|
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 ... |
27-485 |
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: 989.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 27 NYNTVSGVNGPLVILEKVKFPRYNEIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDVKKTTVEFTGESLRIPVSE 106
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 107 DMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQ 186
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 187 ICRQAGLV-RPTKDVHDGHEENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEY 265
Cdd:TIGR01040 161 ICRQAGLVkLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 266 LAYQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMPNDDITHP 345
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 346 IPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYAKYAIGKDAAAMKAVVGEEAL 425
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 426 SIEDKLSLEFLEKFEKTFITQGAYEDRTVFESLDQAWSLLRIYPKEMLNRISPKILDEFY 485
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFY 460
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
28-485 |
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: 848.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 28 YNTVSGVNGPLVILEKVKFPRYNEIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDVKKTTVEFTGESLRIPVSED 107
Cdd:COG1156 6 YRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELPVSED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 108 MLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQI 187
Cdd:COG1156 86 MLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 188 CRQAGLVrptkdvhdGHEENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLA 267
Cdd:COG1156 166 ARQAKVR--------GEEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAAEYLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 268 YQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMPNDDITHPIP 347
Cdd:COG1156 238 FEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDITHPIP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 348 DLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYAKYAIGKDAAAMKAVVGEEALSI 427
Cdd:COG1156 318 DLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEEALSE 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
5BW9_d 428 EDKLSLEFLEKFEKTFITQGAYEDRTVFESLDQAWSLLRIYPKEMLNRISPKILDEFY 485
Cdd:COG1156 398 TDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYY 455
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
28-485 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 828.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 28 YNTVSGVNGPLVILEKVKFPRYNEIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDVKKTTVEFTGESLRIPVSED 107
Cdd:PRK04196 4 YRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 108 MLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQI 187
Cdd:PRK04196 84 MLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 188 CRQAGLVrptkdvhdGHEENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLA 267
Cdd:PRK04196 164 ARQAKVL--------GEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 268 YQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMPNDDITHPIP 347
Cdd:PRK04196 236 FEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 348 DLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYAKYAIGKDAAAMKAVVGEEALSI 427
Cdd:PRK04196 316 DLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
5BW9_d 428 EDKLSLEFLEKFEKTFITQGAYEDRTVFESLDQAWSLLRIYPKEMLNRISPKILDEFY 485
Cdd:PRK04196 396 RDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYH 453
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
28-485 |
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: 706.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 28 YNTVSGVNGPLVILEKVKFPRYNEIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDVKKTTVEFTGESLRIPVSED 107
Cdd:TIGR01041 2 YSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 108 MLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQI 187
Cdd:TIGR01041 82 MLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 188 CRQAGlVRptkdvhdGHEENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLA 267
Cdd:TIGR01041 162 ARQAT-VR-------GEESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 268 YQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMPNDDITHPIP 347
Cdd:TIGR01041 234 FEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 348 DLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYAKYAIGKDAAAMKAVVGEEALSI 427
Cdd:TIGR01041 314 DLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
5BW9_d 428 EDKLSLEFLEKFEKTFITQGAYEDRTVFESLDQAWSLLRIYPKEMLNRISPKILDEFY 485
Cdd:TIGR01041 394 RDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYH 451
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
99-388 |
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: 613.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 99 SLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGL 178
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 179 PHNEIAAQICRQAGLVrptkdvhdGHEENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRL 258
Cdd:cd01135 81 PHNELAAQIARQAGVV--------GSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 259 ALTTAEYLAYQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMP 338
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
5BW9_d 339 NDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIG 388
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
28-483 |
1.21e-119 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 358.58 E-value: 1.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 28 YNTVSGVNGPLVILeKVKFPRYNEIVNLTLPDGTvRQGQVLEIRGDRAIVQVFEGTSGIDVKkTTVEFTGESLRIPVSED 107
Cdd:PRK02118 5 YTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGISTG-DEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 108 MLGRIFDGSGRPIDNGPKVFAEDyLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQI 187
Cdd:PRK02118 82 LLGRRFNGSGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 188 CRQAglvrptkdvhdgheENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLA 267
Cdd:PRK02118 161 ALQA--------------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 268 YQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGrNGSITQIPILTMPNDDITHPIP 347
Cdd:PRK02118 227 LEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHPVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 348 DLTGYITEGQIFvdrqLHNKGIYPpinvLPSLSRLMKSAIGEgMTRKDHGDVSN---QLYAKYAIGKDAAAMkavvGEEa 424
Cdd:PRK02118 306 DNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GFK- 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5BW9_d 425 LSIEDKLSLEFLEKFEKTFItqgayeDRTVF----ESLDQAWSLLRIY--------PKEMLNRISPKILDE 483
Cdd:PRK02118 372 LSNWDEKLLKFSELFESRLM------DLEVNipleEALDLGWKILAQCfhpeevgiKEQLIDKYWPKNCLH 436
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
154-380 |
2.66e-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: 2.66e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 154 GVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQAglvrpTKDVhdgheenfsIVFAAMGVNLETARFFKQDFEENG 233
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA-----SADV---------VVYALIGERGREVREFIEELLGSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 234 SLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQtERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLS 313
Cdd:pfam00006 67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
5BW9_d 314 TIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLS 380
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 ... |
101-382 |
1.06e-108 |
|
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: 324.41 E-value: 1.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 101 RIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPH 180
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 181 NEIAAQICRQAGlvrptkdvhdgHEENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLAL 260
Cdd:cd19476 81 TVLAMQLARNQA-----------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 261 TTAEYLAYQtERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMPND 340
Cdd:cd19476 150 TIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
5BW9_d 341 DITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRL 382
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 ... |
390-484 |
2.36e-55 |
|
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: 180.32 E-value: 2.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 390 GMTRKDHGDVSNQLYAKYAIGKDAAAMKAVVGEEALSIEDKLSLEFLEKFEKTFITQGAYEDRTVFESLDQAWSLLRIYP 469
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
5BW9_d 470 KEMLNRISPKILDEF 484
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
51-408 |
5.82e-49 |
|
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: 174.45 E-value: 5.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 51 EIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDVKkTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAED 130
Cdd:COG1157 42 ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPG-ARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 131 YLDINGSPINPYAR--IypEEMISTGVSAIDTMNSIARGQKIPIFSASG------LphneiaAQICRQAglvrpTKDVhd 202
Cdd:COG1157 121 RRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL------GMIARNT-----EADV-- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 203 gheenfsIVFAAMGvnlETAR----FFKQDFEENGsLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTeRHVLTIl 278
Cdd:COG1157 186 -------NVIALIG---ERGRevreFIEDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQG-KNVLLL- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 279 tdMSS---YADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRveGRNGSITQI-PILTmPNDDITHPIPDLTGYIT 354
Cdd:COG1157 253 --MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAFyTVLV-EGDDMNDPIADAVRGIL 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
5BW9_d 355 EGQIFVDRQLHNKGIYPPINVLPSLSRLMkSAIgegmTRKDHGDVSN---QLYAKYA 408
Cdd:COG1157 328 DGHIVLSRKLAERGHYPAIDVLASISRVM-PDI----VSPEHRALARrlrRLLARYE 379
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
101-382 |
3.33e-48 |
|
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: 167.74 E-value: 3.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 101 RIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPH 180
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 181 NEIAAQICRQAGlvrptKDVhdgheenfsIVFAAMGvnlETAR----FFKQDFEENGsLERTSLFLNLANDPTIERIITP 256
Cdd:cd01136 81 STLLGMIARNTD-----ADV---------NVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 257 RLALTTAEYLAYQTErHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRveGRNGSITQIPILT 336
Cdd:cd01136 143 YTATAIAEYFRDQGK-KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
5BW9_d 337 MPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRL 382
Cdd:cd01136 220 VEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
65-389 |
5.36e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 155.61 E-value: 5.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 65 GQVLEIRGDRAIVQVFEGTSGIDVKKTtVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYAR 144
Cdd:PRK08472 56 GMVVVIEKEQFGISPFSFIEGFKIGDK-VFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 145 IYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRqaGLVRPTKdvhdgheenfsiVFAAMGvnlETARF 224
Cdd:PRK08472 135 GLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVK--GCLAPIK------------VVALIG---ERGRE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 225 FKQDFEEN--GSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTeRHVLTILTDMSSYADALREVSAAREEVPGRR 302
Cdd:PRK08472 198 IPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQG-LDVLFIMDSVTRFAMAQREIGLALGEPPTSK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 303 GYPGYMYTDLSTIYERAGRVEGRnGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRL 382
Cdd:PRK08472 277 GYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRV 355
|
....*..
5BW9_d 383 MKSAIGE 389
Cdd:PRK08472 356 MNDIISP 362
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
48-408 |
6.53e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 155.30 E-value: 6.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 48 RYNEIVNLTLPDGTVR-QGQVLEIRGDRAIVQVFEGTSGIDvKKTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKV 126
Cdd:PRK06936 43 RIGELCYLRNPDNSLSlQAEVIGFAQHQALLTPLGEMYGIS-SNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 127 FAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQAglvrpTKDVhdghee 206
Cdd:PRK06936 122 EPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSA-----EVDV------ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 207 nfsIVFAAMGV-NLETARFFKQDFEENGsLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTERhVLTILTDMSSYA 285
Cdd:PRK06936 191 ---TVLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKR-VLLLMDSVTRFA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 286 DALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGrvEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLH 365
Cdd:PRK06936 266 RAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLA 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
5BW9_d 366 NKGIYPPINVLPSLSRLMKSAIGegmtrKDHGDVSN---QLYAKYA 408
Cdd:PRK06936 344 AANHYPAIDVLRSASRVMNQIVS-----KEHKTWAGrlrELLAKYE 384
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
52-465 |
7.80e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 155.36 E-value: 7.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 52 IVNLTLPDgtVRQGQ------------VLEIRGDRAIVQVFEGTSGIDVKKTtVEFTGESLRIPVSEDMLGRIFDGSGRP 119
Cdd:PRK06820 40 LLRASLPG--VAQGElcriepqgmlaeVVSIEQEMALLSPFASSDGLRCGQW-VTPLGHMHQVQVGADLAGRILDGLGAP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 120 IDNGPKVfAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICrqaglvrptkd 199
Cdd:PRK06820 117 IDGGPPL-TGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC----------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 200 vhdGHEENFSIVFAAMGvnlETARFFKQDFEENGSLE---RTSLFLNLANDPTIERIITPRLALTTAEYLAYQTeRHVLT 276
Cdd:PRK06820 185 ---ADSAADVMVLALIG---ERGREVREFLEQVLTPEaraRTVVVVATSDRPALERLKGLSTATTIAEYFRDRG-KKVLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 277 ILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEG 356
Cdd:PRK06820 258 MADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 357 QIFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEGmtRKDHGDVSNQLYAKYaigkDAAAMKAVVGEEALSiEDKLSLEFL 436
Cdd:PRK06820 336 HIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAG--QLAMAQKLRRMLACY----QEIELLVRVGEYQAG-EDLQADEAL 408
|
410 420 430
....*....|....*....|....*....|.
5BW9_d 437 EKFE--KTFITQGAYEDRTVFESLDQAWSLL 465
Cdd:PRK06820 409 QRYPaiCAFLQQDHSETAHLETTLEHLAQVV 439
|
|
| 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 ... |
28-98 |
1.17e-39 |
|
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core, that is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex which forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349742 [Multi-domain] Cd Length: 72 Bit Score: 137.95 E-value: 1.17e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5BW9_d 28 YNTVSGVNGPLVILEKVKFPRYNEIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDVKKTTVEFTGE 98
Cdd:cd18118 2 YRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
93-465 |
1.00e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 143.71 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 93 VEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPI 172
Cdd:PRK07721 84 VEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 173 FSASGLPHNEIAAQICRQAglvrpTKDVHdgheenfsiVFAAMGvnlETAR----FFKQDFEENGsLERTSLFLNLANDP 248
Cdd:PRK07721 164 FAGSGVGKSTLMGMIARNT-----SADLN---------VIALIG---ERGRevreFIERDLGPEG-LKRSIVVVATSDQP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 249 TIERIITPRLALTTAEYLAYQTeRHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEgrNGS 328
Cdd:PRK07721 226 ALMRIKGAYTATAIAEYFRDQG-LNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 329 ITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSN---QLYA 405
Cdd:PRK07721 303 ITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLS 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 406 KYAIGKDAAAMKAVVGEEALSIEDklSLEFLEKFEkTFITQGAYEDRTVFESLDQAWSLL 465
Cdd:PRK07721 378 TYQNSEDLINIGAYKRGSSREIDE--AIQFYPQII-SFLKQGTDEKATFEESIQALLSLF 434
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
57-419 |
1.56e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 140.47 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 57 LPDGTVrqGQVLEIRGDRAIVQVFEGTSGIDVKKTtVEFTGESLRIPVSEDMLGRIFDGSGRPIDNG--PKVFAEDYldi 134
Cdd:PRK07594 49 KPGEEL--AEVVGINGSKALLSPFTSTIGLHCGQQ-VMALRRRHQVPVGEALLGRVIDGFGRPLDGRelPDVCWKDY--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 135 NGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQaglvrPTKDVHdgheenfsiVFAA 214
Cdd:PRK07594 123 DAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNA-----PDADSN---------VLVL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 215 MGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTERhVLTILTDMSSYADALREVSAA 294
Cdd:PRK07594 189 IGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 295 REEVPGRRGYPGYMYTDLSTIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPIN 374
Cdd:PRK07594 268 AGETAVSGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAID 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
5BW9_d 375 VLPSLSRLMKSAIGE-----GMTRKDHGDVSNQL-----YAKYAIGKDAAAMKAV 419
Cdd:PRK07594 346 VLATLSRVFPVVTSHehrqlAAILRRCLALYQEVellirIGEYQRGVDTDTDKAI 400
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
101-465 |
3.68e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 139.87 E-value: 3.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 101 RIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPH 180
Cdd:PRK05688 102 RLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 181 NEIAAQICRQAglvrpTKDVhdgheenfsIVFAAMGvnlETARFFKQDFEE---NGSLERTSLFLNLANDPTIERIITPR 257
Cdd:PRK05688 182 SVLLGMMTRFT-----EADI---------IVVGLIG---ERGREVKEFIEHilgEEGLKRSVVVASPADDAPLMRLRAAM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 258 LALTTAEYLAYQTERhVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTM 337
Cdd:PRK05688 245 YCTRIAEYFRDKGKN-VLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVLS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 338 PNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIG-EGMTRKDHgdvSNQLYAKYAIGKDAAAM 416
Cdd:PRK05688 324 EGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQSRDLISV 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
5BW9_d 417 KAVV-GEEAlsiEDKLSLEFLEKFEKtFITQGAYEDRTVFESLDQAWSLL 465
Cdd:PRK05688 401 GAYVaGGDP---ETDLAIARFPHLVQ-FLRQGLRENVSLAQSREQLAAIF 446
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
55-386 |
1.24e-35 |
|
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: 139.06 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 55 LTLPDGtvRQGQVLEIRGDRAIVQVFEGTSGIDvKKTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYldi 134
Cdd:TIGR00962 52 IEFEGG--VQGIALNLEEDSVGAVIMGDYSDIR-EGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEF--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 135 ngSPINPYA-----RIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQ-ICRQAGlvrptKDVHdgheenf 208
Cdd:TIGR00962 126 --SPVEKIApgvieRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDtIINQKD-----SDVY------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 209 sIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTErHVLTILTDMSSYADAL 288
Cdd:TIGR00962 192 -CIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGK-HALIIYDDLSKQAVAY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 289 REVSAAREEVPGRRGYPGYMYTDLSTIYERAGRV--EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHN 366
Cdd:TIGR00962 270 RQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFN 349
|
330 340
....*....|....*....|
5BW9_d 367 KGIYPPINVLPSLSRLMKSA 386
Cdd:TIGR00962 350 SGIRPAINVGLSVSRVGGAA 369
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
48-432 |
7.81e-35 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 135.67 E-value: 7.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 48 RYNEIVNLTLPDGTVRQ-GQVLEIRGDRAIVQVFEGTSGIDvKKTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKV 126
Cdd:PRK09099 44 TLGELCELRQRDGTLLQrAEVVGFSRDVALLSPFGELGGLS-RGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 127 FAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQAGLvrptkDVHdghee 206
Cdd:PRK09099 123 DCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQC-----DVN----- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 207 nfsiVFAAMGV-NLETARFFKQDFEENGsLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTERhVLTILTDMSSYA 285
Cdd:PRK09099 193 ----VIALIGErGREVREFIELILGEDG-MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 286 DALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLH 365
Cdd:PRK09099 267 RAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 366 NKGIYPPINVLPSLSRLMKSaigegMTRKDHGDVSN---QLYAK------------YAIGKDAAAMKAVVGEEAlsIEDK 430
Cdd:PRK09099 345 ARNQYPAIDVLGSLSRVMPQ-----VVPREHVQAAGrlrQLLAKhrevetllqvgeYRAGSDPVADEAIAKIDA--IRDF 417
|
..
5BW9_d 431 LS 432
Cdd:PRK09099 418 LS 419
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
100-381 |
1.72e-34 |
|
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: 130.76 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 100 LRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDY--LDINGSPINPyaRIYPEEMISTGVSAIDTMNSIARGQKIPIFSASG 177
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERrrVESKAPGIIP--RQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 178 LPHNEIAAQ-ICRQAGlvrptKDVHdgheenfsIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITP 256
Cdd:cd01132 80 TGKTAIAIDtIINQKG-----KKVY--------CIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 257 RLALTTAEYLAYqTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRV--EGRNGSITQIPI 334
Cdd:cd01132 147 YAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLsdELGGGSLTALPI 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
5BW9_d 335 LTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSR 381
Cdd:cd01132 226 IETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
97-412 |
1.28e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 132.52 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 97 GESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSAS 176
Cdd:PRK08972 92 GEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 177 GLPHNEIAAQICRQAglvrpTKDVhdgheenfsIVFAAMGvnlETARFFKQDFEE---NGSLERTSLFLNLANDPTIERI 253
Cdd:PRK08972 172 GVGKSVLLGMMTRGT-----TADV---------IVVGLVG---ERGREVKEFIEEilgEEGRARSVVVAAPADTSPLMRL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 254 ITPRLALTTAEYLAYQTeRHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIP 333
Cdd:PRK08972 235 KGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 334 ILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVS---NQLYAKYAIG 410
Cdd:PRK08972 314 TVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQN 388
|
..
5BW9_d 411 KD 412
Cdd:PRK08972 389 RD 390
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
27-446 |
4.22e-33 |
|
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: 131.38 E-value: 4.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 27 NYNTVSGVNGPLVileKVKFPRYN--EIVNLTLPDGTVRQGQVLEIR---GD---RAIVqvFEGTSGIdVKKTTVEFTGE 98
Cdd:TIGR01039 1 TKGKVVQVIGPVV---DVEFEQGElpRIYNALKVQNRAESELTLEVAqhlGDdtvRTIA--MGSTDGL-VRGLEVIDTGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 99 SLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINpYARIYPE-EMISTGVSAIDTMNSIARGQKIPIFSASG 177
Cdd:TIGR01039 75 PISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPS-FEEQSTKvEILETGIKVIDLLAPYAKGGKIGLFGGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 178 LPHNEIAAQicrqagLVRPTKDVHDGHEenfsiVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPR 257
Cdd:TIGR01039 154 VGKTVLIQE------LINNIAKEHGGYS-----VFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 258 LALTTAEYLAYQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAgrVEGRNGSITQIPILTM 337
Cdd:TIGR01039 223 TGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKTGSITSVQAVYV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 338 PNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMK-SAIGEgmtrkDHGDVSNQLYAKYAIGKDAAAM 416
Cdd:TIGR01039 301 PADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQILQRYKELQDI 375
|
410 420 430
....*....|....*....|....*....|
5BW9_d 417 KAVVGEEALSIEDKLSLEFLEKFEKtFITQ 446
Cdd:TIGR01039 376 IAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
57-381 |
4.29e-33 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 131.96 E-value: 4.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 57 LPDgtVRQGQVLEIRGD-RAIVQVFE----------GTSGIDvKKTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPK 125
Cdd:PRK13343 44 LPD--AALDELLRFEGGsRGFAFNLEeelvgavlldDTADIL-AGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 126 VFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQ-ICRQAGlvrptKDVHdgh 204
Cdd:PRK13343 121 LQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDaIINQKD-----SDVI--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 205 eenfsIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTeRHVLTILTDMSSY 284
Cdd:PRK13343 193 -----CVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQG-QDALIVYDDLSKH 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 285 ADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRN--GSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDR 362
Cdd:PRK13343 267 AAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDS 346
|
330
....*....|....*....
5BW9_d 363 QLHNKGIYPPINVLPSLSR 381
Cdd:PRK13343 347 DLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
59-386 |
6.56e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 130.50 E-value: 6.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 59 DGTVRQGQVLEIRGDRAIVQVFEgtSGIDVKKTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDN-GPKVFAEDYLDINGS 137
Cdd:PRK06002 58 DGGTHLGEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPIDGlGPLAPGTRPMSIDAT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 138 PINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQAGLvrptkdvhDgheenfSIVFAAMGv 217
Cdd:PRK06002 136 APPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAF--------D------TVVIALVG- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 218 nlETARFFKQDFEEN--GSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTERhVLTILTDMSSYADALREVSAAR 295
Cdd:PRK06002 201 --ERGREVREFLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGEN-VLLIVDSVTRFAHAAREVALAA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 296 EEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINV 375
Cdd:PRK06002 278 GEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDP 357
|
330
....*....|.
5BW9_d 376 LPSLSRLMKSA 386
Cdd:PRK06002 358 LASISRLARHA 368
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
51-465 |
6.17e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 127.98 E-value: 6.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 51 EIVNLTLPDGTV----RQ--GQVLEI-------RGDRAIVQVFEGTSGID------VKKTTVEFTGESLRIPVSEDMLGR 111
Cdd:PRK07960 40 EATGLQLPLGATcvieRQngSETHEVesevvgfNGQRLFLMPLEEVEGILpgarvyARNISGEGLQSGKQLPLGPALLGR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 112 IFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICR-- 189
Cdd:PRK07960 120 VLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARyt 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 190 QAglvrptkDVhdgheenfsIVFAAMGvnlETARFFKqDFEEN--GSLERT-SLFLNLANDptieriITPRLALTTAEYL 266
Cdd:PRK07960 200 QA-------DV---------IVVGLIG---ERGREVK-DFIENilGAEGRArSVVIAAPAD------VSPLLRMQGAAYA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 267 AYQTE------RHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMPND 340
Cdd:PRK07960 254 TRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 341 DITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEGMTRKdhgdVSN--QLYAKYAIGKDAAAMKA 418
Cdd:PRK07960 334 DQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR----VRQfkQLLSSFQRNRDLVSVGA 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
5BW9_d 419 -VVGEEALSieDKlSLEFLEKFEKtFITQGAYEdRTVFESLDQAWSLL 465
Cdd:PRK07960 410 yAKGSDPML--DK-AIALWPQLEA-FLQQGIFE-RADWEDSLQALERI 452
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
91-386 |
1.99e-31 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 126.62 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 91 TTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKI 170
Cdd:CHL00059 65 SSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 171 PIFSASGLPHNEIAAQ-ICRQAGlvrptkdvhdgheENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPT 249
Cdd:CHL00059 145 LIIGDRQTGKTAVATDtILNQKG-------------QNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 250 IERIITPRLALTTAEYLAYqTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGR--NG 327
Cdd:CHL00059 212 TLQYLAPYTGAALAEYFMY-RGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQlgEG 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
5BW9_d 328 SITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSA 386
Cdd:CHL00059 291 SMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
66-461 |
2.65e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 125.48 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 66 QVLEIRGDRAIVQVFEGTSGIdVKKTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARI 145
Cdd:PRK06793 56 EVIAIEKENNMLLPFEQTEKV-CYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFERE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 146 YPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQAglvrptkdvhdghEENFSIVFAAMGVNLETARFF 225
Cdd:PRK06793 135 EITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNA-------------KADINVISLVGERGREVKDFI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 226 KQDFEENGsLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTeRHVLTILTDMSSYADALREVSAAREEVPgRRGYP 305
Cdd:PRK06793 202 RKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQG-NNVLLMMDSVTRFADARRSVDIAVKELP-IGGKT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 306 GYMYTDLSTIYERAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKS 385
Cdd:PRK06793 279 LLMESYMKKLLERSGKTQ--KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5BW9_d 386 AIGEgmtrkDHGDVSNQLYAKYAIGKDaAAMKAVVGEEALSIEDKLSLEFLEKFE--KTFITQGAyEDRTVFESLDQA 461
Cdd:PRK06793 357 IVSP-----NHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEgiNTFLKQGR-SDSFQFDDIVEA 427
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
13-383 |
8.57e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 124.32 E-value: 8.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 13 KKAVEQGFNVKPRLNYNTVSGVNGPLVILE-KVKFPRYNEIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDvKKT 91
Cdd:PRK08927 3 AALAAAIGDIDTLVIYGRVVAVRGLLVEVAgPIHALSVGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVR-RGC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 92 TVEFTGESLRIPVSEDMLGRIFDGSGRPIDN-GPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKI 170
Cdd:PRK08927 82 RAVIANAAAAVRPSRAWLGRVVNALGEPIDGkGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 171 PIFSASGLPHNEIAAQICRQAglvrpTKDVhdgheenfsIVFAAMGvnlETAR----FFKQDFEENGsLERTSLFLNLAN 246
Cdd:PRK08927 162 GIFAGSGVGKSVLLSMLARNA-----DADV---------SVIGLIG---ERGRevqeFLQDDLGPEG-LARSVVVVATSD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 247 DPTIERIITPRLALTTAEYLAYQtERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRN 326
Cdd:PRK08927 224 EPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGE 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
5BW9_d 327 GSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLM 383
Cdd:PRK08927 303 GTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
66-382 |
2.06e-29 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 120.10 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 66 QVLEIRGDRAIVQVFEGTSGIDvKKTTVEFTGESLRIPVSEDMLGRIFDGSGR-------PIDNGPKVfaeDYLDINGSP 138
Cdd:PRK08149 47 QVVGFQRERTILSLIGNAQGLS-RQVVLKPTGKPLSVWVGEALLGAVLDPTGKiverfdaPPTVGPIS---EERVIDVAP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 139 INPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQAglvrpTKDVHdgheenfsiVFAAMGvn 218
Cdd:PRK08149 123 PSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHS-----EADVF---------VIGLIG-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 219 lETARF---FKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTERhVLTILTDMSSYADALREVSAAR 295
Cdd:PRK08149 187 -ERGREvteFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKR-VVLFIDSMTRYARALRDVALAA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 296 EEVPGRRGYPGYMYTDLSTIYERAGRVegRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINV 375
Cdd:PRK08149 265 GELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDV 342
|
....*..
5BW9_d 376 LPSLSRL 382
Cdd:PRK08149 343 LKSVSRV 349
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
30-467 |
1.12e-27 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 116.81 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 30 TVSGVNGPLVILEKVKFPRYNEIV---NLTLPdgtvrqGQVLEIRGDRAIVQVFEGTSGIDVkKTTVEFTGESLRIPVSE 106
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVrvgEEGLI------GEIIRIEGDKATIQVYEETSGIKP-GEPVEFTGEPLSVELGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 107 DMLGRIFDGSGRPIDN--------------------------------GPKVFAEDYL---------------------- 132
Cdd:PRK04192 79 GLLGSIFDGIQRPLDElaeksgdflergvyvpaldrekkweftptvkvGDKVEAGDILgtvqetpsiehkimvppgvsgt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 133 ----------------------DINGSPIN-----------PYA-RIYPEEMISTGVSAIDTMNSIARGQK--IPIFSAS 176
Cdd:PRK04192 159 vkeivsegdytvddtiavledeDGEGVELTmmqkwpvrrprPYKeKLPPVEPLITGQRVIDTFFPVAKGGTaaIPGPFGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 177 G---LPHneiaaQICRQAglvrpTKDVhdgheenfsIVFAAMG------VnlETARFFKQ--DFEENGSL-ERTSLFLNL 244
Cdd:PRK04192 239 GktvTQH-----QLAKWA-----DADI---------VIYVGCGergnemT--EVLEEFPEliDPKTGRPLmERTVLIANT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 245 ANDPTIER---IITprlALTTAEYlaY-QTERHVLtILTDMSS-YADALREVSAAREEVPGRRGYPGYMYTDLSTIYERA 319
Cdd:PRK04192 298 SNMPVAAReasIYT---GITIAEY--YrDMGYDVL-LMADSTSrWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 320 GRVE---GRNGSITQIPILTMPNDDITHPIPDLTGYITEgqIF--VDRQLHNKGIYPPINVLPSLSrLMKSAIGEGMTRK 394
Cdd:PRK04192 372 GRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVK--VFwaLDAELADRRHFPAINWLTSYS-LYLDQVAPWWEEN 448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5BW9_d 395 DHGDVSNqlYAKYAI-----GKDAAAMKAVVGEEALSIEDKLSLEFLEKFEKTFITQGAYEDRTVFESLDQAWSLLRI 467
Cdd:PRK04192 449 VDPDWRE--LRDEAMdllqrEAELQEIVRLVGPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKL 524
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
102-381 |
2.99e-27 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 113.85 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 102 IPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHN 181
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 182 EIAAQICRqaglvrptkdvhdGHEENFSIVfAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALT 261
Cdd:PRK05922 172 SLLSTIAK-------------GSKSTINVI-ALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 262 TAEYLAYQTERhVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEgrNGSITQI-PILTMPNd 340
Cdd:PRK05922 238 IAEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYPN- 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....
5BW9_d 341 ditHP--IPDLTGYITEGQIFVDRQlhNKGIY-PPINVLPSLSR 381
Cdd:PRK05922 314 ---HPdiFTDYLKSLLDGHFFLTPQ--GKALAsPPIDILTSLSR 352
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
101-383 |
1.12e-26 |
|
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: 109.23 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 101 RIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPiNPYARIYPE-EMISTGVSAIDTMNSIARGQKIPIFSASG-- 177
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA-PEFVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 178 -------LPHNeIAAQicrqaglvrptkdvHDGheenFSiVFAAMGVNLETARFFKQDFEENG-----SLERTSLFLNLA 245
Cdd:cd01133 80 ktvlimeLINN-IAKA--------------HGG----YS-VFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 246 NDPTIERIITPRLALTTAEYLAYQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVegR 325
Cdd:cd01133 140 NEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST--K 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
5BW9_d 326 NGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLM 383
Cdd:cd01133 218 KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
59-420 |
3.65e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 110.75 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 59 DGTVRQGQVLEIRGDRAIVQVFEGTSGI--DVKKTTVEFTGEsLRIpvSEDMLGRIFDGSGRPIDNGPKVFAEDYLDING 136
Cdd:PRK07196 48 DETFIEAQVVGFDRDITYLMPFKHPGGVlgGARVFPSEQDGE-LLI--GDSWLGRVINGLGEPLDGKGQLGGSTPLQQQL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 137 SPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRqaglvrptkdvhdgHEENFSIVFAAMG 216
Cdd:PRK07196 125 PQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITR--------------YTQADVVVVGLIG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 217 VNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLAyQTERHVLTILTDMSSYADALREVSAARE 296
Cdd:PRK07196 191 ERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYR-DKGHDVLLLVDSLTRYAMAQREIALSLG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 297 EVPGRRGYPGYMYTDLSTIYERAGRVEGrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVL 376
Cdd:PRK07196 270 EPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDIS 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
5BW9_d 377 PSLSRLMKSAIGegmtrKDHGDVSNQL---YAKYAIGKDAAAMKAVV 420
Cdd:PRK07196 349 QSISRCMSQVIG-----SQQAKAASLLkqcYADYMAIKPLIPLGGYV 390
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-381 |
1.58e-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: 103.58 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 1 MVLSDKELFAINKKAVEQgFNVKPRL-NYNTVSGVNGPLVI---LEKVkfpRYNEIvnLTLPDGTvrQGQVLEIRGDRAI 76
Cdd:COG0056 1 MQIRPEEISSIIKQQIEN-YDPEVEVeEVGTVLSVGDGIARvygLPNA---MAGEL--LEFPGGV--YGMALNLEEDNVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 77 VQVFEGTSGI---DvkktTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINgspinpyaRIYP------ 147
Cdd:COG0056 73 VVLLGDYEGIkegD----TVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVE--------RPAPgvidrq 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 148 --EEMISTGVSAIDTMNSIARGQKipifsasglphnE------------IAAQ-ICRQAGlvrptKDVHdgheenfsIVF 212
Cdd:COG0056 141 pvHEPLQTGIKAIDAMIPIGRGQR------------EliigdrqtgktaIAIDtIINQKG-----KDVI--------CIY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 213 AAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTeRHVLTILTDMSSYADALREVS 292
Cdd:COG0056 196 VAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQG-KDVLIVYDDLSKHAVAYRELS 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 293 AAREEVPGRRGYPG---YMYtdlSTIYERAGRV--EGRNGSITQIPIL-TMPNddithpipDLTGY-------ITEGQIF 359
Cdd:COG0056 275 LLLRRPPGREAYPGdvfYLH---SRLLERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIF 343
|
410 420
....*....|....*....|..
5BW9_d 360 VDRQLHNKGIYPPINVLPSLSR 381
Cdd:COG0056 344 LESDLFNAGIRPAINVGLSVSR 365
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
92-381 |
1.36e-22 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 100.91 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 92 TVEFTGESLRIPVSEDMLGRIFDGSGRPIDN-GPkvfaedyldINGSPINPYARIYP--------EEMISTGVSAIDTMN 162
Cdd:PRK09281 87 TVKRTGRILEVPVGEALLGRVVNPLGQPIDGkGP---------IEATETRPVERKAPgvidrksvHEPLQTGIKAIDAMI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 163 SIARGQKIPIfsasglphneiaaqIC-RQAG---------LVRPTKDVHdgheenfsIVFAAMGVNLETARFFKQDFEEN 232
Cdd:PRK09281 158 PIGRGQRELI--------------IGdRQTGktaiaidtiINQKGKDVI--------CIYVAIGQKASTVAQVVRKLEEH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 233 GSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTeRHVLTILTDMSSYADALREVSAAREEVPGRRGYPG---YMY 309
Cdd:PRK09281 216 GAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLH 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
5BW9_d 310 tdlSTIYERAGRV--EGRNGSITQIPIL-TMPNDdITHPIPdlTGY--ITEGQIFVDRQLHNKGIYPPINVLPSLSR 381
Cdd:PRK09281 295 ---SRLLERAAKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
27-431 |
1.82e-22 |
|
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: 100.16 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 27 NYNTVSGVNGPLVileKVKFPR------YNEIVNLTLPDGTVrqgqVLEI---RGD---RAIVqvFEGTSGIdVKKTTVE 94
Cdd:COG0055 4 NTGKIVQVIGPVV---DVEFPEgelpaiYNALEVENEGGGEL----VLEVaqhLGDntvRCIA--MDSTDGL-VRGMEVI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 95 FTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPiNPYARIYPE-EMISTGVSAIDTMNSIARGQKIPIF 173
Cdd:COG0055 74 DTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPA-PPFEEQSTKtEILETGIKVIDLLAPYAKGGKIGLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 174 SASG---------LPHNeIAAQicrqaglvrptkdvHDGheenFSiVFAAMGvnlETARF---FKQDFEENGSLERTSLF 241
Cdd:COG0055 153 GGAGvgktvlimeLIHN-IAKE--------------HGG----VS-VFAGVG---ERTREgndLYREMKESGVLDKTALV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 242 LNLANDPTIERIITPRLALTTAEYLAYQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGR 321
Cdd:COG0055 210 FGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 322 VegRNGSITQIPILTMPNDDITHPIP-------DLTgyitegqIFVDRQLHNKGIYPPINVLPSLSRLMKSAI-GEgmtr 393
Cdd:COG0055 290 T--KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE---- 356
|
410 420 430 440
....*....|....*....|....*....|....*....|.
5BW9_d 394 kDHGDVSN---QLYAKYAIGKDAAAMkavVGEEALSIEDKL 431
Cdd:COG0055 357 -EHYRVARevqRILQRYKELQDIIAI---LGMDELSEEDKL 393
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
49-391 |
5.34e-20 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 93.18 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 49 YNEIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDVKKTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFA 128
Cdd:PTZ00185 64 YNTIIMIQVSPTTFAAGLVFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTRS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 129 EDYLD-------INGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIA-AQICRQaglVRPTKDV 200
Cdd:PTZ00185 144 RALLEseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvSTIINQ---VRINQQI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 201 HdghEENFSI-VFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTeRHVLTILT 279
Cdd:PTZ00185 221 L---SKNAVIsIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRG-RHCLCVYD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 280 DMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVE-GRNG-SITQIPILTMPNDDITHPIPDLTGYITEGQ 357
Cdd:PTZ00185 297 DLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKGGgSVTALPIVETLSNDVTAYIVTNVISITDGQ 376
|
330 340 350
....*....|....*....|....*....|....
5BW9_d 358 IFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEGM 391
Cdd:PTZ00185 377 IYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
108-381 |
5.61e-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: 89.94 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 108 MLGRIFDGSGRP---IDNGPKVFAEDYLDINGSPIN---PYA-RIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPH 180
Cdd:cd01134 10 LLGSIFDGIQRPlevIAETGSIFIPRGVNVQRWPVRqprPVKeKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 181 NEIAAQICRQAglvrpTKDVhdgheenfsIVFAAMGVN-LETAR----FFKQDFEENGS--LERTSLFLNLANDPTIERI 253
Cdd:cd01134 90 TVISQSLSKWS-----NSDV---------VIYVGCGERgNEMAEvleeFPELKDPITGEslMERTVLIANTSNMPVAARE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 254 ITPRLALTTAEYLAYQTeRHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVE-----GRNGS 328
Cdd:cd01134 156 ASIYTGITIAEYFRDMG-YNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRclgspGREGS 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
5BW9_d 329 ITQIPILTMPNDDITHPIPDLTGYITegQIF--VDRQLHNKGIYPPINVLPSLSR 381
Cdd:cd01134 235 VTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
102-407 |
1.21e-18 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 88.88 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 102 IPVSEDMLGRIFDGSGRPIDNGPKVFA-EDYLDINGSPINPYARIYP----EEMISTGVSAIDTMNSIARGQKIPIF--S 174
Cdd:PRK07165 73 VKTSKEYFGKIIDIDGNIIYPEAQNPLsKKFLPNTSSIFNLAHGLMTvktlNEQLYTGIIAIDLLIPIGKGQRELIIgdR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 175 ASGLPHNEIAAqICRQAglvrptkdvhdghEENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPtIERII 254
Cdd:PRK07165 153 QTGKTHIALNT-IINQK-------------NTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 255 TPRLALTTAEYLAYQTErhVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNgSITQIPI 334
Cdd:PRK07165 218 APYVAMAHAENISYNDD--VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK-TITALPI 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5BW9_d 335 LTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLmKSAIGEGMTRKDHGDVsNQLYAKY 407
Cdd:PRK07165 295 LQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRT-GSSVQSKTITKVAGEI-SKIYRAY 365
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
28-98 |
2.10e-17 |
|
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: 76.58 E-value: 2.10e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
5BW9_d 28 YNTVSGVNGPLVILEKVKFPRYNEIVNLTLPDG---TVRQGQVLEIRGDRAIVQVFEGTSGIDVkKTTVEFTGE 98
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLSR-GALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
235-380 |
3.78e-16 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 81.99 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 235 LERTSLFLNLANDPTIERIITPRLALTTAEYlaYQTERHVLTILTDMSS-YADALREVSAAREEVPGRRGYPGYMYTDLS 313
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEY--FRDMGYDVALMADSTSrWAEALREISGRLEEMPGEEGYPAYLASKLA 794
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
5BW9_d 314 TIYERAGRV-----EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLS 380
Cdd:PRK14698 795 EFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
96-446 |
1.19e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 79.31 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 96 TGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDyldinGSPINPYARIYPE-----EMISTGVSAIDTMNSIARGQKI 170
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRT-----TSPIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGKI 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 171 PIFSASGLPHN----EIAAQICRQAGLVRptkdvhdgheenfsiVFAAMGvnlETAR----FFKQDFE------ENGSLE 236
Cdd:CHL00060 165 GLFGGAGVGKTvlimELINNIAKAHGGVS---------------VFGGVG---ERTRegndLYMEMKEsgvineQNIAES 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 237 RTSLFLNLANDPTIERIITPRLALTTAEYLAYQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIY 316
Cdd:CHL00060 227 KVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 317 ERAGRVegRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAI-GEgmtrkD 395
Cdd:CHL00060 307 ERITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----E 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
5BW9_d 396 HGDVSN---QLYAKYaigKDAAAMKAVVGEEALSIEDKLSLEFLEKFEKtFITQ 446
Cdd:CHL00060 380 HYETAQrvkQTLQRY---KELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 429
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
31-97 |
2.21e-14 |
|
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: 67.96 E-value: 2.21e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 31 VSGVNGPLVILEKVKFPRYNEIVNLTLP---DGTVRQGQVLEIRGDRAIVQVFEGTSGIDVkKTTVEFTG 97
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVElveFGSLVLGEVLNLGGDKVRVQVFGGTSGLSR-GDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
396-466 |
2.32e-07 |
|
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: 48.21 E-value: 2.32e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5BW9_d 396 HGDVSNQLYAKYAIGKDAAAMKAVVGEEALSIEDKLSLEFLEKFEKtFITQGAYEDRTVFESLDQAWSLLR 466
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
34-121 |
9.45e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 51.56 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5BW9_d 34 VNGPLVILEKVKFPRYNEIVNLTlPDGTVrqGQVLEIRGDRAIVQVFEGTSGIDVKKtTVEFTGESLRIPVSEDMLGRIF 113
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVVRVG-ELGLI--GEIIRLEGDKAVIQVYEETAGLKPGE-PVEGTGSSLSVELGPGLLTSIY 85
|
....*...
5BW9_d 114 DGSGRPID 121
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 ... |
28-98 |
2.51e-06 |
|
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: 44.82 E-value: 2.51e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
5BW9_d 28 YNTVSGVNGPLVILEKVKFPRYNEIV---NLTLPdgtvrqGQVLEIRGDRAIVQVFEGTSGIDVKKtTVEFTGE 98
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVrvgEEGLI------GEIIRLEGDKATIQVYEETSGLKVGE-PVERTGK 67
|
|
| |
