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Conserved domains on  [gi|924532048|gb|ALC18297|]
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ATP synthase F0 b subunit [Desulfuromonas soudanensis]

Protein Classification

ATP synthase F0 subunit B( domain architecture ID 12950672)

ATP synthase Fo subunit b is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 48-179 2.78e-30

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


:

Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 107.91  E-value: 2.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  48 DFLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGEL 127
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 924532048 128 EREKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLK 179
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
 
Name Accession Description Interval E-value
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 48-179 2.78e-30

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 107.91  E-value: 2.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  48 DFLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGEL 127
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 924532048 128 EREKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLK 179
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 48-198 1.57e-29

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 106.80  E-value: 1.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  48 DFLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGEL 127
Cdd:COG0711    2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 924532048 128 EREKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKV 198
Cdd:COG0711   82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 57-194 6.74e-22

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 87.14  E-value: 6.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  57 AVTFGILAYFITK----PIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKI 132
Cdd:PRK05759  11 LIAFLILVWFIMKfvwpPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAAQIIEEA 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 924532048 133 LLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEY 194
Cdd:PRK05759  91 KAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKL 152
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 49-178 6.12e-17

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 73.50  E-value: 6.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048   49 FLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELE 128
Cdd:pfam00430   2 LVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 924532048  129 REKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLL 178
Cdd:pfam00430  82 KEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLL 131
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 57-198 6.28e-15

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 68.58  E-value: 6.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048   57 AVTFGILAYFITK----PIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKI 132
Cdd:TIGR01144   2 LISFILLVWFCMKyvwpPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEEA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 924532048  133 LLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKV 198
Cdd:TIGR01144  82 KAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
 
Name Accession Description Interval E-value
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 48-179 2.78e-30

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 107.91  E-value: 2.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  48 DFLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGEL 127
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 924532048 128 EREKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLK 179
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 48-198 1.57e-29

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 106.80  E-value: 1.57e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  48 DFLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGEL 127
Cdd:COG0711    2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 924532048 128 EREKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKV 198
Cdd:COG0711   82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 57-194 6.74e-22

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 87.14  E-value: 6.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  57 AVTFGILAYFITK----PIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKI 132
Cdd:PRK05759  11 LIAFLILVWFIMKfvwpPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAAQIIEEA 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 924532048 133 LLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEY 194
Cdd:PRK05759  91 KAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKL 152
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 49-178 6.12e-17

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 73.50  E-value: 6.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048   49 FLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELE 128
Cdd:pfam00430   2 LVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 924532048  129 REKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLL 178
Cdd:pfam00430  82 KEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLL 131
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 54-192 1.00e-16

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 74.22  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  54 FNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKIL 133
Cdd:PRK07352  27 INLAIVIGLLYYFGRGFLGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIE 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 924532048 134 LNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVN 192
Cdd:PRK07352 107 KQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLID 165
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 43-202 1.48e-15

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 70.72  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  43 GVLLKDFLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIR 122
Cdd:PRK14473   5 GINLGLLIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQAQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048 123 REGELEREKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKVGELN 202
Cdd:PRK14473  85 ERARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAALGRRN 164
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 57-198 6.28e-15

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 68.58  E-value: 6.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048   57 AVTFGILAYFITK----PIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKI 132
Cdd:TIGR01144   2 LISFILLVWFCMKyvwpPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEEA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 924532048  133 LLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKV 198
Cdd:TIGR01144  82 KAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 54-192 4.44e-13

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 64.44  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  54 FNFAVTFGILAYFITK----PIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELER 129
Cdd:PRK14472  22 FWTAVTFVIVLLILKKiawgPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKLR 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 924532048 130 EKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVN 192
Cdd:PRK14472 102 AEITEKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVD 164
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 49-198 5.63e-12

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 61.35  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  49 FLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELE 128
Cdd:PRK14471  11 FFWQTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEKM 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 924532048 129 REKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFT-ADDNTRLVNEYMHKV 198
Cdd:PRK14471  91 IADAKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRKELSnKEKQHKLVEKMLGDV 161
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 56-202 1.37e-11

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 60.42  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  56 FAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKILLN 135
Cdd:PRK13460  26 FLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDALKLKNKLLEE 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924532048 136 AREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKVGELN 202
Cdd:PRK13460 106 TNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIETELAKLGKLS 172
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 55-199 7.28e-11

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 58.14  E-value: 7.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  55 NFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKILL 134
Cdd:PRK13461  14 NFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEYKSKAENVYEEIVK 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924532048 135 NAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKVG 199
Cdd:PRK13461  94 EAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIKDFISKVG 158
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 49-195 3.93e-10

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 56.77  E-value: 3.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  49 FLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELE 128
Cdd:PRK06231  51 FIAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQL 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924532048 129 REKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYM 195
Cdd:PRK06231 131 KSELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFI 197
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 42-200 4.52e-10

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 56.07  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  42 GGVLLKDFLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEI 121
Cdd:PRK13453  14 GGVEWGTVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDA 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 924532048 122 RREGELEREKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKVGE 200
Cdd:PRK13453  94 KVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKEAGD 172
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 39-148 2.49e-08

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 51.17  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  39 AVDGGVLLKDFLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIY 118
Cdd:PRK08475  15 ASLGATEQYDIIERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIV 94

                         90       100       110
                 ....*....|....*....|....*....|.
gi 924532048 119 AEIRREGELEREKILLNAR-EMAEKIKQEAE 148
Cdd:PRK08475  95 ETAKKEAYILTQKIEKQTKdDIENLIKSFEE 125
PRK13455 PRK13455
F0F1 ATP synthase subunit B; Provisional
 56-199 6.23e-08

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184062 [Multi-domain]  Cd Length: 184  Bit Score: 50.57  E-value: 6.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  56 FAVTFGILAYF-ITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKILL 134
Cdd:PRK13455  36 FLLFIGILVYFkVPGMIGGMLDKRAEGIRSELEEARALREEAQTLLASYERKQREVQEQADRIVAAAKDEAQAAAEQAKA 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 924532048 135 NAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKVG 199
Cdd:PRK13455 116 DLEASIARRLAAAEDQIASAEAAAVKAVRDRAVSVAVAAAADVIAKQMTAADANALIDEAIKEVE 180
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 55-201 1.99e-07

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 49.81  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  55 NFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKILL 134
Cdd:PRK14474  14 NFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEQQRASFMAQAQEAADEQRQHLLN 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 924532048 135 NAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKVGEL 201
Cdd:PRK14474  94 EAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAALADLANATLEQQIVGIFIARLEHL 160
PRK09173 PRK09173
F0F1 ATP synthase subunit B; Validated
 60-198 4.06e-07

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 169691 [Multi-domain]  Cd Length: 159  Bit Score: 47.81  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  60 FGILAYF-ITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKILLNARE 138
Cdd:PRK09173  15 LALVVYLkVPGMIARSLDARADRIKNELAEARRLREEAQQLLAEYQRKRKEAEKEAADIVAAAEREAEALTAEAKRKTEE 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048 139 MAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKV 198
Cdd:PRK09173  95 YVARRNKLAEQKIAQAETDAINAVRSSAVDLAIAAAEKLLAEKVDAKAASELFKDALAQV 154
PRK09174 PRK09174
F0F1 ATP synthase subunit B;
57-161 9.33e-07

F0F1 ATP synthase subunit B;


Pssm-ID: 169692 [Multi-domain]  Cd Length: 204  Bit Score: 47.48  E-value: 9.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  57 AVTFGILAYFITKPIRKGLAG----RREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYA----EIRREGELE 128
Cdd:PRK09174  60 AITFGLFYLFMSRVILPRIGGiietRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSIAQaareAAKAKAEAE 139

                         90       100       110
                 ....*....|....*....|....*....|...
gi 924532048 129 REKIllnAREMAEKIKqEAEKTAAHEVTKACSE 161
Cdd:PRK09174 140 RAAI---EASLEKKLK-EAEARIAAIKAKAMAD 168
PRK13428 PRK13428
F0F1 ATP synthase subunit delta; Provisional
 49-186 4.88e-06

F0F1 ATP synthase subunit delta; Provisional


Pssm-ID: 184048 [Multi-domain]  Cd Length: 445  Bit Score: 46.27  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  49 FLYRCFNFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQE-AEAKfAEYDGKLAKASAEIEEIYAEIRREGEL 127
Cdd:PRK13428   4 FIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRlAEAD-QAHTKAVEDAKAEAARVVEEAREDAER 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 924532048 128 EREKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLkRDFTADD 186
Cdd:PRK13428  83 IAEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGELV-RNHVADP 140
atpF CHL00019
ATP synthase CF0 B subunit
 55-201 2.22e-05

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 43.32  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  55 NFAVTFGILAYFITKPIRKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEeiyaEIRREGELEREKILL 134
Cdd:CHL00019  33 NLSVVLGVLIYFGKGVLSDLLDNRKQTILNTIRNSEERREEAIEKLEKARARLRQAELEAD----EIRVNGYSEIEREKE 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 924532048 135 N----AREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLAENLLKRDFTADDNTRLVNEYMHKVGEL 201
Cdd:CHL00019 109 NlinqAKEDLERLENYKNETIRFEQQRAINQVRQQVFQLALQRALGTLNSCLNNELHLRTINANIGLLGAM 179
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
72-158 3.64e-04

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 40.51  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  72 RKGLAGRREGIAQALAQAETARQEAEAKFAEYDGK---------------LAKASAEIEEIYAEIRREGELEREKIllNA 136
Cdd:COG1193  527 RRELEEEREEAERLREELEKLREELEEKLEELEEEkeeilekareeaeeiLREARKEAEELIRELREAQAEEEELK--EA 604

                         90       100
                 ....*....|....*....|..
gi 924532048 137 REMAEKIKQEAEKTAAHEVTKA 158
Cdd:COG1193  605 RKKLEELKQELEEKLEKPKKKA 626
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 82-149 9.30e-04

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 38.77  E-value: 9.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  82 IAQALAQAETARQEAEAKF-AEYDGKLAKASAEIEEIYAEIRREGELEREKILLNAR-EMAEKIKQEAEK 149
Cdd:COG1390   23 LEEAEEEAEKILEEAEEEAeEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKeELIEEVFEEALE 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 75-175 1.35e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  75 LAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEE----IYAEIRREGELEREKILLNAREMAEKIKQEAEKT 150
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaeEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                         90       100
                 ....*....|....*....|....*
gi 924532048 151 AAHEVTKACSELRQETARMAVSLAE 175
Cdd:COG1196  324 ELAELEEELEELEEELEELEEELEE 348
PRK01558 PRK01558
V-type ATP synthase subunit E; Provisional
 112-184 1.66e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179302  Cd Length: 198  Bit Score: 37.82  E-value: 1.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 924532048 112 AEIEEIYAEIRREGELEREKILLNAREMAEKIKQEAEKTAAHEVTKACSELRQETARMAVSLaENLLKRDFTA 184
Cdd:PRK01558  18 EEAERLANEIILEAKEEAEEIIAKAEEEAKELKAKAEKEANDYKRHALEASRQAGRDLLISF-EKSIKSLFKA 89
RpnC COG5464
Recombination-promoting DNA endonuclease RpnC/YadD [Replication, recombination and repair];
78-189 2.17e-03

Recombination-promoting DNA endonuclease RpnC/YadD [Replication, recombination and repair];


Pssm-ID: 444215 [Multi-domain]  Cd Length: 301  Bit Score: 38.02  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  78 RREGIAQALAQAETARQEAEAK--------FAEYDGKLAKASAEIEEIYAEIRREGELeREKILlnarEMAEKIKQEAEK 149
Cdd:COG5464  170 RTDALEELLRLLARLLQEIEDEaqreqleaLIEYIAVKFQPDLEREEIEAMLRLIDEL-KETIM----TIYQELLQEGRE 244

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 924532048 150 TAAHEVTKACSELRQETARmavSLAENLLKRDFTADDNTR 189
Cdd:COG5464  245 EGRQEGREGRQEGRQEGKL---ELALRLLKRRFGLPLELI 281
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
 115-151 2.96e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 37.04  E-value: 2.96e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 924532048 115 EEIYAEIRREGELEREKILLNAREMAEKIKQEAEKTA 151
Cdd:PRK03963   5 ELIIQEINREAEQKIEYILEEAQKEAEKIKEEARKRA 41
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
77-181 5.19e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 37.16  E-value: 5.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  77 GRREgIAQALAQAETARQEAEAkfaeyDGKLAKASAEIEEIYAEIRREGELEREKIllnAREMAEKIKQEAEKTAAHEVT 156
Cdd:COG2268  190 GRRK-IAEIIRDARIAEAEAER-----ETEIAIAQANREAEEAELEQEREIETARI---AEAEAELAKKKAEERREAETA 260

                         90       100
                 ....*....|....*....|....*....
gi 924532048 157 KACSE----LRQETARMAVSLAENLLKRD 181
Cdd:COG2268  261 RAEAEaayeIAEANAEREVQRQLEIAERE 289
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 78-164 5.68e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.11  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  78 RREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREKILlnaREMAEKIKQEAEKTAAHEVTK 157
Cdd:PRK00409 535 KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEII---KELRQLQKGGYASVKAHELIE 611


                 ....*..
gi 924532048 158 ACSELRQ 164
Cdd:PRK00409 612 ARKRLNK 618
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 80-158 5.98e-03

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 36.74  E-value: 5.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 924532048  80 EGIAQALAQAETARQEAEAkfaeydgklAKASAEIEEIYAEIRREGELEREKILLNAREMAEKIKQEAEKTAAHEVTKA 158
Cdd:COG0330  167 EEVQDAMEDRMKAEREREA---------AILEAEGYREAAIIRAEGEAQRAIIEAEAYREAQILRAEGEAEAFRIVAEA 236
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 72-180 8.80e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 36.45  E-value: 8.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924532048  72 RKGLAGRREGIAQALAQAETARQEAEAKFAEYDGKLAKASAEIEEIYAEIRREGELEREkILLNAREMAEKIKQEAEKTA 151
Cdd:COG1196  255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-LEERLEELEEELAELEEELE 333

                         90       100
                 ....*....|....*....|....*....
gi 924532048 152 AHEVTKACSELRQETARMAVSLAENLLKR 180
Cdd:COG1196  334 ELEEELEELEEELEEAEEELEEAEAELAE 362
 
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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