQIGVLPNHAPIATALDIGVLRIRLNDQWLT--MALMGGFARIGNNEITILVNDAEKGSD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1937931316 125 LDLGAARANLEKAQSELSGAadEAARAeiqiRIEANEALVKA 166
Cdd:CHL00063   87 IDPQEAQQTLEIAEANLEKA--EGKKQ----KIEANLALKRA 122
atpC PRK13450
F0F1 ATP synthase subunit epsilon; Provisional
 41-142 9.46e-08

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184059 [Multi-domain]  Cd Length: 132  Bit Score: 48.22  E-value: 9.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  41 TFASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNaDSSVQLLAEEVV 120
Cdd:PRK13450    7 TILTPEKNFYIG-EVKEVITEGLDGDIAILPNHVPLITYLKPTITKIIDENGEKKKIFTSSGVLKVE-NNEVYILCDASE 84

                          90       100
                  ....*....|....*....|..
gi 1937931316 121 TLDMLDLGAARANLEKAQSELS 142
Cdd:PRK13450   85 WPEEIDIKRAENAKKRAEERLR 106
PRK13447 PRK13447
F0F1 ATP synthase subunit epsilon; Provisional
 38-150 2.46e-07

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184057 [Multi-domain]  Cd Length: 136  Bit Score: 47.31  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  38 MSFTFASPTQVFFDGANVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVNADSSVQLLAE 117
Cdd:PRK13447    1 LRLTIATPLAVVVDELDIVSLRAEDASGGFGILPGHADFLTVLRASVVRWRRADGATHYCAVRGGVLRVTGGARVEIACR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1937931316 118 EVVTLDMLdlgaarANLEKAQSELSGAADEAAR 150
Cdd:PRK13447   81 EAVLGEDL------ARLEAVVRAVRAAQLDAAR 107
atpC PRK14735
F0F1 ATP synthase subunit epsilon; Provisional
 54-156 3.45e-07

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 173197 [Multi-domain]  Cd Length: 139  Bit Score: 46.92  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  54 NVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVhAEDGTTTKYFVSSGSVTVnADSSVQLLAEEVVTLDMLDLG---AA 130
Cdd:PRK14735   18 DVDMISAPTKDGRVGILPRHAPLLTILEPGELDI-VKNGVRTPFAISGGFMEV-LPHRVTILADTAERADEIDEAraeQA 95

                          90       100
                  ....*....|....*....|....*.
gi 1937931316 131 RANLEKAQSELSGAADeAARAEIQIR 156
Cdd:PRK14735   96 RAEAEQRRRERQSEQD-LALAEAKLR 120
alt_F1F0_F1_eps TIGR03166
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic ...
 41-151 3.27e-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: 41.18  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  41 TFASPTQVFFDGANVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGsVTVNADSSVQLLAEEVV 120
Cdd:TIGR03166   3 KILTPFRVFLDKLPVTRIVAETESGSFGLLPGHVDCVAALVPGILIYETADGGEHYVAVDQG-ILVKRGADVEVSVRNAV 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1937931316 121 tldmldLGAARANLEKAQSELSGAADEAARA 151
Cdd:TIGR03166  82 ------GGTELEELEEAVRQEFLTLDEQERS 106
atpC PRK13444
F0F1 ATP synthase subunit epsilon; Provisional
 37-139 4.16e-04

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 139576 [Multi-domain]  Cd Length: 127  Bit Score: 38.32  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  37 QMSFTFASPTQVFFDGaNVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHaEDGTTTKYFVSSGSVTVNaDSSVQLLA 116
Cdd:PRK13444    5 KLTVSVISPEKILYKG-EVDSLIVPGSEGFFGILPNHAPLVATLGIGLLEIR-KGEKLKRISVEGGFCEVK-DNQISILT 81

                          90       100
                  ....*....|....*....|...
gi 1937931316 117 EEVVTLDMLDLGAARANLEKAQS 139
Cdd:PRK13444   82 DHGALKEDIDHEHEKKLLAEAEK 104
atpC PRK01474
F0F1 ATP synthase subunit epsilon; Validated
 44-140 8.15e-04

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 100879  Cd Length: 112  Bit Score: 37.16  E-value: 8.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937931316  44 SPTQVFFDgANVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTK--YFVSSG--SVTVNADSSVQLLAEEV 119
Cdd:PRK01474   11 TPLSIAFE-KQAKMVTMPGEEGMFGVLPSHVPMIVSLKAGLVQVYIDDMHKSEntYLISGGvtEVTGNYINIATETAINV 89

                          90       100
                  ....*....|....*....|.
gi 1937931316 120 VTLDMLDLGAARANLEKAQSE 140
Cdd:PRK01474   90 TNLSEAEIATKLLDLQKTLSD 110
atpC PRK13442
F0F1 ATP synthase subunit epsilon; Provisional
 57-117 1.65e-03

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184055 [Multi-domain]  Cd Length: 89  Bit Score: 35.76  E-value: 1.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937931316  57 QVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDGTTTKYFVSSGSVTVnADSSVQLLAE 117
Cdd:PRK13442   24 MVVARTTEGDIGILPGHEPLLGVLESGTVTVVTPGGERISAAVDGGFISF-DSNKLTVLAE 83
PRK06228 PRK06228
F0F1 ATP synthase subunit epsilon; Validated
 36-92 7.29e-03

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 235750 [Multi-domain]  Cd Length: 131  Bit Score: 34.91  E-value: 7.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1937931316  36 GQMSFTFASPTQVFFDGANVRQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHAEDG 92
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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