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Conserved domains on  [gi|497250849|ref|WP_009565066|]
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F0F1 ATP synthase subunit epsilon [Cereibacter sphaeroides]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13447 super family cl32877
F0F1 ATP synthase subunit epsilon; Provisional
 3-138 7.49e-56

F0F1 ATP synthase subunit epsilon; Provisional


The actual alignment was detected with superfamily member PRK13447:

Pssm-ID: 184057 [Multi-domain]  Cd Length: 136  Bit Score: 170.96  E-value: 7.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   3 LTLRVTTPLAAVLEEEGLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRTVTVACR 82
Cdd:PRK13447   1 LRLTIATPLAVVVDELDIVSLRAEDASGGFGILPGHADFLTVLRASVVRWRRADGATHYCAVRGGVLRVTGGARVEIACR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497250849  83 EAVPGEDLARLEAGLKRQAEAADQAARRARGEQVRLHANAIRSLMRHLDRAPGADL 138
Cdd:PRK13447  81 EAVLGEDLARLEAVVRAVRAAQLDAARRARVEQTRLHAQAVRQLLRYLRPERGADG 136
 
Name Accession Description Interval E-value
PRK13447 PRK13447
F0F1 ATP synthase subunit epsilon; Provisional
 3-138 7.49e-56

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184057 [Multi-domain]  Cd Length: 136  Bit Score: 170.96  E-value: 7.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   3 LTLRVTTPLAAVLEEEGLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRTVTVACR 82
Cdd:PRK13447   1 LRLTIATPLAVVVDELDIVSLRAEDASGGFGILPGHADFLTVLRASVVRWRRADGATHYCAVRGGVLRVTGGARVEIACR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497250849  83 EAVPGEDLARLEAGLKRQAEAADQAARRARGEQVRLHANAIRSLMRHLDRAPGADL 138
Cdd:PRK13447  81 EAVLGEDLARLEAVVRAVRAAQLDAARRARVEQTRLHAQAVRQLLRYLRPERGADG 136
alt_F1F0_F1_eps TIGR03166
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic ...
 5-126 6.96e-25

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: 92.03  E-value: 6.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849    5 LRVTTPLAAVLEEEGLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACREA 84
Cdd:TIGR03166   2 LKILTPFRVFLDKLPVTRIVAETESGSFGLLPGHVDCVAALVPGILIYETADGGEHYVAVDQGILVKRGAD-VEVSVRNA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 497250849   85 VPGEDLARLEAGLKRQAEAADQAARRARGEQVRLHANAIRSL 126
Cdd:TIGR03166  81 VGGTELEELEEAVRQEFLTLDEQERSARSAMARLESDFIRRL 122
F1-ATPase_delta cd12152
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
 3-95 3.72e-21

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: 82.56  E-value: 3.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   3 LTLRVTTPLAAVLEEEgLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACR 82
Cdd:cd12152    1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVTPNR-VTILAD 78

                         90
                 ....*....|...
gi 497250849  83 EAVPGEDLARLEA 95
Cdd:cd12152   79 EAERPEDIDVERA 91
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 3-95 7.74e-20

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: 79.46  E-value: 7.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   3 LTLRVTTPLAAVLEEEgLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACR 82
Cdd:COG0355    1 LKLEIVTPERVLFSGE-VESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPNK-VTILAD 78

                         90
                 ....*....|....*
gi 497250849  83 EAVPGEDL--ARLEA 95
Cdd:COG0355   79 TAERAEDIdvERAEE 93
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 3-84 2.42e-18

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: 74.01  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849    3 LTLRVTTPLAAVLEEEGlASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACR 82
Cdd:pfam02823   1 LKLEIVTPERVVFSGEV-EMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPNK-VTILAD 78


                  ..
gi 497250849   83 EA 84
Cdd:pfam02823  79 SA 80
 
Name Accession Description Interval E-value
PRK13447 PRK13447
F0F1 ATP synthase subunit epsilon; Provisional
 3-138 7.49e-56

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184057 [Multi-domain]  Cd Length: 136  Bit Score: 170.96  E-value: 7.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   3 LTLRVTTPLAAVLEEEGLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRTVTVACR 82
Cdd:PRK13447   1 LRLTIATPLAVVVDELDIVSLRAEDASGGFGILPGHADFLTVLRASVVRWRRADGATHYCAVRGGVLRVTGGARVEIACR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497250849  83 EAVPGEDLARLEAGLKRQAEAADQAARRARGEQVRLHANAIRSLMRHLDRAPGADL 138
Cdd:PRK13447  81 EAVLGEDLARLEAVVRAVRAAQLDAARRARVEQTRLHAQAVRQLLRYLRPERGADG 136
alt_F1F0_F1_eps TIGR03166
alternate F1F0 ATPase, F1 subunit epsilon; A small number of taxonomically diverse prokaryotic ...
 5-126 6.96e-25

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: 92.03  E-value: 6.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849    5 LRVTTPLAAVLEEEGLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACREA 84
Cdd:TIGR03166   2 LKILTPFRVFLDKLPVTRIVAETESGSFGLLPGHVDCVAALVPGILIYETADGGEHYVAVDQGILVKRGAD-VEVSVRNA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 497250849   85 VPGEDLARLEAGLKRQAEAADQAARRARGEQVRLHANAIRSL 126
Cdd:TIGR03166  81 VGGTELEELEEAVRQEFLTLDEQERSARSAMARLESDFIRRL 122
F1-ATPase_delta cd12152
mitochondrial ATP synthase delta subunit; The F-ATPase is found in bacterial plasma membranes, ...
 3-95 3.72e-21

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: 82.56  E-value: 3.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   3 LTLRVTTPLAAVLEEEgLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACR 82
Cdd:cd12152    1 LKLEIVTPERVFFSGE-VESVVLPGTEGEFGILPGHAPLVTALKPGVLRIRDEDGEEKYFAVSGGFLEVTPNR-VTILAD 78

                         90
                 ....*....|...
gi 497250849  83 EAVPGEDLARLEA 95
Cdd:cd12152   79 EAERPEDIDVERA 91
AtpC COG0355
FoF1-type ATP synthase, epsilon subunit [Energy production and conversion]; FoF1-type ATP ...
 3-95 7.74e-20

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: 79.46  E-value: 7.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   3 LTLRVTTPLAAVLEEEgLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACR 82
Cdd:COG0355    1 LKLEIVTPERVLFSGE-VESVVAPGAEGEFGILPGHAPLLTALKPGVVRIRTEDGEEEYFAVSGGFLEVQPNK-VTILAD 78

                         90
                 ....*....|....*
gi 497250849  83 EAVPGEDL--ARLEA 95
Cdd:COG0355   79 TAERAEDIdvERAEE 93
ATP-synt_DE_N pfam02823
ATP synthase, Delta/Epsilon chain, beta-sandwich domain; Part of the ATP synthase CF(1). These ...
 3-84 2.42e-18

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: 74.01  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849    3 LTLRVTTPLAAVLEEEGlASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACR 82
Cdd:pfam02823   1 LKLEIVTPERVVFSGEV-EMVVAPGAEGELGILPGHAPLLTALKPGVLRIKTEDGEEEYIAVSGGFLEVQPNK-VTILAD 78


                  ..
gi 497250849   83 EA 84
Cdd:pfam02823  79 SA 80
PRK06228 PRK06228
F0F1 ATP synthase subunit epsilon; Validated
 1-98 5.01e-13

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 235750 [Multi-domain]  Cd Length: 131  Bit Score: 61.87  E-value: 5.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   1 MSLTLRVTTPLAAVLEEEGLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVA 80
Cdd:PRK06228   1 ASMNLKILLPFEVFAEKKGVTRIVAETREGSFGLLPHRLDCVAALVPGILVYETEAEGEVYVAVDEGILVKTGPD-VLVS 79

                         90
                 ....*....|....*...
gi 497250849  81 CREAVPGEDLARLEAGLK 98
Cdd:PRK06228  80 VRNAIGGTDLGELREAVE 97
ATP_synt_epsi TIGR01216
ATP synthase, F1 epsilon subunit (delta in mitochondria); This model describes one of the five ...
 3-95 2.68e-12

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: 59.96  E-value: 2.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849    3 LTLRVTTPLAAVLEEEgLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACR 82
Cdd:TIGR01216   2 LKLEIVTPEGEIYSGE-VESVILPGSEGELGILPGHAPLITALKPGVVRIRKLGDDWEHIAVSGGFAEVQPDK-VTILAD 79

                          90
                  ....*....|...
gi 497250849   83 EAVPGEDLARLEA 95
Cdd:TIGR01216  80 GAVFADDIDEAEA 92
atpC PRK00571
F0F1 ATP synthase subunit epsilon; Validated
 1-98 2.52e-10

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 234796 [Multi-domain]  Cd Length: 135  Bit Score: 54.77  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   1 MSLTLRVTTPLAAVLEEEGlASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGrTVTVA 80
Cdd:PRK00571   2 ATLTVDIVSPEGLIYSGEV-EEVVVPGTEGELGILPGHAPLLTALKPGVVRIKKDDGEEEVIAVSGGFLEVQPD-KVTVL 79

                         90       100
                 ....*....|....*....|
gi 497250849  81 CREAVPGEDL--ARLEAGLK 98
Cdd:PRK00571  80 ADSAERADDIdeARAEEAKE 99
atpE CHL00063
ATP synthase CF1 epsilon subunit
 1-95 2.95e-08

ATP synthase CF1 epsilon subunit


Pssm-ID: 214351 [Multi-domain]  Cd Length: 134  Bit Score: 49.09  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   1 MSLTLRVTTPLAAVLEEEglasirAED-----ASGGFGLLPGHVDLLTVIEAGVLRFRRAEGpWRFCAIRGGVLRATGGR 75
Cdd:CHL00063   1 MTLNLRVLTPNRIVWDSE------VEEiilptNSGQIGVLPNHAPIATALDIGVLRIRLNDQ-WLTMALMGGFARIGNNE 73

                         90       100
                 ....*....|....*....|
gi 497250849  76 tVTVACREAVPGEDLARLEA 95
Cdd:CHL00063  74 -ITILVNDAEKGSDIDPQEA 92
atpC PRK13446
F0F1 ATP synthase subunit epsilon; Provisional
 1-97 3.76e-06

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184056 [Multi-domain]  Cd Length: 136  Bit Score: 43.79  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   1 MSLTLRVTTPLAAVLEEEgLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFrRAEGPWRFCAIRGGVLRATGGR-TVTV 79
Cdd:PRK13446   3 KKLKLEIVTPEKKVLSEE-VDEVGAPGVLGEFGVLPGHAPFLTALKIGELTY-KKGGKTHYVAVNGGFAEVSNNKvTVLA 80

                         90
                 ....*....|....*...
gi 497250849  80 ACREAVPGEDLARLEAGL 97
Cdd:PRK13446  81 ETAERAEEIDVERARAAL 98
atpC PRK14736
F0F1 ATP synthase subunit epsilon; Provisional
 28-92 1.45e-03

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 173198 [Multi-domain]  Cd Length: 133  Bit Score: 36.70  E-value: 1.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497250849  28 ASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGvLRATGGRTVTVACREAVPGEDLAR 92
Cdd:PRK14736  28 SEGEMTVLPGHAPVLTTLKVGVITVTETTGNGKRIYVRGG-FAEIGPTSVTVLAERAAPVEELTP 91
atpC PRK13452
F0F1 ATP synthase subunit epsilon; Provisional
 3-95 1.59e-03

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 106409 [Multi-domain]  Cd Length: 145  Bit Score: 36.65  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   3 LTLRVTTPLAAVLEEEG-LASIRAedASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPwRFCAIRGGVLRATGGRtVTVAC 81
Cdd:PRK13452   6 LKVDVVSPLGSVFKGEAdMVSLRG--SAGEMGIAYGHTELLSTLPAGVVNVRKDQHT-DVLYVSGGIVEVTPTR-VTIMV 81

                         90
                 ....*....|....
gi 497250849  82 REAVPGEDLARLEA 95
Cdd:PRK13452  82 DDMERAENLNQAEA 95
atpC PRK01474
F0F1 ATP synthase subunit epsilon; Validated
 1-98 2.40e-03

F0F1 ATP synthase subunit epsilon; Validated


Pssm-ID: 100879  Cd Length: 112  Bit Score: 35.62  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497250849   1 MSLTLRVT--TPLAAVLEEEG-LASIRAEDasGGFGLLPGHVDLLTVIEAGVLR--FRRAEGPWRFCAIRGGVLRATGGr 75
Cdd:PRK01474   1 MNETILVKiiTPLSIAFEKQAkMVTMPGEE--GMFGVLPSHVPMIVSLKAGLVQvyIDDMHKSENTYLISGGVTEVTGN- 77

                         90       100
                 ....*....|....*....|...
gi 497250849  76 TVTVACREAVPGEDLARLEAGLK 98
Cdd:PRK01474  78 YINIATETAINVTNLSEAEIATK 100
atpC PRK13442
F0F1 ATP synthase subunit epsilon; Provisional
 29-84 3.31e-03

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 184055 [Multi-domain]  Cd Length: 89  Bit Score: 34.61  E-value: 3.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 497250849  29 SGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFCAIRGGVLRATGGRtVTVACREA 84
Cdd:PRK13442  31 EGDIGILPGHEPLLGVLESGTVTVVTPGGERISAAVDGGFISFDSNK-LTVLAERA 85
atpC PRK13444
F0F1 ATP synthase subunit epsilon; Provisional
 3-67 7.09e-03

F0F1 ATP synthase subunit epsilon; Provisional


Pssm-ID: 139576 [Multi-domain]  Cd Length: 127  Bit Score: 34.47  E-value: 7.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497250849   3 LTLRVTTPlAAVLEEEGLASIRAEDASGGFGLLPGHVDLLTVIEAGVLRFRRAEGPWRFcAIRGG 67
Cdd:PRK13444   6 LTVSVISP-EKILYKGEVDSLIVPGSEGFFGILPNHAPLVATLGIGLLEIRKGEKLKRI-SVEGG 68
 
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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