NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|154799628|emb|CAO82834|]
View 

ATPase subunit B, partial [Halorubrum sp. TP025]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK04196 super family cl35252
V-type ATP synthase subunit B; Provisional
 1-165 3.12e-120

V-type ATP synthase subunit B; Provisional


The actual alignment was detected with superfamily member PRK04196:

Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 346.81  E-value: 3.12e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEEEEGgddeegseFAVIFGAMGITQEE 80
Cdd:PRK04196 118 VAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLGEEEN--------FAVVFAAMGITFEE 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:PRK04196 190 ANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGR 269


                 ....*
gi 154799628 161 RGYPG 165
Cdd:PRK04196 270 RGYPG 274
 
Name Accession Description Interval E-value
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 1-165 3.12e-120

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 346.81  E-value: 3.12e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEEEEGgddeegseFAVIFGAMGITQEE 80
Cdd:PRK04196 118 VAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLGEEEN--------FAVVFAAMGITFEE 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:PRK04196 190 ANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGR 269


                 ....*
gi 154799628 161 RGYPG 165
Cdd:PRK04196 270 RGYPG 274
NtpB COG1156
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ...
 1-165 3.13e-118

Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 440770 [Multi-domain]  Cd Length: 462  Bit Score: 341.74  E-value: 3.13e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEEEEGgddeegseFAVIFGAMGITQEE 80
Cdd:COG1156  120 VAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVRGEEEK--------FAVVFAAMGITHDE 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:COG1156  192 ANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGR 271


                 ....*
gi 154799628 161 RGYPG 165
Cdd:COG1156  272 RGYPG 276
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 1-165 2.99e-107

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: 307.23  E-value: 2.99e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEEEEGgddeegseFAVIFGAMGITQEE 80
Cdd:cd01135   44 VARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPHNELAAQIARQAGVVGSEEN--------FAIVFAAMGVTMEE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:cd01135  116 ARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGR 195


                 ....*
gi 154799628 161 RGYPG 165
Cdd:cd01135  196 RGYPG 200
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 1-165 6.62e-78

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: 238.85  E-value: 6.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628    1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQAS-VPEEEEGGDDEEGSEFAVIFGAMGITQE 79
Cdd:TIGR01040 116 YARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGlVKLPTKDVHDGHEDNFAIVFAAMGVNME 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   80 EANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPG 159
Cdd:TIGR01040 196 TARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPG 275


                  ....*.
gi 154799628  160 RRGYPG 165
Cdd:TIGR01040 276 RRGFPG 281
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 13-165 8.02e-63

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: 192.19  E-value: 8.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   13 GVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPeeeeggddeegsefAVIFGAMGITQEEANEFMEDFERTG 92
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD--------------VVVYALIGERGREVREFIEELLGSG 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154799628   93 ALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFeKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPG 165
Cdd:pfam00006  67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPP 138
 
Name Accession Description Interval E-value
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
 1-165 3.12e-120

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 346.81  E-value: 3.12e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEEEEGgddeegseFAVIFGAMGITQEE 80
Cdd:PRK04196 118 VAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLGEEEN--------FAVVFAAMGITFEE 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:PRK04196 190 ANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGR 269


                 ....*
gi 154799628 161 RGYPG 165
Cdd:PRK04196 270 RGYPG 274
NtpB COG1156
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ...
 1-165 3.13e-118

Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 440770 [Multi-domain]  Cd Length: 462  Bit Score: 341.74  E-value: 3.13e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEEEEGgddeegseFAVIFGAMGITQEE 80
Cdd:COG1156  120 VAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVRGEEEK--------FAVVFAAMGITHDE 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:COG1156  192 ANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGR 271


                 ....*
gi 154799628 161 RGYPG 165
Cdd:COG1156  272 RGYPG 276
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
 1-165 2.99e-107

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: 307.23  E-value: 2.99e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEEEEGgddeegseFAVIFGAMGITQEE 80
Cdd:cd01135   44 VARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLPHNELAAQIARQAGVVGSEEN--------FAIVFAAMGVTMEE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:cd01135  116 ARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGR 195


                 ....*
gi 154799628 161 RGYPG 165
Cdd:cd01135  196 RGYPG 200
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
 1-165 6.62e-78

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: 238.85  E-value: 6.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628    1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQAS-VPEEEEGGDDEEGSEFAVIFGAMGITQE 79
Cdd:TIGR01040 116 YARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGlVKLPTKDVHDGHEDNFAIVFAAMGVNME 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   80 EANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPG 159
Cdd:TIGR01040 196 TARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPG 275


                  ....*.
gi 154799628  160 RRGYPG 165
Cdd:TIGR01040 276 RRGFPG 281
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
 13-165 8.02e-63

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: 192.19  E-value: 8.02e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   13 GVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPeeeeggddeegsefAVIFGAMGITQEEANEFMEDFERTG 92
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD--------------VVVYALIGERGREVREFIEELLGSG 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154799628   93 ALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFeKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPG 165
Cdd:pfam00006  67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPP 138
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
 1-165 1.95e-56

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: 178.03  E-value: 1.95e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASvpeeeeggddeEGSEFAVIFGAMGITQEE 80
Cdd:cd19476   42 IERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQA-----------KAHAGVVVFAGIGERGRE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEkDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:cd19476  111 VNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGR 189


                 ....*
gi 154799628 161 RGYPG 165
Cdd:cd19476  190 EGYPP 194
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
 3-165 1.87e-54

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 177.53  E-value: 1.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   3 REYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEeeeggddeegsefaVIFGAMGITQEEAN 82
Cdd:PRK02118 117 RIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARIALQAEADI--------------IILGGMGLTFDDYL 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  83 EFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRG 162
Cdd:PRK02118 183 FFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRG 262


                 ...
gi 154799628 163 YPG 165
Cdd:PRK02118 263 YPG 265
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
 7-164 1.23e-21

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: 88.00  E-value: 1.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   7 EEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEeeeggddeegsefaVIFGAMGITQEEANEFME 86
Cdd:cd01136   48 EQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADV--------------NVIALIGERGREVREFIE 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154799628  87 DFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYP 164
Cdd:cd01136  114 KDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFR-DQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYP 190
fliI PRK08927
flagellar protein export ATPase FliI;
1-164 8.89e-17

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 76.17  E-value: 8.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPeeeeggddeegsefAVIFGAMGITQEE 80
Cdd:PRK08927 133 HSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD--------------VSVIGLIGERGRE 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:PRK08927 199 VQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFR-DQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTT 277


                 ....
gi 154799628 161 RGYP 164
Cdd:PRK08927 278 KGYT 281
PRK08149 PRK08149
FliI/YscN family ATPase;
1-164 1.20e-16

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 75.80  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYP-EEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASvpeeeeggddeegsefAVIF--GAMGIT 77
Cdd:PRK08149 125 YAERRPiREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSE----------------ADVFviGLIGER 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  78 QEEANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEV 157
Cdd:PRK08149 189 GREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFR-DQGKRVVLFIDSMTRYARALRDVALAAGEL 267


                 ....*..
gi 154799628 158 PGRRGYP 164
Cdd:PRK08149 268 PARRGYP 274
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
 10-164 2.28e-16

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: 75.07  E-value: 2.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  10 IETGVSAIDGMNTLVRGQKLPIFSSSGQPHSEL-AMqIARQASVPeeeeggddeegsefAVIFGAMGitqE---EANEFM 85
Cdd:COG1157  141 LDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLlGM-IARNTEAD--------------VNVIALIG---ErgrEVREFI 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  86 EDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYlaF-EKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYP 164
Cdd:COG1157  203 EDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEY--FrDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYP 280
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
2-164 5.48e-16

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 74.02  E-value: 5.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   2 SREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPeeeeggddeegsefAVIFGAMGITQEEA 81
Cdd:PRK06936 138 SRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD--------------VTVLALIGERGREV 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  82 NEFME-DFERTGaLERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGR 160
Cdd:PRK06936 204 REFIEsDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFR-DQGKRVLLLMDSVTRFARAQREIGLAAGEPPTR 281


                 ....
gi 154799628 161 RGYP 164
Cdd:PRK06936 282 RGYP 285
fliI PRK08472
flagellar protein export ATPase FliI;
7-164 5.65e-14

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 68.17  E-value: 5.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   7 EEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPeeeeggddeeGSEFAVIfGAMGitqEEANEFME 86
Cdd:PRK08472 138 DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAP----------IKVVALI-GERG---REIPEFIE 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154799628  87 dFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYP 164
Cdd:PRK08472 204 -KNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK-NQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYP 279
fliI PRK07960
flagellum-specific ATP synthase FliI;
7-164 2.33e-13

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 66.35  E-value: 2.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   7 EEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIAR--QASVpeeeeggddeegsefaVIFGAMGITQEEANEF 84
Cdd:PRK07960 156 EHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARytQADV----------------IVVGLIGERGREVKDF 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  85 MEDFERTGALERSVVFMNLADdpavertVTPRMVLTTAEYLA-FEKDY-----HVLVILTDMTNYCEALREIGAAREEVP 158
Cdd:PRK07960 220 IENILGAEGRARSVVIAAPAD-------VSPLLRMQGAAYATrIAEDFrdrgqHVLLIMDSLTRYAMAQREIALAIGEPP 292


                 ....*.
gi 154799628 159 GRRGYP 164
Cdd:PRK07960 293 ATKGYP 298
PRK09099 PRK09099
type III secretion system ATPase; Provisional
 2-164 2.47e-13

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 66.33  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   2 SREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEEEEggddeegsefaVIFGAMGitqEEA 81
Cdd:PRK09099 139 SRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVI-----------ALIGERG---REV 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  82 NEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRR 161
Cdd:PRK09099 205 REFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFR-DRGLRVLLMMDSLTRFARAQREIGLAAGEPPARR 283


                 ...
gi 154799628 162 GYP 164
Cdd:PRK09099 284 GFP 286
fliI PRK07721
flagellar protein export ATPase FliI;
7-164 2.49e-13

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 66.28  E-value: 2.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   7 EEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASvpeeeeggddEEGSEFAVIfGAMGitqEEANEFME 86
Cdd:PRK07721 139 REPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTS----------ADLNVIALI-GERG---REVREFIE 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154799628  87 -DFERTGaLERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYP 164
Cdd:PRK07721 205 rDLGPEG-LKRSIVVVATSDQPALMRIKGAYTATAIAEYFR-DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYT 281
fliI PRK08972
flagellar protein export ATPase FliI;
2-164 1.23e-12

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 64.34  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   2 SREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIAR--QASVpeeeeggddeegsefaVIFGAMGITQE 79
Cdd:PRK08972 138 SRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRgtTADV----------------IVVGLVGERGR 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  80 EANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPG 159
Cdd:PRK08972 202 EVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFR-DQGLNVLLLMDSLTRYAQAQREIALAVGEPPA 280


                 ....*
gi 154799628 160 RRGYP 164
Cdd:PRK08972 281 TKGYP 285
fliI PRK06002
flagellar protein export ATPase FliI;
12-164 1.69e-12

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 63.86  E-value: 1.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  12 TGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQAsvpeeeeggddeegsEF-AVIFGAMGITQEEANEFMEDFER 90
Cdd:PRK06002 151 TGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARAD---------------AFdTVVIALVGERGREVREFLEDTLA 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154799628  91 tGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYP 164
Cdd:PRK06002 216 -DNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFR-DRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYP 287
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
2-164 2.36e-12

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 63.68  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   2 SREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIAR--QASVpeeeeggddeegsefaVIFGAMGITQE 79
Cdd:PRK06820 139 TRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCAdsAADV----------------MVLALIGERGR 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  80 EANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPG 159
Cdd:PRK06820 203 EVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPA 281


                 ....*
gi 154799628 160 RRGYP 164
Cdd:PRK06820 282 AGSFP 286
fliI PRK07196
flagellar protein export ATPase FliI;
10-164 8.79e-12

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 61.83  E-value: 8.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  10 IETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIAR--QASVpeeeeggddeegsefaVIFGAMGITQEEANEFMED 87
Cdd:PRK07196 139 LDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRytQADV----------------VVVGLIGERGREVKEFIEH 202

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154799628  88 FERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYP 164
Cdd:PRK07196 203 SLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYR-DKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYP 278
fliI PRK05688
flagellar protein export ATPase FliI;
8-164 3.27e-11

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 60.13  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   8 EFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIAR--QASVpeeeeggddeegsefaVIFGAMGITQEEANEFM 85
Cdd:PRK05688 150 EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRftEADI----------------IVVGLIGERGREVKEFI 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154799628  86 EDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYP 164
Cdd:PRK05688 214 EHILGEEGLKRSVVVASPADDAPLMRLRAAMYCTRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYP 291
PRK05922 PRK05922
type III secretion system ATPase; Validated
 2-156 3.97e-11

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 59.92  E-value: 3.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   2 SREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASvpeeeeggddeegSEFAVIfGAMGITQEEA 81
Cdd:PRK05922 133 SRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSK-------------STINVI-ALIGERGREV 198

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 154799628  82 NEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREE 156
Cdd:PRK05922 199 REYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGE 272
fliI PRK06793
flagellar protein export ATPase FliI;
1-158 6.57e-11

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 59.61  E-value: 6.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   1 YSREYPEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPEEeeggddeegsefavIFGAMGITQEE 80
Cdd:PRK06793 131 FEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADIN--------------VISLVGERGRE 196

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154799628  81 ANEFMEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVP 158
Cdd:PRK06793 197 VKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFR-DQGNNVLLMMDSVTRFADARRSVDIAVKELP 273
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
 8-165 8.61e-09

proton translocating ATP synthase, F1 alpha 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. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 273365 [Multi-domain]  Cd Length: 501  Bit Score: 53.16  E-value: 8.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628    8 EFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQI---ARQASVpeeeeggddeegsefAVIFGAMGITQEEANEF 84
Cdd:TIGR00962 143 EPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTiinQKDSDV---------------YCIYVAIGQKASTVAQV 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   85 MEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDyHVLVILTDMTNYCEALREIGAAREEVPGRRGYP 164
Cdd:TIGR00962 208 VRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGK-HALIIYDDLSKQAVAYRQISLLLRRPPGREAFP 286


                  .
gi 154799628  165 G 165
Cdd:TIGR00962 287 G 287
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
12-164 5.14e-08

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 51.11  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  12 TGVSAIDGMNTLVRGQKLPIFSSSGQPHSELamqIARQASVPEEEEGGDdeegsefaVIFGAMGitqEEANEFMEDFERT 91
Cdd:PRK07594 141 TGIRAIDSVATCGEGQRVGIFSAPGVGKSTL---LAMLCNAPDADSNVL--------VLIGERG---REVREFIDFTLSE 206

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154799628  92 GALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYP 164
Cdd:PRK07594 207 ETRKRCVIVVATSDRPALERVRALFVATTIAEFFR-DNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYP 278
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
 88-165 8.56e-08

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: 49.86  E-value: 8.56e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154799628  88 FERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDyHVLVILTDMTNYCEALREIGAAREEVPGRRGYPG 165
Cdd:cd01132  119 LEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGK-HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPG 195
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
 69-165 8.99e-08

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 50.41  E-value: 8.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   69 VIFGAMGITQEEANEFMEDFER-----TGA--LERSVVFMNLADDPAVERTVTPRMVLTTAEYLAfEKDYHVLVILTDMT 141
Cdd:PRK14698  685 VIYIGCGERGNEMTDVLEEFPKlkdpkTGKplMERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALMADSTS 763

                          90       100
                  ....*....|....*....|....
gi 154799628  142 NYCEALREIGAAREEVPGRRGYPG 165
Cdd:PRK14698  764 RWAEALREISGRLEEMPGEEGYPA 787
atpA CHL00059
ATP synthase CF1 alpha subunit
 88-165 1.23e-06

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 46.88  E-value: 1.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154799628  88 FERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLAFEKDyHVLVILTDMTNYCEALREIGAAREEVPGRRGYPG 165
Cdd:CHL00059 191 LQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGR-HTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPG 267
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
 10-165 2.22e-06

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 46.45  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  10 IETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQ-IARQASvpeeeeggddeegSEFAVIFGAMGITQEEANEFMEDF 88
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDaIINQKD-------------SDVICVYVAIGQKASAVARVIETL 212

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154799628  89 ERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLaFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPG 165
Cdd:PRK13343 213 REHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYF-RDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPG 288
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
 6-164 4.03e-05

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: 42.18  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   6 PEEFIETGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQIARQASVPeeeeggddeegsefAVIFGAMGitqEEANEFM 85
Cdd:cd01134   56 PNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSD--------------VVIYVGCG---ERGNEMA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  86 E---DF-----ERTGA--LERSVVFMNLADDPAVERTVTPRMVLTTAEYLafeKD--YHVLvILTDMTN-YCEALREIGA 152
Cdd:cd01134  119 EvleEFpelkdPITGEslMERTVLIANTSNMPVAAREASIYTGITIAEYF---RDmgYNVS-LMADSTSrWAEALREISG 194

                        170
                 ....*....|..
gi 154799628 153 AREEVPGRRGYP 164
Cdd:cd01134  195 RLEEMPAEEGYP 206
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 3-164 6.08e-04

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 38.99  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   3 REYPEEFIETGVSAIDGMNTLVRGQKLPI---FSSsGQphSELAMQIARQASVPEeeeggddeegsefaVIFGAMGitqE 79
Cdd:PRK04192 204 KLPPVEPLITGQRVIDTFFPVAKGGTAAIpgpFGS-GK--TVTQHQLAKWADADI--------------VIYVGCG---E 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  80 EANEFMEDFE--------RTGA--LERSVVFMNLADDPAVERTVTPRMVLTTAEYLafeKD--YHVLvILTDMTN-YCEA 146
Cdd:PRK04192 264 RGNEMTEVLEefpelidpKTGRplMERTVLIANTSNMPVAAREASIYTGITIAEYY---RDmgYDVL-LMADSTSrWAEA 339

                        170
                 ....*....|....*...
gi 154799628 147 LREIGAAREEVPGRRGYP 164
Cdd:PRK04192 340 LREISGRLEEMPGEEGYP 357
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
 12-165 1.15e-03

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 38.48  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  12 TGVSAIDGMNTLVRGQKLPIFSSSGQPHSELAMQ-IARQASVPEEEEGGDdeegsefAVIFGAMGITQEEAN--EFMEDF 88
Cdd:PTZ00185 175 TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVStIINQVRINQQILSKN-------AVISIYVSIGQRCSNvaRIHRLL 247

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154799628  89 ERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYLaFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPG 165
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYF-MNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPG 323
PRK07165 PRK07165
ATP F0F1 synthase subunit alpha;
7-165 2.02e-03

ATP F0F1 synthase subunit alpha;


Pssm-ID: 235951 [Multi-domain]  Cd Length: 507  Bit Score: 37.65  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628   7 EEFIETGVSAIDGMNTLVRGQKLPIF--SSSGQPHSELAMQI-ARQASVpeeeeggddeegsefAVIFGAMGITQEEANE 83
Cdd:PRK07165 124 NEQLYTGIIAIDLLIPIGKGQRELIIgdRQTGKTHIALNTIInQKNTNV---------------KCIYVAIGQKRENLSR 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  84 FMEDFERTGALERSVVfMNLADDPAVERTVTPRMVLTTAEYLAFEKDyhVLVILTDMTNYCEALREIGAAREEVPGRRGY 163
Cdd:PRK07165 189 IYETLKEHDALKNTII-IDAPSTSPYEQYLAPYVAMAHAENISYNDD--VLIVFDDLTKHANIYREIALLTNKPVGKEAF 265


                 ..
gi 154799628 164 PG 165
Cdd:PRK07165 266 PG 267
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
 85-165 8.50e-03

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: 35.79  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154799628  85 MEDFERTGALERSVVFMNLADDPAVERTVTPRMVLTTAEYlaF-EKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGY 163
Cdd:COG0056  209 VETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEY--FmDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAY 286


                 ..
gi 154799628 164 PG 165
Cdd:COG0056  287 PG 288
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH