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Conserved domains on  [gi|19913428|ref|NP_001684|]
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V-type proton ATPase subunit B, brain 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 ...
46-509 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: 1027.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428    46 TYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSE 125
Cdd:TIGR01040   1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   126 DMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQ 205
Cdd:TIGR01040  81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   206 ICRQAGLVKKS-KDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEF 284
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   285 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 364
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   365 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEAL 444
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19913428   445 TSDDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSA 509
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 ...
46-509 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: 1027.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428    46 TYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSE 125
Cdd:TIGR01040   1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   126 DMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQ 205
Cdd:TIGR01040  81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   206 ICRQAGLVKKS-KDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEF 284
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   285 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 364
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   365 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEAL 444
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19913428   445 TSDDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSA 509
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
NtpB COG1156
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ...
43-511 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: 846.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  43 PRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTP 122
Cdd:COG1156   2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 123 VSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEI 202
Cdd:COG1156  82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 203 AAQICRQAGLVKkskdvvdySEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTA 282
Cdd:COG1156 162 AAQIARQAKVRG--------EEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAA 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 283 EFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDIT 362
Cdd:COG1156 234 EYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDIT 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 363 HPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEE 442
Cdd:COG1156 314 HPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEE 393
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19913428 443 ALTSDDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH 511
Cdd:COG1156 394 ALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRAKE 462
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
47-510 0e+00

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 822.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   47 YKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSED 126
Cdd:PRK04196   4 YRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSED 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  127 MLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQI 206
Cdd:PRK04196  84 MLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  207 CRQAGLVKkskdvvdySEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLA 286
Cdd:PRK04196 164 ARQAKVLG--------EEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  287 YQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIP 366
Cdd:PRK04196 236 FEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPIP 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  367 DLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTS 446
Cdd:PRK04196 316 DLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSE 395
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19913428  447 DDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAK 510
Cdd:PRK04196 396 RDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRGK 459
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
118-407 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: 616.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 118 ILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGL 197
Cdd:cd01135   1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 198 PHNEIAAQICRQAGLVKkskdvvdySEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRL 277
Cdd:cd01135  81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 278 ALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMP 357
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 19913428 358 NDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 407
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
173-399 4.10e-110

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: 325.47  E-value: 4.10e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   173 GISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvkkSKDVVdyseenfaiVFAAMGVNMETARFFKSDFEENG 252
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA-----SADVV---------VYALIGERGREVREFIEELLGSG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   253 SMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 332
Cdd:pfam00006  67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913428   333 TIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLS 399
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 ...
46-509 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: 1027.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428    46 TYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSE 125
Cdd:TIGR01040   1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   126 DMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQ 205
Cdd:TIGR01040  81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   206 ICRQAGLVKKS-KDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEF 284
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   285 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 364
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   365 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEAL 444
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19913428   445 TSDDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSA 509
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
NtpB COG1156
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ...
43-511 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: 846.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  43 PRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTP 122
Cdd:COG1156   2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 123 VSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEI 202
Cdd:COG1156  82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 203 AAQICRQAGLVKkskdvvdySEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTA 282
Cdd:COG1156 162 AAQIARQAKVRG--------EEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAA 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 283 EFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDIT 362
Cdd:COG1156 234 EYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDIT 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 363 HPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEE 442
Cdd:COG1156 314 HPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEE 393
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19913428 443 ALTSDDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH 511
Cdd:COG1156 394 ALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRAKE 462
PRK04196 PRK04196
V-type ATP synthase subunit B; Provisional
47-510 0e+00

V-type ATP synthase subunit B; Provisional


Pssm-ID: 235251 [Multi-domain]  Cd Length: 460  Bit Score: 822.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   47 YKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSED 126
Cdd:PRK04196   4 YRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSED 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  127 MLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQI 206
Cdd:PRK04196  84 MLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  207 CRQAGLVKkskdvvdySEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLA 286
Cdd:PRK04196 164 ARQAKVLG--------EEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  287 YQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIP 366
Cdd:PRK04196 236 FEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPIP 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  367 DLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTS 446
Cdd:PRK04196 316 DLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSE 395
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19913428  447 DDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAK 510
Cdd:PRK04196 396 RDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRGK 459
ATP_syn_B_arch TIGR01041
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ...
47-510 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: 711.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428    47 YKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSED 126
Cdd:TIGR01041   2 YSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSED 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   127 MLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQI 206
Cdd:TIGR01041  82 MLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   207 CRQAglvkkskdVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLA 286
Cdd:TIGR01041 162 ARQA--------TVRGEESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   287 YQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIP 366
Cdd:TIGR01041 234 FEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   367 DLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTS 446
Cdd:TIGR01041 314 DLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSE 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19913428   447 DDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAK 510
Cdd:TIGR01041 394 RDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYHPKYRKK 457
V_A-ATPase_B cd01135
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ...
118-407 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: 616.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 118 ILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGL 197
Cdd:cd01135   1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 198 PHNEIAAQICRQAGLVKkskdvvdySEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRL 277
Cdd:cd01135  81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 278 ALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMP 357
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 19913428 358 NDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 407
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
PRK02118 PRK02118
V-type ATP synthase subunit B; Provisional
47-506 5.66e-120

V-type ATP synthase subunit B; Provisional


Pssm-ID: 179373 [Multi-domain]  Cd Length: 436  Bit Score: 359.35  E-value: 5.66e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   47 YKTVSGVNGPLVILDhVKFPRYAEIVHLTLPDGTKRSgQVLEVSGSKAVVQVFEGTSGIdakKTSCE--FTGDILRTPVS 124
Cdd:PRK02118   5 YTKITDITGNVITVE-AEGVGYGELATVERKDGSSLA-QVIRLDGDKVTLQVFGGTRGI---STGDEvvFLGRPMQVTYS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  125 EDMLGRVFNGSGKPIDRGPVvLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAA 204
Cdd:PRK02118  80 ESLLGRRFNGSGKPIDGGPE-LEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  205 QICRQAglvkkskdvvdyseENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEF 284
Cdd:PRK02118 159 RIALQA--------------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEK 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  285 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITHP 364
Cdd:PRK02118 225 FALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHP 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  365 IPDLTGYITEGQIYvdrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRKDHADVSN---QLYACYAIGKDVQAMkavvGE 441
Cdd:PRK02118 304 VPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GF 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913428  442 EaLTSDDLLYLEFLQKFERNFIAQGPyeNRTVFETLDIGWQLL-RIF-PKEMLkrIPQSTLSEFYPR 506
Cdd:PRK02118 371 K-LSNWDEKLLKFSELFESRLMDLEV--NIPLEEALDLGWKILaQCFhPEEVG--IKEQLIDKYWPK 432
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
173-399 4.10e-110

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: 325.47  E-value: 4.10e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   173 GISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvkkSKDVVdyseenfaiVFAAMGVNMETARFFKSDFEENG 252
Cdd:pfam00006   1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA-----SADVV---------VYALIGERGREVREFIEELLGSG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   253 SMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 332
Cdd:pfam00006  67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913428   333 TIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLS 399
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 ...
120-401 2.57e-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: 310.54  E-value: 2.57e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 120 RTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 199
Cdd:cd19476   1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 200 NEIAAQICRQAGlvkkskdvvdySEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLAL 279
Cdd:cd19476  81 TVLAMQLARNQA-----------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 280 TTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPND 359
Cdd:cd19476 150 TIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGD 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 19913428 360 DITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 401
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 ...
409-503 3.30e-62

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: 198.04  E-value: 3.30e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 409 GMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFP 488
Cdd:cd18112   1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
                        90
                ....*....|....*
gi 19913428 489 KEMLKRIPQSTLSEF 503
Cdd:cd18112  81 KEELKRISEEYIDKY 95
ATPase_flagellum-secretory_path_III cd01136
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ...
120-401 5.19e-45

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: 158.88  E-value: 5.19e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 120 RTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 199
Cdd:cd01136   1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 200 NEIAAQICRQAGlvkksKDVVdyseenfaiVFAAMGvnmETAR----FFKSDFEENGsMDNVCLFLNLANDPTIERIITP 275
Cdd:cd01136  81 STLLGMIARNTD-----ADVN---------VIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 276 RLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILT 355
Cdd:cd01136 143 YTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVL 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 19913428 356 MPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 401
Cdd:cd01136 220 VEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
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 ...
46-117 1.20e-39

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: 137.95  E-value: 1.20e-39
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19913428  46 TYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGD 117
Cdd:cd18118   1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
PRK06936 PRK06936
EscN/YscN/HrcN family type III secretion system ATPase;
115-477 8.02e-38

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


Pssm-ID: 180762 [Multi-domain]  Cd Length: 439  Bit Score: 144.12  E-value: 8.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  115 TGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSA 194
Cdd:PRK06936  91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  195 AGLPHNEIAAQICRQAglvkkSKDVVdyseenfaiVFAAMGV-NMETARFFKSDFEENGsMDNVCLFLNLANDPTIERII 273
Cdd:PRK06936 171 AGGGKSTLLASLIRSA-----EVDVT---------VLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  274 TPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRNGSITQIPI 353
Cdd:PRK06936 236 AGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYT 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  354 LTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGegmtrKDHADVSNQLYACYAIGKDVQ 433
Cdd:PRK06936 313 VLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVS-----KEHKTWAGRLRELLAKYEEVE 387
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 19913428  434 AMkAVVGEEALTSDDLLYlEFLQKFE--RNFIAQGPYENRTVFETL 477
Cdd:PRK06936 388 LL-LQIGEYQKGQDKEAD-QAIERIGaiRGFLRQGTHELSHFNETL 431
FliI COG1157
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ...
49-402 9.31e-38

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: 143.63  E-value: 9.31e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  49 TVSGVNGPLVildHVKFPRYA--EIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIdAKKTSCEFTGDILRTPVSED 126
Cdd:COG1157  22 RVTRVVGLLI---EAVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 127 MLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCR--IypEEMIQTGISAIDGMNSIARGQKIPIFSAAG------Lp 198
Cdd:COG1157  98 LLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 199 hneiaAQICRQAglvkkSKDVV------------------DYSEENFA--IVFAAmgvnmeTarffkSDfeengsmdnvc 258
Cdd:COG1157 175 -----GMIARNT-----EADVNvialigergrevrefiedDLGEEGLArsVVVVA------T-----SD----------- 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 259 lflnlanDPTIERIITPRLALTTAEFLAYQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIY 335
Cdd:COG1157 223 -------EPPLMRLRAAYTATAIAEYFRDQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLL 291
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19913428 336 ERAGRveGRNGSITQI-PILTmPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 402
Cdd:COG1157 292 ERAGN--GGKGSITAFyTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
atpA TIGR00962
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ...
115-405 2.40e-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: 143.68  E-value: 2.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   115 TGDILRTPVSEDMLGRVFNGSGKPID-RGPVVlAEDFLDImgQPINPQC--RIYPEEMIQTGISAIDGMNSIARGQKIPI 191
Cdd:TIGR00962  90 TGRILEVPVGDGLLGRVVNALGEPIDgKGPID-SDEFSPV--EKIAPGVieRKSVHEPLQTGIKAIDAMIPIGRGQRELI 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   192 FS--AAGlphneiAAQICRQAGLVKKSKDVVdyseenfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTI 269
Cdd:TIGR00962 167 IGdrQTG------KTAVAIDTIINQKDSDVY--------CIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSAS 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   270 ERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGR 344
Cdd:TIGR00962 233 LQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKG 308
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19913428   345 NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 405
Cdd:TIGR00962 309 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAA 369
PRK06820 PRK06820
EscN/YscN/HrcN family type III secretion system ATPase;
85-484 2.10e-36

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


Pssm-ID: 180712 [Multi-domain]  Cd Length: 440  Bit Score: 139.95  E-value: 2.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   85 QVLEVSGSKAVVQVFEGTSGIDAKKTsCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVvLAEDFLDIMGQPINPQCRI 164
Cdd:PRK06820  64 EVVSIEQEMALLSPFASSDGLRCGQW-VTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLTRQ 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  165 YPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICrqaglvkkskdvvDYSEENfAIVFAAMGV-NMETARF 243
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC-------------ADSAAD-VMVLALIGErGREVREF 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  244 FKSDFEENGSMDNVcLFLNLANDPTIERIITPRLALTTAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGF 323
Cdd:PRK06820 208 LEQVLTPEARARTV-VVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSF 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  324 PGYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK 403
Cdd:PRK06820 286 PPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMP 363
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  404 SAIGEGmtRKDHADVSNQLYACYaigKDVQAMKAVvgEEALTSDDLLYLEFLQKFE--RNFIAQGPYENRTVFETLDIGW 481
Cdd:PRK06820 364 QIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEHLA 436

                 ...
gi 19913428  482 QLL 484
Cdd:PRK06820 437 QVV 439
fliI PRK08472
flagellar protein export ATPase FliI;
119-470 1.66e-34

flagellar protein export ATPase FliI;


Pssm-ID: 181439 [Multi-domain]  Cd Length: 434  Bit Score: 134.81  E-value: 1.66e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  119 LRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLP 198
Cdd:PRK08472  90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  199 HNEIAAQIcrqaglVKKSKDVVDyseenfaiVFAAMGvnmETARFFKSDFEEN--GSMDNVCLFLNLANDPTIERIITPR 276
Cdd:PRK08472 170 KSTLMGMI------VKGCLAPIK--------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGAF 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  277 LALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRnGSITQIPILTM 356
Cdd:PRK08472 233 CAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLV 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  357 PNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGegmtrKDHADVSNQLYACYAIGKDVQAMk 436
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIIS-----PEHKLAARKFKRLYSLLKENEVL- 384
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 19913428  437 AVVGEEALTSDDLLYLEFLQK-FERNFIAQGPYEN 470
Cdd:PRK08472 385 IRIGAYQKGNDKELDEAISKKeFMEQFLKQNPNEL 419
F1-ATPase_alpha_CD cd01132
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ...
118-400 3.27e-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: 3.27e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 118 ILRTPVSEDMLGRVFNGSGKPID-RGPVVLAEDFL------DIMG-QPINpqcriypeEMIQTGISAIDGMNSIARGQKI 189
Cdd:cd01132   1 IVEVPVGEALLGRVVDALGNPIDgKGPIQTKERRRveskapGIIPrQSVN--------EPLQTGIKAIDSLIPIGRGQRE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 190 PIFSAaglphneiaaqicRQAGlvkKSKDVVD----YSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLAN 265
Cdd:cd01132  73 LIIGD-------------RQTG---KTAIAIDtiinQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATAS 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 266 DPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV- 341
Cdd:cd01132 137 DPAPLQYLAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLs 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 342 -EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR 400
Cdd:cd01132 213 dELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
atpA CHL00059
ATP synthase CF1 alpha subunit
115-405 1.93e-30

ATP synthase CF1 alpha subunit


Pssm-ID: 176999 [Multi-domain]  Cd Length: 485  Bit Score: 123.92  E-value: 1.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  115 TGDILRTPVSEDMLGRVFNGSGKPID-RGPVVLAEDFL-DIMGQPINPQCRIYpeEMIQTGISAIDGMNSIARGQKIPIF 192
Cdd:CHL00059  70 TGKIAQIPVSEAYLGRVVNALAKPIDgKGEISASESRLiESPAPGIISRRSVY--EPLQTGLIAIDSMIPIGRGQRELII 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  193 SAaglphneiaaqicRQAG---------LVKKSKDVVdyseenfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNL 263
Cdd:CHL00059 148 GD-------------RQTGktavatdtiLNQKGQNVI--------CVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAET 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  264 ANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGR 340
Cdd:CHL00059 207 ADSPATLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAK 282
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913428  341 VEGR--NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 405
Cdd:CHL00059 283 LSSQlgEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
PRK07594 PRK07594
EscN/YscN/HrcN family type III secretion system ATPase;
85-433 1.93e-30

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


Pssm-ID: 136438 [Multi-domain]  Cd Length: 433  Bit Score: 123.14  E-value: 1.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   85 QVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDiLRTPVSEDMLGRVFNGSGKPID--RGPVVLAEDfLDIMGQPinPQC 162
Cdd:PRK07594  56 EVVGINGSKALLSPFTSTIGLHCGQQVMALRRR-HQVPVGEALLGRVIDGFGRPLDgrELPDVCWKD-YDAMPPP--AMV 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  163 RIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskDVVdyseenfaiVFAAMGVNMETAR 242
Cdd:PRK07594 132 RQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA-----DSN---------VLVLIGERGREVR 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  243 FFkSDFEENGSMDNVCLFLNLAND-PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRR 321
Cdd:PRK07594 198 EF-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSG 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  322 GFPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 401
Cdd:PRK07594 276 EYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRV 353
                        330       340       350
                 ....*....|....*....|....*....|..
gi 19913428  402 MKSAIGEgmtrkDHADVSNQLYACYAIGKDVQ 433
Cdd:PRK07594 354 FPVVTSH-----EHRQLAAILRRCLALYQEVE 380
PRK09099 PRK09099
type III secretion system ATPase; Provisional
67-465 9.24e-30

type III secretion system ATPase; Provisional


Pssm-ID: 169656 [Multi-domain]  Cd Length: 441  Bit Score: 121.41  E-value: 9.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   67 RYAEIVHLTLPDGT-KRSGQVLEVSGSKAVVQVFEGTSGIdAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVV 145
Cdd:PRK09099  44 TLGELCELRQRDGTlLQRAEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  146 LAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvkkSKDVVdysee 225
Cdd:PRK09099 123 DCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGT-----QCDVN----- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  226 nfaiVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAE 305
Cdd:PRK09099 193 ----VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRFAR 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  306 ALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHN 385
Cdd:PRK09099 268 AQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAA 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  386 RQIYPPINVLPSLSRLMKSaigegMTRKDHADVSNQLYACYAIGKDVQAMKAvVGEEALTSDDLLYlEFLQKFE--RNFI 463
Cdd:PRK09099 346 RNQYPAIDVLGSLSRVMPQ-----VVPREHVQAAGRLRQLLAKHREVETLLQ-VGEYRAGSDPVAD-EAIAKIDaiRDFL 418

                 ..
gi 19913428  464 AQ 465
Cdd:PRK09099 419 SQ 420
fliI PRK05688
flagellar protein export ATPase FliI;
117-439 3.14e-29

flagellar protein export ATPase FliI;


Pssm-ID: 168181 [Multi-domain]  Cd Length: 451  Bit Score: 119.84  E-value: 3.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  117 DILRTPVSEDMLGRVFNGSGKPID-RGPVVlAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAA 195
Cdd:PRK05688  99 DTGRLPMGMSMLGRVLDGAGRALDgKGPMK-AEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGT 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  196 GLPHNEIAAQICRqaglvkkskdvvdYSEENFAIVfaamGVNMETARFFKSDFEE---NGSMDNVCLFLNLANDPTIERI 272
Cdd:PRK05688 178 GVGKSVLLGMMTR-------------FTEADIIVV----GLIGERGREVKEFIEHilgEEGLKRSVVVASPADDAPLMRL 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  273 ITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIP 352
Cdd:PRK05688 241 RAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFY 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  353 ILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKdhADVSNQLYACYAIGKDV 432
Cdd:PRK05688 320 TVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRR--AQRFKQLWSRYQQSRDL 397

                 ....*..
gi 19913428  433 QAMKAVV 439
Cdd:PRK05688 398 ISVGAYV 404
fliI PRK06002
flagellar protein export ATPase FliI;
2-405 1.00e-28

flagellar protein export ATPase FliI;


Pssm-ID: 235666 [Multi-domain]  Cd Length: 450  Bit Score: 118.56  E-value: 1.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428    2 ALRAMRGIV-NGAAPELPVPTGGPAvgaREqalaVSRnylsqprlTYKTVSGVngplvildhVKFPRYAEIVHLTLPDGT 80
Cdd:PRK06002   6 ALARLAALVeRYAAPEPLVRIGGTV---SE----VTA--------SHYRVRGL---------SRFVRLGDFVAIRADGGT 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   81 KRsGQVLEVSGSKAVVQVFEgtSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPID-RGPVVLAEDFLDIMGQPIN 159
Cdd:PRK06002  62 HL-GEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPIDgLGPLAPGTRPMSIDATAPP 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  160 PQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAG-------LV-KKSKDVVDYSEEnfaivf 231
Cdd:PRK06002 139 AMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAfdtvviaLVgERGREVREFLED------ 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  232 aAMGVNMETARFFKSDFEENGSMdnvclflnlandptieRIITPRLALTTAEFLAYQCEKhVLVILTDMSSYAEALREVS 311
Cdd:PRK06002 213 -TLADNLKKAVAVVATSDESPMM----------------RRLAPLTATAIAEYFRDRGEN-VLLIVDSVTRFAHAAREVA 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  312 AAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPP 391
Cdd:PRK06002 275 LAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPA 354
                        410
                 ....*....|....
gi 19913428  392 INVLPSLSRLMKSA 405
Cdd:PRK06002 355 VDPLASISRLARHA 368
PRK13343 PRK13343
F0F1 ATP synthase subunit alpha; Provisional
115-400 2.52e-28

F0F1 ATP synthase subunit alpha; Provisional


Pssm-ID: 183987 [Multi-domain]  Cd Length: 502  Bit Score: 117.71  E-value: 2.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  115 TGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEdfldiMGQPINpqcRIYPEEM--------IQTGISAIDGMNSIARG 186
Cdd:PRK13343  91 TGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQAT-----ARRPLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGRG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  187 QKIPIFSAAGLPHNEIAAQicrqAGLVKKSKDVVdyseenfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLAND 266
Cdd:PRK13343 163 QRELIIGDRQTGKTAIAID----AIINQKDSDVI--------CVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASD 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  267 PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRN- 345
Cdd:PRK13343 231 PPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELg 309
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19913428  346 -GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR 400
Cdd:PRK13343 310 gGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
fliI PRK07721
flagellar protein export ATPase FliI;
113-431 3.69e-28

flagellar protein export ATPase FliI;


Pssm-ID: 181092 [Multi-domain]  Cd Length: 438  Bit Score: 116.75  E-value: 3.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  113 EFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIF 192
Cdd:PRK07721  85 EATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  193 SAAGLPHNEIAAQICRQAglvkkSKDVvdyseeNfaiVFAAMGVN-METARFFKSDFEENGSMDNVcLFLNLANDPTIER 271
Cdd:PRK07721 165 AGSGVGKSTLMGMIARNT-----SADL------N---VIALIGERgREVREFIERDLGPEGLKRSI-VVVATSDQPALMR 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  272 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQI 351
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGSITAF 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  352 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHADVSN---QLYACYAI 428
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQN 381

                 ...
gi 19913428  429 GKD 431
Cdd:PRK07721 382 SED 384
PRK08149 PRK08149
FliI/YscN family ATPase;
115-401 5.71e-28

FliI/YscN family ATPase;


Pssm-ID: 236166 [Multi-domain]  Cd Length: 428  Bit Score: 115.86  E-value: 5.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  115 TGDILRTPVSEDMLGRVFNGSGKPIDR--GPVVLAEDF--LDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIP 190
Cdd:PRK08149  76 TGKPLSVWVGEALLGAVLDPTGKIVERfdAPPTVGPISeeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  191 IFSAAGLPHNEIAAQICRQA-------GLV-KKSKDVVDYSEEnfaivfaamgvnmetarffksdFEENGSMDNVCLFLN 262
Cdd:PRK08149 156 IFASAGCGKTSLMNMLIEHSeadvfviGLIgERGREVTEFVES----------------------LRASSRREKCVLVYA 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  263 LANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVe 342
Cdd:PRK08149 214 TSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT- 291
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19913428  343 gRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 401
Cdd:PRK08149 292 -LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
46-465 5.95e-28

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: 116.36  E-value: 5.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428    46 TYKTVSGVNGPLVildHVKFPRYA--EIVHLTLPDGTKRSGQVLEVS---GSKAVVQVFEGTSGIDAKKTSCEFTGDILR 120
Cdd:TIGR01039   1 TKGKVVQVIGPVV---DVEFEQGElpRIYNALKVQNRAESELTLEVAqhlGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   121 TPVSEDMLGRVFNGSGKPID-RGPVVLAEDFldimgqPINPQCRIYPE-----EMIQTGISAIDGMNSIARGQKIPIFSA 194
Cdd:TIGR01039  78 VPVGKETLGRIFNVLGEPIDeKGPIPAKERW------PIHRKAPSFEEqstkvEILETGIKVIDLLAPYAKGGKIGLFGG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   195 AGLPHN----EIAAQICRQAGlvkkskdvvDYSeenfaiVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIE 270
Cdd:TIGR01039 152 AGVGKTvliqELINNIAKEHG---------GYS------VFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGA 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   271 RIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQ 350
Cdd:TIGR01039 217 RMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKTGSITS 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   351 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrkDHADVSNQLYACYAIG 429
Cdd:TIGR01039 295 VQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQILQRY 369
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 19913428   430 KDVQAMKAVVGEEALTSDDLLYLEFLQKFERnFIAQ 465
Cdd:TIGR01039 370 KELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
fliI PRK07960
flagellum-specific ATP synthase FliI;
120-460 8.92e-28

flagellum-specific ATP synthase FliI;


Pssm-ID: 181182 [Multi-domain]  Cd Length: 455  Bit Score: 115.65  E-value: 8.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  120 RTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 199
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  200 NEIAAQICR--QAglvkkskDVvdyseenfaIVFAAMGvnmETARFFKsDFEEN-----GSMDNVCLflnlandpTIERI 272
Cdd:PRK07960 189 SVLLGMMARytQA-------DV---------IVVGLIG---ERGREVK-DFIENilgaeGRARSVVI--------AAPAD 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  273 ITPRLALTTAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNG 346
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  347 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKdhADVSNQLYACY 426
Cdd:PRK07960 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR--VRQFKQLLSSF 398
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 19913428  427 AIGKDVQAmkavVGEEALTSDDLL--------YLE-FLQK--FER 460
Cdd:PRK07960 399 QRNRDLVS----VGAYAKGSDPMLdkaialwpQLEaFLQQgiFER 439
fliI PRK06793
flagellar protein export ATPase FliI;
122-431 1.50e-27

flagellar protein export ATPase FliI;


Pssm-ID: 180696 [Multi-domain]  Cd Length: 432  Bit Score: 114.69  E-value: 1.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  122 PVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNE 201
Cdd:PRK06793  92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  202 IAAQICRQAglvKKSKDVVDYSEENfaivfaamgvNMETARFFKSDFEENGsMDNVCLFLNLANDPTIERIITPRLALTT 281
Cdd:PRK06793 172 LLGMIAKNA---KADINVISLVGER----------GREVKDFIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSI 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  282 AEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDD 360
Cdd:PRK06793 238 AEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQ--KGSITGIYTVLVDGDD 312
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19913428  361 ITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHADVSNQLYACYAIGKD 431
Cdd:PRK06793 313 LNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
PRK09281 PRK09281
F0F1 ATP synthase subunit alpha; Validated
115-400 2.40e-25

F0F1 ATP synthase subunit alpha; Validated


Pssm-ID: 236448 [Multi-domain]  Cd Length: 502  Bit Score: 109.00  E-value: 2.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  115 TGDILRTPVSEDMLGRVFNGSGKPID-RGPVVlAEDFLD--------IMGQPINpqcriypeEMIQTGISAIDGMNSIAR 185
Cdd:PRK09281  91 TGRILEVPVGEALLGRVVNPLGQPIDgKGPIE-ATETRPverkapgvIDRKSVH--------EPLQTGIKAIDAMIPIGR 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  186 GQKIPIfsaaglphneiaaqIC-RQAG---------LVKKSKDVVdyseenfaIVFAAMGVNMETARFFKSDFEENGSMD 255
Cdd:PRK09281 162 GQRELI--------------IGdRQTGktaiaidtiINQKGKDVI--------CIYVAIGQKASTVAQVVRKLEEHGAME 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  256 NVCLFLNLANDPTIERIITPRLALTTAEFLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLa 332
Cdd:PRK09281 220 YTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL- 297
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19913428  333 tiYERAGRV--EGRNGSITQIPIL-TMPNDdITHPIPdlTGY--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 400
Cdd:PRK09281 298 --LERAAKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
fliI PRK08972
flagellar protein export ATPase FliI;
122-437 4.46e-25

flagellar protein export ATPase FliI;


Pssm-ID: 181599 [Multi-domain]  Cd Length: 444  Bit Score: 107.48  E-value: 4.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  122 PVSEDMLGRVFNGSGKPID-RGPVvLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHN 200
Cdd:PRK08972  98 PVGMSLLGRVIDGVGNPLDgLGPI-YTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  201 EIAAQICRQAglvkkSKDVvdyseenfaIVFAAMGvnmETARFFKSDFEE----NGSMDNVCLFLNLANDPTIeRIITPR 276
Cdd:PRK08972 177 VLLGMMTRGT-----TADV---------IVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RLKGCE 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  277 LALTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTM 356
Cdd:PRK08972 239 TATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLT 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  357 PNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHADVS---NQLYACYAIGKDVQ 433
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDLI 392

                 ....
gi 19913428  434 AMKA 437
Cdd:PRK08972 393 SIGA 396
fliI PRK07196
flagellar protein export ATPase FliI;
78-427 5.26e-24

flagellar protein export ATPase FliI;


Pssm-ID: 180875 [Multi-domain]  Cd Length: 434  Bit Score: 104.20  E-value: 5.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   78 DGTKRSGQVLEVSGSKAVVQVFEGTSGI--DAKKTSCEFTGDILrtpVSEDMLGRVFNGSGKPID-RGPVVlAEDFLDIM 154
Cdd:PRK07196  48 DETFIEAQVVGFDRDITYLMPFKHPGGVlgGARVFPSEQDGELL---IGDSWLGRVINGLGEPLDgKGQLG-GSTPLQQQ 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  155 GQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskdvvdYSEENFAIVFAAM 234
Cdd:PRK07196 124 LPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITR-------------YTQADVVVVGLIG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  235 GVNMETARFFKSDFEENGSMDNVcLFLNLANDPTIERIITPRLALTTAEFlaYQCEKH-VLVILTDMSSYAEALREVSAA 313
Cdd:PRK07196 191 ERGREVKEFIEHSLQAAGMAKSV-VVAAPADESPLMRIKATELCHAIATY--YRDKGHdVLLLVDSLTRYAMAQREIALS 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  314 REEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPIN 393
Cdd:PRK07196 268 LGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAID 346
                        330       340       350
                 ....*....|....*....|....*....|....
gi 19913428  394 VLPSLSRLMKSAIGegmtrKDHADVSNQLYACYA 427
Cdd:PRK07196 347 ISQSISRCMSQVIG-----SQQAKAASLLKQCYA 375
AtpA COG0056
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ...
115-400 2.95e-23

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: 102.81  E-value: 2.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 115 TGDILRTPVSEDMLGRVFNGSGKPID-RGPVVlAEDFL-------DIMG-QPINpqcriypeEMIQTGISAIDGMNSIAR 185
Cdd:COG0056  91 TGRILSVPVGEALLGRVVDPLGRPIDgKGPIE-AEERRpverpapGVIDrQPVH--------EPLQTGIKAIDAMIPIGR 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 186 GQKipifsaaglphnEIaaqIC--RQAG---------LVKKSKDVVdyseenfaIVFAAMGVNMETARFFKSDFEENGSM 254
Cdd:COG0056 162 GQR------------EL---IIgdRQTGktaiaidtiINQKGKDVI--------CIYVAIGQKASTVAQVVETLEEHGAM 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 255 DNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDL 331
Cdd:COG0056 219 EYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHSRL 297
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19913428 332 atiYERAGRV--EGRNGSITQIPIL-TMPNddithpipDLTGY-------ITEGQIYVDRQLHNRQIYPPINVLPSLSR 400
Cdd:COG0056 298 ---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
PRK05922 PRK05922
type III secretion system ATPase; Validated
122-400 4.97e-23

type III secretion system ATPase; Validated


Pssm-ID: 102061 [Multi-domain]  Cd Length: 434  Bit Score: 101.52  E-value: 4.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  122 PVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNE 201
Cdd:PRK05922  93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  202 IAAQIcrqaglVKKSKDVVDyseenfaiVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTT 281
Cdd:PRK05922 173 LLSTI------AKGSKSTIN--------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTI 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  282 AEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQI-PILTMPNdd 360
Cdd:PRK05922 239 AEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYPN-- 313
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 19913428  361 itHP--IPDLTGYITEGQIYVDRQlHNRQIYPPINVLPSLSR 400
Cdd:PRK05922 314 --HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
fliI PRK08927
flagellar protein export ATPase FliI;
43-402 1.54e-21

flagellar protein export ATPase FliI;


Pssm-ID: 236351 [Multi-domain]  Cd Length: 442  Bit Score: 96.97  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   43 PRLTYKTVSGVNGPLV-ILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIdAKKTSCEFTGDILRT 121
Cdd:PRK08927  14 TLVIYGRVVAVRGLLVeVAGPIHALSVGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGV-RRGCRAVIANAAAAV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  122 PVSEDMLGRVFNGSGKPID-RGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHN 200
Cdd:PRK08927  93 RPSRAWLGRVVNALGEPIDgKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  201 EIAAQICRQAglvkkSKDVvdyseenfaivfAAMGVNMETAR----FFKSDFEENGSMDNVcLFLNLANDPTIERIITPR 276
Cdd:PRK08927 173 VLLSMLARNA-----DADV------------SVIGLIGERGRevqeFLQDDLGPEGLARSV-VVVATSDEPALMRRQAAY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  277 LALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTM 356
Cdd:PRK08927 235 LTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLV 313
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 19913428  357 PNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 402
Cdd:PRK08927 314 DGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
F1-ATPase_beta_CD cd01133
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ...
120-402 5.15e-21

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: 93.05  E-value: 5.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 120 RTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPinpqcriyPE--------EMIQTGISAIDGMNSIARGQKIPI 191
Cdd:cd01133   1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA--------PEfvelsteqEILETGIKVVDLLAPYAKGGKIGL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 192 FSAAG---------LPHNeiaaqicrqaglVKKSKDVvdYSeenfaiVFAAMGvnmETAR--------FFKSDFEENGSM 254
Cdd:cd01133  73 FGGAGvgktvlimeLINN------------IAKAHGG--YS------VFAGVG---ERTRegndlyheMKESGVINLDGL 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 255 DNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 334
Cdd:cd01133 130 SKVALVYGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSL 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19913428 335 YERAGRVegRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 402
Cdd:cd01133 210 QERITST--KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
PRK07165 PRK07165
ATP F0F1 synthase subunit alpha;
124-400 2.71e-19

ATP F0F1 synthase subunit alpha;


Pssm-ID: 235951 [Multi-domain]  Cd Length: 507  Bit Score: 90.80  E-value: 2.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  124 SEDMLGRVFNGSGKPI-DRGPVVLAEDFLD----IMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIF--SAAG 196
Cdd:PRK07165  76 SKEYFGKIIDIDGNIIyPEAQNPLSKKFLPntssIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIgdRQTG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  197 LPH---NEIAAQicrqaglvkkskdvvdySEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPtIERII 273
Cdd:PRK07165 156 KTHialNTIINQ-----------------KNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYL 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  274 TPRLALTTAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNgSITQIPI 353
Cdd:PRK07165 218 APYVAMAHAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK-TITALPI 294
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 19913428  354 LTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR 400
Cdd:PRK07165 295 LQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
254-400 1.25e-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: 86.09  E-value: 1.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 254 MDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLAT 333
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19913428 334 IYERAGRVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR 400
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
49-456 1.85e-17

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 85.22  E-value: 1.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   49 TVSGVNGPLVILDHVKFPRYAEIVHLtlpDGTKRSGQVLEVSGSKAVVQVFEGTSGIdAKKTSCEFTGDilrtPVSED-- 126
Cdd:PRK04192   6 KIVRVSGPLVVAEGMGGARMYEVVRV---GEEGLIGEIIRIEGDKATIQVYEETSGI-KPGEPVEFTGE----PLSVElg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  127 --MLGRVFNG-----------SGKPIDRG---------------PVVLAEDFL---DIMGQ-------------PINPQC 162
Cdd:PRK04192  78 pgLLGSIFDGiqrpldelaekSGDFLERGvyvpaldrekkweftPTVKVGDKVeagDILGTvqetpsiehkimvPPGVSG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  163 RI----------------------------------------------YPEEMIQTGISAIDGMNSIARGQK--IPIFSA 194
Cdd:PRK04192 158 TVkeivsegdytvddtiavlededgegveltmmqkwpvrrprpykeklPPVEPLITGQRVIDTFFPVAKGGTaaIPGPFG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  195 AG---LPHneiaaQICRQAglvkkSKDVVdyseenfaiVFAAMG--VNmETARFFKsDFEE-------NGSMDNVCLFLN 262
Cdd:PRK04192 238 SGktvTQH-----QLAKWA-----DADIV---------IYVGCGerGN-EMTEVLE-EFPElidpktgRPLMERTVLIAN 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  263 LANDPTIER---IITprlALTTAEF---LAYqcekHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 336
Cdd:PRK04192 297 TSNMPVAAReasIYT---GITIAEYyrdMGY----DVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYE 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  337 RAGRVE---GRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSrLMKSAIGEGMTRK 413
Cdd:PRK04192 370 RAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQVAPWWEEN 448
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 19913428  414 DHADVS---NQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLE--------FLQ 456
Cdd:PRK04192 449 VDPDWRelrDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEvarliredFLQ 502
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
254-399 7.35e-16

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 80.84  E-value: 7.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428   254 MDNVCLFLNLANDPTIERIITPRLALTTAEF---LAYQcekhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 330
Cdd:PRK14698  717 MERTVLIANTSNMPVAAREASIYTGITIAEYfrdMGYD----VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASK 792
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19913428   331 LATIYERAGRV-----EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLS 399
Cdd:PRK14698  793 LAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
PTZ00185 PTZ00185
ATPase alpha subunit; Provisional
115-410 1.34e-15

ATPase alpha subunit; Provisional


Pssm-ID: 140212 [Multi-domain]  Cd Length: 574  Bit Score: 79.31  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  115 TGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDI--------MGQPiNPQCRIYPEEMIQTGISAIDGMNSIARG 186
Cdd:PTZ00185 111 TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTRSRALLESeqtlgkvdAGAP-NIVSRSPVNYNLLTGFKAVDTMIPIGRG 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  187 QKIPIFSAAGLPHNEIA-AQICRQaglVKKSKDVVdySEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLAN 265
Cdd:PTZ00185 190 QRELIVGDRQTGKTSIAvSTIINQ---VRINQQIL--SKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAA 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  266 DPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GR 344
Cdd:PTZ00185 265 EPAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGK 343
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19913428  345 NG-SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 410
Cdd:PTZ00185 344 GGgSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
atpB CHL00060
ATP synthase CF1 beta subunit
115-465 1.41e-14

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 75.85  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  115 TGDILRTPVSEDMLGRVFNGSGKPIDR-GPVVLAEDFldimgqPINPQCRIYPE-----EMIQTGISAIDGMNSIARGQK 188
Cdd:CHL00060  90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTS------PIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  189 IPIFSAAGLPHN----EIAAQICRQAGLVKKSKDVVDYSEENFAIvFAAM---GV-NmetarffksdfEENGSMDNVCLF 260
Cdd:CHL00060 164 IGLFGGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGNDL-YMEMkesGViN-----------EQNIAESKVALV 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  261 LNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 340
Cdd:CHL00060 232 YGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  341 VegRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHADVS 419
Cdd:CHL00060 312 T--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----EHYETA 384
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19913428  420 N------QLYacyaigKDVQAMKAVVGEEALTSDDLLYLEFLQKFERnFIAQ 465
Cdd:CHL00060 385 QrvkqtlQRY------KELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 429
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
115-448 7.22e-14

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: 73.59  E-value: 7.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 115 TGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPinpqcriyPE--------EMIQTGISAIDGMNSIARG 186
Cdd:COG0055  75 TGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPA--------PPfeeqstktEILETGIKVIDLLAPYAKG 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 187 QKIPIFSAAG---------LPHNeIAAQicrQAGlvkkskdvvdYSeenfaiVFAAMGvnmETARF---FKSDFEENGSM 254
Cdd:COG0055 147 GKIGLFGGAGvgktvlimeLIHN-IAKE---HGG----------VS------VFAGVG---ERTREgndLYREMKESGVL 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 255 DNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 334
Cdd:COG0055 204 DKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGAL 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428 335 YERAGRVegRNGSITQIPILTMPNDDITHPIP-------DLTgyitegqIYVDRQLHNRQIYPPINVLPSLSRLMKSAI- 406
Cdd:COG0055 284 QERITST--KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIv 354
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 19913428 407 GEgmtrkDHADVSN------QLYacyaigKDVQAMKAVVGEEALTSDD 448
Cdd:COG0055 355 GE-----EHYRVARevqrilQRY------KELQDIIAILGMDELSEED 391
ATP-synt_ab_N pfam02874
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ...
50-116 7.88e-11

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: 57.94  E-value: 7.88e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428    50 VSGVNGPLVILDHVKFPRYAEIVHLTLP---DGTKRSGQVLEVSGSKAVVQVFEGTSGIDaKKTSCEFTG 116
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, ...
415-485 2.37e-10

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: 56.30  E-value: 2.37e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19913428 415 HADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERnFIAQGPYENRTVFETLDIGWQLLR 485
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, ...
47-117 1.20e-09

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: 54.63  E-value: 1.20e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19913428  47 YKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDG---TKRSGQVLEVSGSKAVVQVFEGTSGIDaKKTSCEFTGD 117
Cdd:cd01426   1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLS-RGALVEPTGR 73
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
53-140 3.06e-04

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 43.47  E-value: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428    53 VNGPLVILDHVKFPRYAEIVHLtlpDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKtSCEFTGDILRTPVSEDMLGRVF 132
Cdd:PRK14698   10 VTGPLVIADGMKGAKMYEVVRV---GELGLIGEIIRLEGDKAVIQVYEETAGLKPGE-PVEGTGSSLSVELGPGLLTSIY 85

                  ....*...
gi 19913428   133 NGSGKPID 140
Cdd:PRK14698   86 DGIQRPLE 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 ...
49-105 3.42e-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: 35.96  E-value: 3.42e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19913428  49 TVSGVNGPLVILDHVKFPRYAEIV---HLTLPdgtkrsGQVLEVSGSKAVVQVFEGTSGI 105
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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