|
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 ... |
99-543 |
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: 991.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 99 FAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPV 178
Cdd:TIGR01040 20 FPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 179 VMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKS-KAVLDYH 257
Cdd:TIGR01040 100 VLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKLPtKDVHDGH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 258 DDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSY 337
Cdd:TIGR01040 180 EDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 338 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQL 417
Cdd:TIGR01040 260 ADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 418 HNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFI 497
Cdd:TIGR01040 340 HNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFI 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 767914686 498 NQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 543
Cdd:TIGR01040 420 AQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
102-543 |
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: 822.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 102 YAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMA 181
Cdd:COG1156 27 YGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELPVSEDMLGRVFNGLGRPIDGGPPIIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 182 EDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKskavldyhDDNF 261
Cdd:COG1156 107 EKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVRGE--------EEKF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 262 AIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEAL 341
Cdd:COG1156 179 AVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAAEYLAFEKGMHVLVILTDMTNYCEAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 342 REVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQ 421
Cdd:COG1156 259 REISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIVLSRDLHRKG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 422 IYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGP 501
Cdd:COG1156 339 IYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQGF 418
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 767914686 502 YENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 543
Cdd:COG1156 419 DENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRA 460
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
102-543 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 796.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 102 YAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMA 181
Cdd:PRK04196 25 YGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 182 EDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKskavldyhDDNF 261
Cdd:PRK04196 105 EKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLGE--------EENF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 262 AIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEAL 341
Cdd:PRK04196 177 AVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEAL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 342 REVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQ 421
Cdd:PRK04196 257 REISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 422 IYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGP 501
Cdd:PRK04196 337 IYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQGF 416
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 767914686 502 YENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 543
Cdd:PRK04196 417 DENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRG 458
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
100-538 |
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: 684.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 100 AQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVV 179
Cdd:TIGR01041 21 VAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSEDMLGRILNGSGEPIDGGPEI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 180 MAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKskavldyhDD 259
Cdd:TIGR01041 101 VPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQIARQATVRGE--------ES 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 260 NFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAE 339
Cdd:TIGR01041 173 EFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLAFEKDMHVLVILTDMTNYCE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 340 ALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHN 419
Cdd:TIGR01041 253 ALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIPDLTGYITEGQIVLSRELHR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 420 RQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQ 499
Cdd:TIGR01041 333 KGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSERDRKYLKFADLFERKFVRQ 412
|
410 420 430
....*....|....*....|....*....|....*....
gi 767914686 500 GPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFY 538
Cdd:TIGR01041 413 GFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYH 451
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
152-441 |
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: 620.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 152 ILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGL 231
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 232 PHNEIAAQICRQAGLVKkskavldyHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRL 311
Cdd:cd01135 81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 312 ALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMP 391
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767914686 392 NDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 441
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
91-541 |
2.41e-119 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 359.35 E-value: 2.41e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 91 ISVSATWVfaQYAEIVHFTLPDGTqRSGQVLEVAGTKAIVQVFEGTSGI--DARKTtceFTGDILRTPVSEDMLGRVFNG 168
Cdd:PRK02118 16 ITVEAEGV--GYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGIstGDEVV---FLGRPMQVTYSESLLGRRFNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 169 SGKPIDKGPVVMAEDfLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvk 248
Cdd:PRK02118 90 SGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARIALQA---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 249 kskavldyhdDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVL 328
Cdd:PRK02118 165 ----------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 329 VILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrGGSITQIPILTMPNDDITHPIPDLTGFITE 408
Cdd:PRK02118 235 VLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHPVPDNTGYITE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 409 GQIYvdrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRKDHGDVSN---QLYACYAIGKDVQAMkavvGEEaLTSEDLLY 485
Cdd:PRK02118 314 GQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GFK-LSNWDEKL 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767914686 486 LEFLQKFEKNFINQG---PYEnrsvfESLDLGWKLL-RIF-PKEMLkrIPQAVIDEFYSRE 541
Cdd:PRK02118 380 LKFSELFESRLMDLEvniPLE-----EALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKN 433
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
207-433 |
1.71e-105 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 315.06 E-value: 1.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 207 GISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGlvkkskavldyHDdnfAIVFAAMGVNMETARFFKSDFEQNG 286
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS-----------AD---VVVYALIGERGREVREFIEELLGSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 287 TMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 366
Cdd:pfam00006 67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767914686 367 TIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 433
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 ... |
154-435 |
9.52e-105 |
|
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: 315.55 E-value: 9.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 154 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPH 233
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 234 NEIAAQICRQAglvKKSKAvldyhddnFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLAL 313
Cdd:cd19476 81 TVLAMQLARNQ---AKAHA--------GVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 314 TTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPND 393
Cdd:cd19476 150 TIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767914686 394 DITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 435
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 ... |
443-537 |
1.81e-63 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 202.28 E-value: 1.81e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 443 GMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFP 522
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 767914686 523 KEMLKRIPQAVIDEF 537
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
154-435 |
1.32e-41 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 150.40 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 154 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPH 233
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 234 NEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETAR----FFKSDFEQNGtMGNVCLFLNLANDPTIERIITP 309
Cdd:cd01136 81 STLLGMIAR--------------NTDADVNVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 310 RLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILT 389
Cdd:cd01136 143 YTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767914686 390 MPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 435
Cdd:cd01136 220 VEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
104-439 |
2.19e-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: 144.45 E-value: 2.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 104 EIVHFtlPDGTQRSGQVLEVAGTKAIVqvFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVmAE 182
Cdd:TIGR00962 50 ELIEF--EGGVQGIALNLEEDSVGAVI--MGDYSDI-REGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDgKGPID-SD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 183 DFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGlvKKSKAV---LDYHDD 259
Cdd:TIGR00962 124 EFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGD-------------RQTG--KTAVAIdtiINQKDS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 260 NFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAE 339
Cdd:TIGR00962 189 DVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 340 ALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVD 414
Cdd:TIGR00962 268 AYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 344
|
330 340
....*....|....*....|....*
gi 767914686 415 RQLHNRQIYPPINVLPSLSRLMKSA 439
Cdd:TIGR00962 345 SDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
104-436 |
7.76e-37 |
|
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: 141.71 E-value: 7.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 104 EIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAED 183
Cdd:COG1157 42 ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 184 FLDINGQPINPHSR--IypEEMIQTGISPIDVMNSIARGQKIPIFSAAG------LphneiaAQICRQA-------GLV- 247
Cdd:COG1157 121 RRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL------GMIARNTeadvnviALIg 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 248 -------------------KKSkavldyhddnfaIVFAAmgvnmeTarffkSDfeqngtmgnvclflnlanDPTIERIIT 308
Cdd:COG1157 193 ergrevrefieddlgeeglARS------------VVVVA------T-----SD------------------EPPLMRLRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 309 PRLALTTAEFLAYQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQI 385
Cdd:COG1157 232 AYTATAIAEYFRDQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAF 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 767914686 386 -PILTmPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 436
Cdd:COG1157 306 yTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
119-518 |
4.01e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 137.25 E-value: 4.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 119 QVLEVAGTKAIVQVFEGTSGIDARKTTcEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINPHSRI 198
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGLRCGQWV-TPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 199 YPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETARFF 278
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA--------------DSAADVMVLALIG---ERGREV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 279 KSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLALTTAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRR 355
Cdd:PRK06820 205 REFLEQVLTpeaRARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 356 GFPGYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 435
Cdd:PRK06820 284 SFPPSVFANLPRLLERTGNSDR--GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 436 MKSAIGEGmtRKDHGDVSNQLYACYaigKDVQAMKAVvgEEALTSEDLLYLEFLQKFE--KNFINQGPYENRSVFESLDL 513
Cdd:PRK06820 362 MPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEH 434
|
....*
gi 767914686 514 GWKLL 518
Cdd:PRK06820 435 LAQVV 439
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
149-436 |
1.28e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 135.65 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 149 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSA 228
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 229 AGLPHNEIAAQICRQAglvkkskavldyhdDNFAIVFAAMGV-NMETARFFKSDFEQNGtMGNVCLFLNLANDPTIERII 307
Cdd:PRK06936 171 AGGGKSTLLASLIRSA--------------EVDVTVLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 308 TPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRGGSITQIPI 387
Cdd:PRK06936 236 AGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYT 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767914686 388 LTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 436
Cdd:PRK06936 313 VLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVM 361
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
152-434 |
8.44e-33 |
|
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: 126.52 E-value: 8.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 152 ILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP-INPHSRIYpeEMIQTGISPIDVMNSIARGQKipifsaa 229
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDgKGPIQTKERRRVESKAPgIIPRQSVN--EPLQTGIKAIDSLIPIGRGQR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 230 glphnEIaaqIC--RQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIE 304
Cdd:cd01132 72 -----EL---IIgdRQTG--KTAIAIdtiINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 305 RIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRG 379
Cdd:cd01132 142 QYLAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGG 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767914686 380 GSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 434
Cdd:cd01132 218 GSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
153-442 |
2.27e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 129.03 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 153 LRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLP 232
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 233 HNEIAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQN--GTMGNVCLFLNLANDPTIERIITPR 310
Cdd:PRK08472 170 KSTLMGMI------VKGCLAPIK--------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGAF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 311 LALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILTM 390
Cdd:PRK08472 233 CAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLV 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767914686 391 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGE 442
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
119-442 |
5.59e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 122.37 E-value: 5.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 119 QVLEVAGTKAIVQVFEGTSGIdarktTCEFTGDILR----TPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINP 194
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGL-----HCGQQVMALRrrhqVPVGEALLGRVIDGFGRPLDGRELPDVC-WKDYDAMPPPA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 195 HSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyhDDNfaiVFAAMGVNMET 274
Cdd:PRK07594 130 MVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA-----------DSN---VLVLIGERGRE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 275 ARFFkSDFEQNGTMGNVCLFLNLAND-PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPG 353
Cdd:PRK07594 196 VREF-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 354 RRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 433
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLS 351
|
....*....
gi 767914686 434 RLMKSAIGE 442
Cdd:PRK07594 352 RVFPVVTSH 360
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
151-511 |
8.86e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 122.15 E-value: 8.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 151 DILRTPVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAA 229
Cdd:PRK05688 99 DTGRLPMGMSMLGRVLDGAGRALDgKGPM-KAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 230 GLphneiaaqicrqaglvkkSKAVLDYHDDNFA----IVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIER 305
Cdd:PRK05688 178 GV------------------GKSVLLGMMTRFTeadiIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 306 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQI 385
Cdd:PRK05688 240 LRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 386 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG-EGMTRKDHgdvSNQLYACYAIGK 464
Cdd:PRK05688 319 YTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQSR 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 767914686 465 DVQAMKAVV-GEEALTSEDLLYLEFLQKfeknFINQGPYENRSVFESL 511
Cdd:PRK05688 396 DLISVGAYVaGGDPETDLAIARFPHLVQ----FLRQGLRENVSLAQSR 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
100-436 |
2.60e-29 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 120.64 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 100 AQYAEIVHFTLPDGT--QRsGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGP 177
Cdd:PRK09099 43 VTLGELCELRQRDGTllQR-AEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 178 VVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyh 257
Cdd:PRK09099 121 PLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQC----------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 258 DDNFAIVFAAMGvnMETARFFKSDFEQNGtMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSY 337
Cdd:PRK09099 190 DVNVIALIGERG--REVREFIELILGEDG-MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 338 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQL 417
Cdd:PRK09099 266 ARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREI 343
|
330
....*....|....*....
gi 767914686 418 HNRQIYPPINVLPSLSRLM 436
Cdd:PRK09099 344 AARNQYPAIDVLGSLSRVM 362
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
99-439 |
2.68e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 120.49 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 99 FAQYAEIVHFTLPDGTQRsGQVLEVAGTKAIVQVFEgtSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGP 177
Cdd:PRK06002 46 FVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPIDgLGP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 178 VVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGlphneiaaqicrqaglVKKSK--AVLD 255
Cdd:PRK06002 123 LAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSG----------------VGKSTllAMLA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 256 YHDDNFAIVFAAMGVNMETARFFKSDfeqngTMGNvclflNLANDPTI-----E----RIITPRLALTTAEFLAYQCEKh 326
Cdd:PRK06002 187 RADAFDTVVIALVGERGREVREFLED-----TLAD-----NLKKAVAVvatsdEspmmRRLAPLTATAIAEYFRDRGEN- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 327 VLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFI 406
Cdd:PRK06002 256 VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGT 335
|
330 340 350
....*....|....*....|....*....|...
gi 767914686 407 TEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 439
Cdd:PRK06002 336 LDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
149-439 |
5.63e-29 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 120.07 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 149 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP--InphSRIYPEEMIQTGISPIDVMNSIARGQKIPI 225
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDgKGEISASESRLIESPAPgiI---SRRSVYEPLQTGLIAIDSMIPIGRGQRELI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 226 FSAaglphneiaaqicRQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPT 302
Cdd:CHL00059 147 IGD-------------RQTG--KTAVATdtiLNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 303 IERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRVEGR- 378
Cdd:CHL00059 212 TLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSQl 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767914686 379 -GGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 439
Cdd:CHL00059 288 gEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
149-434 |
8.04e-29 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 120.02 E-value: 8.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 149 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFldingqPINphsRIYPEEM--------IQTGISPIDVMNSIAR 219
Cdd:PRK13343 91 TGRVLEVPVGDGLLGRVIDPLGRPLDgGGPLQATARR------PLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 220 GQKIPIFSAAGLPHNEIAAQicrqaglvkkskAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAN 299
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIAID------------AIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEAS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 300 DPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV--EG 377
Cdd:PRK13343 230 DPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLspEL 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767914686 378 RGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 434
Cdd:PRK13343 309 GGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
141-522 |
2.93e-28 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 117.58 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 141 ARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARG 220
Cdd:PRK07960 96 ARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 221 QKIPIFSAAGLPHNEIAAQICR--QAGLvkkskavldyhddnfaIVFAAMGvnmETARFFKsDFEQN--GTMGnvclfln 296
Cdd:PRK07960 176 QRMGLFAGSGVGKSVLLGMMARytQADV----------------IVVGLIG---ERGREVK-DFIENilGAEG------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 297 LANDPTIERI--ITPRLALTTAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 368
Cdd:PRK07960 229 RARSVVIAAPadVSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPAL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 369 YERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKd 448
Cdd:PRK07960 309 VERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR- 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767914686 449 hgdVSN--QLYACYAIGKDVQAmkavVGEEALTSEDLL--YLEFLQKFEKnFINQGPYEnRSVFEslDLGWKLLRIFP 522
Cdd:PRK07960 388 ---VRQfkQLLSSFQRNRDLVS----VGAYAKGSDPMLdkAIALWPQLEA-FLQQGIFE-RADWE--DSLQALERIFP 454
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
147-524 |
4.60e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 113.66 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 147 EFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIF 226
Cdd:PRK07721 85 EATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 227 SAAGLPHNEIAAQICRQaglvkkSKAVLDyhddnfaiVFAAMGV-NMETARFFKSDFEQNGTMGNVcLFLNLANDPTIER 305
Cdd:PRK07721 165 AGSGVGKSTLMGMIARN------TSADLN--------VIALIGErGREVREFIERDLGPEGLKRSI-VVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 306 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrgGSITQI 385
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS--GSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 386 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSN---QLYACYAi 462
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQ- 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767914686 463 gkdvqamkavvgeealTSEDLLYL------------EFLQKFEK--NFINQGPYENRSVFESLDlgwKLLRIFPKE 524
Cdd:PRK07721 381 ----------------NSEDLINIgaykrgssreidEAIQFYPQiiSFLKQGTDEKATFEESIQ---ALLSLFGKG 437
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
135-499 |
6.67e-27 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 113.66 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 135 GTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFldingqPINPHSRIYPE-----EMIQTGI 208
Cdd:TIGR01039 59 STDGL-VRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDeKGPIPAKERW------PIHRKAPSFEEqstkvEILETGI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 209 SPIDVMNSIARGQKIPIFSAAGLPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMGVNMETARFFKSDFEQ 284
Cdd:TIGR01039 132 KVIDLLAPYAKGGKIGLFGGAGVGKTvliqELINNIAKEHGGYS---------------VFAGVGERTREGNDLYHEMKE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 285 NGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 364
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 365 LATIYERAgrVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEg 443
Cdd:TIGR01039 277 MGELQERI--TSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE- 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 767914686 444 mtrkDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKnFINQ 499
Cdd:TIGR01039 354 ----EHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
156-465 |
2.13e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 111.99 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 156 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 235
Cdd:PRK06793 92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 236 IAAQICRQAglvkksKAvldyhDDNFAIVFAAMGvnMETARFFKSDFEQNGTMGNVcLFLNLANDPTIERIITPRLALTT 315
Cdd:PRK06793 172 LLGMIAKNA------KA-----DINVISLVGERG--REVKDFIRKELGEEGMRKSV-VVVATSDESHLMQLRAAKLATSI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 316 AEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDD 394
Cdd:PRK06793 238 AEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQK--GSITGIYTVLVDGDD 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767914686 395 ITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSNQLYACYAIGKD 465
Cdd:PRK06793 313 LNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| 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 ... |
99-151 |
4.62e-25 |
|
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: 98.27 E-value: 4.62e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 767914686 99 FAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGD 151
Cdd:cd18118 20 GVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
149-435 |
3.55e-24 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 105.08 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 149 TGDILRTPVSEDMLGRVFNGSGKPIDK--GPVVMAEDF--LDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIP 224
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGKIVERfdAPPTVGPISeeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 225 IFSAAGLPHNEIAAQICRQAglvkkskavldyHDDNFAIvfaamGVNMETARF---FKSDFEQNGTMGNVCLFLNLANDP 301
Cdd:PRK08149 156 IFASAGCGKTSLMNMLIEHS------------EADVFVI-----GLIGERGREvteFVESLRASSRREKCVLVYATSDFS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 302 TIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRGGS 381
Cdd:PRK08149 219 SVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGS 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767914686 382 ITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 435
Cdd:PRK08149 296 ITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
149-434 |
1.38e-23 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 103.99 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 149 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVmAEDFLDIN----G----QPINphsriypeEMIQTGISPIDVMNSIAR 219
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQPIDgKGPIE-ATETRPVErkapGvidrKSVH--------EPLQTGIKAIDAMIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 220 GQKIPIfsaaglphneiaaqIC-RQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFL 295
Cdd:PRK09281 162 GQRELI--------------IGdRQTG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 296 NLANDPTIERIITPRLALTTAEFLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERA 372
Cdd:PRK09281 226 ATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERA 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767914686 373 GRV--EGRGGSITQIPIL-TMPNDdITHPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 434
Cdd:PRK09281 302 AKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
156-471 |
1.58e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 103.24 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 156 PVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHN 234
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDgLGPI-YTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 235 EIAAQICRqaglvkKSKAVLdyhddnfaIVFAAMGvnmETARFFKSDFEQ----NGTMGNVCLFLNLANDPTIeRIITPR 310
Cdd:PRK08972 177 VLLGMMTR------GTTADV--------IVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 311 LALTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTM 390
Cdd:PRK08972 239 TATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 391 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVS---NQLYACYAIGKDVQ 467
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDLI 392
|
....
gi 767914686 468 AMKA 471
Cdd:PRK08972 393 SIGA 396
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
112-492 |
1.94e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 103.05 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 112 DGTQRSGQVLEVAGTKAIVQVFEGTSGI--DARKTTCEFTGDILrtpVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDIN 188
Cdd:PRK07196 48 DETFIEAQVVGFDRDITYLMPFKHPGGVlgGARVFPSEQDGELL---IGDSWLGRVINGLGEPLDgKGQL-GGSTPLQQQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 189 GQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAM 268
Cdd:PRK07196 124 LPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITR--------------YTQADVVVVGLI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 269 GVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFlaYQCEKH-VLVILTDMSSYAEALREVSAA 347
Cdd:PRK07196 190 GERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATY--YRDKGHdVLLLVDSLTRYAMAQREIALS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 348 REEVPGRRGFPGYMYTDLATIYERAGRVEGrGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPIN 427
Cdd:PRK07196 268 LGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAID 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767914686 428 VLPSLSRLMKSAIGegmtrKDHGDVSNQLYACYAIGKDVQAMKA----VVGEEALTSEDLLYLEFLQKF 492
Cdd:PRK07196 347 ISQSISRCMSQVIG-----SQQAKAASLLKQCYADYMAIKPLIPlggyVAGADPMADQAVHYYPAITQF 410
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
112-436 |
3.65e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 102.36 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 112 DGTQRSGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQ 190
Cdd:PRK08927 50 GGRPVPCEVVGFRGDRALLMPFGPLEGV-RRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDgKGPLPQGPVPYPLRAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 191 PINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGlphneiaaqicrqaglVKKSK--AVLDYHDDNFAIVFAAM 268
Cdd:PRK08927 129 PPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSG----------------VGKSVllSMLARNADADVSVIGLI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 269 GvnmETAR----FFKSDFEQNGTMGNVcLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREV 344
Cdd:PRK08927 193 G---ERGRevqeFLQDDLGPEGLARSV-VVVATSDEPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 345 SAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYP 424
Cdd:PRK08927 268 GLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYP 347
|
330
....*....|..
gi 767914686 425 PINVLPSLSRLM 436
Cdd:PRK08927 348 AINVLKSVSRTM 359
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
100-434 |
7.18e-22 |
|
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: 98.96 E-value: 7.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 100 AQYAEIVHFtlPDGTQrsGQVL-----EVAgtkaIVqVFEGTSGIDArKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID 174
Cdd:COG0056 47 AMAGELLEF--PGGVY--GMALnleedNVG----VV-LLGDYEGIKE-GDTVKRTGRILSVPVGEALLGRVVDPLGRPID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 175 -KGPVVmAEDFLDING--------QPINphsriypeEMIQTGISPIDVMNSIARGQKipifsaaglphnEIaaqIC--RQ 243
Cdd:COG0056 117 gKGPIE-AEERRPVERpapgvidrQPVH--------EPLQTGIKAIDAMIPIGRGQR------------EL---IIgdRQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 244 AGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLA 320
Cdd:COG0056 173 TG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 321 YQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDDI 395
Cdd:COG0056 251 DQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTALPIIETQAGDV 326
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767914686 396 THPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 434
Cdd:COG0056 327 SAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
156-434 |
1.02e-21 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 97.67 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 156 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 235
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 236 IAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLA 312
Cdd:PRK05922 173 LLSTI------AKGSKSTIN--------VIALIG---ERGREVREYIEQHKEglaAQRTIIIASPAHETAPTKVIAGRAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 313 LTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrGGSITQI-PILTMP 391
Cdd:PRK05922 236 MTIAEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYP 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767914686 392 NdditHP--IPDLTGFITEGQIYVDRQlHNRQIYPPINVLPSLSR 434
Cdd:PRK05922 313 N----HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
154-436 |
8.31e-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: 92.67 E-value: 8.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 154 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPinPH-SRIYPE-EMIQTGISPIDVMNSIARGQKIPIFSAAG- 230
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA--PEfVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 231 --------LPHNeIAAqicRQAGLVkkskavldyhddnfaiVFAAMGvnmETAR--------FFKSDFEQNGTMGNVCLF 294
Cdd:cd01133 79 gktvlimeLINN-IAK---AHGGYS----------------VFAGVG---ERTRegndlyheMKESGVINLDGLSKVALV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 295 LNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 374
Cdd:cd01133 136 YGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITS 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767914686 375 VegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 436
Cdd:cd01133 216 T--KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
170-460 |
6.89e-18 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 86.57 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 170 GKPID-KGPVVMAEDFLDINGQPINPHSRIYP-----------EEMIQTGISPIDVMNSIARGQKIPIFSAaglphneia 237
Cdd:PRK07165 81 GKIIDiDGNIIYPEAQNPLSKKFLPNTSSIFNlahglmtvktlNEQLYTGIIAIDLLIPIGKGQRELIIGD--------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 238 aqicRQAGlvKKSKA---VLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPtIERIITPRLALT 314
Cdd:PRK07165 152 ----RQTG--KTHIAlntIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 315 TAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILTMPNDD 394
Cdd:PRK07165 225 HAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNR-KTITALPILQTVDND 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767914686 395 ITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLmKSAIGEGMTRKDHGDVsNQLYACY 460
Cdd:PRK07165 302 ITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRT-GSSVQSKTITKVAGEI-SKIYRAY 365
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
288-434 |
1.02e-17 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 83.78 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 288 MGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLAT 367
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767914686 368 IYERAGRVE-----GRGGSITQIPILTMPNDDITHPIPDLTGFITegQIY--VDRQLHNRQIYPPINVLPSLSR 434
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
149-444 |
1.58e-16 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 82.78 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 149 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLD-------INGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQ 221
Cdd:PTZ00185 111 TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTRSRALLEseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 222 KIPIFSAAGLPHNEIA-AQICRQaglVKKSKAVLDyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAND 300
Cdd:PTZ00185 191 RELIVGDRQTGKTSIAvSTIINQ---VRINQQILS--KNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 301 PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GRG 379
Cdd:PTZ00185 266 PAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKG 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767914686 380 G-SITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 444
Cdd:PTZ00185 345 GgSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
288-433 |
1.56e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 80.07 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 288 MGNVCLFLNLANDPTIERIITPRLALTTAEF---LAYQcekhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 364
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYfrdMGYD----VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASK 792
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767914686 365 LATIYERAGRV-----EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 433
Cdd:PRK14698 793 LAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
149-499 |
5.21e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 77.77 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 149 TGDILRTPVSEDMLGRVFNGSGKPIDK-GPVVMAEDFldingqPINPHSRIYPE-----EMIQTGISPIDVMNSIARGQK 222
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTS------PIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 223 IPIFSAAGLPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMG--------VNMETaRFFKSDFEQNGTMGN 290
Cdd:CHL00060 164 IGLFGGAGVGKTvlimELINNIAKAHGGVS---------------VFGGVGertregndLYMEM-KESGVINEQNIAESK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 291 VCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 370
Cdd:CHL00060 228 VALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 371 RAGRVegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmtrkdhg 450
Cdd:CHL00060 308 RITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRI---------- 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 767914686 451 dVSNQLYAC----------YaigKDVQAMKAVVGEEALTSEDLLYLEFLQKFEkNFINQ 499
Cdd:CHL00060 376 -VGEEHYETaqrvkqtlqrY---KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 429
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
326-490 |
3.03e-13 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 72.12 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 326 HVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE---GRGGSITQIPILTMPNDDITHPIPDL 402
Cdd:PRK04192 325 DVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQN 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 403 TGFITEGQIYVDRQLHNRQIYPPINVLPSLSrLMKSAIGEGMTRK---DHGDVSNQLYACYAIGKDVQAMKAVVGEEALT 479
Cdd:PRK04192 405 TLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQVAPWWEENvdpDWRELRDEAMDLLQREAELQEIVRLVGPDALP 483
|
170
....*....|....*....
gi 767914686 480 SEDLLYLE--------FLQ 490
Cdd:PRK04192 484 EEDRLILEvarliredFLQ 502
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
136-482 |
4.57e-13 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 71.27 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 136 TSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMN 215
Cdd:COG0055 63 TDGL-VRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 216 SIARGQKIPIFSAAG---------LPHNeIAAQicrQAGLVkkskavldyhddnfaiVFAAMGvnmETARF---FKSDFE 283
Cdd:COG0055 142 PYAKGGKIGLFGGAGvgktvlimeLIHN-IAKE---HGGVS----------------VFAGVG---ERTREgndLYREMK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 284 QNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYT 363
Cdd:COG0055 199 ESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914686 364 DLATIYERAGRVegRGGSITQIPILTMPNDDITHPIP-------DLTgfitegqIYVDRQLHNRQIYPPINVLPSLSRLM 436
Cdd:COG0055 279 EMGALQERITST--KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRIL 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 767914686 437 KSAI-GEgmtrkDHGDVSN------QLYacyaigKDVQAMKAVVGEEALTSED 482
Cdd:COG0055 350 DPLIvGE-----EHYRVARevqrilQRY------KELQDIIAILGMDELSEED 391
|
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| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
449-519 |
1.14e-08 |
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ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 51.68 E-value: 1.14e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767914686 449 HGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKnFINQGPYENRSVFESLDLGWKLLR 519
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPETIEDTLEKLYPIKE 70
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| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
100-150 |
1.91e-06 |
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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: 45.61 E-value: 1.91e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767914686 100 AQYAEIVHFtlpdGTQRSGQVLEVAGTKAIVQVFEGTSGIDaRKTTCEFTG 150
Cdd:pfam02874 24 ALEVELVEF----GSLVLGEVLNLGGDKVRVQVFGGTSGLS-RGDEVKRTG 69
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| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
104-151 |
1.64e-04 |
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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: 39.99 E-value: 1.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 767914686 104 EIVHFTLPDG---TQRSGQVLEVAGTKAIVQVFEGTSGIDaRKTTCEFTGD 151
Cdd:cd01426 24 EVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLS-RGALVEPTGR 73
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