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Conserved domains on  [gi|11467683|ref|NP_050735|]
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ATP synthase CF0 B' subunit (chloroplast) [Guillardia theta]

Protein Classification

ATP synthase subunit b'( domain architecture ID 10000099)

chloroplastic ATP synthase subunit b' is a component of F(1)F(0) ATP synthase that produces ATP from ADP in the presence of a proton or sodium gradient

Gene Ontology:  GO:0015078|GO:0015986|GO:0045263|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 4-159 1.60e-60

ATP synthase CF0 B' subunit; Validated


:

Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 184.42  E-value: 1.60e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683    4 YLYILALQIAEAESEGGLFDFNATLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYE 83
Cdd:CHL00118   1 MIISILILILAEEGAGGLFDFNATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEILAKANELTKQYE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11467683   84 KDLAQERREAQLIISVAQKEAQDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSN 159
Cdd:CHL00118  81 QELSKARKEAQLEITQSQKEAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLLIK 156
 
Name Accession Description Interval E-value
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 4-159 1.60e-60

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 184.42  E-value: 1.60e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683    4 YLYILALQIAEAESEGGLFDFNATLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYE 83
Cdd:CHL00118   1 MIISILILILAEEGAGGLFDFNATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEILAKANELTKQYE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11467683   84 KDLAQERREAQLIISVAQKEAQDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSN 159
Cdd:CHL00118  81 QELSKARKEAQLEITQSQKEAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLLIK 156
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 27-157 9.20e-25

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: 92.50  E-value: 9.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683  27 TLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQD 106
Cdd:cd06503   1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 11467683 107 IVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLL 157
Cdd:cd06503  81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKIL 131
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 26-161 2.72e-16

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: 71.36  E-value: 2.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683  26 ATLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQ 105
Cdd:COG0711   1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 11467683 106 DIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:COG0711  81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKEL 136
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 ...
 27-157 9.69e-14

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: 64.26  E-value: 9.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683    27 TLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQD 106
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 11467683   107 IVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLL 157
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLL 131
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 32-161 2.73e-06

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: 44.70  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683    32 AVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVALE 111
Cdd:TIGR01144   2 LISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEEA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 11467683   112 IKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:TIGR01144  82 KAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNI 131
 
Name Accession Description Interval E-value
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 4-159 1.60e-60

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 184.42  E-value: 1.60e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683    4 YLYILALQIAEAESEGGLFDFNATLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYE 83
Cdd:CHL00118   1 MIISILILILAEEGAGGLFDFNATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEILAKANELTKQYE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11467683   84 KDLAQERREAQLIISVAQKEAQDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSN 159
Cdd:CHL00118  81 QELSKARKEAQLEITQSQKEAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLLIK 156
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 21-158 2.18e-40

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 132.82  E-value: 2.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   21 LFDFNATLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVA 100
Cdd:PRK07353   1 LFDFDATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 11467683  101 QKEAQDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLS 158
Cdd:PRK07353  81 EAEADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDALSRQILEKLLA 138
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 27-157 9.20e-25

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: 92.50  E-value: 9.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683  27 TLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQD 106
Cdd:cd06503   1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 11467683 107 IVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLL 157
Cdd:cd06503  81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKIL 131
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 26-161 2.72e-16

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: 71.36  E-value: 2.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683  26 ATLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQ 105
Cdd:COG0711   1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 11467683 106 DIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:COG0711  81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKEL 136
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 23-161 1.87e-15

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 69.03  E-value: 1.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   23 DFNATLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQK 102
Cdd:PRK05759   2 NLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKK 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 11467683  103 EAQDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:PRK05759  82 RAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGREL 140
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 ...
 27-157 9.69e-14

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: 64.26  E-value: 9.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683    27 TLPLMAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQD 106
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 11467683   107 IVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLL 157
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLL 131
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 33-161 3.35e-13

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 63.40  E-value: 3.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   33 VQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVALEI 112
Cdd:PRK14473  16 INFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQAQERARAQEAEII 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 11467683  113 KQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:PRK14473  96 AQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAEL 144
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 33-161 1.29e-09

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 54.26  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   33 VQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVALEI 112
Cdd:PRK13460  24 VTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDALKLKNKLL 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 11467683  113 KQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:PRK13460 104 EETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQL 152
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 33-161 2.06e-09

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 53.37  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   33 VQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVALEI 112
Cdd:PRK13453  26 LTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQQQEQII 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 11467683  113 KQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:PRK13453 106 HEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEI 154
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 18-161 5.87e-09

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 52.50  E-value: 5.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   18 EGGLFDFNATLPL-MAVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLI 96
Cdd:PRK14472  10 SGGLLSPNPGLIFwTAVTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKI 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11467683   97 ISVAQKEAQDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:PRK14472  90 IREGKEYAEKLRAEITEKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSL 154
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 36-161 2.67e-07

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 47.35  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   36 LLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVALEIKQA 115
Cdd:PRK13461  16 IILLLILKHFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEYKSKAENVYEEIVKEA 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 11467683  116 QKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:PRK13461  96 HEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESI 141
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 15-145 1.01e-06

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 46.10  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   15 AESEGGlFDFNATLpLMAVQILLFMVILNAVFYNP--VAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERRE 92
Cdd:PRK07352   9 TEAEGG-FGLNLNL-LETNLINLAIVIGLLYYFGRgfLGKILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQE 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 11467683   93 AQLIISVAQKEAQDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQV 145
Cdd:PRK07352  87 AERIRADAKARAEAIRAEIEKQAIEDMARLKQTAAADLSAEQERVIAQLRREA 139
PRK09174 PRK09174
F0F1 ATP synthase subunit B;
36-139 1.98e-06

F0F1 ATP synthase subunit B;


Pssm-ID: 169692 [Multi-domain]  Cd Length: 204  Bit Score: 45.56  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   36 LLFMVILNAVFYNPVAKV--------LDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDI 107
Cdd:PRK09174  56 LLWLAITFGLFYLFMSRVilpriggiIETRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSIAQAAREAAKAK 135

                         90       100       110
                 ....*....|....*....|....*....|..
gi 11467683  108 VALEIKQAQKDTELLVNEATSQLNSQKQKALS 139
Cdd:PRK09174 136 AEAERAAIEASLEKKLKEAEARIAAIKAKAMA 167
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 32-161 2.73e-06

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: 44.70  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683    32 AVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVALE 111
Cdd:TIGR01144   2 LISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEEA 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 11467683   112 IKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:TIGR01144  82 KAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNI 131
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 28-156 5.33e-06

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 43.52  E-value: 5.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   28 LPLMAVQILLFM---VILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEA 104
Cdd:PRK08476   7 PYLMLATFVVFLlliVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQKAIAKA 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 11467683  105 QDIVALEIKQAQKDTELLVNEATSQLNSQKQKALSALEDQVNTLTEQIKSKL 156
Cdd:PRK08476  87 KEEAEKKIEAKKAELESKYEAFAKQLANQKQELKEQLLSQMPEFKEALNAKL 138
PRK09173 PRK09173
F0F1 ATP synthase subunit B; Validated
 33-134 3.13e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 169691 [Multi-domain]  Cd Length: 159  Bit Score: 38.95  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   33 VQILLFMVILnAVFYNP--VAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVAl 110
Cdd:PRK09173   9 VGLVLFLALV-VYLKVPgmIARSLDARADRIKNELAEARRLREEAQQLLAEYQRKRKEAEKEAADIVAAAEREAEALTA- 86

                         90       100
                 ....*....|....*....|....
gi 11467683  111 eikQAQKDTELLVNEATSqLNSQK 134
Cdd:PRK09173  87 ---EAKRKTEEYVARRNK-LAEQK 106
PRK13455 PRK13455
F0F1 ATP synthase subunit B; Provisional
 17-161 8.70e-04

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184062 [Multi-domain]  Cd Length: 184  Bit Score: 37.86  E-value: 8.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   17 SEGGLFDFNATLPLMAVQILLFMVILNAvFYNP--VAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQ 94
Cdd:PRK13455  18 AGGPFFSLSNTDFVVTLAFLLFIGILVY-FKVPgmIGGMLDKRAEGIRSELEEARALREEAQTLLASYERKQREVQEQAD 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11467683   95 LIISVAQKEAQdivaLEIKQAQKDTELLVNE----ATSQLNSQKQKALSALEDQVNTLTEQIKSKLLSNQL 161
Cdd:PRK13455  97 RIVAAAKDEAQ----AAAEQAKADLEASIARrlaaAEDQIASAEAAAVKAVRDRAVSVAVAAAADVIAKQM 163
PRK13454 PRK13454
F0F1 ATP synthase subunit B'; Provisional
 34-129 9.04e-04

F0F1 ATP synthase subunit B'; Provisional


Pssm-ID: 184061 [Multi-domain]  Cd Length: 181  Bit Score: 37.88  E-value: 9.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   34 QILLFMVILNAVFY-------NPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQD 106
Cdd:PRK13454  33 QIFWLLVTLVAIYFvltrvalPRIGAVLAERQGTITNDLAAAEELKQKAVEAEKAYNKALADARAEAQRIVAETRAEIQA 112

                         90       100
                 ....*....|....*....|...
gi 11467683  107 IVALEIKQAqkDTELLVNEATSQ 129
Cdd:PRK13454 113 ELDVAIAKA--DAEIAAKAAESE 133
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 32-145 3.62e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 36.14  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   32 AVQILLFMVILNAVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVALE 111
Cdd:PRK08475  29 TINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIVETAKKEAYILTQKI 108

                         90       100       110
                 ....*....|....*....|....*....|....
gi 11467683  112 IKQAQKDTELLVNEATSQLNSQKQKALSALEDQV 145
Cdd:PRK08475 109 EKQTKDDIENLIKSFEELMEFEVRKMEREVVEEV 142
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 30-142 8.61e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 35.20  E-value: 8.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11467683   30 LMAVQILLFMVILnaVFYNPVAKVLDEREEYIRKNLTQASDILAKAEAITKQYEKDLAQERREAQLIISVAQKEAQDIVA 109
Cdd:PRK06231  55 LIAFSILLLLGIF--LFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLKS 132

                         90       100       110
                 ....*....|....*....|....*....|...
gi 11467683  110 LEIKQAQKDTELLVNEATSQLNSQKQKALSALE 142
Cdd:PRK06231 133 ELEKEANRQANLIIFQARQEIEKERRELKEQLQ 165
 
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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