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Conserved domains on  [gi|1437703007|emb|STX33273|]
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H+-transporting ATP synthase chain b [Legionella birminghamensis]

Protein Classification

F0F1 ATP synthase subunit B( domain architecture ID 11481619)

F0F1 ATP synthase subunit B is part of the membrane proton channel of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane

Gene Ontology:  GO:0015986|GO:0015078|GO:0045263
PubMed:  7961438|15473999|15078220

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 8.37e-52

F0F1 ATP synthase subunit B; Validated


:

Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 161.87  E-value: 8.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   1 MEINLTLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKAT 80
Cdd:PRK05759    1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437703007  81 RRASQLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK05759   81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 8.37e-52

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 161.87  E-value: 8.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   1 MEINLTLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKAT 80
Cdd:PRK05759    1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437703007  81 RRASQLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK05759   81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 10-156 8.17e-33

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: 113.27  E-value: 8.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007  10 QMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQLIEE 89
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437703007  90 AKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 6-156 2.43e-30

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: 107.18  E-value: 2.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   6 TLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQ 85
Cdd:COG0711     2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437703007  86 LIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:COG0711    82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 6-137 1.30e-27

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: 99.43  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   6 TLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQ 85
Cdd:cd06503     1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1437703007  86 LIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILK 137
Cdd:cd06503    81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
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 ...
 6-136 4.18e-20

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: 80.43  E-value: 4.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   6 TLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQ 85
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1437703007  86 LIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKIL 136
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLL 131
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 8.37e-52

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 161.87  E-value: 8.37e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   1 MEINLTLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKAT 80
Cdd:PRK05759    1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1437703007  81 RRASQLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK05759   81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 10-156 8.17e-33

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: 113.27  E-value: 8.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007  10 QMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQLIEE 89
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437703007  90 AKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 6-156 2.43e-30

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: 107.18  E-value: 2.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   6 TLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQ 85
Cdd:COG0711     2 TLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1437703007  86 LIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:COG0711    82 IAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 6-137 1.30e-27

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: 99.43  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   6 TLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQ 85
Cdd:cd06503     1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1437703007  86 LIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILK 137
Cdd:cd06503    81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
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 ...
 6-136 4.18e-20

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: 80.43  E-value: 4.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   6 TLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQ 85
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1437703007  86 LIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKIL 136
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLL 131
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 23-156 8.24e-16

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 70.22  E-value: 8.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007  23 KFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQLIEEAKEEAKLEAQKQV 102
Cdd:PRK14472   37 KIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKLRAEITEKAHTEAKKMI 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1437703007 103 KLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK14472  117 ASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDL 170
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 10-138 5.77e-14

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 65.20  E-value: 5.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007  10 QMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQLIEE 89
Cdd:PRK14471   14 QTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEKMIAD 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1437703007  90 AKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKK 138
Cdd:PRK14471   94 AKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRK 142
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 6-155 7.49e-12

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 59.92  E-value: 7.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   6 TLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQ 85
Cdd:PRK13453   20 TVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007  86 LIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEE 155
Cdd:PRK13453  100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 3-156 3.11e-09

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 52.62  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   3 INLTL-IVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATR 81
Cdd:PRK14473    6 INLGLlIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQAQE 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437703007  82 RASQLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK14473   86 RARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAAL 160
PRK13428 PRK13428
F0F1 ATP synthase subunit delta; Provisional
 6-156 1.06e-08

F0F1 ATP synthase subunit delta; Provisional


Pssm-ID: 184048 [Multi-domain]  Cd Length: 445  Bit Score: 52.81  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   6 TLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKAtRRASQ 85
Cdd:PRK13428    3 TFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEA-REDAE 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437703007  86 LIEEAKEEAKLEAQKQVKlAHEQLQQEINRAK--DDLRKQVAQLAVASAEKILKKTI-DIQANSALLDNLIEEI 156
Cdd:PRK13428   82 RIAEQLRAQADAEAERIK-VQGARQVQLLRAQltRQLRLELGHESVRQAGELVRNHVaDPAQQSATVDRFLDEL 154
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 1-156 1.55e-08

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 50.82  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   1 MEINLTLIVQMLV-FAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKA 79
Cdd:PRK13461    1 MEINIPTIIATIInFIILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437703007  80 TRRASQLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK13461   81 KSKAENVYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIKDFISKV 157
PRK09173 PRK09173
F0F1 ATP synthase subunit B; Validated
 29-156 2.55e-08

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 169691 [Multi-domain]  Cd Length: 159  Bit Score: 50.12  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007  29 LAKAMEERQEKIADGLAAAERGRKELE--LAQHRVKDelKQAKAHSAEIIEKATRRASQLIEEAKEEAKLEAQKQVKLAH 106
Cdd:PRK09173   27 IARSLDARADRIKNELAEARRLREEAQqlLAEYQRKR--KEAEKEAADIVAAAEREAEALTAEAKRKTEEYVARRNKLAE 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1437703007 107 EQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK09173  105 QKIAQAETDAINAVRSSAVDLAIAAAEKLLAEKVDAKAASELFKDALAQV 154
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 3-156 5.69e-08

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 49.57  E-value: 5.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   3 INLTLIVQMLVfaafvWFTMKFvwppLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRR 82
Cdd:PRK07352   27 INLAIVIGLLY-----YFGRGF----LGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKAR 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437703007  83 ASQLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK07352   98 AEAIRAEIEKQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDRSIANL 171
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 8-156 1.37e-07

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 48.69  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   8 IVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQLI 87
Cdd:PRK06231   52 IAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLK 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437703007  88 EEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK06231  132 SELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIREL 200
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 1-156 1.79e-06

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 45.40  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   1 MEINLTLIVQMLV-FAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKA 79
Cdd:PRK13460   12 LDVNPGLVVWTLVtFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEA 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1437703007  80 TRRASQLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK13460   92 KSDALKLKNKLLEETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIETELAKL 168
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 5-136 1.03e-04

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 40.96  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   5 LTLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRAS 84
Cdd:PRK14474    6 FTVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEQQRASFMAQAQEAAD 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1437703007  85 QLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKIL 136
Cdd:PRK14474   86 EQRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAAL 137
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 2-136 1.40e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 36.91  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   2 EINLTLIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATR 81
Cdd:PRK07353    3 DFDATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEAEA 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1437703007  82 RASQLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKIL 136
Cdd:PRK07353   83 EADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDALSRQILEKLL 137
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 7-123 1.42e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 36.98  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   7 LIVQMLVFAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQL 86
Cdd:PRK08476   10 MLATFVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQKAIAKAKEE 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1437703007  87 IEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQ 123
Cdd:PRK08476   90 AEKKIEAKKAELESKYEAFAKQLANQKQELKEQLLSQ 126
PRK13455 PRK13455
F0F1 ATP synthase subunit B; Provisional
 6-156 3.11e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184062 [Multi-domain]  Cd Length: 184  Bit Score: 36.32  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007   6 TLIVQMLVFAAFVWFTMKFVWPP-LAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRAS 84
Cdd:PRK13455   28 TDFVVTLAFLLFIGILVYFKVPGmIGGMLDKRAEGIRSELEEARALREEAQTLLASYERKQREVQEQADRIVAAAKDEAQ 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437703007  85 QLIEEAKEEAKLEAQKQVKLAHEQLQQEINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSALLDNLIEEI 156
Cdd:PRK13455  108 AAAEQAKADLEASIARRLAAAEDQIASAEAAAVKAVRDRAVSVAVAAAADVIAKQMTAADANALIDEAIKEV 179
PRK09174 PRK09174
F0F1 ATP synthase subunit B;
14-147 4.33e-03

F0F1 ATP synthase subunit B;


Pssm-ID: 169692 [Multi-domain]  Cd Length: 204  Bit Score: 35.93  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437703007  14 FAAFVWFTMKFVWPPLAKAMEERQEKIADGLAAAERGRKELELAQHRVKDELKQAKAHSAEIIEKATRRASQLIEEAKEE 93
Cdd:PRK09174   63 FGLFYLFMSRVILPRIGGIIETRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSIAQAAREAAKAKAEAERAA 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1437703007  94 AKLEAQKQVKLAHEQlqqeINRAKDDLRKQVAQLAVASAEKILKKTIDIQANSA 147
Cdd:PRK09174  143 IEASLEKKLKEAEAR----IAAIKAKAMADVGSIAEETAAAIVEQLIGGTADKA 192
 
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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