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Conserved domains on  [gi|1720361930|ref|XP_030101070|]
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ATP synthase subunit delta, mitochondrial isoform X1 [Mus musculus]

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 6.49e-37

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: 123.39  E-value: 6.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFFDSAnVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNaDSSVQLLAE 117
Cdd:cd12152     1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVT-PNRVTILAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720361930 118 EAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEA 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 6.49e-37

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: 123.39  E-value: 6.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFFDSAnVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNaDSSVQLLAE 117
Cdd:cd12152     1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVT-PNRVTILAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720361930 118 EAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEA 162
Cdd:cd12152    79 EAERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 38-168 1.02e-25

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: 95.26  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADsSVQLLAE 117
Cdd:COG0355     1 LKLEIVTPERVLF-SGEVESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPN-KVTILAD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720361930 118 EAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 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 1.31e-18

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: 76.91  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  44 SPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADSsVQLLAEEAVTLD 123
Cdd:TIGR01216   8 TPEGEIY-SGEVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPDK-VTILADGAVFAD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720361930 124 MLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 168
Cdd:TIGR01216  86 DIDEAEAEKALEAAEKLLESAEDDKDLAEALLKLKKARAQLEALE 130
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 38-168 1.93e-18

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 76.34  E-value: 1.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTF--ASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADsSVQLL 115
Cdd:PRK00571    2 ATLTVdiVSPEGLIY-SGEVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPD-KVTVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720361930 116 AEEAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 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 ...
 38-119 8.54e-16

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: 68.23  E-value: 8.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADsSVQLLAE 117
Cdd:pfam02823   1 LKLEIVTPERVVF-SGEVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPN-KVTILAD 78


                  ..
gi 1720361930 118 EA 119
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, ...
 38-162 6.49e-37

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: 123.39  E-value: 6.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFFDSAnVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNaDSSVQLLAE 117
Cdd:cd12152     1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVT-PNRVTILAD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720361930 118 EAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEA 162
Cdd:cd12152    79 EAERPEDIDVERAEEALERAEERLAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 38-168 1.02e-25

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: 95.26  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADsSVQLLAE 117
Cdd:COG0355     1 LKLEIVTPERVLF-SGEVESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPN-KVTILAD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720361930 118 EAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 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 1.31e-18

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: 76.91  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  44 SPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADSsVQLLAEEAVTLD 123
Cdd:TIGR01216   8 TPEGEIY-SGEVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPDK-VTILADGAVFAD 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720361930 124 MLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 168
Cdd:TIGR01216  86 DIDEAEAEKALEAAEKLLESAEDDKDLAEALLKLKKARAQLEALE 130
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 38-168 1.93e-18

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 76.34  E-value: 1.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTF--ASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADsSVQLL 115
Cdd:PRK00571    2 ATLTVdiVSPEGLIY-SGEVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPD-KVTVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720361930 116 AEEAVTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRIEANEALVKALE 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 ...
 38-119 8.54e-16

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: 68.23  E-value: 8.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADsSVQLLAE 117
Cdd:pfam02823   1 LKLEIVTPERVVF-SGEVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPN-KVTILAD 78


                  ..
gi 1720361930 118 EA 119
Cdd:pfam02823  79 SA 80
atpC PRK13448
F0F1 ATP synthase subunit epsilon; Provisional
 40-151 9.90e-14

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 139579 [Multi-domain]  Cd Length: 135  Bit Score: 64.41  E-value: 9.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  40 FTFASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVhTEDGTTTKYFVSSGSVTVnADSSVQLLAEEA 119
Cdd:PRK13448    6 FDLVSPEKLAF-SGEVDQVDIPGVEGDFGVLAGHAPVVAVIRPGILTV-TAGGNQQKIVVLGGLAEV-SEKGLTVLADVA 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720361930 120 VTLDMLDLGAARANLEKAQSELSG-AADEAARA 151
Cdd:PRK13448   83 TSVADLDLAQFAATIAEMEAQLAGkVGDELDRA 115
atpC PRK13446
F0F1 ATP synthase subunit epsilon; Provisional
 52-158 2.12e-12

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184056 [Multi-domain]  Cd Length: 136  Bit Score: 60.74  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  52 SANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVhTEDGTTTKYFVSSGSVTVnADSSVQLLAEEAVTLDMLDLGAAR 131
Cdd:PRK13446   18 SEEVDEVGAPGVLGEFGVLPGHAPFLTALKIGELTY-KKGGKTHYVAVNGGFAEV-SNNKVTVLAETAERAEEIDVERAR 95

                          90       100
                  ....*....|....*....|....*..
gi 1720361930 132 ANLEKAQSELSGAADEAARAEIQIRIE 158
Cdd:PRK13446   96 AALERAEQRLKKLTPEDDSARAEAALE 122
atpE CHL00063
ATP synthase CF1 epsilon subunit
 45-166 1.25e-10

ATP synthase CF1 epsilon subunit


Pssm-ID: 214351 [Multi-domain]  Cd Length: 134  Bit Score: 56.03  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  45 PTQVFFDSaNVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTkyFVSSGSVTVNADSSVQLLAEEAVTLDM 124
Cdd:CHL00063   10 PNRIVWDS-EVEEIILPTNSGQIGVLPNHAPIATALDIGVLRIRLNDQWLT--MALMGGFARIGNNEITILVNDAEKGSD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720361930 125 LDLGAARANLEKAQSELSGAadEAARAeiqiRIEANEALVKA 166
Cdd:CHL00063   87 IDPQEAQQTLEIAEANLEKA--EGKKQ----KIEANLALKRA 122
atpC PRK13449
ATP synthase F1 subunit epsilon;
38-120 4.04e-10

ATP synthase F1 subunit epsilon;


Pssm-ID: 184058 [Multi-domain]  Cd Length: 88  Bit Score: 53.62  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYF-VSSGSVTVNADsSVQLLA 116
Cdd:PRK13449    4 LHFELVTPERLLR-SGEVDMVVVPGTEGDFGVLAGHAPFMTTLREGEVTVYSSDGAAPEVFhVQGGFAEVNEK-GLTILA 81


                  ....
gi 1720361930 117 EEAV 120
Cdd:PRK13449   82 EHAV 85
atpC PRK13443
F0F1 ATP synthase subunit epsilon; Provisional
 38-150 6.72e-10

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 237388 [Multi-domain]  Cd Length: 136  Bit Score: 54.16  E-value: 6.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFfDSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGtTTKYFVSSGSVTVNADsSVQLLAE 117
Cdd:PRK13443    5 LQFDLVSPERRL-ASFQATAVQIPGADGDMTAMEGHAPTITTLRPGILRAHGPSG-TQEYAVTGGFAEINAT-SISVLAE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720361930 118 EAVTLDMLD-------LGAARANLEKAQSELS-GAADEAAR 150
Cdd:PRK13443   82 KAIPVEELTgavldefIAEARELASVALPENEpGDVDDAAK 122
atpC PRK14736
F0F1 ATP synthase subunit epsilon; Provisional
 40-163 2.00e-09

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 173198 [Multi-domain]  Cd Length: 133  Bit Score: 52.87  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  40 FTFASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNAdSSVQLLAEEA 119
Cdd:PRK14736    6 FDLVGPERTLY-SGEVEAVQLPGSEGEMTVLPGHAPVLTTLKVGVITVTETTGNGKRIYVRGGFAEIGP-TSVTVLAERA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720361930 120 VTLDMLDLGAARANLEKAQSELSGAADEAARAEIQIRI----EANEAL 163
Cdd:PRK14736   84 APVEELTPEMIDREIEAVEMERDATQDLDKREALNAQIvqmqEAKATL 131
atpC PRK13450
F0F1 ATP synthase subunit epsilon; Provisional
 41-142 8.30e-09

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184059 [Multi-domain]  Cd Length: 132  Bit Score: 51.30  E-value: 8.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  41 TFASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNaDSSVQLLAEEAV 120
Cdd:PRK13450    7 TILTPEKNFY-IGEVKEVITEGLDGDIAILPNHVPLITYLKPTITKIIDENGEKKKIFTSSGVLKVE-NNEVYILCDASE 84

                          90       100
                  ....*....|....*....|..
gi 1720361930 121 TLDMLDLGAARANLEKAQSELS 142
Cdd:PRK13450   85 WPEEIDIKRAENAKKRAEERLR 106
PRK13447 PRK13447
F0F1 ATP synthase subunit epsilon; Provisional
 38-160 1.88e-08

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184057 [Multi-domain]  Cd Length: 136  Bit Score: 50.39  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  38 MSFTFASPTQVFFDSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVNADSSVQLLAE 117
Cdd:PRK13447    1 LRLTIATPLAVVVDELDIVSLRAEDASGGFGILPGHADFLTVLRASVVRWRRADGATHYCAVRGGVLRVTGGARVEIACR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720361930 118 EAVTLDmlDLGAARANLEKAQSELSGAADEaARAEiQIRIEAN 160
Cdd:PRK13447   81 EAVLGE--DLARLEAVVRAVRAAQLDAARR-ARVE-QTRLHAQ 119
atpC PRK14735
F0F1 ATP synthase subunit epsilon; Provisional
 52-156 2.46e-08

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 173197 [Multi-domain]  Cd Length: 139  Bit Score: 50.00  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  52 SANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVhTEDGTTTKYFVSSG-------SVTVNADSsvqllAEEAVTLDM 124
Cdd:PRK14735   16 SDDVDMISAPTKDGRVGILPRHAPLLTILEPGELDI-VKNGVRTPFAISGGfmevlphRVTILADT-----AERADEIDE 89

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720361930 125 LDLGAARANLEKAQSELSGAADeAARAEIQIR 156
Cdd:PRK14735   90 ARAEQARAEAEQRRRERQSEQD-LALAEAKLR 120
alt_F1F0_F1_eps TIGR03166
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic ...
 41-151 9.69e-08

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: 48.12  E-value: 9.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  41 TFASPTQVFFDSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGsVTVNADSSVQLLAEEAV 120
Cdd:TIGR03166   3 KILTPFRVFLDKLPVTRIVAETESGSFGLLPGHVDCVAALVPGILIYETADGGEHYVAVDQG-ILVKRGADVEVSVRNAV 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720361930 121 tldmldLGAARANLEKAQSELSGAADEAARA 151
Cdd:TIGR03166  82 ------GGTELEELEEAVRQEFLTLDEQERS 106
atpC PRK13442
F0F1 ATP synthase subunit epsilon; Provisional
 52-119 1.50e-05

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184055 [Multi-domain]  Cd Length: 89  Bit Score: 41.54  E-value: 1.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720361930  52 SANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTKYFVSSGSVTVnADSSVQLLAEEA 119
Cdd:PRK13442   19 SGEATMVVARTTEGDIGILPGHEPLLGVLESGTVTVVTPGGERISAAVDGGFISF-DSNKLTVLAERA 85
atpC PRK01474
F0F1 ATP synthase subunit epsilon; Validated
 44-140 1.17e-04

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 100879  Cd Length: 112  Bit Score: 39.47  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  44 SPTQVFFDSaNVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDGTTTK--YFVSSGsVTVNADSSVQLLAEEAVT 121
Cdd:PRK01474   11 TPLSIAFEK-QAKMVTMPGEEGMFGVLPSHVPMIVSLKAGLVQVYIDDMHKSEntYLISGG-VTEVTGNYINIATETAIN 88

                          90       100
                  ....*....|....*....|..
gi 1720361930 122 LDML---DLGAARANLEKAQSE 140
Cdd:PRK01474   89 VTNLseaEIATKLLDLQKTLSD 110
atpC PRK13444
F0F1 ATP synthase subunit epsilon; Provisional
 37-139 2.68e-04

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 139576 [Multi-domain]  Cd Length: 127  Bit Score: 38.71  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720361930  37 QMSFTFASPTQVFFdSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTedGTTTKYFVSSGSVTVNADSSVQLLA 116
Cdd:PRK13444    5 KLTVSVISPEKILY-KGEVDSLIVPGSEGFFGILPNHAPLVATLGIGLLEIRK--GEKLKRISVEGGFCEVKDNQISILT 81

                          90       100
                  ....*....|....*....|...
gi 1720361930 117 EEAVTLDMLDLGAARANLEKAQS 139
Cdd:PRK13444   82 DHGALKEDIDHEHEKKLLAEAEK 104
PRK06228 PRK06228
F0F1 ATP synthase subunit epsilon; Validated
 45-92 1.21e-03

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 235750 [Multi-domain]  Cd Length: 131  Bit Score: 37.22  E-value: 1.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720361930  45 PTQVFFDSANVKQVDVPTLTGAFGILASHVPTLQVLRPGLVVVHTEDG 92
Cdd:PRK06228   10 PFEVFAEKKGVTRIVAETREGSFGLLPHRLDCVAALVPGILVYETEAE 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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