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Conserved domains on  [gi|158262971|gb|ABW24262|]
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F-ATPase beta-subunit, partial [Streptococcus pneumoniae]

Protein Classification

F0F1 ATP synthase subunit beta( domain architecture ID 1903243)

F0F1 ATP synthase subunit beta is part of the catalytic core of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane and is found in bacterial, mitochondrial, and chloroplast membranes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AtpD super family cl43008
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-251 0e+00

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


The actual alignment was detected with superfamily member COG0055:

Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 543.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   1 ALVVYKNDERKtkIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFtED 80
Cdd:COG0055   31 ALEVENEGGGE--LVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPI-EA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  81 AERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERT 160
Cdd:COG0055  108 KERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 161 REGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 240
Cdd:COG0055  188 REGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 267

                        250
                 ....*....|.
gi 158262971 241 SAVGYQPTLAT 251
Cdd:COG0055  268 SAVGYQPTLAT 278
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-251 0e+00

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 543.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   1 ALVVYKNDERKtkIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFtED 80
Cdd:COG0055   31 ALEVENEGGGE--LVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPI-EA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  81 AERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERT 160
Cdd:COG0055  108 KERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 161 REGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 240
Cdd:COG0055  188 REGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 267

                        250
                 ....*....|.
gi 158262971 241 SAVGYQPTLAT 251
Cdd:COG0055  268 SAVGYQPTLAT 278
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 13-251 9.46e-168

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 471.13  E-value: 9.46e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   13 KIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPT 92
Cdd:TIGR01039  38 ELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAK-ERWPIHRKAPS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   93 FDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKE 172
Cdd:TIGR01039 117 FEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKE 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262971  173 SGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 275
atpB CHL00060
ATP synthase CF1 beta subunit
 1-251 2.65e-158

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 448.34  E-value: 2.65e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   1 ALVVYKNDE--RKTKIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFt 78
Cdd:CHL00060  42 ALVVKGRDTagQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPV- 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  79 EDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGE 158
Cdd:CHL00060 121 DTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 159 RTREGNDLYWEMKESGVIE-------KTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSE 231
Cdd:CHL00060 201 RTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSE 280

                        250       260
                 ....*....|....*....|
gi 158262971 232 VSALLGRMPSAVGYQPTLAT 251
Cdd:CHL00060 281 VSALLGRMPSAVGYQPTLST 300
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 52-251 1.05e-148

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: 415.85  E-value: 1.05e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  52 SVPVGKETLGRVFNVLGDTIDlEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 131
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPID-ERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 132 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKESGVI-----EKTAMVFGQMNEPPGARMRVALTGLTIAEY 206
Cdd:cd01133   80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEY 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 158262971 207 FRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:cd01133  160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLAT 204
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 106-251 1.23e-66

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: 205.28  E-value: 1.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  106 GIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQehgGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQ 185
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262971  186 MNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFS 142
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 118-239 7.07e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 44.67  E-value: 7.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   118 KGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGvgertregndlywEMKESGVIEKTAMVFGQMNEPPGARMRVA 197
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 158262971   198 LTGLTIAEYFRdvegqDVLLFIDNIFRFTQAGSEVSALLGRM 239
Cdd:smart00382  68 RLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
 
Name Accession Description Interval E-value
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-251 0e+00

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 543.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   1 ALVVYKNDERKtkIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFtED 80
Cdd:COG0055   31 ALEVENEGGGE--LVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPI-EA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  81 AERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERT 160
Cdd:COG0055  108 KERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 161 REGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 240
Cdd:COG0055  188 REGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 267

                        250
                 ....*....|.
gi 158262971 241 SAVGYQPTLAT 251
Cdd:COG0055  268 SAVGYQPTLAT 278
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 13-251 9.46e-168

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 471.13  E-value: 9.46e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   13 KIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPT 92
Cdd:TIGR01039  38 ELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAK-ERWPIHRKAPS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   93 FDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKE 172
Cdd:TIGR01039 117 FEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKE 196

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262971  173 SGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 275
atpB CHL00060
ATP synthase CF1 beta subunit
 1-251 2.65e-158

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 448.34  E-value: 2.65e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   1 ALVVYKNDE--RKTKIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFt 78
Cdd:CHL00060  42 ALVVKGRDTagQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPV- 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  79 EDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGE 158
Cdd:CHL00060 121 DTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 159 RTREGNDLYWEMKESGVIE-------KTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSE 231
Cdd:CHL00060 201 RTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSE 280

                        250       260
                 ....*....|....*....|
gi 158262971 232 VSALLGRMPSAVGYQPTLAT 251
Cdd:CHL00060 281 VSALLGRMPSAVGYQPTLST 300
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
 52-251 1.05e-148

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: 415.85  E-value: 1.05e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  52 SVPVGKETLGRVFNVLGDTIDlEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 131
Cdd:cd01133    1 SVPVGEETLGRIFNVLGEPID-ERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 132 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKESGVI-----EKTAMVFGQMNEPPGARMRVALTGLTIAEY 206
Cdd:cd01133   80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEY 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 158262971 207 FRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:cd01133  160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLAT 204
alt_F1F0_F1_bet TIGR03305
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ...
 10-251 1.34e-120

alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.


Pssm-ID: 132348 [Multi-domain]  Cd Length: 449  Bit Score: 351.05  E-value: 1.34e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   10 RKTKIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTeDAERQPIHKK 89
Cdd:TIGR03305  30 REGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGNTIDRREPPK-DVEWRSVHQA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   90 APTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWE 169
Cdd:TIGR03305 109 PPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYRE 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  170 MKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTL 249
Cdd:TIGR03305 189 MKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTL 268


                  ..
gi 158262971  250 AT 251
Cdd:TIGR03305 269 GT 270
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 52-251 1.47e-89

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: 265.86  E-value: 1.47e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  52 SVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 131
Cdd:cd19476    1 SVPVGPELLGRILDGLGEPLDGLPPIKTK-QRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 132 KTVLIQELIHNIAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvE 211
Cdd:cd19476   80 KTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-N 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 158262971 212 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:cd19476  159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFT 198
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 106-251 1.23e-66

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: 205.28  E-value: 1.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  106 GIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQehgGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQ 185
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262971  186 MNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:pfam00006  78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFS 142
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 28-248 5.33e-40

Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440771 [Multi-domain]  Cd Length: 433  Bit Score: 142.86  E-value: 5.33e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  28 RTIAM--ESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFtEDAERQPIHKKAPTFDELSTSSEILET 105
Cdd:COG1157   65 RVLLMplGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPL-PGEERRPLDAPPPNPLERARITEPLDT 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 106 GIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTRE-----GNDLYWE-MKESGVIEKT 179
Cdd:COG1157  144 GVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEAD---VNVIALIGERGREvrefiEDDLGEEgLARSVVVVAT 220

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262971 180 AmvfgqmNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 248
Cdd:COG1157  221 S------DEPPLMRLRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPS 282
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 52-248 4.88e-38

Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.


Pssm-ID: 410880 [Multi-domain]  Cd Length: 265  Bit Score: 133.84  E-value: 4.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  52 SVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 131
Cdd:cd01136    1 SIPVGDGLLGRVIDALGEPLDGKGLPDEP-ERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 132 KTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvE 211
Cdd:cd01136   80 KSTLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-Q 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 158262971 212 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 248
Cdd:cd01136  156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPS 192
PRK08149 PRK08149
FliI/YscN family ATPase;
34-245 8.57e-33

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 123.57  E-value: 8.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  34 STDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLG---DTIDLEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVI 110
Cdd:PRK08149  63 NAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGkivERFDAPPTVGPISEERVIDVAPPSYAERRPIREPLITGVRAI 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 111 DLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPP 190
Cdd:PRK08149 143 DGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEAD---VFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSS 219

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 158262971 191 GARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY 245
Cdd:PRK08149 220 VDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGY 273
fliI PRK08927
flagellar protein export ATPase FliI;
28-248 2.14e-30

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 117.00  E-value: 2.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  28 RTIAM--ESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDAERQPIHKKAPTFDELSTSSEILET 105
Cdd:PRK08927  65 RALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 106 GIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTRE-----GNDLYWE-MKESGVIEKT 179
Cdd:PRK08927 145 GVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEgLARSVVVVAT 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262971 180 AmvfgqmNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 248
Cdd:PRK08927 222 S------DEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPT 283
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
33-249 2.98e-30

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 116.84  E-value: 2.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  33 ESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPftEDAERQPIHKKAPTFDELSTSSEILETGIKVIDL 112
Cdd:PRK06820  79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP--LTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDG 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 113 LAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGA 192
Cdd:PRK06820 157 ILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAAD---VMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALE 233

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 158262971 193 RMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTL 249
Cdd:PRK06820 234 RLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSV 289
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 18-240 1.11e-29

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 115.78  E-value: 1.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  18 VALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPfTEDAERQPIHKKAPTFDELS 97
Cdd:PRK13343  62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGP-LQATARRPLERPAPAIIERD 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  98 TSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhnIAQEHGG-ISVFAGVGERTREGNDLYWEMKESGVI 176
Cdd:PRK13343 141 FVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGAL 218

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262971 177 EKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 240
Cdd:PRK13343 219 EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPP 281
fliI PRK06002
flagellar protein export ATPase FliI;
61-251 2.23e-28

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 111.63  E-value: 2.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  61 GRVFNVLGDTIDLEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELi 140
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 141 hniAQEHGGISV-FAGVGERTREGNdlywEMKE---SGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVL 216
Cdd:PRK06002 186 ---ARADAFDTVvIALVGERGREVR----EFLEdtlADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD-RGENVL 257

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 158262971 217 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:PRK06002 258 LIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFS 292
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
37-249 6.67e-28

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 110.23  E-value: 6.67e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  37 GLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDlEAPFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPY 116
Cdd:PRK06936  81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFD-GGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 117 LKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGND-LYWEMKESGvIEKTAMVFGQMNEPPGARMR 195
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRSAEVD---VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAK 235

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158262971 196 VALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTL 249
Cdd:PRK06936 236 AGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSV 288
fliI PRK07721
flagellar protein export ATPase FliI;
47-248 2.04e-27

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 109.04  E-value: 2.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  47 TGRPISVPVGKETLGRVFNVLGDTIDLE------APFTEDA------ERQPIhkkaptfdelstsSEILETGIKVIDLLA 114
Cdd:PRK07721  87 TGKPLEVKVGSGLIGQVLDALGEPLDGSalpkglAPVSTDQdppnplKRPPI-------------REPMEVGVRAIDSLL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 115 PYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGND-LYWEMKESGvIEKTAMVFGQMNEPPGAR 193
Cdd:PRK07721 154 TVGKGQRVGIFAGSGVGKSTLMGMIARNTSAD---LNVIALIGERGREVREfIERDLGPEG-LKRSIVVVATSDQPALMR 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 158262971 194 MRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 248
Cdd:PRK07721 230 IKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPS 283
fliI PRK08472
flagellar protein export ATPase FliI;
13-251 8.38e-27

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 107.08  E-value: 8.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  13 KIVLEVALELGDGMVRTIAMES--------TDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFtEDAERQ 84
Cdd:PRK08472  44 KIESSDNGKECLGMVVVIEKEQfgispfsfIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAI-DYERYA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  85 PIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHN-IAQehggISVFAGVGERTRE- 162
Cdd:PRK08472 123 PIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGcLAP----IKVVALIGERGREi 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 163 --------GNDLywemkesgviEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSA 234
Cdd:PRK08472 199 pefieknlGGDL----------ENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGL 267

                        250
                 ....*....|....*..
gi 158262971 235 LLGRMPSAVGYQPTLAT 251
Cdd:PRK08472 268 ALGEPPTSKGYPPSVLS 284
fliI PRK06793
flagellar protein export ATPase FliI;
13-240 1.71e-26

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 106.22  E-value: 1.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  13 KIVLEV-ALELGDGMVrtIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEApftEDAERQPIHKKAP 91
Cdd:PRK06793  52 NVLCEViAIEKENNML--LPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEA---ENIPLQKIKLDAP 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  92 TFDELSTS--SEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGND-LYW 168
Cdd:PRK06793 127 PIHAFEREeiTDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD---INVISLVGERGREVKDfIRK 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262971 169 EMKESGvIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 240
Cdd:PRK06793 204 ELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELP 273
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 25-249 2.41e-26

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 106.01  E-value: 2.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  25 GMVRTIAMES----TDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFDELSTSS 100
Cdd:PRK09099  66 GFSRDVALLSpfgeLGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCD-ELVPVIAAPPDPMSRRMVE 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 101 EILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTA 180
Cdd:PRK09099 145 APLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSV 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262971 181 MVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTL 249
Cdd:PRK09099 222 VVCATSDRSSIERAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSV 289
fliI PRK08972
flagellar protein export ATPase FliI;
33-248 5.69e-25

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 102.09  E-value: 5.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  33 ESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDaerQPIHKKAPTFDELSTS--SEILETGIKVI 110
Cdd:PRK08972  77 EELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTD---QRASRHSPPINPLSRRpiTEPLDVGVRAI 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 111 DLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWE-MKESGViEKTAMVFGQMNEP 189
Cdd:PRK08972 154 NAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEiLGEEGR-ARSVVVAAPADTS 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 158262971 190 PGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 248
Cdd:PRK08972 230 PLMRLKGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPS 287
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 50-251 6.57e-24

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: 96.87  E-value: 6.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  50 PISVPVGKETLGRVF----NVLGDTIDLEAPFTE---DAERQPIHKKAPTFDELsTSSEILETGIKVIDLLAPYLKGGKV 122
Cdd:cd01134    1 PLSVELGPGLLGSIFdgiqRPLEVIAETGSIFIPrgvNVQRWPVRQPRPVKEKL-PPNVPLLTGQRVLDTLFPVAKGGTA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 123 GLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERtreGND----------LYWEMKESGVIEKTAMVFGQMNEPPGA 192
Cdd:cd01134   80 AIPGPFGCGKTVISQSLSKWSNSD---VVIYVGCGER---GNEmaevleefpeLKDPITGESLMERTVLIANTSNMPVAA 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 158262971 193 RMRVALTGLTIAEYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:cd01134  154 REASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGA 211
PRK05922 PRK05922
type III secretion system ATPase; Validated
 38-245 8.97e-24

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 98.82  E-value: 8.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  38 LTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEdAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYL 117
Cdd:PRK05922  77 VALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPK-THLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLG 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 118 KGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDlYWEMKESGVIE-KTAMVFGQMNEPPGARMRV 196
Cdd:PRK05922 156 KGQRIGVFSEPGSGKSSLLSTIAKGSKST---INVIALIGERGREVRE-YIEQHKEGLAAqRTIIIASPAHETAPTKVIA 231

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 158262971 197 ALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY 245
Cdd:PRK05922 232 GRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHY 279
fliI PRK05688
flagellar protein export ATPase FliI;
34-249 2.04e-22

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 95.18  E-value: 2.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  34 STDGLTRGMEVL---DTGRpisVPVGKETLGRVFNVLGDTIDLEAPFTEDAErqpIHKKAPTFDELSTS--SEILETGIK 108
Cdd:PRK05688  84 SVAGIAPGARVVplaDTGR---LPMGMSMLGRVLDGAGRALDGKGPMKAEDW---VPMDGPTINPLNRHpiSEPLDVGIR 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 109 VIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNE 188
Cdd:PRK05688 158 SINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADD 234

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262971 189 PPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTL 249
Cdd:PRK05688 235 APLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSV 294
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 51-240 5.02e-22

F1 ATP synthase alpha 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 alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-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: 410876 [Multi-domain]  Cd Length: 274  Bit Score: 91.85  E-value: 5.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  51 ISVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGV 130
Cdd:cd01132    2 VEVPVGEALLGRVVDALGNPIDGKGPIQTK-ERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 131 GKTVLIQELIHNiAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDv 210
Cdd:cd01132   81 GKTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD- 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 158262971 211 EGQDVLLFIDNIFRFTQAGSEVSALLGRMP 240
Cdd:cd01132  159 NGKHALIIYDDLSKQAVAYRQMSLLLRRPP 188
fliI PRK07196
flagellar protein export ATPase FliI;
37-248 1.09e-21

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 93.03  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  37 GLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDAerqPIHKKAPTFDELSTSS--EILETGIKVIDLLA 114
Cdd:PRK07196  74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST---PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 115 PYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARM 194
Cdd:PRK07196 151 TIGKGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRI 227

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158262971 195 RVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 248
Cdd:PRK07196 228 KATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPS 280
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
34-247 1.43e-21

EscN/YscN/HrcN family type III secretion system ATPase;


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 92.71  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  34 STDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTID-----------LEAPFTEDAERQPIhkkaptfdelstsSEI 102
Cdd:PRK07594  72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDgrelpdvcwkdYDAMPPPAMVRQPI-------------TQP 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 103 LETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELihnIAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMV 182
Cdd:PRK07594 139 LMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAML---CNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIV 215

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262971 183 FGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQP 247
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPP 279
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 50-251 1.42e-20

V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. 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. This subfamily consists of the non-catalytic beta subunit.


Pssm-ID: 410879 [Multi-domain]  Cd Length: 282  Bit Score: 88.05  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  50 PISVPVGKETLGRVFNVLGDTIDLEAPFTEDAER----QPIHKKAPTFDElstssEILETGIKVIDLLAPYLKGGKVGLF 125
Cdd:cd01135    1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLdingPPINPVARIYPE-----EMIQTGISAIDVMNTLVRGQKLPIF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 126 GGAGvgktvliqeLIHN-----IA-------QEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGAR 193
Cdd:cd01135   76 SGSG---------LPHNelaaqIArqagvvgSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIER 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158262971 194 MRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:cd01135  147 IITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYT 204
fliI PRK07960
flagellum-specific ATP synthase FliI;
32-249 4.50e-19

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 85.61  E-value: 4.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  32 MESTDGLTRGMEVLdtGRPIS---------VPVGKETLGRVFNVLGDTID-LEAPftEDAERQPIHkkAPTFDELSTS-- 99
Cdd:PRK07960  82 LEEVEGILPGARVY--ARNISgeglqsgkqLPLGPALLGRVLDGSGKPLDgLPAP--DTGETGALI--TPPFNPLQRTpi 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 100 SEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERTREGNDLYWEMKESGVIEKT 179
Cdd:PRK07960 156 EHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQAD---VIVVGLIGERGREVKDFIENILGAEGRARS 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 180 AMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTL 249
Cdd:PRK07960 233 VVIAAPADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSV 301
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 3-245 5.22e-19

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 85.26  E-value: 5.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   3 VVYKNDERKTKIVLEValelGDGMVRTIAMESTDGL-TRGMEVLDTGRPISVPVGKETLGRVFNVLGDTID-LEAPFTED 80
Cdd:PRK04196  31 IELPNGEKRRGQVLEV----SEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDgGPEIIPEK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  81 aeRQPIHKKA--PTFDElsTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGvgktvliqeLIHN-----IAQ-------E 146
Cdd:PRK04196 107 --RLDINGAPinPVARE--YPEEFIQTGISAIDGLNTLVRGQKLPIFSGSG---------LPHNelaaqIARqakvlgeE 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 147 HGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFT 226
Cdd:PRK04196 174 ENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYC 253

                        250
                 ....*....|....*....
gi 158262971 227 QAGSEVSALLGRMPSAVGY 245
Cdd:PRK04196 254 EALREISAAREEVPGRRGY 272
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 15-240 3.26e-18

FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439826 [Multi-domain]  Cd Length: 504  Bit Score: 83.16  E-value: 3.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  15 VLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDaERQPIHKKAPTFD 94
Cdd:COG0056   59 VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAE-ERRPVERPAPGVI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  95 ELSTSSEILETGIKVIDLLAPylkggkVG------LFGGAGVGKTVLIQELIhnIAQEHGG-ISVFAGVGERT----REG 163
Cdd:COG0056  138 DRQPVHEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTAIAIDTI--INQKGKDvICIYVAIGQKAstvaQVV 209

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262971 164 NDLywemKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 240
Cdd:COG0056  210 ETL----EEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRPP 281
ATP-synt_F1_beta_N cd18115
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ...
 1-51 1.80e-17

F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-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 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.


Pssm-ID: 349739 [Multi-domain]  Cd Length: 76  Bit Score: 74.48  E-value: 1.80e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158262971   1 ALVVykNDERKTKIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPI 51
Cdd:cd18115   28 ALEV--KGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 51-251 3.74e-17

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 80.21  E-value: 3.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  51 ISVPVGKEtlGRVFNVLGD---TID-----LEAPFTEDAERQPIHK----KAPTFDELSTSSEILETGIKVIDLLAPYLK 118
Cdd:PRK04192 149 IMVPPGVS--GTVKEIVSEgdyTVDdtiavLEDEDGEGVELTMMQKwpvrRPRPYKEKLPPVEPLITGQRVIDTFFPVAK 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 119 GGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFAGVGERtreGNdlywEMKE------------SG--VIEKTAMVFG 184
Cdd:PRK04192 227 GGTAAIPGPFGSGKTVTQHQLAKWADAD---IVIYVGCGER---GN----EMTEvleefpelidpkTGrpLMERTVLIAN 296

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262971 185 QMNEPPGARMRVALTGLTIAEYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:PRK04192 297 TSNMPVAAREASIYTGITIAEYYRDM-GYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLAS 362
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
 15-240 1.00e-16

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 78.95  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  15 VLEVALELGDGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFtEDAERQPIHKKAPTFD 94
Cdd:PRK09281  59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPI-EATETRPVERKAPGVI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  95 ELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhnIAQEHGGI-----------SVFAGVGErtreg 163
Cdd:PRK09281 138 DRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTI--INQKGKDViciyvaigqkaSTVAQVVR----- 210

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262971 164 ndlywEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 240
Cdd:PRK09281 211 -----KLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 35-245 2.95e-15

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 74.30  E-value: 2.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  35 TDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEApfteDAERQPIHKKAPTFDELS--TSSEILETGIKVIDL 112
Cdd:PRK02118  58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGP----ELEGEPIEIGGPSVNPVKriVPREMIRTGIPMIDV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 113 LAPYLKGGKVGLFGGAGVGktvlIQELIHNIA-QEHGGISVFAGVGERtregNDLYW----EMKESGVIEKTAMVFGQMN 187
Cdd:PRK02118 134 FNTLVESQKIPIFSVSGEP----YNALLARIAlQAEADIIILGGMGLT----FDDYLffkdTFENAGALDRTVMFIHTAS 205

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158262971 188 EPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY 245
Cdd:PRK02118 206 DPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGY 263
atpA CHL00059
ATP synthase CF1 alpha subunit
 36-240 7.42e-14

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 70.38  E-value: 7.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  36 DGLT--RGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDLEAPFTEDAERqPIHKKAPTFDELSTSSEILETGIKVIDLL 113
Cdd:CHL00059  57 DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESR-LIESPAPGIISRRSVYEPLQTGLIAIDSM 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 114 APYLKGGKVGLFGGAGVGKTVLIQELIHNiAQEHGGISVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGAR 193
Cdd:CHL00059 136 IPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQ 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 158262971 194 MRVALTGLTIAEYFRdVEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 240
Cdd:CHL00059 215 YLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 24-245 9.88e-14

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 70.07  E-value: 9.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  24 DGMVRTIAMESTDGLTRGMEVLDTGRPISVPVGKETLGRVFNVLGDTIDL------EAPFTEDAERQPIHKKAPTFDELS 97
Cdd:PTZ00185  88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVglltrsRALLESEQTLGKVDAGAPNIVSRS 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  98 TSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHN-------IAQEHGGISVFAGVGERTREGNDLYWEM 170
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLL 247

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262971 171 KESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY 245
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAY 321
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 18-245 1.10e-13

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: 69.75  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   18 VALELGDGMVRT-------------IAMESTDGLTRGMEVLD-TGRPISVPVGKETLGRVFNVLGDTIDLEAP-FTE--- 79
Cdd:TIGR01040  27 VNLTLPDGTVRSgqvlevsgnkavvQVFEGTSGIDAKKTTCEfTGDILRTPVSEDMLGRVFNGSGKPIDKGPPvLAEdyl 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   80 DAERQPIHKKAPTFDElstssEILETGIKVIDLLAPYLKGGKVGLFGGAG-------------VGKTVLIQELIHNIAQE 146
Cdd:TIGR01040 107 DINGQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaaqicrqAGLVKLPTKDVHDGHED 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  147 HGGIsVFAGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFT 226
Cdd:TIGR01040 182 NFAI-VFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYA 260

                         250
                  ....*....|....*....
gi 158262971  227 QAGSEVSALLGRMPSAVGY 245
Cdd:TIGR01040 261 DALREVSAAREEVPGRRGF 279
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 139-251 2.71e-12

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 66.20  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  139 LIHNIAQEH-------GGISVFAGVGERTREGNDLYWEMKE-------SGVIEKTAMVFGQMNEPPGARMRVALTGLTIA 204
Cdd:PRK14698  666 LLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIA 745

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 158262971  205 EYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 251
Cdd:PRK14698  746 EYFRDM-GYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLAS 791
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
 13-48 5.37e-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: 51.39  E-value: 5.37e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 158262971   13 KIVLEVALELGDGMVRTIAMESTDGLTRGMEVLDTG 48
Cdd:pfam02874  34 SLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
rho TIGR00767
transcription termination factor Rho; This RNA helicase, the transcription termination factor ...
 96-241 2.71e-06

transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]


Pssm-ID: 162030 [Multi-domain]  Cd Length: 415  Bit Score: 47.76  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   96 LSTSSEILETgiKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAG-VGERTREGNDlyweMKESG 174
Cdd:TIGR00767 147 LETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLlIDERPEEVTD----MQRSV 220

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262971  175 VIEKTAMVFgqmNEPPGARMRVAltGLTIAEYFRDVE-GQDVLLFIDNIFRFTQAGSEVSALLGRMPS 241
Cdd:TIGR00767 221 KGEVVASTF---DEPASRHVQVA--EMVIEKAKRLVEhKKDVVILLDSITRLARAYNTVTPASGKVLS 283
rho_factor_C cd01128
C-terminal ATP binding domain of transcription termination factor rho; Transcription ...
 108-241 3.66e-06

C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.


Pssm-ID: 410872 [Multi-domain]  Cd Length: 249  Bit Score: 46.81  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 108 KVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAG-VGERTREGNDlyweMKESGVIEKTAMVFgqm 186
Cdd:cd01128    5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSVKGEVVASTF--- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 158262971 187 NEPPGARMRVALTGLTIAEyfRDVE-GQDVLLFIDNIFRFTQAGSEVSALLGRMPS 241
Cdd:cd01128   78 DEPPERHVQVAEMVIEKAK--RLVEhGKDVVILLDSITRLARAYNTVVPSSGKTLS 131
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 118-239 7.07e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 44.67  E-value: 7.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   118 KGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFAGvgertregndlywEMKESGVIEKTAMVFGQMNEPPGARMRVA 197
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 158262971   198 LTGLTIAEYFRdvegqDVLLFIDNIFRFTQAGSEVSALLGRM 239
Cdd:smart00382  68 RLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
PRK07165 PRK07165
ATP F0F1 synthase subunit alpha;
57-241 1.44e-03

ATP F0F1 synthase subunit alpha;


Pssm-ID: 235951 [Multi-domain]  Cd Length: 507  Bit Score: 39.57  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  57 KETLGRVFNVLGDTIDLEA----PFTEDAERQPIHKKAPTFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGK 132
Cdd:PRK07165  77 KEYFGKIIDIDGNIIYPEAqnplSKKFLPNTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGK 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 133 TVLIQELIhnIAQEHGGIS-VFAGVGERTREGNDLYWEMKESGVIEKTaMVFGQMNEPPGARMRVALTGLTIAE---YFr 208
Cdd:PRK07165 157 THIALNTI--INQKNTNVKcIYVAIGQKRENLSRIYETLKEHDALKNT-IIIDAPSTSPYEQYLAPYVAMAHAEnisYN- 232

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 158262971 209 dvegQDVLLFID------NIFRftqagsEVSALLGR------MPS 241
Cdd:PRK07165 233 ----DDVLIVFDdltkhaNIYR------EIALLTNKpvgkeaFPG 267
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 82-172 1.52e-03

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 39.62  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971   82 ERQPIHKKAPTFDELSTSSEILeTGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhnIAQEHGGISV------FAG 155
Cdd:PRK14698  191 QRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGDTLI--LTKEFGLIKIkdlyeiLDG 267

                          90
                  ....*....|....*..
gi 158262971  156 VGERTREGNDLYWEMKE 172
Cdd:PRK14698  268 KGKKTVEGNEEWTELEE 284
rho PRK09376
transcription termination factor Rho; Provisional
 88-228 2.45e-03

transcription termination factor Rho; Provisional


Pssm-ID: 236490 [Multi-domain]  Cd Length: 416  Bit Score: 38.58  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971  88 KKAPTFDELS----TSSEILETGI------KVIDLLAPYLKGGKvGLFggagV-----GKTVLIQELIHNIAQEHGGISV 152
Cdd:PRK09376 128 RNRPLFENLTplypNERLRLETGNpedlstRIIDLIAPIGKGQR-GLI----VappkaGKTVLLQNIANSITTNHPEVHL 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262971 153 FAG-VGERTREGNDlyweMKES---GVIEKTamvfgqMNEPPGARMRVAltGLTIAEYFRDVE-GQDVLLFIDNIFRFTQ 227
Cdd:PRK09376 203 IVLlIDERPEEVTD----MQRSvkgEVVAST------FDEPAERHVQVA--EMVIEKAKRLVEhGKDVVILLDSITRLAR 270


                 .
gi 158262971 228 A 228
Cdd:PRK09376 271 A 271
 
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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