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Conserved domains on  [gi|22416381|gb|AAM96207|]
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vacuolar ATPase 68 kDa subunit A, partial [Drosophila melanogaster]

Protein Classification

NtpA superfamily protein( domain architecture ID 1014353)

NtpA superfamily protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04192 super family cl35250
V-type ATP synthase subunit A; Provisional
 1-241 7.23e-112

V-type ATP synthase subunit A; Provisional


The actual alignment was detected with superfamily member PRK04192:

Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 332.90  E-value: 7.23e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381    1 VTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLRD 80
Cdd:PRK04192  15 VVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSIFDGIQRPLDE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381   81 IGVMTnSIYIPKGVNTTALSRSEMWEFNPLnVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYIAPAGNYNLED 160
Cdd:PRK04192  95 LAEKS-GDFLERGVYVPALDREKKWEFTPT-VKVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKEIVSEGDYTVDD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381  161 IV--LETEfDGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYS 238
Cdd:PRK04192 173 TIavLEDE-DGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWA 251


                 ...
gi 22416381  239 NSD 241
Cdd:PRK04192 252 DAD 254
 
Name Accession Description Interval E-value
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 1-241 7.23e-112

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 332.90  E-value: 7.23e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381    1 VTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLRD 80
Cdd:PRK04192  15 VVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSIFDGIQRPLDE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381   81 IGVMTnSIYIPKGVNTTALSRSEMWEFNPLnVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYIAPAGNYNLED 160
Cdd:PRK04192  95 LAEKS-GDFLERGVYVPALDREKKWEFTPT-VKVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKEIVSEGDYTVDD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381  161 IV--LETEfDGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYS 238
Cdd:PRK04192 173 TIavLEDE-DGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWA 251


                 ...
gi 22416381  239 NSD 241
Cdd:PRK04192 252 DAD 254
ATP-synt_ab_Xtn pfam16886
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ...
 71-192 2.66e-61

ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the alpha-beta catalytic subunit of VATA or V-type proton ATPase catalytic subunit at the N-terminal end. It is found from bacteria to humans, and was not modelled in family ATP-synt_ab, pfam00006.


Pssm-ID: 465299 [Multi-domain]  Cd Length: 120  Bit Score: 187.99  E-value: 2.66e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381    71 FDGIQRPLRDIGVMTNSiYIPKGVNTTALSRSEMWEFNPlNVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYI 150
Cdd:pfam16886   1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTP-TVKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTEI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 22416381   151 APAGNYNLEDIVLETEFDGEITKHTMLQVWPVRQPRPVTEKL 192
Cdd:pfam16886  79 APEGEYTVEDTIAEVEDEGKEKELTMMQKWPVRRPRPYKEKL 120
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 57-241 5.74e-55

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 177.77  E-value: 5.74e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381  57 PLSVELGPGIMGSIFDGIQRPLRDIgVMTNSIYIPKGVNTtalsrsemwefnplnvrvgshitggdlygvvhentlvkqr 136
Cdd:cd01134   1 PLSVELGPGLLGSIFDGIQRPLEVI-AETGSIFIPRGVNV---------------------------------------- 39

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381 137 mivaprakgtvryiapagnynledivletefdgeitkhtmlQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGT 216
Cdd:cd01134  40 -----------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78

                       170       180
                ....*....|....*....|....*
gi 22416381 217 TAIPGAFGCGKTVISQALSKYSNSD 241
Cdd:cd01134  79 AAIPGPFGCGKTVISQSLSKWSNSD 103
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 24-78 9.49e-03

V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273410 [Multi-domain]  Cd Length: 466  Bit Score: 36.62  E-value: 9.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 22416381    24 GEIIRLEGDMATIQVYEETSGVTVGDPVLR-TGKPLSVELGPGIMGSIFDGIQRPL 78
Cdd:TIGR01040  39 GQVLEVSGNKAVVQVFEGTSGIDAKKTTCEfTGDILRTPVSEDMLGRVFNGSGKPI 94
 
Name Accession Description Interval E-value
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 1-241 7.23e-112

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 332.90  E-value: 7.23e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381    1 VTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLRD 80
Cdd:PRK04192  15 VVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSIFDGIQRPLDE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381   81 IGVMTnSIYIPKGVNTTALSRSEMWEFNPLnVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYIAPAGNYNLED 160
Cdd:PRK04192  95 LAEKS-GDFLERGVYVPALDREKKWEFTPT-VKVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKEIVSEGDYTVDD 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381  161 IV--LETEfDGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYS 238
Cdd:PRK04192 173 TIavLEDE-DGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWA 251


                 ...
gi 22416381  239 NSD 241
Cdd:PRK04192 252 DAD 254
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 1-229 1.01e-70

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 233.38  E-value: 1.01e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381     1 VTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLRD 80
Cdd:PRK14698   15 VIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSIYDGIQRPLEV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381    81 IGVMTNSiYIPKGVNTTALSRSEMWEFNPlNVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYIAPAGNYNLED 160
Cdd:PRK14698   95 IREKSGD-FIARGISAPALPRDKKWHFIP-KVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVEIADEGEYTIEE 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381   161 IVLETEF-DGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTV 229
Cdd:PRK14698  173 VIAKVKTpSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCV 242
ATP-synt_ab_Xtn pfam16886
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ...
 71-192 2.66e-61

ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the alpha-beta catalytic subunit of VATA or V-type proton ATPase catalytic subunit at the N-terminal end. It is found from bacteria to humans, and was not modelled in family ATP-synt_ab, pfam00006.


Pssm-ID: 465299 [Multi-domain]  Cd Length: 120  Bit Score: 187.99  E-value: 2.66e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381    71 FDGIQRPLRDIGVMTNSiYIPKGVNTTALSRSEMWEFNPlNVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYI 150
Cdd:pfam16886   1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTP-TVKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTEI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 22416381   151 APAGNYNLEDIVLETEFDGEITKHTMLQVWPVRQPRPVTEKL 192
Cdd:pfam16886  79 APEGEYTVEDTIAEVEDEGKEKELTMMQKWPVRRPRPYKEKL 120
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 57-241 5.74e-55

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 177.77  E-value: 5.74e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381  57 PLSVELGPGIMGSIFDGIQRPLRDIgVMTNSIYIPKGVNTtalsrsemwefnplnvrvgshitggdlygvvhentlvkqr 136
Cdd:cd01134   1 PLSVELGPGLLGSIFDGIQRPLEVI-AETGSIFIPRGVNV---------------------------------------- 39

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381 137 mivaprakgtvryiapagnynledivletefdgeitkhtmlQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGT 216
Cdd:cd01134  40 -----------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78

                       170       180
                ....*....|....*....|....*
gi 22416381 217 TAIPGAFGCGKTVISQALSKYSNSD 241
Cdd:cd01134  79 AAIPGPFGCGKTVISQSLSKWSNSD 103
ATP-synt_V_A-type_alpha_N cd18119
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of ...
 1-56 2.19e-32

V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.


Pssm-ID: 349743 [Multi-domain]  Cd Length: 67  Bit Score: 112.62  E-value: 2.19e-32
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22416381   1 VTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGK 56
Cdd:cd18119  12 VVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 176-240 9.11e-13

RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410884 [Multi-domain]  Cd Length: 270  Bit Score: 65.94  E-value: 9.11e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22416381 176 MLQVWPVRQPRP-VTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNS 240
Cdd:cd19476  28 TKQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAK 93
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 201-241 7.34e-10

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 56.98  E-value: 7.34e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 22416381   201 GQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSD 241
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD 41
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 17-138 2.48e-09

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 56.58  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381   17 VGYYELV----------GEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPlRDIGVMTN 86
Cdd:PRK02118  23 VGYGELAtverkdgsslAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKP-IDGGPELE 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 22416381   87 SIYIPKGVNTtalsrsemweFNPLN-------VRVGshITGGDLYgvvheNTLVKQRMI 138
Cdd:PRK02118 102 GEPIEIGGPS----------VNPVKrivpremIRTG--IPMIDVF-----NTLVESQKI 143
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 1-55 7.96e-09

ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.


Pssm-ID: 427029 [Multi-domain]  Cd Length: 69  Bit Score: 51.01  E-value: 7.96e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22416381     1 VTAEAMSGSA--MYELVRVGYYE----LVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTG 55
Cdd:pfam02874   9 VDVEFGIGRLpgLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
PRK08149 PRK08149
FliI/YscN family ATPase;
139-241 3.20e-06

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 47.30  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22416381  139 VAPRAKGTVryIAPAGNynledIVLEteFDGEITKHTMLQVWPV-RQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTT 217
Cdd:PRK08149  84 VGEALLGAV--LDPTGK-----IVER--FDAPPTVGPISEERVIdVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154

                         90       100
                 ....*....|....*....|....
gi 22416381  218 AIPGAFGCGKTVISQALSKYSNSD 241
Cdd:PRK08149 155 GIFASAGCGKTSLMNMLIEHSEAD 178
ATP-synt_F1_V1_A1_AB_FliI_N cd01426
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
 1-56 1.89e-05

ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases 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. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.


Pssm-ID: 349738 [Multi-domain]  Cd Length: 73  Bit Score: 41.53  E-value: 1.89e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22416381   1 VTAEAMSGSAMYELVRVG------YYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGK 56
Cdd:cd01426  12 VEAELEGEVAIGEVCEIErgdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 6-78 2.98e-04

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 41.44  E-value: 2.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22416381    6 MSGSAMYELVRV--GYYELVGEiirLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPL 78
Cdd:PRK13343  44 LPDAALDELLRFegGSRGFAFN---LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPL 115
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 178-234 8.53e-04

F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.


Pssm-ID: 410877 [Multi-domain]  Cd Length: 277  Bit Score: 39.51  E-value: 8.53e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 22416381 178 QVWPV-RQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQAL 234
Cdd:cd01133  30 ERWPIhREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMEL 87
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 24-78 1.24e-03

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 39.37  E-value: 1.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22416381   24 GEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPL 78
Cdd:PRK09099  62 AEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPI 116
fliI PRK07721
flagellar protein export ATPase FliI;
39-78 4.61e-03

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 37.78  E-value: 4.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 22416381   39 YEETSGVTVGDPVLRTGKPLSVELGPGIMGSIFDGIQRPL 78
Cdd:PRK07721  72 YTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPL 111
ATP-synt_V_A-type_beta_N cd18118
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 ...
 17-56 6.61e-03

V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core, that is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex which forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.


Pssm-ID: 349742 [Multi-domain]  Cd Length: 72  Bit Score: 34.33  E-value: 6.61e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 22416381  17 VGYYELV-----------GEIIRLEGDMATIQVYEETSGVTVGDPVLR-TGK 56
Cdd:cd18118  21 VKYGEIVeitlpdgevrrGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRfTGE 72
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 24-78 9.49e-03

V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273410 [Multi-domain]  Cd Length: 466  Bit Score: 36.62  E-value: 9.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 22416381    24 GEIIRLEGDMATIQVYEETSGVTVGDPVLR-TGKPLSVELGPGIMGSIFDGIQRPL 78
Cdd:TIGR01040  39 GQVLEVSGNKAVVQVFEGTSGIDAKKTTCEfTGDILRTPVSEDMLGRVFNGSGKPI 94
 
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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