|
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 ... |
11-455 |
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: 980.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 11 FAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPV 90
Cdd:TIGR01040 20 FPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 91 VMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKS-KAVLDYH 169
Cdd:TIGR01040 100 VLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKLPtKDVHDGH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 170 DDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSY 249
Cdd:TIGR01040 180 EDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 250 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQL 329
Cdd:TIGR01040 260 ADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 330 HNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFI 409
Cdd:TIGR01040 340 HNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFI 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1622859044 410 NQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 455
Cdd:TIGR01040 420 AQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
14-455 |
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: 815.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 14 YAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMA 93
Cdd:COG1156 27 YGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELPVSEDMLGRVFNGLGRPIDGGPPIIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 94 EDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKskavldyhDDNF 173
Cdd:COG1156 107 EKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVRGE--------EEKF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 174 AIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEAL 253
Cdd:COG1156 179 AVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAAEYLAFEKGMHVLVILTDMTNYCEAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 254 REVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQ 333
Cdd:COG1156 259 REISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIVLSRDLHRKG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 334 IYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGP 413
Cdd:COG1156 339 IYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQGF 418
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622859044 414 YENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 455
Cdd:COG1156 419 DENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRA 460
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
14-455 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 788.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 14 YAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMA 93
Cdd:PRK04196 25 YGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 94 EDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKskavldyhDDNF 173
Cdd:PRK04196 105 EKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQAKVLGE--------EENF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 174 AIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEAL 253
Cdd:PRK04196 177 AVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEAL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 254 REVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQ 333
Cdd:PRK04196 257 REISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 334 IYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGP 413
Cdd:PRK04196 337 IYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQGF 416
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1622859044 414 YENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 455
Cdd:PRK04196 417 DENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRG 458
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
12-450 |
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: 676.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 12 AQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVV 91
Cdd:TIGR01041 21 VAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSEDMLGRILNGSGEPIDGGPEI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 92 MAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKskavldyhDD 171
Cdd:TIGR01041 101 VPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQIARQATVRGE--------ES 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 172 NFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAE 251
Cdd:TIGR01041 173 EFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLAFEKDMHVLVILTDMTNYCE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 252 ALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHN 331
Cdd:TIGR01041 253 ALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIPDLTGYITEGQIVLSRELHR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 332 RQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQ 411
Cdd:TIGR01041 333 KGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSERDRKYLKFADLFERKFVRQ 412
|
410 420 430
....*....|....*....|....*....|....*....
gi 1622859044 412 GPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFY 450
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 ... |
64-353 |
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: 613.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 64 ILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGL 143
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 144 PHNEIAAQICRQAGLVKkskavldyHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRL 223
Cdd:cd01135 81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 224 ALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMP 303
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622859044 304 NDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 353
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
14-453 |
2.65e-118 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 353.18 E-value: 2.65e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 14 YAEIVHFTLPDGTqRSGQVLEVAGTKAIVQVFEGTSGI--DARKTtceFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVV 91
Cdd:PRK02118 25 YGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGIstGDEVV---FLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 92 MAEDfLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvkkskavldyhdD 171
Cdd:PRK02118 101 EGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARIALQA--------------E 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 172 NFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAE 251
Cdd:PRK02118 166 ADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 252 ALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYvdrqLHN 331
Cdd:PRK02118 246 ALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFY----LRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 332 RQIYPpinvLPSLSRLMKSAIGEgMTRKDHGDVSN---QLYACYAIGKDVQAMkavvGEEaLTSEDLLYLEFLQKFEKNF 408
Cdd:PRK02118 321 GRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GFK-LSNWDEKLLKFSELFESRL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622859044 409 INQG---PYEnrsvfESLDLGWKLL-RIF-PKEMLkrIPQAVIDEFYSRE 453
Cdd:PRK02118 391 MDLEvniPLE-----EALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKN 433
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
119-345 |
6.14e-106 |
|
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: 313.52 E-value: 6.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 119 GISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGlvkkskavldyHDdnfAIVFAAMGVNMETARFFKSDFEQNG 198
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS-----------AD---VVVYALIGERGREVREFIEELLGSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 199 TMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 278
Cdd:pfam00006 67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622859044 279 TIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 345
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 ... |
66-347 |
8.95e-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: 312.85 E-value: 8.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 66 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPH 145
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 146 NEIAAQICRQAglvKKSKAvldyhddnFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLAL 225
Cdd:cd19476 81 TVLAMQLARNQ---AKAHA--------GVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 226 TTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPND 305
Cdd:cd19476 150 TIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622859044 306 DITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 347
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 ... |
355-449 |
5.42e-64 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 201.51 E-value: 5.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 355 GMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFP 434
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 1622859044 435 KEMLKRIPQAVIDEF 449
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
66-347 |
7.94e-42 |
|
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: 149.63 E-value: 7.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 66 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPH 145
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 146 NEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETAR----FFKSDFEQNGtMGNVCLFLNLANDPTIERIITP 221
Cdd:cd01136 81 STLLGMIAR--------------NTDADVNVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 222 RLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILT 301
Cdd:cd01136 143 YTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622859044 302 MPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 347
Cdd:cd01136 220 VEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
16-351 |
2.73e-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: 142.91 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 16 EIVHFtlPDGTQRSGQVLEVAGTKAIVqvFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVmAE 94
Cdd:TIGR00962 50 ELIEF--EGGVQGIALNLEEDSVGAVI--MGDYSDI-REGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDgKGPID-SD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 95 DFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGlvKKSKAV---LDYHDD 171
Cdd:TIGR00962 124 EFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGD-------------RQTG--KTAVAIdtiINQKDS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 172 NFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAE 251
Cdd:TIGR00962 189 DVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 252 ALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVD 326
Cdd:TIGR00962 268 AYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 344
|
330 340
....*....|....*....|....*
gi 1622859044 327 RQLHNRQIYPPINVLPSLSRLMKSA 351
Cdd:TIGR00962 345 SDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
16-348 |
6.68e-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: 140.55 E-value: 6.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 16 EIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAED 95
Cdd:COG1157 42 ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 96 FLDINGQPINPHSR--IypEEMIQTGISPIDVMNSIARGQKIPIFSAAG------LphneiaAQICRQA-------GLV- 159
Cdd:COG1157 121 RRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL------GMIARNTeadvnviALIg 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 160 -------------------KKSkavldyhddnfaIVFAAmgvnmeTarffkSDfeqngtmgnvclflnlanDPTIERIIT 220
Cdd:COG1157 193 ergrevrefieddlgeeglARS------------VVVVA------T-----SD------------------EPPLMRLRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 221 PRLALTTAEFLAYQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQI 297
Cdd:COG1157 232 AYTATAIAEYFRDQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAF 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622859044 298 -PILTmPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 348
Cdd:COG1157 306 yTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
31-430 |
1.58e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 136.87 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 31 QVLEVAGTKAIVQVFEGTSGIDARKTTcEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINPHSRI 110
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGLRCGQWV-TPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 111 YPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETARFF 190
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA--------------DSAADVMVLALIG---ERGREV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 191 KSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLALTTAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRR 267
Cdd:PRK06820 205 REFLEQVLTpeaRARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 268 GFPGYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 347
Cdd:PRK06820 284 SFPPSVFANLPRLLERTGNSDR--GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 348 MKSAIGEGmtRKDHGDVSNQLYACYaigKDVQAMKAVvgEEALTSEDLLYLEFLQKFE--KNFINQGPYENRSVFESLDL 425
Cdd:PRK06820 362 MPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEH 434
|
....*
gi 1622859044 426 GWKLL 430
Cdd:PRK06820 435 LAQVV 439
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
61-348 |
6.80e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 134.88 E-value: 6.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 61 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSA 140
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 141 AGLPHNEIAAQICRQAglvkkskavldyhdDNFAIVFAAMGV-NMETARFFKSDFEQNGtMGNVCLFLNLANDPTIERII 219
Cdd:PRK06936 171 AGGGKSTLLASLIRSA--------------EVDVTVLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 220 TPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRGGSITQIPI 299
Cdd:PRK06936 236 AGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYT 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622859044 300 LTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 348
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 ... |
64-346 |
1.20e-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: 124.98 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 64 ILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP-INPHSRIYpeEMIQTGISPIDVMNSIARGQKIPIFSAa 141
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDgKGPIQTKERRRVESKAPgIIPRQSVN--EPLQTGIKAIDSLIPIGRGQRELIIGD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 142 glphneiaaqicRQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERI 218
Cdd:cd01132 78 ------------RQTG--KTAIAIdtiINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 219 ITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGS 293
Cdd:cd01132 144 LAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGS 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622859044 294 ITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 346
Cdd:cd01132 220 LTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
65-354 |
2.90e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 127.49 E-value: 2.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 65 LRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLP 144
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 145 HNEIAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQN--GTMGNVCLFLNLANDPTIERIITPR 222
Cdd:PRK08472 170 KSTLMGMI------VKGCLAPIK--------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGAF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 223 LALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILTM 302
Cdd:PRK08472 233 CAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLV 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622859044 303 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGE 354
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
9-351 |
2.52e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 122.41 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 9 SSFAQYAEIVHFTLPDGTQRsGQVLEVAGTKAIVQVFEgtSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-K 87
Cdd:PRK06002 44 SRFVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPIDgL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 88 GPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGlphneiaaqicrqaglVKKSK--AV 165
Cdd:PRK06002 121 GPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSG----------------VGKSTllAM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 166 LDYHDDNFAIVFAAMGVNMETARFFKSDfeqngTMGNvclflNLANDPTI---------ERIITPRLALTTAEFLAYQCE 236
Cdd:PRK06002 185 LARADAFDTVVIALVGERGREVREFLED-----TLAD-----NLKKAVAVvatsdespmMRRLAPLTATAIAEYFRDRGE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 237 KhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTG 316
Cdd:PRK06002 255 N-VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIR 333
|
330 340 350
....*....|....*....|....*....|....*
gi 1622859044 317 FITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 351
Cdd:PRK06002 334 GTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
31-354 |
2.77e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 121.98 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 31 QVLEVAGTKAIVQVFEGTSGIdarktTCEFTGDILR----TPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINP 106
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGL-----HCGQQVMALRrrhqVPVGEALLGRVIDGFGRPLDGRELPDVC-WKDYDAMPPPA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 107 HSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyhDDNfaiVFAAMGVNMET 186
Cdd:PRK07594 130 MVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA-----------DSN---VLVLIGERGRE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 187 ARFFkSDFEQNGTMGNVCLFLNLAND-PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPG 265
Cdd:PRK07594 196 VREF-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 266 RRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 345
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLS 351
|
....*....
gi 1622859044 346 RLMKSAIGE 354
Cdd:PRK07594 352 RVFPVVTSH 360
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
63-423 |
1.09e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 120.61 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 63 DILRTPVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAA 141
Cdd:PRK05688 99 DTGRLPMGMSMLGRVLDGAGRALDgKGPM-KAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 142 GLphneiaaqicrqaglvkkSKAVLDYHDDNFA----IVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIER 217
Cdd:PRK05688 178 GV------------------GKSVLLGMMTRFTeadiIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 218 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQI 297
Cdd:PRK05688 240 LRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 298 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG-EGMTRKDHgdvSNQLYACYAIGK 376
Cdd:PRK05688 319 YTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQSR 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622859044 377 DVQAMKAVV-GEEALTSEDLLYLEFLQKfeknFINQGPYENRSVFESL 423
Cdd:PRK05688 396 DLISVGAYVaGGDPETDLAIARFPHLVQ----FLRQGLRENVSLAQSR 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
12-348 |
1.70e-29 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 119.87 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 12 AQYAEIVHFTLPDGT--QRsGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGP 89
Cdd:PRK09099 43 VTLGELCELRQRDGTllQR-AEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 90 VVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyh 169
Cdd:PRK09099 121 PLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQC----------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 170 DDNFAIVFAAMGvnMETARFFKSDFEQNGtMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSY 249
Cdd:PRK09099 190 DVNVIALIGERG--REVREFIELILGEDG-MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 250 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQL 329
Cdd:PRK09099 266 ARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREI 343
|
330
....*....|....*....
gi 1622859044 330 HNRQIYPPINVLPSLSRLM 348
Cdd:PRK09099 344 AARNQYPAIDVLGSLSRVM 362
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
61-351 |
3.27e-29 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 119.68 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 61 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP--InphSRIYPEEMIQTGISPIDVMNSIARGQKIPI 137
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDgKGEISASESRLIESPAPgiI---SRRSVYEPLQTGLIAIDSMIPIGRGQRELI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 138 FSAaglphneiaaqicRQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPT 214
Cdd:CHL00059 147 IGD-------------RQTG--KTAVATdtiLNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 215 IERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRVEGR- 290
Cdd:CHL00059 212 TLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSQl 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622859044 291 -GGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 351
Cdd:CHL00059 288 gEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
61-346 |
6.95e-29 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 118.86 E-value: 6.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 61 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFldingqPINphsRIYPEEM--------IQTGISPIDVMNSIAR 131
Cdd:PRK13343 91 TGRVLEVPVGDGLLGRVIDPLGRPLDgGGPLQATARR------PLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 132 GQKIPIFSAAGLPHNEIAAQicrqaglvkkskAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAN 211
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIAID------------AIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEAS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 212 DPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV--EG 289
Cdd:PRK13343 230 DPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLspEL 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622859044 290 RGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 346
Cdd:PRK13343 309 GGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
53-434 |
2.40e-28 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 116.81 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 53 ARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARG 132
Cdd:PRK07960 96 ARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 133 QKIPIFSAAGLPHNEIAAQICR--QAGLvkkskavldyhddnfaIVFAAMGvnmETARFFKsDFEQN--GTMGnvclfln 208
Cdd:PRK07960 176 QRMGLFAGSGVGKSVLLGMMARytQADV----------------IVVGLIG---ERGREVK-DFIENilGAEG------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 209 LANDPTIERI--ITPRLALTTAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 280
Cdd:PRK07960 229 RARSVVIAAPadVSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPAL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 281 YERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKd 360
Cdd:PRK07960 309 VERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR- 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622859044 361 hgdVSN--QLYACYAIGKDVQAmkavVGEEALTSEDLL--YLEFLQKFEKnFINQGPYEnRSVFEslDLGWKLLRIFP 434
Cdd:PRK07960 388 ---VRQfkQLLSSFQRNRDLVS----VGAYAKGSDPMLdkAIALWPQLEA-FLQQGIFE-RADWE--DSLQALERIFP 454
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
59-377 |
7.22e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 112.12 E-value: 7.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 59 EFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIF 138
Cdd:PRK07721 85 EATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 139 SAAGLPHNEIAAQICRQaglvkkSKAVLDyhddnfaiVFAAMGVN-METARFFKSDFEQNGTMGNVcLFLNLANDPTIER 217
Cdd:PRK07721 165 AGSGVGKSTLMGMIARN------TSADLN--------VIALIGERgREVREFIERDLGPEGLKRSI-VVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 218 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrgGSITQI 297
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS--GSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 298 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSN---QLYACYAI 374
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQN 381
|
...
gi 1622859044 375 GKD 377
Cdd:PRK07721 382 SED 384
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
68-377 |
9.79e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 111.99 E-value: 9.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 68 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 147
Cdd:PRK06793 92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 148 IAAQICRQAglvkksKAvldyhDDNFAIVFAAMGvnMETARFFKSDFEQNGTMGNVcLFLNLANDPTIERIITPRLALTT 227
Cdd:PRK06793 172 LLGMIAKNA------KA-----DINVISLVGERG--REVKDFIRKELGEEGMRKSV-VVVATSDESHLMQLRAAKLATSI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 228 AEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDD 306
Cdd:PRK06793 238 AEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQK--GSITGIYTVLVDGDD 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622859044 307 ITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSNQLYACYAIGKD 377
Cdd:PRK06793 313 LNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
47-411 |
1.56e-26 |
|
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: 111.73 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 47 GTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFldingqPINPHSRIYPE-----EMIQTGI 120
Cdd:TIGR01039 59 STDGL-VRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDeKGPIPAKERW------PIHRKAPSFEEqstkvEILETGI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 121 SPIDVMNSIARGQKIPIFSAAGLPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMGVNMETARFFKSDFEQ 196
Cdd:TIGR01039 132 KVIDLLAPYAKGGKIGLFGGAGVGKTvliqELINNIAKEHGGYS---------------VFAGVGERTREGNDLYHEMKE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 197 NGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 276
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 277 LATIYERAgrVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEg 355
Cdd:TIGR01039 277 MGELQERI--TSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE- 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622859044 356 mtrkDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKnFINQ 411
Cdd:TIGR01039 354 ----EHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| 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 ... |
10-63 |
4.36e-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: 97.88 E-value: 4.36e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1622859044 10 SFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGD 63
Cdd:cd18118 19 KGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
61-347 |
3.42e-24 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 104.31 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 61 TGDILRTPVSEDMLGRVFNGSGKPIDK--GPVVMAEDF--LDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIP 136
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGKIVERfdAPPTVGPISeeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 137 IFSAAGLPHNEIAAQICRQAglvkkskavldyHDDNFAIvfaamGVNMETARF---FKSDFEQNGTMGNVCLFLNLANDP 213
Cdd:PRK08149 156 IFASAGCGKTSLMNMLIEHS------------EADVFVI-----GLIGERGREvteFVESLRASSRREKCVLVYATSDFS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 214 TIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRGGS 293
Cdd:PRK08149 219 SVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGS 295
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1622859044 294 ITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 347
Cdd:PRK08149 296 ITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
53-404 |
1.77e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 102.28 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 53 ARKTTCEFTGDILrtpVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIAR 131
Cdd:PRK07196 79 ARVFPSEQDGELL---IGDSWLGRVINGLGEPLDgKGQL-GGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 132 GQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAN 211
Cdd:PRK07196 155 GQRVGLMAGSGVGKSVLLGMITR--------------YTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPAD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 212 DPTIERIITPRLALTTAEFlaYQCEKH-VLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGr 290
Cdd:PRK07196 221 ESPLMRIKATELCHAIATY--YRDKGHdVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 291 GGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGegmtrKDHGDVSNQLYA 370
Cdd:PRK07196 298 NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIG-----SQQAKAASLLKQ 372
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622859044 371 CYAIGKDVQAMKA----VVGEEALTSEDLLYLEFLQKF 404
Cdd:PRK07196 373 CYADYMAIKPLIPlggyVAGADPMADQAVHYYPAITQF 410
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
68-383 |
1.97e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 102.09 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 68 PVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHN 146
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDgLGPI-YTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 147 EIAAQICRqaglvkKSKAVLdyhddnfaIVFAAMGvnmETARFFKSDFEQ----NGTMGNVCLFLNLANDPTIeRIITPR 222
Cdd:PRK08972 177 VLLGMMTR------GTTADV--------IVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 223 LALTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTM 302
Cdd:PRK08972 239 TATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 303 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVS---NQLYACYAIGKDVQ 379
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDLI 392
|
....
gi 1622859044 380 AMKA 383
Cdd:PRK08972 393 SIGA 396
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
61-346 |
2.38e-23 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 102.45 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 61 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVmAEDFLDIN----G----QPINphsriypeEMIQTGISPIDVMNSIAR 131
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQPIDgKGPIE-ATETRPVErkapGvidrKSVH--------EPLQTGIKAIDAMIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 132 GQKIPIfsaaglphneiaaqIC-RQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFL 207
Cdd:PRK09281 162 GQRELI--------------IGdRQTG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 208 NLANDPTIERIITPRLALTTAEFLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERA 284
Cdd:PRK09281 226 ATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERA 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622859044 285 GRV--EGRGGSITQIPIL-TMPNDdITHPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 346
Cdd:PRK09281 302 AKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
24-348 |
3.33e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 101.59 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 24 DGTQRSGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQ 102
Cdd:PRK08927 50 GGRPVPCEVVGFRGDRALLMPFGPLEGV-RRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDgKGPLPQGPVPYPLRAP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 103 PINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGlphneiaaqicrqaglVKKSK--AVLDYHDDNFAIVFAAM 180
Cdd:PRK08927 129 PPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSG----------------VGKSVllSMLARNADADVSVIGLI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 181 GvnmETAR----FFKSDFEQNGTMGNVcLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREV 256
Cdd:PRK08927 193 G---ERGRevqeFLQDDLGPEGLARSV-VVVATSDEPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 257 SAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYP 336
Cdd:PRK08927 268 GLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYP 347
|
330
....*....|..
gi 1622859044 337 PINVLPSLSRLM 348
Cdd:PRK08927 348 AINVLKSVSRTM 359
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
68-346 |
7.43e-22 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 97.67 E-value: 7.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 68 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 147
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 148 IAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLA 224
Cdd:PRK05922 173 LLSTI------AKGSKSTIN--------VIALIG---ERGREVREYIEQHKEglaAQRTIIIASPAHETAPTKVIAGRAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 225 LTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrGGSITQI-PILTMP 303
Cdd:PRK05922 236 MTIAEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYP 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622859044 304 NdditHP--IPDLTGFITEGQIYVDRQlHNRQIYPPINVLPSLSR 346
Cdd:PRK05922 313 N----HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
12-346 |
1.48e-21 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 97.03 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 12 AQYAEIVHFtlPDGTQrsGQVL-----EVAgtkaiVQVFEGTSGIDArKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID 86
Cdd:COG0056 47 AMAGELLEF--PGGVY--GMALnleedNVG-----VVLLGDYEGIKE-GDTVKRTGRILSVPVGEALLGRVVDPLGRPID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 87 -KGPVVmAEDFLDING--------QPINphsriypeEMIQTGISPIDVMNSIARGQKipifsaaglphnEIaaqIC--RQ 155
Cdd:COG0056 117 gKGPIE-AEERRPVERpapgvidrQPVH--------EPLQTGIKAIDAMIPIGRGQR------------EL---IIgdRQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 156 AGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLA 232
Cdd:COG0056 173 TG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 233 YQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDDI 307
Cdd:COG0056 251 DQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTALPIIETQAGDV 326
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622859044 308 THPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 346
Cdd:COG0056 327 SAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
66-348 |
9.82e-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: 91.90 E-value: 9.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 66 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPinPH-SRIYPE-EMIQTGISPIDVMNSIARGQKIPIFSAAG- 142
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA--PEfVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 143 --------LPHNeIAAqicRQAGLVkkskavldyhddnfaiVFAAMGvnmETAR--------FFKSDFEQNGTMGNVCLF 206
Cdd:cd01133 79 gktvlimeLINN-IAK---AHGGYS----------------VFAGVG---ERTRegndlyheMKESGVINLDGLSKVALV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 207 LNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 286
Cdd:cd01133 136 YGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITS 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622859044 287 VegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 348
Cdd:cd01133 216 T--KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
200-346 |
5.85e-18 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 83.78 E-value: 5.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 200 MGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLAT 279
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622859044 280 IYERAGRVE-----GRGGSITQIPILTMPNDDITHPIPDLTGFITegQIY--VDRQLHNRQIYPPINVLPSLSR 346
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
82-372 |
1.35e-17 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 85.02 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 82 GKPID-KGPVVMAEDFLDINGQPINPHSRIYP-----------EEMIQTGISPIDVMNSIARGQKIPIFSAaglphneia 149
Cdd:PRK07165 81 GKIIDiDGNIIYPEAQNPLSKKFLPNTSSIFNlahglmtvktlNEQLYTGIIAIDLLIPIGKGQRELIIGD--------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 150 aqicRQAGlvKKSKA---VLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPtIERIITPRLALT 226
Cdd:PRK07165 152 ----RQTG--KTHIAlntIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 227 TAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILTMPNDD 306
Cdd:PRK07165 225 HAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNR-KTITALPILQTVDND 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622859044 307 ITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLmKSAIGEGMTRKDHGDVsNQLYACY 372
Cdd:PRK07165 302 ITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRT-GSSVQSKTITKVAGEI-SKIYRAY 365
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-356 |
1.29e-16 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 82.40 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 61 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLD-------INGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQ 133
Cdd:PTZ00185 111 TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTRSRALLEseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 134 KIPIFSAAGLPHNEIA-AQICRQaglVKKSKAVLDyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAND 212
Cdd:PTZ00185 191 RELIVGDRQTGKTSIAvSTIINQ---VRINQQILS--KNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 213 PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GRG 291
Cdd:PTZ00185 266 PAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKG 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622859044 292 G-SITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 356
Cdd:PTZ00185 345 GgSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
200-345 |
1.62e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 79.30 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 200 MGNVCLFLNLANDPTIERIITPRLALTTAEFlaYQCEKHVLVILTDMSS-YAEALREVSAAREEVPGRRGFPGYMYTDLA 278
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEY--FRDMGYDVALMADSTSrWAEALREISGRLEEMPGEEGYPAYLASKLA 794
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622859044 279 TIYERAGRV-----EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 345
Cdd:PRK14698 795 EFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
61-411 |
5.05e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 77.00 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 61 TGDILRTPVSEDMLGRVFNGSGKPIDK-GPVVMAEDFldingqPINPHSRIYPE-----EMIQTGISPIDVMNSIARGQK 134
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTS------PIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 135 IPIFSAAGLPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMG--------VNMETaRFFKSDFEQNGTMGN 202
Cdd:CHL00060 164 IGLFGGAGVGKTvlimELINNIAKAHGGVS---------------VFGGVGertregndLYMEM-KESGVINEQNIAESK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 203 VCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 282
Cdd:CHL00060 228 VALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 283 RAGRVegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmtrkdhg 362
Cdd:CHL00060 308 RITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRI---------- 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622859044 363 dVSNQLYAC----------YaigKDVQAMKAVVGEEALTSEDLLYLEFLQKFEkNFINQ 411
Cdd:CHL00060 376 -VGEEHYETaqrvkqtlqrY---KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 429
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
238-402 |
2.69e-13 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 71.74 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 238 HVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE---GRGGSITQIPILTMPNDDITHPIPDL 314
Cdd:PRK04192 325 DVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQN 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 315 TGFITEGQIYVDRQLHNRQIYPPINVLPSLSrLMKSAIGEGMTRK---DHGDVSNQLYACYAIGKDVQAMKAVVGEEALT 391
Cdd:PRK04192 405 TLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQVAPWWEENvdpDWRELRDEAMDLLQREAELQEIVRLVGPDALP 483
|
170
....*....|....*....
gi 1622859044 392 SEDLLYLE--------FLQ 402
Cdd:PRK04192 484 EEDRLILEvarliredFLQ 502
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
48-394 |
8.55e-13 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 70.12 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 48 TSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMN 127
Cdd:COG0055 63 TDGL-VRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 128 SIARGQKIPIFSAAG---------LPHNeIAAQicrQAGLVkkskavldyhddnfaiVFAAMGvnmETARF---FKSDFE 195
Cdd:COG0055 142 PYAKGGKIGLFGGAGvgktvlimeLIHN-IAKE---HGGVS----------------VFAGVG---ERTREgndLYREMK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 196 QNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYT 275
Cdd:COG0055 199 ESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622859044 276 DLATIYERAGRVegRGGSITQIPILTMPNDDITHPIP-------DLTgfitegqIYVDRQLHNRQIYPPINVLPSLSRLM 348
Cdd:COG0055 279 EMGALQERITST--KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRIL 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1622859044 349 KSAI-GEgmtrkDHGDVSN------QLYacyaigKDVQAMKAVVGEEALTSED 394
Cdd:COG0055 350 DPLIvGE-----EHYRVARevqrilQRY------KELQDIIAILGMDELSEED 391
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
361-431 |
1.71e-08 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 50.91 E-value: 1.71e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622859044 361 HGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKnFINQGPYENRSVFESLDLGWKLLR 431
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 ... |
12-62 |
3.04e-06 |
|
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: 44.84 E-value: 3.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622859044 12 AQYAEIVHFtlpdGTQRSGQVLEVAGTKAIVQVFEGTSGIDaRKTTCEFTG 62
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, ... |
16-63 |
1.99e-04 |
|
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: 39.60 E-value: 1.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1622859044 16 EIVHFTLPDG---TQRSGQVLEVAGTKAIVQVFEGTSGIDaRKTTCEFTGD 63
Cdd:cd01426 24 EVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLS-RGALVEPTGR 73
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