NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488619137|ref|WP_002555986|]
View 

MULTISPECIES: F0F1 ATP synthase subunit B [Pseudomonas]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 6.55e-62

F0F1 ATP synthase subunit B; Validated


:

Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 187.68  E-value: 6.55e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   1 MNINATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAK 80
Cdd:PRK05759   1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488619137  81 KRGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK05759  81 KRAAQIIEEAKAEAEAEAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 6.55e-62

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 187.68  E-value: 6.55e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   1 MNINATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAK 80
Cdd:PRK05759   1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488619137  81 KRGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 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 3.82e-41

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: 134.45  E-value: 3.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   10 QSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDE 89
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488619137   90 ARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 5-156 7.43e-36

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: 121.43  E-value: 7.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   5 ATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGT 84
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488619137  85 QIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:COG0711   81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 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 1.37e-33

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: 114.84  E-value: 1.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488619137  86 IVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILG 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 ...
 6-137 4.69e-23

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: 88.14  E-value: 4.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137    6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488619137   86 IVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILG 137
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 1-156 6.55e-62

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 187.68  E-value: 6.55e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   1 MNINATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAK 80
Cdd:PRK05759   1 MNLNGTLIGQLIAFLILVWFIMKFVWPPIMKALEERQKKIADGLAAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488619137  81 KRGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 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 3.82e-41

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: 134.45  E-value: 3.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   10 QSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDE 89
Cdd:TIGR01144   1 QLISFILLVWFCMKYVWPPLAKAIETRQKKIADGLASAERAKKEAALAQKKAQVILKEAKDEAQEIIENANKRGSEILEE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488619137   90 ARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:TIGR01144  81 AKAEAREEREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 5-156 7.43e-36

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: 121.43  E-value: 7.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   5 ATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGT 84
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488619137  85 QIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:COG0711   81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 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 1.37e-33

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: 114.84  E-value: 1.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488619137  86 IVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILG 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 ...
 6-137 4.69e-23

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: 88.14  E-value: 4.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137    6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:pfam00430   1 TLVTQLIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488619137   86 IVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILG 137
Cdd:pfam00430  81 LKEEIVAAAEAEAERIIEQAAAEIEQEKDRALAELRQQVVALAVQIAEKLLE 132
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 11-156 2.17e-22

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 87.56  E-value: 2.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  11 SVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEA 90
Cdd:PRK14472  25 AVTFVIVLLILKKIAWGPILSALEEREKGIQSSIDRAHSAKDEAEAILRKNRELLAKADAEADKIIREGKEYAEKLRAEI 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488619137  91 RETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK14472 105 TEKAHTEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDL 170
PRK14471 PRK14471
F0F1 ATP synthase subunit B; Provisional
 10-156 1.73e-18

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184695 [Multi-domain]  Cd Length: 164  Bit Score: 77.14  E-value: 1.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  10 QSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDE 89
Cdd:PRK14471  14 QTILFLILLLLLAKFAWKPILGAVKEREDSIKNALASAEEARKEMQNLQADNERLLKEARAERDAILKEAREIKEKMIAD 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488619137  90 ARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATI-DQNAHAELVNKLAAEI 156
Cdd:PRK14471  94 AKEEAQVEGDKMIEQAKASIESEKNAAMAEIKNQVANLSVEIAEKVLRKELsNKEKQHKLVEKMLGDV 161
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 1-156 7.78e-17

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 73.03  E-value: 7.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   1 MNINATLIGQSVAFFIFVIFCMK-FVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQA 79
Cdd:PRK14473   4 LGINLGLLIAQLINFLLLIFLLRtFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQA 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488619137  80 KKRGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK14473  84 QERARAQEAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAAL 160
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 1-150 3.81e-16

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 70.85  E-value: 3.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   1 MNINATLIGQSVAFFIFVIFCMK-FVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQA 79
Cdd:PRK13461   1 MEINIPTIIATIINFIILLLILKhFFFDKIKAVIDSRQSEIDNKIEKADEDQKKARELKLKNERELKNAKEEGKKIVEEY 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488619137  80 KKRGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVN 150
Cdd:PRK13461  81 KSKAENVYEEIVKEAHEEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIK 151
PRK13428 PRK13428
F0F1 ATP synthase subunit delta; Provisional
 6-135 1.39e-15

F0F1 ATP synthase subunit delta; Provisional


Pssm-ID: 184048 [Multi-domain]  Cd Length: 445  Bit Score: 72.46  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:PRK13428   3 TFIGQLIGFAVIVFLVWRFVVPPVRRLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAER 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488619137  86 IVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKI 135
Cdd:PRK13428  83 IAEQLRAQADAEAERIKVQGARQVQLLRAQLTRQLRLELGHESVRQAGEL 132
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 8-156 2.25e-12

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 61.78  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   8 IGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIV 87
Cdd:PRK06231  52 IAHLIAFSILLLLGIFLFWKPTQRFLNKRKELIEAEINQANELKQQAQQLLENAKQRHENALAQAKEIIDQANYEALQLK 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488619137  88 DEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK06231 132 SELEKEANRQANLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIREL 200
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 6-155 6.84e-10

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 54.53  E-value: 6.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:PRK13453  20 TVIVTVLTFIVLLALLKKFAWGPLKDVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKLKETQEEVQKILEDAKVQARQ 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  86 IVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAE 155
Cdd:PRK13453 100 QQEQIIHEANVRANGMIETAQSEINSQKERAIADINNQVSELSVLIASKVLRKEISEQDQKALVDKYLKE 169
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
 7-151 3.89e-09

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 52.65  E-value: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   7 LIGQSVAFFIFVIFCMKFVWppviAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQI 86
Cdd:PRK07352  26 LINLAIVIGLLYYFGRGFLG----KILEERREAILQALKEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAI 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488619137  87 VDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNK 151
Cdd:PRK07352 102 RAEIEKQAIEDMARLKQTAAADLSAEQERVIAQLRREAAELAIAKAESQLPGRLDEDAQQRLIDR 166
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 3-138 6.30e-09

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 51.54  E-value: 6.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   3 INATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGL-DAASRAARDLELAQEKAgQQLREAKAQAAEIIEQAKK 81
Cdd:PRK07353   4 FDATLPLMAVQFVLLTFILNALFYKPVGKVVEEREDYIRTNRaEAKERLAEAEKLEAQYE-QQLASARKQAQAVIAEAEA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488619137  82 RGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGA 138
Cdd:PRK07353  83 EADKLAAEALAEAQAEAQASKEKARREIEQQKQAALAQLEQQVDALSRQILEKLLAA 139
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 6-156 1.68e-07

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 49.04  E-value: 1.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   6 TLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ 85
Cdd:PRK14474   7 TVVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQSLEQQRASFMAQAQEAADE 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488619137  86 IVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK14474  87 QRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQMVKIIRAALADLANATLEQQIVGIFIARL 157
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 12-151 3.58e-07

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 47.33  E-value: 3.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  12 VAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEAR 91
Cdd:PRK13460  24 VTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAIVAEAKSDALKLKNKLL 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  92 ETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNK 151
Cdd:PRK13460 104 EETNNEVKAQKDQAVKEIELAKGKALSQLQNQIVEMTITIASKVLEKQLKKEDYKAFIET 163
PRK09173 PRK09173
F0F1 ATP synthase subunit B; Validated
 12-156 5.91e-07

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 169691 [Multi-domain]  Cd Length: 159  Bit Score: 46.27  E-value: 5.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  12 VAFFIFVIFCMKFVWPPVIA-ALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEA 90
Cdd:PRK09173   9 VGLVLFLALVVYLKVPGMIArSLDARADRIKNELAEARRLREEAQQLLAEYQRKRKEAEKEAADIVAAAEREAEALTAEA 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488619137  91 RETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK09173  89 KRKTEEYVARRNKLAEQKIAQAETDAINAVRSSAVDLAIAAAEKLLAEKVDAKAASELFKDALAQV 154
atpG CHL00118
ATP synthase CF0 B' subunit; Validated
 3-137 3.46e-06

ATP synthase CF0 B' subunit; Validated


Pssm-ID: 214369 [Multi-domain]  Cd Length: 156  Bit Score: 44.21  E-value: 3.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   3 INATLIGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAardLELAQEKAGQ---QLREAKAQAAEIIEQA 79
Cdd:CHL00118  21 FNATLPLMALQFLLLMVLLNIILYKPLLKVLDERKEYIRKNLTKASEI---LAKANELTKQyeqELSKARKEAQLEITQS 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488619137  80 KKRGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAEKILG 137
Cdd:CHL00118  98 QKEAKEIVENELKQAQKYIDSLLNEATKQLEAQKEKALKSLEEQVDTLSDQIEEKLLI 155
PRK09174 PRK09174
F0F1 ATP synthase subunit B;
12-155 5.11e-06

F0F1 ATP synthase subunit B;


Pssm-ID: 169692 [Multi-domain]  Cd Length: 204  Bit Score: 44.40  E-value: 5.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  12 VAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEAR 91
Cdd:PRK09174  61 ITFGLFYLFMSRVILPRIGGIIETRRDRIAQDLDQAARLKQEADAAVAAYEQELAQARAKAHSIAQAAREAAKAKAEAER 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488619137  92 ETARVEADRVKAQAQAEIEqelnGVKDALRAQLGSLAVNGA----EKILGATIDQNAHAELVNKLAAE 155
Cdd:PRK09174 141 AAIEASLEKKLKEAEARIA----AIKAKAMADVGSIAEETAaaivEQLIGGTADKASVAAAVKAARAS 204
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 8-111 1.26e-05

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 42.69  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   8 IGQSVAFFIFVIFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIV 87
Cdd:PRK08475  26 IERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDALKKLEEAKEKAELIVETAKKEAYILT 105

                         90       100
                 ....*....|....*....|....
gi 488619137  88 DEaretarveadrVKAQAQAEIEQ 111
Cdd:PRK08475 106 QK-----------IEKQTKDDIEN 118
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
 54-155 2.69e-05

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


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 42.24  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  54 LELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQLGSLAVNGAE 133
Cdd:COG1390   12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEEAL 91

                         90       100
                 ....*....|....*....|..
gi 488619137 134 KILGATIDQNAHAELVNKLAAE 155
Cdd:COG1390   92 EKLKNLPKDPEYKELLKKLLKE 113
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 3-123 1.15e-04

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 40.06  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137   3 INATLIGQSVAFFIFVIFCM-KFVWPPVIAALHERQKKIADGLDAASraardlelaqeKAGQQLREAKAQAAEIIEQAKK 81
Cdd:PRK08476   5 VNPYLMLATFVVFLLLIVILnSWLYKPLLKFMDNRNASIKNDLEKVK-----------TNSSDVSEIEHEIETILKNARE 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488619137  82 RGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKDALRAQ 123
Cdd:PRK08476  74 EANKIRQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQ 115
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
 33-104 2.82e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 38.68  E-value: 2.82e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488619137  33 LHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARETAR---VEADRVKAQ 104
Cdd:COG3599   50 LEELEEELEEYRELEETLQKTLVVAQETAEEVKENAEKEAELIIKEAELEAEKIIEEAQEKARkivREIEELKRQ 124
PRK01005 PRK01005
V-type ATP synthase subunit E; Provisional
 35-156 5.32e-04

V-type ATP synthase subunit E; Provisional


Pssm-ID: 179204 [Multi-domain]  Cd Length: 207  Bit Score: 38.61  E-value: 5.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  35 ERQKKIADGLDAASraardLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAQAEIEQELN 114
Cdd:PRK01005   8 DKLKQICDALREET-----LKPAEEEAGAIVHNAKEQAKRIIAEAQEEAEKIIRSAEETADQKLKQGESALVQAGKRSLE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488619137 115 GVKDALRAQLGSLAVngAEKILGATIDQNAHAELVNKLAAEI 156
Cdd:PRK01005  83 SLKQAVENKIFRESL--GEWLEHVLTDPEVSAKLIQALVQAI 122
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 66-112 6.66e-04

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 38.05  E-value: 6.66e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488619137  66 REAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAQAEIEQE 112
Cdd:PRK02292  12 DEARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQL 58
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 46-144 1.04e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 37.67  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  46 AASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARE----TARVEADRVKAQAQAEIeqeLNGVKDALR 121
Cdd:PRK02292  14 ARARASEIRAEADEEAEEIIAEAEADAEEILEDREAEAEREIEQLREqelsSAKLEAKRERLNARKEV---LEDVRNQVE 90

                         90       100
                 ....*....|....*....|...
gi 488619137 122 AQLGSLAVNGAEKILGATIDQNA 144
Cdd:PRK02292  91 DEIASLDGDKREELTKSLLDAAD 113
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 29-114 1.63e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.88  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  29 VIAALHERQKKIADGLDAASRAARDLE-----LAQEKAGQQLREAKA------QAAEIIEQAKKRGTQIVDEARETARVE 97
Cdd:PRK00409 521 LIASLEELERELEQKAEEAEALLKEAEklkeeLEEKKEKLQEEEDKLleeaekEAQQAIKEAKKEADEIIKELRQLQKGG 600

                         90
                 ....*....|....*..
gi 488619137  98 ADRVKAQAQAEIEQELN 114
Cdd:PRK00409 601 YASVKAHELIEARKRLN 617
fliH PRK06032
flagellar assembly protein H; Validated
 66-149 3.72e-03

flagellar assembly protein H; Validated


Pssm-ID: 235679 [Multi-domain]  Cd Length: 199  Bit Score: 36.12  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  66 REAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAQAEIEQ-------ELNGVKDALRAQLGSLAVNGAEKILGA 138
Cdd:PRK06032  24 RAAAEFAQAVAEAEAAAYAQGFAAGQREAAAQSERRLADALERIAQaaagllaALAAVEHEMETEAADLALAVARKIAGA 103

                         90
                 ....*....|.
gi 488619137 139 TIDQNAHAELV 149
Cdd:PRK06032 104 ALAAEPLAEIT 114
V_ATP_synt_G TIGR01147
vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in ...
 57-108 4.08e-03

vacuolar ATP synthase, subunit G; This model describes the vacuolar ATP synthase G subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. V-ATPases are multi-subunit enzymes composed of two functional domains: A transmembrane Vo domain and a peripheral catalytic domain V1. The G subunit is one of the subunits of the catalytic domain. V-ATPases are responsible for the acidification of endosomes and lysosomes, which are part of the central vacuolar system. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130217 [Multi-domain]  Cd Length: 113  Bit Score: 35.19  E-value: 4.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488619137   57 AQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAQAE 108
Cdd:TIGR01147   3 SQTQGIQQLLQAEKRAAEKVSEARKRKTKRLKQAKEEAQKEVEKYKQQREKE 54
PRK12704 PRK12704
phosphodiesterase; Provisional
 56-118 8.79e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 35.52  E-value: 8.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488619137  56 LAQEKAGQQLREAKAQAAEIIEQAKKRGTQIVDEARETARVEADRVKAQAQAEIEQELNGVKD 118
Cdd:PRK12704  24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK 86
NtpH COG2811
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ...
 45-110 8.87e-03

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


Pssm-ID: 442060 [Multi-domain]  Cd Length: 108  Bit Score: 34.12  E-value: 8.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488619137  45 DAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGTQ----IVDEARETARVEADRVKAQAQAEIE 110
Cdd:COG2811   12 EAEEEADEIIEEAKEEREERIAEAREEAEEIIEQAEEEAEEeaqeRLEEAREEAEAEAEEIIEEGEKEAE 81
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH