|
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 ... |
37-500 |
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: 1013.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 37 TYTTVSGVNGPLVILDNVKFPRYAEIVHLTLPDGTKRSGQVLEVIGTKAVVQVFEGTSGIDAKKTACEFTGDILRTPVSE 116
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 117 DMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQ 196
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 197 ICRQAGLVQKS-KDVTDYSSENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEY 275
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 276 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 355
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 356 IPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEAL 435
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18874534 436 TSDDLLYLEFLQKFEKNFIAQGAYDNRTAFETLDIGWQLLRIFPKEMLKRIPQSTLAEFYPRESA 500
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
34-501 |
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: 835.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 34 PRLTYTTVSGVNGPLVILDNVKFPRYAEIVHLTLPDGTKRSGQVLEVIGTKAVVQVFEGTSGIDAKKTACEFTGDILRTP 113
Cdd:COG1156 2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 114 VSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEI 193
Cdd:COG1156 82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 194 AAQICRQAGLVQkskdvtdySSENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTA 273
Cdd:COG1156 162 AAQIARQAKVRG--------EEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 274 EYLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDIT 353
Cdd:COG1156 234 EYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDIT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 354 HPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEE 433
Cdd:COG1156 314 HPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18874534 434 ALTSDDLLYLEFLQKFEKNFIAQGAYDNRTAFETLDIGWQLLRIFPKEMLKRIPQSTLAEFYPRESAA 501
Cdd:COG1156 394 ALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRAK 461
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
38-501 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 808.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 38 YTTVSGVNGPLVILDNVKFPRYAEIVHLTLPDGTKRSGQVLEVIGTKAVVQVFEGTSGIDAKKTACEFTGDILRTPVSED 117
Cdd:PRK04196 4 YRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 118 MLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQI 197
Cdd:PRK04196 84 MLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 198 CRQAGLVQkskdvtdySSENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEYLA 277
Cdd:PRK04196 164 ARQAKVLG--------EEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 278 YQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIP 357
Cdd:PRK04196 236 FEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 358 DLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTS 437
Cdd:PRK04196 316 DLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18874534 438 DDLLYLEFLQKFEKNFIAQGAYDNRTAFETLDIGWQLLRIFPKEMLKRIPQSTLAEFYPRESAA 501
Cdd:PRK04196 396 RDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRGK 459
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
38-497 |
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: 695.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 38 YTTVSGVNGPLVILDNVKFPRYAEIVHLTLPDGTKRSGQVLEVIGTKAVVQVFEGTSGIDAKKTACEFTGDILRTPVSED 117
Cdd:TIGR01041 2 YSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 118 MLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQI 197
Cdd:TIGR01041 82 MLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 198 CRQAGLVQkskdvtdySSENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEYLA 277
Cdd:TIGR01041 162 ARQATVRG--------EESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 278 YQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIP 357
Cdd:TIGR01041 234 FEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 358 DLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTS 437
Cdd:TIGR01041 314 DLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 438 DDLLYLEFLQKFEKNFIAQGAYDNRTAFETLDIGWQLLRIFPKEMLKRIPQSTLAEFYPR 497
Cdd:TIGR01041 394 RDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYHPK 453
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
109-398 |
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: 615.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 109 ILRTPVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGL 188
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 189 PHNEIAAQICRQAGLVQkskdvtdySSENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRL 268
Cdd:cd01135 81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 269 ALTTAEYLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMP 348
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 18874534 349 NDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 398
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
38-498 |
5.04e-122 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 364.36 E-value: 5.04e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 38 YTTVSGVNGPLVILDnVKFPRYAEIVHLTLPDGTKRSgQVLEVIGTKAVVQVFEGTSGI--DAKKTaceFTGDILRTPVS 115
Cdd:PRK02118 5 YTKITDITGNVITVE-AEGVGYGELATVERKDGSSLA-QVIRLDGDKVTLQVFGGTRGIstGDEVV---FLGRPMQVTYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 116 EDMLGRVFNGSGKPIDRGPTgLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAA 195
Cdd:PRK02118 80 ESLLGRRFNGSGKPIDGGPE-LEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 196 QICRQAglvqkskdvtdyssENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEY 275
Cdd:PRK02118 159 RIALQA--------------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 276 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITHP 355
Cdd:PRK02118 225 FALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 356 IPDLTGYITEGQVYvdrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRKDHADVSN---QLYACYAIGKDVQAMkavvGE 432
Cdd:PRK02118 304 VPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GF 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18874534 433 EaLTSDDLLYLEFLQKFEKNFIAQGAydNRTAFETLDIGWQLL-RIF-PKEMLkrIPQSTLAEFYPRE 498
Cdd:PRK02118 371 K-LSNWDEKLLKFSELFESRLMDLEV--NIPLEEALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKN 433
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
164-390 |
2.40e-110 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 326.24 E-value: 2.40e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 164 GISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvqkSKDVtdyssenfaIVFAAMGVNMETARFFKSDFEENG 243
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA-----SADV---------VVYALIGERGREVREFIEELLGSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 244 SMDNVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 323
Cdd:pfam00006 67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18874534 324 TIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLS 390
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 ... |
111-392 |
4.01e-102 |
|
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: 307.46 E-value: 4.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 111 RTPVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 190
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 191 NEIAAQICRQAGlvqkskdvtdySSENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLAL 270
Cdd:cd19476 81 TVLAMQLARNQA-----------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 271 TTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPND 350
Cdd:cd19476 150 TIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 18874534 351 DITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRL 392
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 ... |
400-494 |
1.49e-60 |
|
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: 193.80 E-value: 1.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 400 GMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFEKNFIAQGAYDNRTAFETLDIGWQLLRIFP 479
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 18874534 480 KEMLKRIPQSTLAEF 494
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
111-392 |
9.84e-45 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 158.11 E-value: 9.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 111 RTPVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 190
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 191 NEIAAQICRQAGlvqksKDVtdyssenfaIVFAAMGvnmETAR----FFKSDFEENGsMDNVCLFLNLANDPTIERIITP 266
Cdd:cd01136 81 STLLGMIARNTD-----ADV---------NVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 267 RLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILT 346
Cdd:cd01136 143 YTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 18874534 347 MPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRL 392
Cdd:cd01136 220 VEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| ATP-synt_V_A-type_beta_N |
cd18118 |
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 ... |
37-108 |
1.67e-38 |
|
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: 134.86 E-value: 1.67e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18874534 37 TYTTVSGVNGPLVILDNVKFPRYAEIVHLTLPDGTKRSGQVLEVIGTKAVVQVFEGTSGIDAKKTACEFTGD 108
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
106-424 |
4.94e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 144.51 E-value: 4.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 106 TGDILRTPVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSA 185
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 186 AGLPHNEIAAQICRQAglvqkSKDVTdyssenfaiVFAAMGV-NMETARFFKSDFEENGsMDNVCLFLNLANDPTIERII 264
Cdd:PRK06936 171 AGGGKSTLLASLIRSA-----EVDVT---------VLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 265 TPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRNGSITQIPI 344
Cdd:PRK06936 236 AGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 345 LTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGegmtrKDHADVSNQLYACYAIGKDVQ 424
Cdd:PRK06936 313 VLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVS-----KEHKTWAGRLRELLAKYEEVE 387
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
106-396 |
1.53e-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: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 106 TGDILRTPVSEDMLGRVFNGSGKPID-RGPTgLAEDYLDImgQPINPQC--RIYPEEMIQTGISAIDGMNSIARGQKIPI 182
Cdd:TIGR00962 90 TGRILEVPVGDGLLGRVVNALGEPIDgKGPI-DSDEFSPV--EKIAPGVieRKSVHEPLQTGIKAIDAMIPIGRGQRELI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 183 FS--AAGlphneiAAQICRQAGLVQKSKDVTdyssenfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTI 260
Cdd:TIGR00962 167 IGdrQTG------KTAVAIDTIINQKDSDVY--------CIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSAS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 261 ERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGR 335
Cdd:TIGR00962 233 LQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKG 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18874534 336 NGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSA 396
Cdd:TIGR00962 309 GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
76-475 |
1.54e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 140.33 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 76 QVLEVIGTKAVVQVFEGTSGIDAKKTAcEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPtGLAEDYLDIMGQPINPQCRI 155
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGLRCGQWV-TPLGHMHQVQVGADLAGRILDGLGAPIDGGP-PLTGQWRELDCPPPSPLTRQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 156 YPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvqkSKDVtdyssenfaIVFAAMGvnmETARFF 235
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADS-----AADV---------MVLALIG---ERGREV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 236 KSDFEENGSMD---NVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRR 312
Cdd:PRK06820 205 REFLEQVLTPEaraRTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 313 GFPGYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRL 392
Cdd:PRK06820 284 SFPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 393 MKSAIGEGmtRKDHADVSNQLYACYaigKDVQAMKAVvgEEALTSDDLLYLEFLQKFE--KNFIAQGAYDNRTAFETLDI 470
Cdd:PRK06820 362 MPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEH 434
|
....*
gi 18874534 471 GWQLL 475
Cdd:PRK06820 435 LAQVV 439
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
61-393 |
2.27e-36 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 139.78 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 61 EIVHLTLPDGTKRSGQVLEVIGTKAVVQVFEGTSGIdAKKTACEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPTGLAED 140
Cdd:COG1157 42 ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 141 YLDIMGQPINPQCR--IypEEMIQTGISAIDGMNSIARGQKIPIFSAAG------LphneiaAQICRQAglvqkSKDVtd 212
Cdd:COG1157 121 RRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL------GMIARNT-----EADV-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 213 yssenfaIVFAAMGvnmETAR----FFKSDFEENGsMDNVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVIl 288
Cdd:COG1157 186 -------NVIALIG---ERGRevreFIEDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQ-GKNVLLL- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 289 tdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQI-PILTmPNDDITHPIPDLTGYIT 364
Cdd:COG1157 253 --MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAFyTVLV-EGDDMNDPIADAVRGIL 327
|
330 340
....*....|....*....|....*....
gi 18874534 365 EGQVYVDRQLHNRQIYPPINVLPSLSRLM 393
Cdd:COG1157 328 DGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
110-399 |
1.21e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 132.12 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 110 LRTPVSEDMLGRVFNGSGKPID-RGPTGLAEdYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGL 188
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDgKGAIDYER-YAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 189 PHNEIAAQICRQAGLVQKskdvtdyssenfaiVFAAMGvnmETARFFKSDFEEN--GSMDNVCLFLNLANDPTIERIITP 266
Cdd:PRK08472 169 GKSTLMGMIVKGCLAPIK--------------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 267 RLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRnGSITQIPILT 346
Cdd:PRK08472 232 FCAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVL 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 18874534 347 MPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGE 399
Cdd:PRK08472 310 VEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
109-391 |
6.52e-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: 6.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 109 ILRTPVSEDMLGRVFNGSGKPID-RGPTGLAEDY-LDIMGQPINPQCRIYpeEMIQTGISAIDGMNSIARGQKIPIFSAa 186
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDgKGPIQTKERRrVESKAPGIIPRQSVN--EPLQTGIKAIDSLIPIGRGQRELIIGD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 187 glphneiaaqicRQAG---------LVQKSKDVTdyssenfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLAND 257
Cdd:cd01132 78 ------------RQTGktaiaidtiINQKGKKVY--------CIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 258 PTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV-- 332
Cdd:cd01132 138 PAPLQYLAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsd 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18874534 333 EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSR 391
Cdd:cd01132 214 ELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
106-489 |
7.27e-31 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 125.08 E-value: 7.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 106 TGDILRTPVSEDMLGRVFNGSGKPID-RGPTGLAEDYL-DIMGQPINPQCRIYpeEMIQTGISAIDGMNSIARGQKIPIF 183
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDgKGEISASESRLiESPAPGIISRRSVY--EPLQTGLIAIDSMIPIGRGQRELII 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 184 SAaglphneiaaqicRQAG---------LVQKSKDVTdyssenfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNL 254
Cdd:CHL00059 148 GD-------------RQTGktavatdtiLNQKGQNVI--------CVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAET 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 255 ANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGR 331
Cdd:CHL00059 207 ADSPATLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 332 VEGR--NGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAigegmtrkdhadv 409
Cdd:CHL00059 283 LSSQlgEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA------------- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 410 snqlyacyaigkDVQAMKAVVGEealtsddlLYLEFLQKFEKNFIAQGA--YDNRTAFEtLDIGwQLLRifpkEMLKRiP 487
Cdd:CHL00059 350 ------------QIKAMKQVAGK--------LKLELAQFAELEAFAQFAsdLDKATQNQ-LARG-QRLR----ELLKQ-S 402
|
..
gi 18874534 488 QS 489
Cdd:CHL00059 403 QS 404
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
58-393 |
1.32e-30 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 123.73 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 58 RYAEIVHLTLPDGTKRsgQVLEVIG---TKAVVQVFEGTSGIdAKKTACEFTGDILRTPVSEDMLGRVFNGSGKPIDRGP 134
Cdd:PRK09099 44 TLGELCELRQRDGTLL--QRAEVVGfsrDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 135 TGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvqkSKDVTdys 214
Cdd:PRK09099 121 PLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGT-----QCDVN--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 215 senfaiVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSY 294
Cdd:PRK09099 193 ------VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 295 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQL 374
Cdd:PRK09099 266 ARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREI 343
|
330
....*....|....*....
gi 18874534 375 HNRQIYPPINVLPSLSRLM 393
Cdd:PRK09099 344 AARNQYPAIDVLGSLSRVM 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
72-424 |
1.34e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 123.52 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 72 KRSGQVLEVI---GTKAVVQVFEGTSGIDAKKTACEFTGDiLRTPVSEDMLGRVFNGSGKPID--RGPTGLAEDYlDIMG 146
Cdd:PRK07594 49 KPGEELAEVVginGSKALLSPFTSTIGLHCGQQVMALRRR-HQVPVGEALLGRVIDGFGRPLDgrELPDVCWKDY-DAMP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 147 QPinPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvqkskDVTdyssenfaiVFAAMG 226
Cdd:PRK07594 127 PP--AMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA-----DSN---------VLVLIG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 227 VNMETARFFkSDFEENGSMDNVCLFLNLAND-PTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAR 305
Cdd:PRK07594 191 ERGREVREF-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 306 EEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINV 385
Cdd:PRK07594 269 GETAVSGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDV 346
|
330 340 350
....*....|....*....|....*....|....*....
gi 18874534 386 LPSLSRLMKSAIGEgmtrkDHADVSNQLYACYAIGKDVQ 424
Cdd:PRK07594 347 LATLSRVFPVVTSH-----EHRQLAAILRRCLALYQEVE 380
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
37-456 |
2.03e-29 |
|
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: 120.59 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 37 TYTTVSGVNGPLVildNVKFPRYA--EIVHLTLPDGTKRSGQVLEV---IGTKAVVQVFEGTSGIDAKKTACEFTGDILR 111
Cdd:TIGR01039 1 TKGKVVQVIGPVV---DVEFEQGElpRIYNALKVQNRAESELTLEVaqhLGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 112 TPVSEDMLGRVFNGSGKPID-RGPTGlAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 190
Cdd:TIGR01039 78 VPVGKETLGRIFNVLGEPIDeKGPIP-AKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 191 N----EIAAQICRQAGlvqkskdvtDYSsenfaiVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITP 266
Cdd:TIGR01039 157 TvliqELINNIAKEHG---------GYS------VFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 267 RLALTTAEYLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILT 346
Cdd:TIGR01039 222 LTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKTGSITSVQAVY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 347 MPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrkDHADVSNQLYACYAIGKDVQA 425
Cdd:TIGR01039 300 VPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQILQRYKELQD 374
|
410 420 430
....*....|....*....|....*....|.
gi 18874534 426 MKAVVGEEALTSDDLLYLEFLQKFEKnFIAQ 456
Cdd:TIGR01039 375 IIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
108-430 |
2.03e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 120.22 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 108 DILRTPVSEDMLGRVFNGSGKPID-RGPTGlAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAA 186
Cdd:PRK05688 99 DTGRLPMGMSMLGRVLDGAGRALDgKGPMK-AEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 187 GlphneiaaqicrqaglVQKS---KDVTDYSSENFAIVfaamGVNMETARFFKSDFEE---NGSMDNVCLFLNLANDPTI 260
Cdd:PRK05688 178 G----------------VGKSvllGMMTRFTEADIIVV----GLIGERGREVKEFIEHilgEEGLKRSVVVASPADDAPL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 261 ERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSIT 340
Cdd:PRK05688 238 MRLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSIT 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 341 QIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKdhADVSNQLYACYAIG 420
Cdd:PRK05688 317 AFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRR--AQRFKQLWSRYQQS 394
|
330
....*....|
gi 18874534 421 KDVQAMKAVV 430
Cdd:PRK05688 395 RDLISVGAYV 404
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
104-422 |
3.52e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 119.44 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 104 EFTGDILRTPVSEDMLGRVFNGSGKPIDRG--PTGLAEDYLDimGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIP 181
Cdd:PRK07721 85 EATGKPLEVKVGSGLIGQVLDALGEPLDGSalPKGLAPVSTD--QDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 182 IFSAAGLPHNEIAAQICRQAglvqkSKDVTdyssenfaiVFAAMGVN-METARFFKSDFEENGSMDNVcLFLNLANDPTI 260
Cdd:PRK07721 163 IFAGSGVGKSTLMGMIARNT-----SADLN---------VIALIGERgREVREFIERDLGPEGLKRSI-VVVATSDQPAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 261 ERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSIT 340
Cdd:PRK07721 228 MRIKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGSIT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 341 QIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHADVSN---QLYACY 417
Cdd:PRK07721 305 AFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTY 379
|
....*
gi 18874534 418 AIGKD 422
Cdd:PRK07721 380 QNSED 384
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
106-391 |
5.80e-29 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 119.63 E-value: 5.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 106 TGDILRTPVSEDMLGRVFNGSGKPIDRGPTGLAEDYLdimgqPINpqcRIYPEEM--------IQTGISAIDGMNSIARG 177
Cdd:PRK13343 91 TGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARR-----PLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 178 QKIPIFSAAGLPHNEIAAQicrqAGLVQKSKDVTdyssenfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLAND 257
Cdd:PRK13343 163 QRELIIGDRQTGKTAIAID----AIINQKDSDVI--------CVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 258 PTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRN- 336
Cdd:PRK13343 231 PPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELg 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 18874534 337 -GSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSR 391
Cdd:PRK13343 310 gGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
111-479 |
7.69e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 118.73 E-value: 7.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 111 RTPVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPH 190
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 191 NEIAAQICR--QAglvqkskDVtdyssenfaIVFAAMGvnmETARFFKsDFEEN-----GSMDNVCLflnlandpTIERI 263
Cdd:PRK07960 189 SVLLGMMARytQA-------DV---------IVVGLIG---ERGREVK-DFIENilgaeGRARSVVI--------AAPAD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 264 ITPRLALTTAEYLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNG 337
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 338 SITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKdhADVSNQLYACY 417
Cdd:PRK07960 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR--VRQFKQLLSSF 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18874534 418 AIGKDVQAmkavVGEEALTSDDLL--YLEFLQKFEKnFIAQGAYDnRTAFEtlDIGWQLLRIFP 479
Cdd:PRK07960 399 QRNRDLVS----VGAYAKGSDPMLdkAIALWPQLEA-FLQQGIFE-RADWE--DSLQALERIFP 454
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
106-392 |
8.95e-29 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 118.17 E-value: 8.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 106 TGDILRTPVSEDMLGRVFNGSGKPIDR----GPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIP 181
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGKIVERfdapPTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 182 IFSAAGLPHNEIAAQICRQA-------GLV-QKSKDVTDY--------SSENFAIVFAAmgvnmetarffkSDFeengsm 245
Cdd:PRK08149 156 IFASAGCGKTSLMNMLIEHSeadvfviGLIgERGREVTEFveslrassRREKCVLVYAT------------SDF------ 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 246 dnvclflnlandPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 325
Cdd:PRK08149 218 ------------SSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRL 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18874534 326 YERAGRVegRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRL 392
Cdd:PRK08149 285 LERPGAT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
16-396 |
2.83e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 117.02 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 16 EAAARQHAQAV--VR--NYISQPRLTYTTVSGVngplvildnVKFPRYAEIVHLTLPDGTKRsGQVLEVIGTKAVVQVFE 91
Cdd:PRK06002 11 AALVERYAAPEplVRigGTVSEVTASHYRVRGL---------SRFVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 92 gtSGIDAKKTACEFTGDILRTPVSEDMLGRVFNGSGKPID-RGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDG 170
Cdd:PRK06002 81 --PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPIDgLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 171 MNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvqkskdvtDyssenfAIVFAAMGvnmETARFFKSDFEEN--GSMDNV 248
Cdd:PRK06002 159 FTPLCAGQRIGIFAGSGVGKSTLLAMLARADAF--------D------TVVIALVG---ERGREVREFLEDTlaDNLKKA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 249 CLFLNLANDPTIERIITPRLALTTAEYLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYER 328
Cdd:PRK06002 222 VAVVATSDESPMMRRLAPLTATAIAEYFRDRGEN-VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLER 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18874534 329 AGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSA 396
Cdd:PRK06002 301 AGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
113-422 |
9.60e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 115.07 E-value: 9.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 113 PVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNE 192
Cdd:PRK06793 92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 193 IAAQICRQA-------GLV-QKSKDVTDyssenfaivfaamgvnmetarFFKSDFEENGsMDNVCLFLNLANDPTIERII 264
Cdd:PRK06793 172 LLGMIAKNAkadinviSLVgERGREVKD---------------------FIRKELGEEG-MRKSVVVVATSDESHLMQLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 265 TPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEgrNGSITQIP 343
Cdd:PRK06793 230 AAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQ--KGSITGIY 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18874534 344 ILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHADVSNQLYACYAIGKD 422
Cdd:PRK06793 305 TVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
113-428 |
7.64e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 109.79 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 113 PVSEDMLGRVFNGSGKPID-RGPTGlAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHN 191
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDgLGPIY-TDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 192 EIAAQICRQAglvqkSKDVtdyssenfaIVFAAMGvnmETARFFKSDFEE----NGSMDNVCLFLNLANDPTIeRIITPR 267
Cdd:PRK08972 177 VLLGMMTRGT-----TADV---------IVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 268 LALTTAEYLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTM 347
Cdd:PRK08972 239 TATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 348 PNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHADVS---NQLYACYAIGKDVQ 424
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDLI 392
|
....
gi 18874534 425 AMKA 428
Cdd:PRK08972 393 SIGA 396
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
106-391 |
2.06e-25 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 109.00 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 106 TGDILRTPVSEDMLGRVFNGSGKPID-RGPTGlAEDYLD--------IMGQPINpqcriypeEMIQTGISAIDGMNSIAR 176
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQPIDgKGPIE-ATETRPverkapgvIDRKSVH--------EPLQTGIKAIDAMIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 177 GQKIPIfsaaglphneiaaqIC-RQAG---------LVQKSKDVTdyssenfaIVFAAMGVNMETARFFKSDFEENGSMD 246
Cdd:PRK09281 162 GQRELI--------------IGdRQTGktaiaidtiINQKGKDVI--------CIYVAIGQKASTVAQVVRKLEEHGAME 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 247 NVCLFLNLANDPTIERIITPRLALTTAEYLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLa 323
Cdd:PRK09281 220 YTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL- 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18874534 324 tiYERAGRV--EGRNGSITQIPIL-TMPNdDITHPIPdlTGY--ITEGQVYVDRQLHNRQIYPPINVLPSLSR 391
Cdd:PRK09281 298 --LERAAKLsdELGGGSLTALPIIeTQAG-DVSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
98-418 |
4.45e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 104.59 E-value: 4.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 98 AKKTACEFTGDILrtpVSEDMLGRVFNGSGKPID-RGPTGlAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIAR 176
Cdd:PRK07196 79 ARVFPSEQDGELL---IGDSWLGRVINGLGEPLDgKGQLG-GSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 177 GQKIPIFSAAGLPHNEIAAQICRqaglvqkskdvtdYSSENFAIVFAAMGVNMETARFFKSDFEENGSMDNVcLFLNLAN 256
Cdd:PRK07196 155 GQRVGLMAGSGVGKSVLLGMITR-------------YTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSV-VVAAPAD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 257 DPTIERIITPRLALTTAEYlaYQCEKH-VLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGr 335
Cdd:PRK07196 221 ESPLMRIKATELCHAIATY--YRDKGHdVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 336 NGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGegmtrKDHADVSNQLYA 415
Cdd:PRK07196 298 NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIG-----SQQAKAASLLKQ 372
|
...
gi 18874534 416 CYA 418
Cdd:PRK07196 373 CYA 375
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
106-391 |
6.36e-23 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 101.65 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 106 TGDILRTPVSEDMLGRVFNGSGKPID-RGPTgLAEDYL-------DIMG-QPINpqcriypeEMIQTGISAIDGMNSIAR 176
Cdd:COG0056 91 TGRILSVPVGEALLGRVVDPLGRPIDgKGPI-EAEERRpverpapGVIDrQPVH--------EPLQTGIKAIDAMIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 177 GQKipifsaaglphnEIaaqIC--RQAG---------LVQKSKDVTdyssenfaIVFAAMGVNMETARFFKSDFEENGSM 245
Cdd:COG0056 162 GQR------------EL---IIgdRQTGktaiaidtiINQKGKDVI--------CIYVAIGQKASTVAQVVETLEEHGAM 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 246 DNVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDL 322
Cdd:COG0056 219 EYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHSRL 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18874534 323 atiYERAGRV--EGRNGSITQIPIL-TMPNddithpipDLTGY-------ITEGQVYVDRQLHNRQIYPPINVLPSLSR 391
Cdd:COG0056 298 ---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
113-391 |
1.45e-22 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 99.98 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 113 PVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNE 192
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 193 IAAQICRqaglvqkskdvtdySSENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTT 272
Cdd:PRK05922 173 LLSTIAK--------------GSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 273 AEYLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQI-PILTMPNdd 351
Cdd:PRK05922 239 AEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYPN-- 313
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 18874534 352 itHP--IPDLTGYITEGQVYVDRQlHNRQIYPPINVLPSLSR 391
Cdd:PRK05922 314 --HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
34-393 |
7.01e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 98.13 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 34 PRLTYTTVSGVNGPLVildNVKFPRYAEIVHLTLPDGTKRSGQVL-EVIG---TKAVVQVFEGTSGIdAKKTACEFTGDI 109
Cdd:PRK08927 14 TLVIYGRVVAVRGLLV---EVAGPIHALSVGARIVVETRGGRPVPcEVVGfrgDRALLMPFGPLEGV-RRGCRAVIANAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 110 LRTPVSEDMLGRVFNGSGKPID-RGPTGLAEDYLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGL 188
Cdd:PRK08927 90 AAVRPSRAWLGRVVNALGEPIDgKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 189 PHNEIAAQICRQAglvqkSKDVtdyssenfaivfAAMGVNMETAR----FFKSDFEENGSMDNVcLFLNLANDPTIERII 264
Cdd:PRK08927 170 GKSVLLSMLARNA-----DADV------------SVIGLIGERGRevqeFLQDDLGPEGLARSV-VVVATSDEPALMRRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 265 TPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPI 344
Cdd:PRK08927 232 AAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFT 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 18874534 345 LTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLM 393
Cdd:PRK08927 311 VLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
111-393 |
3.63e-21 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 93.44 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 111 RTPVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPinpqcriyPE--------EMIQTGISAIDGMNSIARGQKIPI 182
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA--------PEfvelsteqEILETGIKVVDLLAPYAKGGKIGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 183 FSAAG---------LPHNeiaaqicrqaglVQKSKDVtdYSsenfaiVFAAMGvnmETAR--------FFKSDFEENGSM 245
Cdd:cd01133 73 FGGAGvgktvlimeLINN------------IAKAHGG--YS------VFAGVG---ERTRegndlyheMKESGVINLDGL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 246 DNVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 325
Cdd:cd01133 130 SKVALVYGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSL 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18874534 326 YERAGRVegRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLM 393
Cdd:cd01133 210 QERITST--KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
245-391 |
1.93e-20 |
|
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: 91.48 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 245 MDNVCLFLNLANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLAT 324
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18874534 325 IYERAGRVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQVY--VDRQLHNRQIYPPINVLPSLSR 391
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
115-391 |
1.44e-18 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 88.49 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 115 SEDMLGRVFNGSGKPI-DRGPTGLAEDYLD----IMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIF--SAAG 187
Cdd:PRK07165 76 SKEYFGKIIDIDGNIIyPEAQNPLSKKFLPntssIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIgdRQTG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 188 LPHNEIAAQICrqaglvQKSKDVTdyssenfaIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPtIERIITPR 267
Cdd:PRK07165 156 KTHIALNTIIN------QKNTNVK--------CIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYLAPY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 268 LALTTAEYLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNgSITQIPILTM 347
Cdd:PRK07165 221 VAMAHAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK-TITALPILQT 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 18874534 348 PNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSR 391
Cdd:PRK07165 298 VDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
40-460 |
1.58e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 88.69 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 40 TVSGVNGPLVILDNVKFPRYAEIVHLtlpDGTKRSGQVLEVIGTKAVVQVFEGTSGIdAKKTACEFTGDilrtPVSED-- 117
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVRV---GEEGLIGEIIRIEGDKATIQVYEETSGI-KPGEPVEFTGE----PLSVElg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 118 --MLGRVFNG-----------SGKPIDRG---------------PTGLAEDYL---DIMGQ-------------PINPQC 153
Cdd:PRK04192 78 pgLLGSIFDGiqrpldelaekSGDFLERGvyvpaldrekkweftPTVKVGDKVeagDILGTvqetpsiehkimvPPGVSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 154 RI----------------------------------------------YPEEMIQTGISAIDGMNSIARGQK--IPIFSA 185
Cdd:PRK04192 158 TVkeivsegdytvddtiavlededgegveltmmqkwpvrrprpykeklPPVEPLITGQRVIDTFFPVAKGGTaaIPGPFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 186 AG---LPHneiaaQICRQAglvqkSKDVtdyssenfaIVFAAMG--VNmETARFFKsDFEE-------NGSMDNVCLFLN 253
Cdd:PRK04192 238 SGktvTQH-----QLAKWA-----DADI---------VIYVGCGerGN-EMTEVLE-EFPElidpktgRPLMERTVLIAN 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 254 LANDPTIER---IITprlALTTAEY---LAYqcekHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 327
Cdd:PRK04192 297 TSNMPVAAReasIYT---GITIAEYyrdMGY----DVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 328 RAGRVE---GRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSrLMKSAIGEGMTRK 404
Cdd:PRK04192 370 RAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQVAPWWEEN 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18874534 405 ---DHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLE--------FLQkfeknfiaQGAYD 460
Cdd:PRK04192 449 vdpDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEvarliredFLQ--------QNAFD 507
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
245-502 |
4.71e-17 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 84.69 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 245 MDNVCLFLNLANDPTIERIITPRLALTTAEY---LAYQcekhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 321
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYfrdMGYD----VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASK 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 322 LATIYERAGRV-----EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLM--- 393
Cdd:PRK14698 793 LAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVdav 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 394 -----KSAIGEGMTRKDHADVSNQLYAcyaigkDVQAMKAVVGEEALTSDDLLYLEFLQKFEKNFIAQGAYDNRTAF--- 465
Cdd:PRK14698 873 kdwwhKNVDPEWKAMRDKAMELLQKEA------ELQEIVRIVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYcpp 946
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 18874534 466 -ETLDIGWQLLRIFPKEM---LKRIPQSTLAEFYPRESAAR 502
Cdd:PRK14698 947 eKQVTMMRVLLNFYDKTMdaiSRGVPLEEIAKLPVREEIGR 987
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
106-401 |
2.18e-15 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 78.93 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 106 TGDILRTPVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDI--------MGQPiNPQCRIYPEEMIQTGISAIDGMNSIARG 177
Cdd:PTZ00185 111 TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTRSRALLESeqtlgkvdAGAP-NIVSRSPVNYNLLTGFKAVDTMIPIGRG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 178 QKIPIFSAAGLPHNEIAAqicrqAGLVQKSKDVTDYSSENFAI-VFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLAN 256
Cdd:PTZ00185 190 QRELIVGDRQTGKTSIAV-----STIINQVRINQQILSKNAVIsIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 257 DPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GR 335
Cdd:PTZ00185 265 EPAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGK 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18874534 336 NG-SITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 401
Cdd:PTZ00185 344 GGgSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
40-439 |
2.67e-15 |
|
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: 78.21 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 40 TVSGVNGPLVildNVKFPRYA-----EIVHLTLPDGTKRsgqVLEV---IGTKAVVQV-FEGTSGIdAKKTACEFTGDIL 110
Cdd:COG0055 7 KIVQVIGPVV---DVEFPEGElpaiyNALEVENEGGGEL---VLEVaqhLGDNTVRCIaMDSTDGL-VRGMEVIDTGAPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 111 RTPVSEDMLGRVFNGSGKPIDRGPTGLAEDYLDIMGQPinpqcriyPE--------EMIQTGISAIDGMNSIARGQKIPI 182
Cdd:COG0055 80 SVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPA--------PPfeeqstktEILETGIKVIDLLAPYAKGGKIGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 183 FSAAG---------LPHNeIAAQicrQAGlvqkskdvtdYSsenfaiVFAAMGvnmETARF---FKSDFEENGSMDNVCL 250
Cdd:COG0055 152 FGGAGvgktvlimeLIHN-IAKE---HGG----------VS------VFAGVG---ERTREgndLYREMKESGVLDKTAL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 251 FLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 330
Cdd:COG0055 209 VFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERIT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 331 RVegRNGSITQIPILTMPNDDITHPIP-------DLTgyitegqVYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmt 402
Cdd:COG0055 289 ST--KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE--- 356
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 18874534 403 rkDHADVSN------QLYacyaigKDVQAMKAVVGEEALTSDD 439
Cdd:COG0055 357 --EHYRVARevqrilQRY------KELQDIIAILGMDELSEED 391
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
106-456 |
1.08e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 73.15 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 106 TGDILRTPVSEDMLGRVFNGSGKPIDR-GPTGLAEdyldimGQPINPQCRIYPE-----EMIQTGISAIDGMNSIARGQK 179
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRT------TSPIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 180 IPIFSAAGLPHN----EIAAQICRQAGLVQKSKDVTDYSSENFAIvFAAM---GV-NmetarffksdfEENGSMDNVCLF 251
Cdd:CHL00060 164 IGLFGGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGNDL-YMEMkesGViN-----------EQNIAESKVALV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 252 LNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 331
Cdd:CHL00060 232 YGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITS 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 332 VegRNGSITQIPILTMPNDDITHPIPDLTGYITEGQVYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHADVS 410
Cdd:CHL00060 312 T--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----EHYETA 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 18874534 411 N------QLYacyaigKDVQAMKAVVGEEALTSDDLLYLEFLQKFEkNFIAQ 456
Cdd:CHL00060 385 QrvkqtlQRY------KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 429
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
41-107 |
4.27e-10 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 55.63 E-value: 4.27e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 41 VSGVNGPLVILDNVKFPRYAEIVHLTLP---DGTKRSGQVLEVIGTKAVVQVFEGTSGIDaKKTACEFTG 107
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVElveFGSLVLGEVLNLGGDKVRVQVFGGTSGLS-RGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
38-108 |
1.33e-09 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 54.24 E-value: 1.33e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18874534 38 YTTVSGVNGPLVILDNVKFPRYAEIVHLTLPDG---TKRSGQVLEVIGTKAVVQVFEGTSGIDaKKTACEFTGD 108
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLS-RGALVEPTGR 73
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
406-476 |
3.55e-09 |
|
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: 53.22 E-value: 3.55e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18874534 406 HADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFEKnFIAQGAYDNRTAFETLDIGWQLLR 476
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
44-131 |
4.28e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 43.09 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 44 VNGPLVILDNVKFPRYAEIVHLtlpDGTKRSGQVLEVIGTKAVVQVFEGTSGIDAKKTAcEFTGDILRTPVSEDMLGRVF 123
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVVRV---GELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPV-EGTGSSLSVELGPGLLTSIY 85
|
....*...
gi 18874534 124 NGSGKPID 131
Cdd:PRK14698 86 DGIQRPLE 93
|
|
| ATP-synt_V_A-type_alpha_N |
cd18119 |
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of ... |
40-96 |
2.26e-03 |
|
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349743 [Multi-domain] Cd Length: 67 Bit Score: 36.73 E-value: 2.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18874534 40 TVSGVNGPLVILDNVKFPRYAEIV---HLTLPdgtkrsGQVLEVIGTKAVVQVFEGTSGI 96
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELVrvgEEGLI------GEIIRLEGDKATIQVYEETSGL 56
|
|
| |
