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Conserved domains on  [gi|1055252981|ref|WP_066921821|]
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ATPase [Steroidobacter denitrificans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06228 super family cl35451
F0F1 ATP synthase subunit epsilon; Validated
 5-137 7.69e-39

F0F1 ATP synthase subunit epsilon; Validated


The actual alignment was detected with superfamily member PRK06228:

Pssm-ID: 235750 [Multi-domain]  Cd Length: 131  Bit Score: 127.36  E-value: 7.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   5 DQMQVYVRLPARILFEGPA-TRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAV 83
Cdd:PRK06228    1 ASMNLKILLPFEVFAEKKGvTRIVAETREGSFGLLPHRLDCVAALVPGILVYETEAEGEVYVAVDEGILVKTGPDVLVSV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1055252981  84 RRGVHGADLESLRETVGERFAGMEDEERASRAALSRLEADMVRRFATLrrpHHE 137
Cdd:PRK06228   81 RNAIGGTDLGELREAVEQEFLTLDERERSVRSALAKLESGFIRRFMEL---KHD 131
 
Name Accession Description Interval E-value
PRK06228 PRK06228
F0F1 ATP synthase subunit epsilon; Validated
 5-137 7.69e-39

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 235750 [Multi-domain]  Cd Length: 131  Bit Score: 127.36  E-value: 7.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   5 DQMQVYVRLPARILFEGPA-TRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAV 83
Cdd:PRK06228    1 ASMNLKILLPFEVFAEKKGvTRIVAETREGSFGLLPHRLDCVAALVPGILVYETEAEGEVYVAVDEGILVKTGPDVLVSV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1055252981  84 RRGVHGADLESLRETVGERFAGMEDEERASRAALSRLEADMVRRFATLrrpHHE 137
Cdd:PRK06228   81 RNAIGGTDLGELREAVEQEFLTLDERERSVRSALAKLESGFIRRFMEL---KHD 131
alt_F1F0_F1_eps TIGR03166
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic ...
 13-128 1.51e-34

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: 116.30  E-value: 1.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981  13 LPARILFEG-PATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAVRRGVHGAD 91
Cdd:TIGR03166   6 TPFRVFLDKlPVTRIVAETESGSFGLLPGHVDCVAALVPGILIYETADGGEHYVAVDQGILVKRGADVEVSVRNAVGGTE 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1055252981  92 LESLRETVGERFAGMEDEERASRAALSRLEADMVRRF 128
Cdd:TIGR03166  86 LEELEEAVRQEFLTLDEQERSARSAMARLESDFIRRL 122
F1-ATPase_delta cd12152
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
 7-125 1.20e-25

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: 93.73  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   7 MQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAVRRG 86
Cdd:cd12152     1 LKLEIVTPERVFFSGEVESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVTPNRVTILADEA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1055252981  87 VHGADLESLRETVGERFA----GMEDEERASRAALSRLEADMV 125
Cdd:cd12152    81 ERPEDIDVERAEEALERAeerlAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 7-132 2.06e-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: 90.63  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   7 MQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAVRRG 86
Cdd:COG0355     1 LKLEIVTPERVLFSGEVESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPNKVTILADTA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1055252981  87 VHGADL--ESLRETVGERFAGMedEERASRAALSRLEADMVRRFATLR 132
Cdd:COG0355    81 ERAEDIdvERAEEAKERAEERL--EEAKDDIDYARAEAALARALARLR 126
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 7-85 1.03e-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: 77.09  E-value: 1.03e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055252981   7 MQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAVRR 85
Cdd:pfam02823   1 LKLEIVTPERVVFSGEVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPNKVTILADS 79
 
Name Accession Description Interval E-value
PRK06228 PRK06228
F0F1 ATP synthase subunit epsilon; Validated
 5-137 7.69e-39

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 235750 [Multi-domain]  Cd Length: 131  Bit Score: 127.36  E-value: 7.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   5 DQMQVYVRLPARILFEGPA-TRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAV 83
Cdd:PRK06228    1 ASMNLKILLPFEVFAEKKGvTRIVAETREGSFGLLPHRLDCVAALVPGILVYETEAEGEVYVAVDEGILVKTGPDVLVSV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1055252981  84 RRGVHGADLESLRETVGERFAGMEDEERASRAALSRLEADMVRRFATLrrpHHE 137
Cdd:PRK06228   81 RNAIGGTDLGELREAVEQEFLTLDERERSVRSALAKLESGFIRRFMEL---KHD 131
alt_F1F0_F1_eps TIGR03166
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic ...
 13-128 1.51e-34

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: 116.30  E-value: 1.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981  13 LPARILFEG-PATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAVRRGVHGAD 91
Cdd:TIGR03166   6 TPFRVFLDKlPVTRIVAETESGSFGLLPGHVDCVAALVPGILIYETADGGEHYVAVDQGILVKRGADVEVSVRNAVGGTE 85

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1055252981  92 LESLRETVGERFAGMEDEERASRAALSRLEADMVRRF 128
Cdd:TIGR03166  86 LEELEEAVRQEFLTLDEQERSARSAMARLESDFIRRL 122
F1-ATPase_delta cd12152
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
 7-125 1.20e-25

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: 93.73  E-value: 1.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   7 MQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAVRRG 86
Cdd:cd12152     1 LKLEIVTPERVFFSGEVESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVTPNRVTILADEA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1055252981  87 VHGADLESLRETVGERFA----GMEDEERASRAALSRLEADMV 125
Cdd:cd12152    81 ERPEDIDVERAEEALERAeerlAQAKDEREKARAEAALERALA 123
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 7-132 2.06e-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: 90.63  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   7 MQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAVRRG 86
Cdd:COG0355     1 LKLEIVTPERVLFSGEVESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPNKVTILADTA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1055252981  87 VHGADL--ESLRETVGERFAGMedEERASRAALSRLEADMVRRFATLR 132
Cdd:COG0355    81 ERAEDIdvERAEEAKERAEERL--EEAKDDIDYARAEAALARALARLR 126
PRK13447 PRK13447
F0F1 ATP synthase subunit epsilon; Provisional
 7-137 7.22e-22

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184057 [Multi-domain]  Cd Length: 136  Bit Score: 84.29  E-value: 7.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   7 MQVYVRLPARILFEGPATR-LVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEG-LLLKKGHTVEIAVR 84
Cdd:PRK13447    1 LRLTIATPLAVVVDELDIVsLRAEDASGGFGILPGHADFLTVLRASVVRWRRADGATHYCAVRGGvLRVTGGARVEIACR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1055252981  85 RGVHGADLESLRETVGERFAGMEDEERASRAALSRLEADMVRRFATLRRPHHE 137
Cdd:PRK13447   81 EAVLGEDLARLEAVVRAVRAAQLDAARRARVEQTRLHAQAVRQLLRYLRPERG 133
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 7-85 1.03e-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: 77.09  E-value: 1.03e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055252981   7 MQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAVRR 85
Cdd:pfam02823   1 LKLEIVTPERVVFSGEVEMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPNKVTILADS 79
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 4-124 2.05e-10

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 54.77  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   4 ADQMQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAV 83
Cdd:PRK00571    1 MATLTVDIVSPEGLIYSGEVEEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPDKVTVLA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1055252981  84 RRGVHGADLeslretvgerfagmeDEERAsRAALSRLEADM 124
Cdd:PRK00571   81 DSAERADDI---------------DEARA-EEAKERAEEAL 105
ATP_synt_epsi TIGR01216
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
 7-122 3.74e-09

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: 51.49  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   7 MQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVEIAVRRG 86
Cdd:TIGR01216   2 LKLEIVTPEGEIYSGEVESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPDKVTILADGA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1055252981  87 VHGADL-----ESLRETVGERFAGMEDEERASRA------ALSRLEA 122
Cdd:TIGR01216  82 VFADDIdeaeaEKALEAAEKLLESAEDDKDLAEAllklkkARAQLEA 128
atpC PRK13450
F0F1 ATP synthase subunit epsilon; Provisional
 4-121 1.04e-08

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184059 [Multi-domain]  Cd Length: 132  Bit Score: 50.15  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   4 ADQMQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTV---- 79
Cdd:PRK13450    1 ANNIKLTILTPEKNFYIGEVKEVITEGLDGDIAILPNHVPLITYLKPTITKIIDENGEKKKIFTSSGVLKVENNEVyilc 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1055252981  80 -------EIAVRRGvhgadlESLRETVGERFAGME--DEERASRA---ALSRLE 121
Cdd:PRK13450   81 dasewpeEIDIKRA------ENAKKRAEERLRKKDeiDVKRAELAlfrAIARIK 128
atpC PRK13444
F0F1 ATP synthase subunit epsilon; Provisional
 3-93 3.79e-06

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 139576 [Multi-domain]  Cd Length: 127  Bit Score: 43.33  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   3 MADQMQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDApEQVFGIDEGLLLKKGHTVEIA 82
Cdd:PRK13444    2 MAKKLTVSVISPEKILYKGEVDSLIVPGSEGFFGILPNHAPLVATLGIGLLEIRKGEK-LKRISVEGGFCEVKDNQISIL 80

                          90
                  ....*....|.
gi 1055252981  83 VRRGVHGADLE 93
Cdd:PRK13444   81 TDHGALKEDID 91
atpC PRK13442
F0F1 ATP synthase subunit epsilon; Provisional
 1-86 1.58e-05

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184055 [Multi-domain]  Cd Length: 89  Bit Score: 40.77  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   1 MSMADqMQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVFGIDEGLLLKKGHTVE 80
Cdd:PRK13442    1 MAGAT-LHVNIVAADRPVWSGEATMVVARTTEGDIGILPGHEPLLGVLESGTVTVVTPGGERISAAVDGGFISFDSNKLT 79


                  ....*.
gi 1055252981  81 IAVRRG 86
Cdd:PRK13442   80 VLAERA 85
atpC PRK13446
F0F1 ATP synthase subunit epsilon; Provisional
 3-133 6.19e-05

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184056 [Multi-domain]  Cd Length: 136  Bit Score: 39.94  E-value: 6.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   3 MADQMQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTpldapeqvfgideglllKKGHTVEIA 82
Cdd:PRK13446    1 MAKKLKLEIVTPEKKVLSEEVDEVGAPGVLGEFGVLPGHAPFLTALKIGELTYK-----------------KGGKTHYVA 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055252981  83 VRRG---VHGADLESLRETvGERfAGMEDEERAsRAALSRLEA---------DMVRRFATLRR 133
Cdd:PRK13446   64 VNGGfaeVSNNKVTVLAET-AER-AEEIDVERA-RAALERAEQrlkkltpedDSARAEAALER 123
atpC PRK13448
F0F1 ATP synthase subunit epsilon; Provisional
 14-110 4.84e-04

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 139579 [Multi-domain]  Cd Length: 135  Bit Score: 37.83  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981  14 PARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDAPEQVF---GIDEglLLKKGHTVEIAVRRGVHGA 90
Cdd:PRK13448   11 PEKLAFSGEVDQVDIPGVEGDFGVLAGHAPVVAVIRPGILTVTAGGNQQKIVvlgGLAE--VSEKGLTVLADVATSVADL 88

                          90       100
                  ....*....|....*....|
gi 1055252981  91 DLESLRETVGERFAGMEDEE 110
Cdd:PRK13448   89 DLAQFAATIAEMEAQLAGKV 108
atpE CHL00063
ATP synthase CF1 epsilon subunit
 7-55 1.17e-03

ATP synthase CF1 epsilon subunit


Pssm-ID: 214351 [Multi-domain]  Cd Length: 134  Bit Score: 36.77  E-value: 1.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1055252981   7 MQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLV 55
Cdd:CHL00063    3 LNLRVLTPNRIVWDSEVEEIILPTNSGQIGVLPNHAPIATALDIGVLRI 51
atpC PRK01474
F0F1 ATP synthase subunit epsilon; Validated
 3-92 1.71e-03

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 100879  Cd Length: 112  Bit Score: 36.00  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055252981   3 MADQMQVYVRLPARILFEGPATRLVATAANGSFGILPNHIDFVTALVPSVLLVTPLDA--PEQVFGIDEGLLLKKGHTVE 80
Cdd:PRK01474    1 MNETILVKIITPLSIAFEKQAKMVTMPGEEGMFGVLPSHVPMIVSLKAGLVQVYIDDMhkSENTYLISGGVTEVTGNYIN 80

                          90
                  ....*....|..
gi 1055252981  81 IAVRRGVHGADL 92
Cdd:PRK01474   81 IATETAINVTNL 92
 
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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