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Conserved domains on  [gi|19913426|ref|NP_001683|]
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V-type proton ATPase subunit B, kidney isoform [Homo sapiens]

Protein Classification

V-type proton ATPase subunit B( domain architecture ID 11490103)

V-type proton ATPase subunit B is a non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
40-503 0e+00

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: 1015.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426    40 TYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSE 119
Cdd:TIGR01040   1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   120 DMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 199
Cdd:TIGR01040  81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   200 ICRQAGLVKKS-KAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEF 278
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   279 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHP 358
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   359 IPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEAL 438
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19913426   439 TSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 503
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
 
Name Accession Description Interval E-value
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
40-503 0e+00

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: 1015.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426    40 TYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSE 119
Cdd:TIGR01040   1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   120 DMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 199
Cdd:TIGR01040  81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   200 ICRQAGLVKKS-KAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEF 278
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   279 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHP 358
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   359 IPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEAL 438
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19913426   439 TSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 503
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
NtpB COG1156
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ...
37-503 0e+00

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: 839.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  37 PRVTYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTP 116
Cdd:COG1156   2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 117 VSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEI 196
Cdd:COG1156  82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 197 AAQICRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTA 276
Cdd:COG1156 162 AAQIARQAKVRGE--------EEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAA 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 277 EFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDIT 356
Cdd:COG1156 234 EYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDIT 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 357 HPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEE 436
Cdd:COG1156 314 HPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEE 393
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913426 437 ALTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 503
Cdd:COG1156 394 ALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRA 460
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
38-503 0e+00

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 809.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   38 RVTYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPV 117
Cdd:PRK04196   1 LKEYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  118 SEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIA 197
Cdd:PRK04196  81 SEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  198 AQICRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAE 277
Cdd:PRK04196 161 AQIARQAKVLGE--------EENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  278 FLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITH 357
Cdd:PRK04196 233 YLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITH 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  358 PIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEA 437
Cdd:PRK04196 313 PIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEA 392
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19913426  438 LTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 503
Cdd:PRK04196 393 LSERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRG 458
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
112-401 0e+00

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: 612.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 112 ILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGL 191
Cdd:cd01135   1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 192 PHNEIAAQICRQAGLVKkskavldyHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRL 271
Cdd:cd01135  81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 272 ALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMP 351
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 19913426 352 NDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 401
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
167-393 7.24e-105

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: 312.37  E-value: 7.24e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   167 GISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGlvkkskavldyHDdnfAIVFAAMGVNMETARFFKSDFEQNG 246
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS-----------AD---VVVYALIGERGREVREFIEELLGSG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   247 TMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 326
Cdd:pfam00006  67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913426   327 TIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 393
Cdd:pfam00006 146 RLLERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
 
Name Accession Description Interval E-value
V-ATPase_V1_B TIGR01040
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ...
40-503 0e+00

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: 1015.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426    40 TYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSE 119
Cdd:TIGR01040   1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   120 DMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 199
Cdd:TIGR01040  81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   200 ICRQAGLVKKS-KAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEF 278
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   279 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHP 358
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   359 IPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEAL 438
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19913426   439 TSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 503
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
NtpB COG1156
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ...
37-503 0e+00

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: 839.80  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  37 PRVTYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTP 116
Cdd:COG1156   2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 117 VSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEI 196
Cdd:COG1156  82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 197 AAQICRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTA 276
Cdd:COG1156 162 AAQIARQAKVRGE--------EEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAA 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 277 EFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDIT 356
Cdd:COG1156 234 EYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDIT 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 357 HPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEE 436
Cdd:COG1156 314 HPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEE 393
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913426 437 ALTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 503
Cdd:COG1156 394 ALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRA 460
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
38-503 0e+00

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 809.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   38 RVTYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPV 117
Cdd:PRK04196   1 LKEYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  118 SEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIA 197
Cdd:PRK04196  81 SEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  198 AQICRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAE 277
Cdd:PRK04196 161 AQIARQAKVLGE--------EENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  278 FLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITH 357
Cdd:PRK04196 233 YLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITH 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  358 PIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEA 437
Cdd:PRK04196 313 PIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEA 392
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19913426  438 LTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 503
Cdd:PRK04196 393 LSERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRG 458
ATP_syn_B_arch TIGR01041
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ...
41-498 0e+00

ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity with eukaryotic and prokaryotic V-type (H+)-ATPases. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 200071 [Multi-domain]  Cd Length: 458  Bit Score: 693.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426    41 YRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSED 120
Cdd:TIGR01041   2 YSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   121 MLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 200
Cdd:TIGR01041  82 MLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   201 CRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLA 280
Cdd:TIGR01041 162 ARQATVRGE--------ESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   281 YQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIP 360
Cdd:TIGR01041 234 FEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   361 DLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTS 440
Cdd:TIGR01041 314 DLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSE 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19913426   441 EDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFY 498
Cdd:TIGR01041 394 RDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYH 451
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
112-401 0e+00

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: 612.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 112 ILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGL 191
Cdd:cd01135   1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 192 PHNEIAAQICRQAGLVKkskavldyHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRL 271
Cdd:cd01135  81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 272 ALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMP 351
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 19913426 352 NDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 401
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
38-501 1.06e-119

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 358.58  E-value: 1.06e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   38 RVTYRTVCSVNGPLVVLdRVKFAQYAEIVHFTLPDGTqRSGQVLEVAGTKAIVQVFEGTSGI--DARKTtceFTGDILRT 115
Cdd:PRK02118   2 QKIYTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGIstGDEVV---FLGRPMQV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  116 PVSEDMLGRVFNGSGKPIDKGPVVMAEDfLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 195
Cdd:PRK02118  77 TYSESLLGRRFNGSGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  196 IAAQICRQAglvkkskavldyhdDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTT 275
Cdd:PRK02118 156 LLARIALQA--------------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAV 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  276 AEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrGGSITQIPILTMPNDDI 355
Cdd:PRK02118 222 AEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDV 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  356 THPIPDLTGFITEGQIYvdrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRKDHGDVSN---QLYACYAIGKDVQAMkav 432
Cdd:PRK02118 301 THPVPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM--- 368
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19913426  433 vGEEaLTSEDLLYLEFLQKFEKNFINQG---PYEnrsvfESLDLGWKLL-RIF-PKEMLkrIPQAVIDEFYSRE 501
Cdd:PRK02118 369 -GFK-LSNWDEKLLKFSELFESRLMDLEvniPLE-----EALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKN 433
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
167-393 7.24e-105

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: 312.37  E-value: 7.24e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   167 GISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGlvkkskavldyHDdnfAIVFAAMGVNMETARFFKSDFEQNG 246
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS-----------AD---VVVYALIGERGREVREFIEELLGSG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   247 TMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 326
Cdd:pfam00006  67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913426   327 TIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 393
Cdd:pfam00006 146 RLLERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
RecA-like_ion-translocating_ATPases cd19476
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ...
114-395 1.39e-103

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: 311.31  E-value: 1.39e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPH 193
Cdd:cd19476   1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 194 NEIAAQICRQAglvKKSKAvldyhddnFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLAL 273
Cdd:cd19476  81 TVLAMQLARNQ---AKAHA--------GVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 274 TTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPND 353
Cdd:cd19476 150 TIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGD 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 19913426 354 DITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:cd19476 229 DLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
ATP-synt_V_A-type_beta_C cd18112
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ...
403-497 6.67e-64

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


Pssm-ID: 349747 [Multi-domain]  Cd Length: 95  Bit Score: 202.66  E-value: 6.67e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 403 GMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFP 482
Cdd:cd18112   1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
                        90
                ....*....|....*
gi 19913426 483 KEMLKRIPQAVIDEF 497
Cdd:cd18112  81 KEELKRISEEYIDKY 95
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
114-395 4.31e-41

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: 148.48  E-value: 4.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPH 193
Cdd:cd01136   1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 194 NEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETAR----FFKSDFEQNGtMGNVCLFLNLANDPTIERIITP 269
Cdd:cd01136  81 STLLGMIAR--------------NTDADVNVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 270 RLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILT 349
Cdd:cd01136 143 YTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVL 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 19913426 350 MPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:cd01136 220 VEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
64-399 4.09e-37

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: 143.30  E-value: 4.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426    64 EIVHFtlPDGTQRSGQVLEVAGTKAIVqvFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVmAE 142
Cdd:TIGR00962  50 ELIEF--EGGVQGIALNLEEDSVGAVI--MGDYSDI-REGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDgKGPID-SD 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   143 DFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGlvKKSKAV---LDYHDD 219
Cdd:TIGR00962 124 EFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGD-------------RQTG--KTAVAIdtiINQKDS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   220 NFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAE 299
Cdd:TIGR00962 189 DVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAV 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   300 ALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVD 374
Cdd:TIGR00962 268 AYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 344
                         330       340
                  ....*....|....*....|....*
gi 19913426   375 RQLHNRQIYPPINVLPSLSRLMKSA 399
Cdd:TIGR00962 345 SDLFNSGIRPAINVGLSVSRVGGAA 369
ATP-synt_V_A-type_beta_N cd18118
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 ...
40-111 1.99e-36

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


Pssm-ID: 349742 [Multi-domain]  Cd Length: 72  Bit Score: 129.47  E-value: 1.99e-36
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19913426  40 TYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGD 111
Cdd:cd18118   1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
64-396 4.78e-36

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: 139.01  E-value: 4.78e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  64 EIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAED 143
Cdd:COG1157  42 ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEE 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 144 FLDINGQPINPHSR--IypEEMIQTGISPIDVMNSIARGQKIPIFSAAG------LphneiaAQICRQA-------GLV- 207
Cdd:COG1157 121 RRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL------GMIARNTeadvnviALIg 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 208 -------------------KKSkavldyhddnfaIVFAAmgvnmeTarffkSDfeqngtmgnvclflnlanDPTIERIIT 268
Cdd:COG1157 193 ergrevrefieddlgeeglARS------------VVVVA------T-----SD------------------EPPLMRLRA 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 269 PRLALTTAEFLAYQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQI 345
Cdd:COG1157 232 AYTATAIAEYFRDQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAF 305
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 19913426 346 -PILTmPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:COG1157 306 yTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
79-478 4.81e-35

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 136.48  E-value: 4.81e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   79 QVLEVAGTKAIVQVFEGTSGIDARKTTcEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINPHSRI 158
Cdd:PRK06820  64 EVVSIEQEMALLSPFASSDGLRCGQWV-TPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQ 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  159 YPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETARFF 238
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA--------------DSAADVMVLALIG---ERGREV 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  239 KSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLALTTAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRR 315
Cdd:PRK06820 205 REFLEQVLTpeaRARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAG 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  316 GFPGYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:PRK06820 284 SFPPSVFANLPRLLERTGNSDR--GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI 361
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  396 MKSAIGEGmtRKDHGDVSNQLYACYaigKDVQAMKAVvgEEALTSEDLLYLEFLQKFE--KNFINQGPYENRSVFESLDL 473
Cdd:PRK06820 362 MPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEH 434

                 ....*
gi 19913426  474 GWKLL 478
Cdd:PRK06820 435 LAQVV 439
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
109-396 2.37e-34

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 134.49  E-value: 2.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  109 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSA 188
Cdd:PRK06936  91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  189 AGLPHNEIAAQICRQAglvkkskavldyhdDNFAIVFAAMGV-NMETARFFKSDFEQNGtMGNVCLFLNLANDPTIERII 267
Cdd:PRK06936 171 AGGGKSTLLASLIRSA--------------EVDVTVLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  268 TPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRGGSITQIPI 347
Cdd:PRK06936 236 AGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYT 312
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 19913426  348 LTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:PRK06936 313 VLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVM 361
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
112-394 3.25e-32

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: 124.59  E-value: 3.25e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 112 ILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP-INPHSRIYpeEMIQTGISPIDVMNSIARGQKIPIFSAa 189
Cdd:cd01132   1 IVEVPVGEALLGRVVDALGNPIDgKGPIQTKERRRVESKAPgIIPRQSVN--EPLQTGIKAIDSLIPIGRGQRELIIGD- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 190 glphneiaaqicRQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERI 266
Cdd:cd01132  78 ------------RQTG--KTAIAIdtiINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQY 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 267 ITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGS 341
Cdd:cd01132 144 LAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGS 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 19913426 342 ITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:cd01132 220 LTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
fliI PRK08472
flagellar protein export ATPase FliI;
113-402 3.97e-32

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 127.88  E-value: 3.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  113 LRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLP 192
Cdd:PRK08472  90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  193 HNEIAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQN--GTMGNVCLFLNLANDPTIERIITPR 270
Cdd:PRK08472 170 KSTLMGMI------VKGCLAPIK--------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGAF 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  271 LALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILTM 350
Cdd:PRK08472 233 CAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLV 310
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19913426  351 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGE 402
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
79-402 1.37e-29

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 120.83  E-value: 1.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   79 QVLEVAGTKAIVQVFEGTSGIdarktTCEFTGDILR----TPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINP 154
Cdd:PRK07594  56 EVVGINGSKALLSPFTSTIGL-----HCGQQVMALRrrhqVPVGEALLGRVIDGFGRPLDGRELPDVC-WKDYDAMPPPA 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  155 HSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyhDDNfaiVFAAMGVNMET 234
Cdd:PRK07594 130 MVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA-----------DSN---VLVLIGERGRE 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  235 ARFFkSDFEQNGTMGNVCLFLNLAND-PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPG 313
Cdd:PRK07594 196 VREF-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAV 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  314 RRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 393
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLS 351

                 ....*....
gi 19913426  394 RLMKSAIGE 402
Cdd:PRK07594 352 RVFPVVTSH 360
fliI PRK05688
flagellar protein export ATPase FliI;
111-471 3.30e-29

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 119.84  E-value: 3.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  111 DILRTPVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAA 189
Cdd:PRK05688  99 DTGRLPMGMSMLGRVLDGAGRALDgKGPM-KAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGT 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  190 GLphneiaaqicrqaglvkkSKAVLDYHDDNFA----IVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIER 265
Cdd:PRK05688 178 GV------------------GKSVLLGMMTRFTeadiIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMR 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  266 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQI 345
Cdd:PRK05688 240 LRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAF 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  346 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG-EGMTRKDHgdvSNQLYACYAIGK 424
Cdd:PRK05688 319 YTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQSR 395
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 19913426  425 DVQAMKAVV-GEEALTSEDLLYLEFLQKfeknFINQGPYENRSVFESL 471
Cdd:PRK05688 396 DLISVGAYVaGGDPETDLAIARFPHLVQ----FLRQGLRENVSLAQSR 439
atpA CHL00059
ATP synthase CF1 alpha subunit
109-399 5.50e-29

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 119.68  E-value: 5.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  109 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP--InphSRIYPEEMIQTGISPIDVMNSIARGQKIPI 185
Cdd:CHL00059  70 TGKIAQIPVSEAYLGRVVNALAKPIDgKGEISASESRLIESPAPgiI---SRRSVYEPLQTGLIAIDSMIPIGRGQRELI 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  186 FSAaglphneiaaqicRQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPT 262
Cdd:CHL00059 147 IGD-------------RQTG--KTAVATdtiLNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPA 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  263 IERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRVEGR- 338
Cdd:CHL00059 212 TLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSQl 287
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19913426  339 -GGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 399
Cdd:CHL00059 288 gEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
fliI PRK06002
flagellar protein export ATPase FliI;
58-399 6.98e-29

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 118.95  E-value: 6.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   58 KFAQYAEIVHFTLPDGTQRsGQVLEVAGTKAIVQVFEgtSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KG 136
Cdd:PRK06002  45 RFVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPIDgLG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  137 PVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGlphneiaaqicrqaglVKKSK--AVL 214
Cdd:PRK06002 122 PLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSG----------------VGKSTllAML 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  215 DYHDDNFAIVFAAMGVNMETARFFKSDfeqngTMGNvclflNLANDPTI---------ERIITPRLALTTAEFLAYQCEK 285
Cdd:PRK06002 186 ARADAFDTVVIALVGERGREVREFLED-----TLAD-----NLKKAVAVvatsdespmMRRLAPLTATAIAEYFRDRGEN 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  286 hVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGF 365
Cdd:PRK06002 256 -VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRG 334
                        330       340       350
                 ....*....|....*....|....*....|....
gi 19913426  366 ITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 399
Cdd:PRK06002 335 TLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
PRK09099 PRK09099
type III secretion system ATPase; Provisional
60-396 8.58e-29

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 118.33  E-value: 8.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   60 AQYAEIVHFTLPDGT--QRsGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGP 137
Cdd:PRK09099  43 VTLGELCELRQRDGTllQR-AEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  138 VVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyh 217
Cdd:PRK09099 121 PLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQC----------- 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  218 DDNfaiVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSY 297
Cdd:PRK09099 190 DVN---VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRF 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  298 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQL 377
Cdd:PRK09099 266 ARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREI 343
                        330
                 ....*....|....*....
gi 19913426  378 HNRQIYPPINVLPSLSRLM 396
Cdd:PRK09099 344 AARNQYPAIDVLGSLSRVM 362
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
109-394 1.30e-28

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 118.86  E-value: 1.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  109 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFldingqPINphsRIYPEEM--------IQTGISPIDVMNSIAR 179
Cdd:PRK13343  91 TGRVLEVPVGDGLLGRVIDPLGRPLDgGGPLQATARR------PLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGR 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  180 GQKIPIFSAAGLPHNEIAAQicrqaglvkkskAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAN 259
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIAID------------AIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEAS 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  260 DPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV--EG 337
Cdd:PRK13343 230 DPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLspEL 308
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19913426  338 RGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:PRK13343 309 GGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
fliI PRK07960
flagellum-specific ATP synthase FliI;
101-482 6.28e-28

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 116.04  E-value: 6.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  101 ARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARG 180
Cdd:PRK07960  96 ARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRG 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  181 QKIPIFSAAGLPHNEIAAQICR--QAGLvkkskavldyhddnfaIVFAAMGvnmETARFFKsDFEQN--GTMGnvclfln 256
Cdd:PRK07960 176 QRMGLFAGSGVGKSVLLGMMARytQADV----------------IVVGLIG---ERGREVK-DFIENilGAEG------- 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  257 LANDPTIERI--ITPRLALTTAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 328
Cdd:PRK07960 229 RARSVVIAAPadVSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPAL 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  329 YERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKd 408
Cdd:PRK07960 309 VERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR- 387
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19913426  409 hgdVSN--QLYACYAIGKDVQAmkavVGEEALTSEDLL--YLEFLQKFEKnFINQGPYEnRSVFEslDLGWKLLRIFP 482
Cdd:PRK07960 388 ---VRQfkQLLSSFQRNRDLVS----VGAYAKGSDPMLdkAIALWPQLEA-FLQQGIFE-RADWE--DSLQALERIFP 454
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
40-459 6.28e-27

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: 113.28  E-value: 6.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426    40 TYRTVCSVNGPLVvldRVKFAQYA--EIVHFTLPDGTQRSGQVLEVAG------TKAIVqvFEGTSGIdARKTTCEFTGD 111
Cdd:TIGR01039   1 TKGKVVQVIGPVV---DVEFEQGElpRIYNALKVQNRAESELTLEVAQhlgddtVRTIA--MGSTDGL-VRGLEVIDTGA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   112 ILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFldingqPINPHSRIYPE-----EMIQTGISPIDVMNSIARGQKIPI 185
Cdd:TIGR01039  75 PISVPVGKETLGRIFNVLGEPIDeKGPIPAKERW------PIHRKAPSFEEqstkvEILETGIKVIDLLAPYAKGGKIGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   186 FSAAGLPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDP 261
Cdd:TIGR01039 149 FGGAGVGKTvliqELINNIAKEHGGYS---------------VFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEP 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   262 TIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRGGS 341
Cdd:TIGR01039 214 PGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKTGS 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   342 ITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrkDHGDVSNQLYACY 420
Cdd:TIGR01039 292 ITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQIL 366
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 19913426   421 AIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKnFINQ 459
Cdd:TIGR01039 367 QRYKELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
fliI PRK07721
flagellar protein export ATPase FliI;
107-425 1.52e-26

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 111.74  E-value: 1.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  107 EFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIF 186
Cdd:PRK07721  85 EATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  187 SAAGLPHNEIAAQICRQaglvkkSKAVLDyhddnfaiVFAAMGVN-METARFFKSDFEQNGTMGNVcLFLNLANDPTIER 265
Cdd:PRK07721 165 AGSGVGKSTLMGMIARN------TSADLN--------VIALIGERgREVREFIERDLGPEGLKRSI-VVVATSDQPALMR 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  266 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrgGSITQI 345
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS--GSITAF 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  346 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSN---QLYACYAI 422
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQN 381

                 ...
gi 19913426  423 GKD 425
Cdd:PRK07721 382 SED 384
fliI PRK06793
flagellar protein export ATPase FliI;
116-425 1.57e-26

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 111.99  E-value: 1.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  116 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 195
Cdd:PRK06793  92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  196 IAAQICRQAglvkksKAvldyhDDNFAIVFAAMGvnMETARFFKSDFEQNGTMGNVcLFLNLANDPTIERIITPRLALTT 275
Cdd:PRK06793 172 LLGMIAKNA------KA-----DINVISLVGERG--REVKDFIRKELGEEGMRKSV-VVVATSDESHLMQLRAAKLATSI 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  276 AEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDD 354
Cdd:PRK06793 238 AEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQK--GSITGIYTVLVDGDD 312
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19913426  355 ITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSNQLYACYAIGKD 425
Cdd:PRK06793 313 LNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
PRK08149 PRK08149
FliI/YscN family ATPase;
32-395 2.71e-24

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 105.08  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   32 NYITHPRvtyrtvcSVNGPLV--VLDRVKFAQYAEIvhftlpdgtQRSGQVLEVAGtKAIVQVFEGTSGI-----DARKT 104
Cdd:PRK08149   5 QRLAHPL-------RIQGPIIeaELPDVAIGEICEI---------RAGWHSNEVIA-RAQVVGFQRERTIlsligNAQGL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  105 TCEF----TGDILRTPVSEDMLGRVFNGSGKPIDK--GPVVMAEDF--LDINGQPINPHSRIYPEEMIQTGISPIDVMNS 176
Cdd:PRK08149  68 SRQVvlkpTGKPLSVWVGEALLGAVLDPTGKIVERfdAPPTVGPISeeRVIDVAPPSYAERRPIREPLITGVRAIDGLLT 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  177 IARGQKIPIFSAAGLPHNEIAAQICRQAglvkkskavldyHDDNFAIvfaamGVNMETARF---FKSDFEQNGTMGNVCL 253
Cdd:PRK08149 148 CGVGQRMGIFASAGCGKTSLMNMLIEHS------------EADVFVI-----GLIGERGREvteFVESLRASSRREKCVL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  254 FLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 333
Cdd:PRK08149 211 VYATSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPG 289
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19913426  334 RVegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:PRK08149 290 AT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
fliI PRK08927
flagellar protein export ATPase FliI;
37-396 8.51e-24

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 103.91  E-value: 8.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   37 PRVTYRTVCSVNGPLV----VLDRVKFAQYAEIVHFtlpDGTQRSGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDI 112
Cdd:PRK08927  14 TLVIYGRVVAVRGLLVevagPIHALSVGARIVVETR---GGRPVPCEVVGFRGDRALLMPFGPLEGV-RRGCRAVIANAA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  113 LRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGl 191
Cdd:PRK08927  90 AAVRPSRAWLGRVVNALGEPIDgKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSG- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  192 phneiaaqicrqaglVKKSK--AVLDYHDDNFAIVFAAMGvnmETAR----FFKSDFEQNGTMGNVcLFLNLANDPTIER 265
Cdd:PRK08927 169 ---------------VGKSVllSMLARNADADVSVIGLIG---ERGRevqeFLQDDLGPEGLARSV-VVVATSDEPALMR 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  266 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQI 345
Cdd:PRK08927 230 RQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGL 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19913426  346 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:PRK08927 309 FTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
109-394 3.58e-23

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 102.45  E-value: 3.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  109 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVmAEDFLDIN----G----QPINphsriypeEMIQTGISPIDVMNSIAR 179
Cdd:PRK09281  91 TGRILEVPVGEALLGRVVNPLGQPIDgKGPIE-ATETRPVErkapGvidrKSVH--------EPLQTGIKAIDAMIPIGR 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  180 GQKIPIfsaaglphneiaaqIC-RQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFL 255
Cdd:PRK09281 162 GQRELI--------------IGdRQTG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVA 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  256 NLANDPTIERIITPRLALTTAEFLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERA 332
Cdd:PRK09281 226 ATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERA 301
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913426  333 GRV--EGRGGSITQIPIL-TMPNDdITHPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:PRK09281 302 AKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
fliI PRK08972
flagellar protein export ATPase FliI;
116-431 4.88e-23

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 101.70  E-value: 4.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  116 PVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHN 194
Cdd:PRK08972  98 PVGMSLLGRVIDGVGNPLDgLGPI-YTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  195 EIAAQICRqaglvkKSKAVLdyhddnfaIVFAAMGvnmETARFFKSDFEQ----NGTMGNVCLFLNLANDPTIeRIITPR 270
Cdd:PRK08972 177 VLLGMMTR------GTTADV--------IVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RLKGCE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  271 LALTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTM 350
Cdd:PRK08972 239 TATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLT 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  351 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVS---NQLYACYAIGKDVQ 427
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDLI 392

                 ....
gi 19913426  428 AMKA 431
Cdd:PRK08972 393 SIGA 396
fliI PRK07196
flagellar protein export ATPase FliI;
72-452 4.99e-23

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 101.51  E-value: 4.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   72 DGTQRSGQVLEVAGTKAIVQVFEGTSGI--DARKTTCEFTGDILrtpVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDIN 148
Cdd:PRK07196  48 DETFIEAQVVGFDRDITYLMPFKHPGGVlgGARVFPSEQDGELL---IGDSWLGRVINGLGEPLDgKGQL-GGSTPLQQQ 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  149 GQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAM 228
Cdd:PRK07196 124 LPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITR--------------YTQADVVVVGLI 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  229 GVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFlaYQCEKH-VLVILTDMSSYAEALREVSAA 307
Cdd:PRK07196 190 GERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATY--YRDKGHdVLLLVDSLTRYAMAQREIALS 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  308 REEVPGRRGFPGYMYTDLATIYERAGRVEGrGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPIN 387
Cdd:PRK07196 268 LGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAID 346
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19913426  388 VLPSLSRLMKSAIGegmtrKDHGDVSNQLYACYAIGKDVQAMKA----VVGEEALTSEDLLYLEFLQKF 452
Cdd:PRK07196 347 ISQSISRCMSQVIG-----SQQAKAASLLKQCYADYMAIKPLIPlggyVAGADPMADQAVHYYPAITQF 410
PRK05922 PRK05922
type III secretion system ATPase; Validated
116-394 7.25e-22

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 98.05  E-value: 7.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  116 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 195
Cdd:PRK05922  93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  196 IAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLA 272
Cdd:PRK05922 173 LLSTI------AKGSKSTIN--------VIALIG---ERGREVREYIEQHKEglaAQRTIIIASPAHETAPTKVIAGRAA 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  273 LTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrGGSITQI-PILTMP 351
Cdd:PRK05922 236 MTIAEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYP 312
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 19913426  352 NdditHP--IPDLTGFITEGQIYVDRQlHNRQIYPPINVLPSLSR 394
Cdd:PRK05922 313 N----HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
60-394 2.41e-21

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: 97.03  E-value: 2.41e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  60 AQYAEIVHFtlPDGTQrsGQVL-----EVAgtkaiVQVFEGTSGIDArKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID 134
Cdd:COG0056  47 AMAGELLEF--PGGVY--GMALnleedNVG-----VVLLGDYEGIKE-GDTVKRTGRILSVPVGEALLGRVVDPLGRPID 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 135 -KGPVVmAEDFLDING--------QPINphsriypeEMIQTGISPIDVMNSIARGQKipifsaaglphnEIaaqIC--RQ 203
Cdd:COG0056 117 gKGPIE-AEERRPVERpapgvidrQPVH--------EPLQTGIKAIDAMIPIGRGQR------------EL---IIgdRQ 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 204 AGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLA 280
Cdd:COG0056 173 TG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFM 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 281 YQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDDI 355
Cdd:COG0056 251 DQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTALPIIETQAGDV 326
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 19913426 356 THPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:COG0056 327 SAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
114-396 1.46e-20

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: 91.51  E-value: 1.46e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPinPH-SRIYPE-EMIQTGISPIDVMNSIARGQKIPIFSAAG- 190
Cdd:cd01133   1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA--PEfVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGv 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 191 --------LPHNeIAAqicRQAGLVkkskavldyhddnfaiVFAAMGvnmETAR--------FFKSDFEQNGTMGNVCLF 254
Cdd:cd01133  79 gktvlimeLINN-IAK---AHGGYS----------------VFAGVG---ERTRegndlyheMKESGVINLDGLSKVALV 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 255 LNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 334
Cdd:cd01133 136 YGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITS 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19913426 335 VegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:cd01133 216 T--KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
PRK07165 PRK07165
ATP F0F1 synthase subunit alpha;
130-420 6.54e-18

ATP F0F1 synthase subunit alpha;


Pssm-ID: 235951 [Multi-domain]  Cd Length: 507  Bit Score: 86.57  E-value: 6.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  130 GKPID-KGPVVMAEDFLDINGQPINPHSRIYP-----------EEMIQTGISPIDVMNSIARGQKIPIFSAaglphneia 197
Cdd:PRK07165  81 GKIIDiDGNIIYPEAQNPLSKKFLPNTSSIFNlahglmtvktlNEQLYTGIIAIDLLIPIGKGQRELIIGD--------- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  198 aqicRQAGlvKKSKA---VLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPtIERIITPRLALT 274
Cdd:PRK07165 152 ----RQTG--KTHIAlntIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMA 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  275 TAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILTMPNDD 354
Cdd:PRK07165 225 HAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNR-KTITALPILQTVDND 301
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19913426  355 ITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLmKSAIGEGMTRKDHGDVsNQLYACY 420
Cdd:PRK07165 302 ITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRT-GSSVQSKTITKVAGEI-SKIYRAY 365
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
248-394 8.98e-18

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: 83.78  E-value: 8.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 248 MGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLAT 327
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19913426 328 IYERAGRVE-----GRGGSITQIPILTMPNDDITHPIPDLTGFITegQIY--VDRQLHNRQIYPPINVLPSLSR 394
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
109-404 2.06e-16

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 82.01  E-value: 2.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  109 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLD-------INGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQ 181
Cdd:PTZ00185 111 TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTRSRALLEseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQ 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  182 KIPIFSAAGLPHNEIA-AQICRQaglVKKSKAVLDyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAND 260
Cdd:PTZ00185 191 RELIVGDRQTGKTSIAvSTIINQ---VRINQQILS--KNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAE 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  261 PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GRG 339
Cdd:PTZ00185 266 PAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKG 344
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19913426  340 G-SITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 404
Cdd:PTZ00185 345 GgSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
248-393 2.18e-15

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 79.30  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   248 MGNVCLFLNLANDPTIERIITPRLALTTAEFlaYQCEKHVLVILTDMSS-YAEALREVSAAREEVPGRRGFPGYMYTDLA 326
Cdd:PRK14698  717 MERTVLIANTSNMPVAAREASIYTGITIAEY--FRDMGYDVALMADSTSrWAEALREISGRLEEMPGEEGYPAYLASKLA 794
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19913426   327 TIYERAGRV-----EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 393
Cdd:PRK14698  795 EFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
atpB CHL00060
ATP synthase CF1 beta subunit
109-459 7.24e-15

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 77.00  E-value: 7.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  109 TGDILRTPVSEDMLGRVFNGSGKPIDK-GPVVMAEDFldingqPINPHSRIYPE-----EMIQTGISPIDVMNSIARGQK 182
Cdd:CHL00060  90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTS------PIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  183 IPIFSAAGLPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMG--------VNMETaRFFKSDFEQNGTMGN 250
Cdd:CHL00060 164 IGLFGGAGVGKTvlimELINNIAKAHGGVS---------------VFGGVGertregndLYMEM-KESGVINEQNIAESK 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  251 VCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 330
Cdd:CHL00060 228 VALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  331 RAGRVegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmtrkdhg 410
Cdd:CHL00060 308 RITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRI---------- 375
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19913426  411 dVSNQLYAC----------YaigKDVQAMKAVVGEEALTSEDLLYLEFLQKFEkNFINQ 459
Cdd:CHL00060 376 -VGEEHYETaqrvkqtlqrY---KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 429
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
43-450 7.32e-14

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 74.05  E-value: 7.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426   43 TVCSVNGPLVVLDRVKFAQYAEIVHFtlpdGTQR-SGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDilrtPVSED- 120
Cdd:PRK04192   6 KIVRVSGPLVVAEGMGGARMYEVVRV----GEEGlIGEIIRIEGDKATIQVYEETSGI-KPGEPVEFTGE----PLSVEl 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  121 ---MLGRVFNG-----------SGKPIDKG---------------PVVMAEDFL---DINGQ-------------PINPH 155
Cdd:PRK04192  77 gpgLLGSIFDGiqrpldelaekSGDFLERGvyvpaldrekkweftPTVKVGDKVeagDILGTvqetpsiehkimvPPGVS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  156 SRI----------------------------------------------YPEEMIQTGISPIDVMNSIARGQK--IPIFS 187
Cdd:PRK04192 157 GTVkeivsegdytvddtiavlededgegveltmmqkwpvrrprpykeklPPVEPLITGQRVIDTFFPVAKGGTaaIPGPF 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  188 AAG---LPHneiaaQICRQAglvkkskavldyhdDNFAIVFAAMGvnmetarffksdfEQNGTMGNV------------- 251
Cdd:PRK04192 237 GSGktvTQH-----QLAKWA--------------DADIVIYVGCG-------------ERGNEMTEVleefpelidpktg 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  252 -------CLFLNLANDPTIER---IITprlALTTAEF---LAYqcekHVLVILTDMSSYAEALREVSAAREEVPGRRGFP 318
Cdd:PRK04192 285 rplmertVLIANTSNMPVAAReasIYT---GITIAEYyrdMGY----DVLLMADSTSRWAEALREISGRLEEMPGEEGYP 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  319 GYMYTDLATIYERAGRVE---GRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSrL 395
Cdd:PRK04192 358 AYLASRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-L 436
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19913426  396 MKSAIGEGMTRK---DHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLE--------FLQ 450
Cdd:PRK04192 437 YLDQVAPWWEENvdpDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEvarliredFLQ 502
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
43-442 9.11e-13

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: 70.12  E-value: 9.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  43 TVCSVNGPlvVLDrVKFAQYA-----EIVHFTLPDGTQRsgqVLEVA-----GT-KAIVqvFEGTSGIdARKTTCEFTGD 111
Cdd:COG0055   7 KIVQVIGP--VVD-VEFPEGElpaiyNALEVENEGGGEL---VLEVAqhlgdNTvRCIA--MDSTDGL-VRGMEVIDTGA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 112 ILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAG- 190
Cdd:COG0055  78 PISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGv 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 191 --------LPHNeIAAQicrQAGLVkkskavldyhddnfaiVFAAMGvnmETARF---FKSDFEQNGTMGNVCLFLNLAN 259
Cdd:COG0055 158 gktvlimeLIHN-IAKE---HGGVS----------------VFAGVG---ERTREgndLYREMKESGVLDKTALVFGQMN 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 260 DPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRG 339
Cdd:COG0055 215 EPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITST--KK 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426 340 GSITQIPILTMPNDDITHPIP-------DLTgfitegqIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHGD 411
Cdd:COG0055 293 GSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE-----EHYR 360
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 19913426 412 VSN------QLYacyaigKDVQAMKAVVGEEALTSED 442
Cdd:COG0055 361 VARevqrilQRY------KELQDIIAILGMDELSEED 391
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
44-110 1.45e-10

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: 57.17  E-value: 1.45e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426    44 VCSVNGPLVVLDRVKFAQYAE--IVHFTLPD-GTQRSGQVLEVAGTKAIVQVFEGTSGIDaRKTTCEFTG 110
Cdd:pfam02874   1 IVQVIGPVVDVEFGIGRLPGLlnALEVELVEfGSLVLGEVLNLGGDKVRVQVFGGTSGLS-RGDEVKRTG 69
ATP-synt_F1_V1_A1_AB_FliI_C cd01429
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
409-479 1.11e-08

ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.


Pssm-ID: 349744 [Multi-domain]  Cd Length: 70  Bit Score: 51.68  E-value: 1.11e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19913426 409 HGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKnFINQGPYENRSVFESLDLGWKLLR 479
Cdd:cd01429   1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPETIEDTLEKLYPIKE 70
ATP-synt_F1_V1_A1_AB_FliI_N cd01426
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
41-111 3.93e-08

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


Pssm-ID: 349738 [Multi-domain]  Cd Length: 73  Bit Score: 50.39  E-value: 3.93e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19913426  41 YRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDG---TQRSGQVLEVAGTKAIVQVFEGTSGIDaRKTTCEFTGD 111
Cdd:cd01426   1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLS-RGALVEPTGR 73
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
44-134 3.50e-04

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 43.47  E-value: 3.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426    44 VCSVNGPLVVLDRVKFAQYAEIVHFtlpDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTcEFTGDILRTPVSEDMLG 123
Cdd:PRK14698    7 IIRVTGPLVIADGMKGAKMYEVVRV---GELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPV-EGTGSSLSVELGPGLLT 82
                          90
                  ....*....|.
gi 19913426   124 RVFNGSGKPID 134
Cdd:PRK14698   83 SIYDGIQRPLE 93
ATP-synt_V_A-type_alpha_N cd18119
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of ...
43-99 2.96e-03

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


Pssm-ID: 349743 [Multi-domain]  Cd Length: 67  Bit Score: 36.35  E-value: 2.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913426  43 TVCSVNGPLVVLDRVKFAQYAEIV---HFTLPdgtqrsGQVLEVAGTKAIVQVFEGTSGI 99
Cdd:cd18119   3 KIYRVSGPVVVAEGMSGAAMYELVrvgEEGLI------GEIIRLEGDKATIQVYEETSGL 56
 
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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