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Conserved domains on  [gi|1278529013|gb|PJA47794.1|]
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ATP synthase F0 subunit B [Candidatus Uhrbacteria bacterium CG_4_9_14_3_um_filter_36_7]

Protein Classification

similar to ATP synthase subunit b( domain architecture ID 11431239)

protein similar to ATP synthase subunit b

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 28-177 8.99e-20

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: 80.99  E-value: 8.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  28 LFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEE 107
Cdd:COG0711     2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013 108 RNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKKAEEVIEK 177
Cdd:COG0711    82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAE 151
 
Name Accession Description Interval E-value
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 28-177 8.99e-20

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: 80.99  E-value: 8.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  28 LFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEE 107
Cdd:COG0711     2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013 108 RNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKKAEEVIEK 177
Cdd:COG0711    82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAE 151
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 28-159 1.68e-19

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: 79.40  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  28 LFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEE 107
Cdd:cd06503     1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1278529013 108 RNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILE 159
Cdd:cd06503    81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 24-165 2.86e-19

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 79.82  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  24 LNAKLFAaQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHE 103
Cdd:PRK05759    3 LNGTLIG-QLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278529013 104 QTEERNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEK 165
Cdd:PRK05759   82 RAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAA 143
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 32-169 3.84e-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: 3.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  32 QLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEERNEK 111
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1278529013 112 MIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKK 169
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKD 138
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 ...
 29-159 1.39e-10

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: 56.17  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  29 FAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEER 108
Cdd:pfam00430   2 LVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1278529013 109 NEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILE 159
Cdd:pfam00430  82 KEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
 
Name Accession Description Interval E-value
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 28-177 8.99e-20

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: 80.99  E-value: 8.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  28 LFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEE 107
Cdd:COG0711     2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013 108 RNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKKAEEVIEK 177
Cdd:COG0711    82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAE 151
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 28-159 1.68e-19

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: 79.40  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  28 LFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEE 107
Cdd:cd06503     1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1278529013 108 RNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILE 159
Cdd:cd06503    81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 24-165 2.86e-19

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 79.82  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  24 LNAKLFAaQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHE 103
Cdd:PRK05759    3 LNGTLIG-QLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKK 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278529013 104 QTEERNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEK 165
Cdd:PRK05759   82 RAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAA 143
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 19-180 2.67e-15

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 69.57  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  19 ISALGLNAKLFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLV 98
Cdd:PRK14473    1 MEKLGINLGLLIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  99 KNAHEQTEERNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILedsiDEKLAKKKAEEVIEKH 178
Cdd:PRK14473   81 AQAQERARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVL----GAELQARGHDALIAES 156


                  ..
gi 1278529013 179 LS 180
Cdd:PRK14473  157 LA 158
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 32-169 3.84e-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: 3.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  32 QLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEERNEK 111
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1278529013 112 MIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKK 169
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKD 138
PRK13428 PRK13428
F0F1 ATP synthase subunit delta; Provisional
 29-160 2.36e-11

F0F1 ATP synthase subunit delta; Provisional


Pssm-ID: 184048 [Multi-domain]  Cd Length: 445  Bit Score: 61.29  E-value: 2.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  29 FAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEER 108
Cdd:PRK13428    4 FIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAERI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1278529013 109 NEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILED 160
Cdd:PRK13428   84 AEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGELVRN 135
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 29-177 5.44e-11

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 58.14  E-value: 5.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  29 FAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEER 108
Cdd:PRK13461    8 IIATIINFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEYKSKAENV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278529013 109 NEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKKAEEVIEK 177
Cdd:PRK13461   88 YEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIKDFISK 156
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 ...
 29-159 1.39e-10

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: 56.17  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  29 FAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEER 108
Cdd:pfam00430   2 LVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1278529013 109 NEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILE 159
Cdd:pfam00430  82 KEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 34-176 1.48e-08

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 51.73  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  34 IHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEERNEKMI 113
Cdd:PRK14472   26 VTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKLRAEIT 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278529013 114 QKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKKAEEVIE 176
Cdd:PRK14472  106 EKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQ 168
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 22-149 5.83e-08

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 49.30  E-value: 5.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  22 LGLNAKLFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNA 101
Cdd:PRK08476    3 LDVNPYLMLATFVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQKA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1278529013 102 HEQTEERNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALL 149
Cdd:PRK08476   83 IAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQELKEQLLSQMPEF 130
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 20-177 8.30e-08

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 49.52  E-value: 8.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  20 SALGLNAKLFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVK 99
Cdd:PRK13453   12 AAGGVEWGTVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILE 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278529013 100 NAHEQTEERNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKKAEEVIEK 177
Cdd:PRK13453   92 DAKVQARQQQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 28-170 1.31e-07

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 49.02  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  28 LFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEE 107
Cdd:PRK14471   10 LFFWQTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEK 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278529013 108 RNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKK 170
Cdd:PRK14471   90 MIADAKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRKELSNKEKQHK 152
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 23-165 2.54e-07

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 48.03  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  23 GLNAKLFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLahtKEMEERL----SSLETEREEIiKNAKQEALNLV 98
Cdd:PRK07352   16 GLNLNLLETNLINLAIVIGLLYYFGRGFLGKILEERREAILQAL---KEAEERLrqaaQALAEAQQKL-AQAQQEAERIR 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278529013  99 KNAHEQTEERNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEK 165
Cdd:PRK07352   92 ADAKARAEAIRAEIEKQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDED 158
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 34-158 1.50e-06

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 45.75  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  34 IHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLVKNAHEQTEERNEKMI 113
Cdd:CHL00118   30 LQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEILAKANELTKQYEQELSKARKEAQLEITQSQKEAKEIVENEL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1278529013 114 QKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKIL 158
Cdd:CHL00118  110 KQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLL 154
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 19-175 1.89e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 40.60  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  19 ISALGLNAKLFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNLV 98
Cdd:PRK06231   41 INELFPNFWVFIAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEII 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278529013  99 KNAHEQTEERNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKKAEEVI 175
Cdd:PRK06231  121 DQANYEALQLKSELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFI 197
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 36-101 7.04e-04

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 39.51  E-value: 7.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278529013   36 FLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSL-----ETEREEIIKNAKQEALNLVKNA 101
Cdd:TIGR01271  230 FLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVkaycwEEAMEKIIKNIRQDELKLTRKI 300
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 18-177 7.62e-04

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 38.47  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  18 GISALGLNAKLFAAQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLAHTKEMEERLSSLETEREEIIKNAKQEALNL 97
Cdd:PRK13460    8 GLSLLDVNPGLVVWTLVTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  98 VKNAHEQTEERNEKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKKAEEVIEK 177
Cdd:PRK13460   88 VAEAKSDALKLKNKLLEETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIETELAK 167
PRK01005 PRK01005
V-type ATP synthase subunit E; Provisional
 83-180 2.53e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179204 [Multi-domain]  Cd Length: 207  Bit Score: 37.07  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  83 REEIIKNAKQEALNLVKNAHEQTEErnekMIQKTKQDVEKIVLDGKKRlieekeimIQETRKEMALLAVQAAKKILED-- 160
Cdd:PRK01005   18 REETLKPAEEEAGAIVHNAKEQAKR----IIAEAQEEAEKIIRSAEET--------ADQKLKQGESALVQAGKRSLESlk 85

                          90       100
                  ....*....|....*....|.
gi 1278529013 161 -SIDEKLAKKKAEEVIEKHLS 180
Cdd:PRK01005   86 qAVENKIFRESLGEWLEHVLT 106
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 31-177 8.60e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 35.95  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  31 AQLIHFLIVAMIFWKWIYRPLVLMIEKRSEKIDKGLaHTKEMEERLSSLETER-EEIIKNAKQEALNLVKNAHEQTEERN 109
Cdd:PRK14474   10 AQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRW-QDAEQRQQEAGQEAERyRQKQQSLEQQRASFMAQAQEAADEQR 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278529013 110 EKMIQKTKQDVEKIVLDGKKRLIEEKEIMIQETRKEMALLAVQAAKKILEDSIDEKLAKKKAEEVIEK 177
Cdd:PRK14474   89 QHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAALADLANATLEQQIVGIFIAR 156
PRK12704 PRK12704
phosphodiesterase; Provisional
 73-179 9.91e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 35.91  E-value: 9.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278529013  73 EERLSSLETEREEIIKNAKQEALNLVKNAHEQTEERNEKMIQKTKQDV---EKIVLDGKKRLIEEKEIMIQET----RKE 145
Cdd:PRK12704   30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELrerRNELQKLEKRLLQKEENLDRKLelleKRE 109

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1278529013 146 MALLAVQAAKKILEDSIDEKlaKKKAEEVIEKHL 179
Cdd:PRK12704  110 EELEKKEKELEQKQQELEKK--EEELEELIEEQL 141
 
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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