|
Name |
Accession |
Description |
Interval |
E-value |
| V-ATPase_V1_A |
TIGR01042 |
V-type (H+)-ATPase V1, A subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
6-598 |
0e+00 |
|
V-type (H+)-ATPase V1, A 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: 273411 [Multi-domain] Cd Length: 591 Bit Score: 1245.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 6 SYGFVYGVSGPVVTAEKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMG 85
Cdd:TIGR01042 1 EYGYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 86 SIFDGIQRPLKDIADITQSIYIPKGVSTNALSREARWDFVVsKDLRVGGHVTGGDIIGTVDENLLIKHKILLPPSACGTI 165
Cdd:TIGR01042 81 NIFDGIQRPLKAIAEQSQSIYIPRGVNVPALDRDKKWEFTP-KKLRVGDHITGGDIYGTVFENSLIKHKIMLPPRARGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 166 TFVAPSGQYTVEDTLLELEFAGRKQKFSMLQIWPVRSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGK 245
Cdd:TIGR01042 160 TYIAPAGNYTVDDTVLEVEFQGVKKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 246 TVISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDFPELTMEVEGVTTSIMKRTALVANTSNMPVAAREASIYTGITLAEY 325
Cdd:TIGR01042 240 TVISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEVDGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 326 FRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKCLGSPEREGSVTIVGAVSPPGGD 405
Cdd:TIGR01042 320 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 406 FADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRALEEFYEKNYPEFVSLRTKCKEILQEEEDLSEIVQLV 485
Cdd:TIGR01042 400 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 486 GKASLAESDKVTLEVAKIIKDDFLQQNGYTKYDRFCPFYKTVGMLKNMIGFYDLARHAVEATAQSDNKITWNVIKDSMGD 565
Cdd:TIGR01042 480 GKDALAETDKITLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQDDNKITWSIIKESLGD 559
|
570 580 590
....*....|....*....|....*....|...
gi 17565854 566 LIYQLSAMKFKDPvADGEAKIRKDYEDLAEAMA 598
Cdd:TIGR01042 560 LLYRLSSMKFEDP-SDGEAKIKADYEKLNEDMQ 591
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
8-604 |
0e+00 |
|
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 440769 [Multi-domain] Cd Length: 583 Bit Score: 918.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 8 GFVYGVSGPVVTAEKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSI 87
Cdd:COG1155 5 GKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLLGNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 88 FDGIQRPLKDIADITqSIYIPKGVSTNALSREARWDFVVSKdlRVGGHVTGGDIIGTVDENLLIKHKILLPPSACGTITF 167
Cdd:COG1155 85 FDGIQRPLDKIAEKS-GDFIPRGVDVPALDREKKWDFTPTV--KVGDKVSAGDILGTVQETPLIEHKIMVPPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 168 VAPSGQYTVEDTLLELE-FAGRKQKFSMLQIWPVRSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKT 246
Cdd:COG1155 162 IAPEGEYTVEDTIAVLEdEDGEEHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 247 VISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDFPELTMEVEGvtTSIMKRTALVANTSNMPVAAREASIYTGITLAEYF 326
Cdd:COG1155 242 VTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELIDPKTG--RPLMERTVLIANTSNMPVAAREASIYTGITIAEYY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 327 RDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKCLGSPerEGSVTIVGAVSPPGGDF 406
Cdd:COG1155 320 RDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGDF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 407 ADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRALEEFYEKNY-PEFVSLRTKCKEILQEEEDLSEIVQLV 485
Cdd:COG1155 398 SEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDENVdPDWSELRNEAMDLLQEEAELQEIVRLV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 486 GKASLAESDKVTLEVAKIIKDDFLQQNGYTKYDRFCPFYKTVGMLKNMIGFYDLARHAVEATAQSDnkitwnVIKDsmGD 565
Cdd:COG1155 478 GEDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLS------EIKE--LP 549
|
570 580 590
....*....|....*....|....*....|....*....
gi 17565854 566 LIYQLSAMKFkdpvaDGEAKIRKDYEDLAEAMANAFRNL 604
Cdd:COG1155 550 LREKIARMKY-----SPENELLEKFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
8-595 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 888.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 8 GFVYGVSGPVVTAEKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSI 87
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 88 FDGIQRPLKDIADITqSIYIPKGVSTNALSREARWDFVVSkdLRVGGHVTGGDIIGTVDENLLIKHKILLPPSACGTITF 167
Cdd:PRK04192 85 FDGIQRPLDELAEKS-GDFLERGVYVPALDREKKWEFTPT--VKVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 168 VAPSGQYTVEDTLLELE-FAGRKQKFSMLQIWPVRSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKT 246
Cdd:PRK04192 162 IVSEGDYTVDDTIAVLEdEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 247 VISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDFPELTMEVEGvtTSIMKRTALVANTSNMPVAAREASIYTGITLAEYF 326
Cdd:PRK04192 242 VTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELIDPKTG--RPLMERTVLIANTSNMPVAAREASIYTGITIAEYY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 327 RDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKCLGSPerEGSVTIVGAVSPPGGDF 406
Cdd:PRK04192 320 RDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGDF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 407 ADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRALEEFYEKN-YPEFVSLRTKCKEILQEEEDLSEIVQLV 485
Cdd:PRK04192 398 SEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEENvDPDWRELRDEAMDLLQREAELQEIVRLV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 486 GKASLAESDKVTLEVAKIIKDDFLQQNGYTKYDRFCPFYKTVGMLKNMIGFYDLARHAVEATAqSDNKITWNVIKDSMGD 565
Cdd:PRK04192 478 GPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGV-PVSEILELEVRDRIAR 556
|
570 580 590
....*....|....*....|....*....|
gi 17565854 566 LIYQLSAMkFKDPVADGEAKIRKDYEDLAE 595
Cdd:PRK04192 557 LKYIPENE-YLEKIDEIFEKLEEELEELIA 585
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
8-591 |
0e+00 |
|
ATP synthase archaeal, A 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: 130115 [Multi-domain] Cd Length: 578 Bit Score: 805.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 8 GFVYGVSGPVVTAEKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSI 87
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 88 FDGIQRPLKDIADITQSiYIPKGVSTNALSREARWDFVvsKDLRVGGHVTGGDIIGTVDENLLIKHKILLPPSACGTITF 167
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGD-FIARGVDAPGLDRDKKWHFK--PTVKEGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 168 VAPSGQYTVEDTLLELEFAGRkQKFSMLQIWPVRSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTV 247
Cdd:TIGR01043 159 IAEEGDYTVEDTIAVVDTDGD-EEIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 248 ISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDFPELTMEVEGvtTSIMKRTALVANTSNMPVAAREASIYTGITLAEYFR 327
Cdd:TIGR01043 238 TQHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPELKDPKTG--KPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 328 DMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKCLGSPEREGSVTIVGAVSPPGGDFA 407
Cdd:TIGR01043 316 DMGYDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDFS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 408 DPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRALEEFYEKNY-PEFVSLRTKCKEILQEEEDLSEIVQLVG 486
Cdd:TIGR01043 396 EPVTQNTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVQDWWHENVdPDWREMRDEAMDLLQKESELQEIVQLVG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 487 KASLAESDKVTLEVAKIIKDDFLQQNGYTKYDRFCPFYKTVGMLKNMIGFYDLARHAVEATAQSDnKITWNVIKDSMGDL 566
Cdd:TIGR01043 476 PDALPERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVE-EILKLEVKEEIGRM 554
|
570 580
....*....|....*....|....*
gi 17565854 567 IYQLSAmKFKDPVADGEAKIRKDYE 591
Cdd:TIGR01043 555 KYEPDN-DILAKIDEILEKIEKEFK 578
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
74-446 |
0e+00 |
|
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: 618.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 74 PLSVELGPGIMGSIFDGIQRPLKDIADiTQSIYIPKGVSTnalsrearwdfvvskdlrvgghvtggdiigtvdenllikh 153
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAE-TGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 154 killppsacgtitfvapsgqytvedtllelefagrkqkfsmlQIWPVRSPRPVTEKLAANNPLLCGQRVLDALFPCVQGG 233
Cdd:cd01134 40 ------------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGG 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 234 TTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDFPELTMEVEGVttSIMKRTALVANTSNMPVAARE 313
Cdd:cd01134 78 TAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGE--SLMERTVLIANTSNMPVAARE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 314 ASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKCLGSPEREGSV 393
Cdd:cd01134 156 ASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSV 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17565854 394 TIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEY 446
Cdd:cd01134 236 TIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
246-595 |
1.68e-119 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 378.60 E-value: 1.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 246 TVISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDFPELTMEVEGvtTSIMKRTALVANTSNMPVAAREASIYTGITLAEY 325
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTG--KPLMERTVLIANTSNMPVAAREASIYTGITIAEY 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 326 FRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKCLGSPEREGSVTIVGAVSPPGGD 405
Cdd:PRK14698 748 FRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGD 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 406 FADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRALEEFYEKNY-PEFVSLRTKCKEILQEEEDLSEIVQL 484
Cdd:PRK14698 828 FSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVdPEWKAMRDKAMELLQKEAELQEIVRI 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 485 VGKASLAESDKVTLEVAKIIKDDFLQQNGYTKYDRFCPFYKTVGMLKNMIGFYDLARHAVEATAQSDnKITWNVIKDSMG 564
Cdd:PRK14698 908 VGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPLE-EIAKLPVREEIG 986
|
330 340 350
....*....|....*....|....*....|.
gi 17565854 565 dliyqlsAMKFKDPVADGEAKIRKDYEDLAE 595
Cdd:PRK14698 987 -------RMKFEPDIEKIKALIDKTNEQFDE 1010
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
219-444 |
7.14e-105 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 315.45 E-value: 7.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 219 GQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDFPEltmevegvtTSIMKRT 298
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLG---------SGALKRT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 299 ALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERA 378
Cdd:pfam00006 72 VVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17565854 379 GRVKclgspEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYS 444
Cdd:pfam00006 152 GRVK-----GKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
194-446 |
1.62e-89 |
|
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: 278.18 E-value: 1.62e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 194 MLQIWPVRSPRP-VTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNS---DAIIYVGCGER 269
Cdd:cd19476 28 TKQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKahaGVVVFAGIGER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 270 GNEMSEVLRDFPEltmevegvtTSIMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALRE 349
Cdd:cd19476 108 GREVNDLYEEFTK---------SGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALRE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 350 ISGRLGEMPADSGYPAYLAARLASFYERAGRVKclgspEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLA 429
Cdd:cd19476 179 MSALLGEPPGREGYPPYLFTKLATLYERAGKVK-----DGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELA 253
|
250
....*....|....*..
gi 17565854 430 QRKHFPSINWLISYSEY 446
Cdd:cd19476 254 RKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
8-252 |
3.26e-71 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 248.01 E-value: 3.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 8 GFVYGVSGPVVTAEKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSI 87
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 88 FDGIQRPLKDIADITQSiYIPKGVSTNALSREARWDFVvsKDLRVGGHVTGGDIIGTVDENLLIKHKILLPPSACGTITF 167
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFI--PKVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 168 VAPSGQYTVEDTLLELEF-AGRKQKFSMLQIWPVRSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKT 246
Cdd:PRK14698 162 IADEGEYTIEEVIAKVKTpSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKC 241
|
....*.
gi 17565854 247 VISQSL 252
Cdd:PRK14698 242 VDGDTL 247
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
88-210 |
6.86e-65 |
|
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the alpha-beta catalytic subunit of VATA or V-type proton ATPase catalytic subunit at the N-terminal end. It is found from bacteria to humans, and was not modelled in family ATP-synt_ab, pfam00006.
Pssm-ID: 465299 [Multi-domain] Cd Length: 120 Bit Score: 208.41 E-value: 6.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 88 FDGIQRPLKDIADITQSiYIPKGVSTNALSREARWDFVVSkdLRVGGHVTGGDIIGTVDENLLIKHKILLPPSACGTITF 167
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTPT--VKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 17565854 168 VAPSGQYTVEDTLLELEFAGRKQKFSMLQIWPVRSPRPVTEKL 210
Cdd:pfam16886 78 IAPEGEYTVEDTIAEVEDEGKEKELTMMQKWPVRRPRPYKEKL 120
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
461-566 |
1.27e-50 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex 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.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 169.88 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 461 FVSLRTKCKEILQEEEDLSEIVQLVGKASLAESDKVTLEVAKIIKDDFLQQNGYTKYDRFCPFYKTVGMLKNMIGFYDLA 540
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....*.
gi 17565854 541 RHAVEAtAQSDNKITWNVIKDSMGDL 566
Cdd:cd18111 81 LEALEK-GVPLSKILELPVREKIARM 105
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
39-511 |
6.14e-46 |
|
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP synthase F1, beta subunit. It is a mixture of members with two different protein functions. The first group is exemplified by Salmonella typhimurium FliI protein. It is needed for flagellar assembly, its ATPase activity is required for flagellation, and it may be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. The second group of proteins function in the export of virulence proteins; exemplified by Yersinia sp. YscN protein an ATPase involved in the type III secretory pathway for the antihost Yops proteins. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273401 [Multi-domain] Cd Length: 440 Bit Score: 168.32 E-value: 6.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 39 LVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLKdiaditqsiyipkgvstnalsr 118
Cdd:TIGR01026 59 LVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSIKVGDGLLGRVLDGLGKPID---------------------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 119 earwdfvvskdlrvgghvTGGDIIGTVDENLLIKhkillPPSAcgtitfvapsgqytvedtllelefagrkqkfsmlqiw 198
Cdd:TIGR01026 117 ------------------GKGKFLDNVETEGLIT-----APIN------------------------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 199 PVRSPrPVTEKLaannplLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEmsevLR 278
Cdd:TIGR01026 137 PLKRA-PIREIL------STGVRSIDGLLTVGKGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGRE----VR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 279 DFPELTMEVEGvttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMP 358
Cdd:TIGR01026 206 EFIEHDLGEEG-----LKRSVVVVATSDQSPLLRLKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 359 ADSGYPAYLAARLASFYERAGrvkclgsPEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSIN 438
Cdd:TIGR01026 281 ATKGYTPSVFSTLPRLLERAG-------ASGKGSITAFYTVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAID 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17565854 439 WLISYSEYMRAL--EEFYEKnypefvslRTKCKEIL---QEEEDLSEIvQLVGKASLAESDKVTLEVAKIIKddFLQQ 511
Cdd:TIGR01026 354 VLASISRLMTAIvsEEHRRA--------ARKFRELLskyKDNEDLIRI-GAYQRGSDRELDFAIAKYPKLER--FLKQ 420
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
15-535 |
2.82e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 163.45 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 15 GPVVTAEKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSIFDGIQRP 94
Cdd:PRK06820 37 GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 95 LKDiaditqsiyipkgvstnalsrearwdfvvskdlrvgghvtggdiigtvdenllikhkilLPPSACgtitfvapsgqy 174
Cdd:PRK06820 117 IDG-----------------------------------------------------------GPPLTG------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 175 tvedTLLELEFAgrkqkfsmlqiwpvrSPRPVTEKLAaNNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSK 254
Cdd:PRK06820 126 ----QWRELDCP---------------PPSPLTRQPI-EQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 255 YSNSDAIIYVGCGERGNEmsevLRDFPELTMevegvTTSIMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVA 334
Cdd:PRK06820 186 DSAADVMVLALIGERGRE----VREFLEQVL-----TPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 335 MMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGrvkclgsPEREGSVTIVGAVSPPGGDFADPVTSAT 414
Cdd:PRK06820 257 LMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG-------NSDRGSITAFYTVLVEGDDMNEPVADEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 415 LGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMraleefyeknyPEFVSLRTKC-----KEILQEEEDLSEIVQlVG--- 486
Cdd:PRK06820 330 RSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-----------PQIVSAGQLAmaqklRRMLACYQEIELLVR-VGeyq 397
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 17565854 487 KASLAESDKvTLEVAKIIKdDFLQQNGytkyDRFCPFYKTVGMLKNMIG 535
Cdd:PRK06820 398 AGEDLQADE-ALQRYPAIC-AFLQQDH----SETAHLETTLEHLAQVVG 440
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
7-534 |
2.79e-42 |
|
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: 157.89 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 7 YGFVYGVSGPVVTAEKMAGS--AMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIM 84
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 85 GSIFDGIQRPLKDIADITQSIYIP-KGVSTNALSRearwdfvvskdlrvgghvtggdiigtvdenllikhkillppsacg 163
Cdd:COG1157 100 GRVLDGLGRPLDGKGPLPGEERRPlDAPPPNPLER--------------------------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 164 titfvapsgqytvedtllelefagrkqkfsmlqiwpvrspRPVTEklaannPLLCGQRVLDALFPCVQG---GTTAipGA 240
Cdd:COG1157 135 ----------------------------------------ARITE------PLDTGVRAIDGLLTVGRGqriGIFA--GS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 241 fGCGKTVISQSLSKYSNSDaIIYVG-CGERGNEmsevLRDFPELTMEVEGvttsiMKRTALVANTSNMPVAAREASIYTG 319
Cdd:COG1157 167 -GVGKSTLLGMIARNTEAD-VNVIAlIGERGRE----VREFIEDDLGEEG-----LARSVVVVATSDEPPLMRLRAAYTA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 320 ITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGrvkclgsPEREGSVTIVGAV 399
Cdd:COG1157 236 TAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAG-------NGGKGSITAFYTV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 400 SPPGGDFADPVTSATLGI-----VqvfwgLDKKLAQRKHFPSINWLISYSEYMRALEEfyeknyPEFVSLRTKCKEIL-- 472
Cdd:COG1157 309 LVEGDDMNDPIADAVRGIldghiV-----LSRKLAERGHYPAIDVLASISRVMPDIVS------PEHRALARRLRRLLar 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17565854 473 -QEEEDLseIvqLVG---KASLAESDKVtleVAKIIK-DDFLQQngytKYDRFCPFYKTVGMLKNMI 534
Cdd:COG1157 378 yEENEDL--I--RIGayqPGSDPELDEA---IALIPAiEAFLRQ----GMDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
214-444 |
7.00e-42 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 151.94 E-value: 7.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 214 NPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEmsevLRDFPELTMEVEGvtts 293
Cdd:cd01136 49 QPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE----VREFIEKDLGEEG---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 294 iMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLAS 373
Cdd:cd01136 121 -LKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPR 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17565854 374 FYERAGrvkclgsPEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYS 444
Cdd:cd01136 200 LLERAG-------NGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| 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 ... |
7-73 |
1.68e-39 |
|
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: 138.81 E-value: 1.68e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17565854 7 YGFVYGVSGPVVTAEKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGK 73
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
202-535 |
1.03e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 142.20 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 202 SPRPVTEKLAANnPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEmsevLRDFP 281
Cdd:PRK06936 133 APAPMSRRLIET-PLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGRE----VREFI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 282 ELTMEVEGvttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADS 361
Cdd:PRK06936 208 ESDLGEEG-----LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 362 GYPAYLAARLASFYERAGrvkclgsPEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLI 441
Cdd:PRK06936 283 GYPPSVFAALPRLMERAG-------QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLR 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 442 SYSEYMRALEEfyeknyPEFVSLRTKCKEILQEEEDLSEIVQL--VGKASLAESDKVTLEVAKIikDDFLQQNgytkYDR 519
Cdd:PRK06936 356 SASRVMNQIVS------KEHKTWAGRLRELLAKYEEVELLLQIgeYQKGQDKEADQAIERIGAI--RGFLRQG----THE 423
|
330
....*....|....*.
gi 17565854 520 FCPFYKTVGMLKNMIG 535
Cdd:PRK06936 424 LSHFNETLNLLETLTQ 439
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
8-512 |
1.57e-36 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274607 [Multi-domain] Cd Length: 411 Bit Score: 141.07 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 8 GFVYGVSGPvvtaeKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSI 87
Cdd:TIGR03496 8 GLVLEAVGL-----RAPVGSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLGRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 88 FDGIQRPLKDIADITQSIYIP-KGVSTNALSRearwdfvvskdlrvgghvtggdiigtvdenllikhkillppsacgtit 166
Cdd:TIGR03496 83 IDGLGRPLDGKGPLDAGERVPlYAPPINPLKR------------------------------------------------ 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 167 fvapsgqytvedtllelefagrkqkfsmlqiwpvrspRPVTEklaannPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKT 246
Cdd:TIGR03496 115 -------------------------------------APIDE------PLDVGVRAINGLLTVGRGQRMGIFAGSGVGKS 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 247 VISQSLSKYSNSDaIIYVG-CGERGNEmsevLRDFPELTMEVEGvttsiMKRTALVANTSNMPVAAREASIYTGITLAEY 325
Cdd:TIGR03496 152 TLLGMMARYTEAD-VVVVGlIGERGRE----VKEFIEDILGEEG-----LARSVVVAATADESPLMRLRAAFYATAIAEY 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 326 FRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRvkclgSPEREGSVTIVGAVSPPGGD 405
Cdd:TIGR03496 222 FRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGN-----GEEGKGSITAFYTVLVEGDD 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 406 FADPVTSATLGIVQvfwG---LDKKLAQRKHFPSINWLISYSEYMRALEEfyeknyPEFVSLRTKCKEIL---QEEEDLS 479
Cdd:TIGR03496 297 QQDPIADAARAILD---GhivLSRELAEQGHYPAIDILASISRVMPDVVS------PEHRQAARRFKQLLsryQENRDLI 367
|
490 500 510
....*....|....*....|....*....|....*
gi 17565854 480 EIvqlvGkASLAESDKVTLE-VAKIIK-DDFLQQN 512
Cdd:TIGR03496 368 SI----G-AYQAGSDPELDQaIALYPRiEAFLQQG 397
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
35-535 |
2.01e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 141.40 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 35 GHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSIFDGIQRPLKDIAditqsiyIPKGVSTN 114
Cdd:PRK07721 51 GDKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSA-------LPKGLAPV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 115 ALSREarwdfvvskdlrvgghvtggdiigtvdenllikhkillPPSacgtitfvapsgqytvedtllelefagrkqkfsm 194
Cdd:PRK07721 124 STDQD--------------------------------------PPN---------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 195 lqiwPVRSPrPVTEKLAAnnpllcGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEms 274
Cdd:PRK07721 132 ----PLKRP-PIREPMEV------GVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIALIGERGRE-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 275 evLRDFPELTMEVEGvttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRL 354
Cdd:PRK07721 199 --VREFIERDLGPEG-----LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 355 GEMPADSGYPAYLAARLASFYERAGrvkclgsPEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHF 434
Cdd:PRK07721 272 GEPPTTKGYTPSVFAILPKLLERTG-------TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQY 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 435 PSINWLISYSEYMRALEEfyeknyPEFVSLRTKCKEIL---QEEEDLSEIvqlvG---KASLAESDKVTLEVAKIIkdDF 508
Cdd:PRK07721 345 PAINVLKSVSRVMNHIVS------PEHKEAANRFRELLstyQNSEDLINI----GaykRGSSREIDEAIQFYPQII--SF 412
|
490 500
....*....|....*....|....*..
gi 17565854 509 LQQNgytkYDRFCPFYKTVGMLKNMIG 535
Cdd:PRK07721 413 LKQG----TDEKATFEESIQALLSLFG 435
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
198-512 |
4.71e-36 |
|
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: 141.01 E-value: 4.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 198 WPVRSPRPVTEKLAANNPLL-CGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSK---YSNSDAIIYVGCGERGNEM 273
Cdd:TIGR01039 108 WPIHRKAPSFEEQSTKVEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINniaKEHGGYSVFAGVGERTREG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 274 SEVLRDFPEltmevegvtTSIMKRTALVANTSNMPVAAREASIYTGITLAEYFRDM-GLNVAMMADSTSRWAEALREISG 352
Cdd:TIGR01039 188 NDLYHEMKE---------SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDNIFRFTQAGSEVSA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 353 RLGEMPADSGYPAYLAARLASFYERAGRVKclgsperEGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRK 432
Cdd:TIGR01039 259 LLGRMPSAVGYQPTLATEMGELQERITSTK-------TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 433 HFPSINWLISYSEYMRAL---EEFYEknypefvsLRTKCKEILQEEEDLSEIVQLVGKASLAESDKVTLEVAKIIKdDFL 509
Cdd:TIGR01039 332 IYPAVDPLDSTSRLLDPSvvgEEHYD--------VARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQ-RFL 402
|
...
gi 17565854 510 QQN 512
Cdd:TIGR01039 403 SQP 405
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
201-511 |
1.38e-34 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 135.89 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 201 RSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLskYSNSDAIIYV-G-CGERGNEMSEVlr 278
Cdd:PRK08149 120 VAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNML--IEHSEADVFViGlIGERGREVTEF-- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 279 dfpeltmeVEGVTTSIMK-RTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEM 357
Cdd:PRK08149 196 --------VESLRASSRReKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGEL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 358 PADSGYPAYLAARLASFYERAGRVKclgsperEGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSI 437
Cdd:PRK08149 268 PARRGYPASVFDSLPRLLERPGATL-------AGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAI 340
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17565854 438 NWLISYSeymRALEEFYEKNYPEfvsLRTKCKEILQEEEDLSEIVQLvGKASLAESDKVTLEVAKIIK-DDFLQQ 511
Cdd:PRK08149 341 DVLKSVS---RVFGQVTDPKHRQ---LAAAFRKLLTRLEELQLFIDL-GEYRRGENADNDRAMDKRPAlEAFLKQ 408
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
7-484 |
2.79e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 135.08 E-value: 2.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 7 YGFVYGVSGPVVTAeKMAGSAMYELVRVGHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGS 86
Cdd:PRK07594 22 WGRIQDVSATLLNA-WLPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 87 IFDGIQRPLKDIADitqsiyiPKGVstnalsrearWdfvvsKDLRVgghvtggdiigtvdenllikhkilLPPsacgtit 166
Cdd:PRK07594 101 VIDGFGRPLDGREL-------PDVC----------W-----KDYDA------------------------MPP------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 167 fvapsgqytvedtllelefagrkqkfsmlqiwPVRSPRPVTEklaannPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKT 246
Cdd:PRK07594 128 --------------------------------PAMVRQPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 247 VISQSLSKYSNSDAIIYVGCGERGNEmsevLRDFPELTMEVEGvttsiMKRTALVANTSNMPVAAREASIYTGITLAEYF 326
Cdd:PRK07594 170 TLLAMLCNAPDADSNVLVLIGERGRE----VREFIDFTLSEET-----RKRCVIVVATSDRPALERVRALFVATTIAEFF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 327 RDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGrvkcLGSperEGSVTIVGAVSPPGGDF 406
Cdd:PRK07594 241 RDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG----MGE---KGSITAFYTVLVEGDDM 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17565854 407 ADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRALEEfyeknyPEFVSLRTKCKEILQEEEDLSEIVQL 484
Cdd:PRK07594 314 NEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTS------HEHRQLAAILRRCLALYQEVELLIRI 385
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
13-515 |
8.28e-33 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 131.49 E-value: 8.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 13 VSGPVVTAEKMAGSAMYELVRV---GHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLR-TGKPLSVELGPGIMGSIF 88
Cdd:PRK04196 10 IKGPLLFVEGVEGVAYGEIVEIelpNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSEDMLGRIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 89 DGIQRPLKDIADITQSIYIP-KGVSTNALSREARWDFVVskdlrvgghvTGgdiIGTVDenllikhkillppsacGTITF 167
Cdd:PRK04196 90 DGLGRPIDGGPEIIPEKRLDiNGAPINPVAREYPEEFIQ----------TG---ISAID----------------GLNTL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 168 VapsgqytvedtllelefagRKQKFsmlqiwPVRS----PrpvTEKLAAnnpllcgQRVLDAlfpcvqggttAIPGafgc 243
Cdd:PRK04196 141 V-------------------RGQKL------PIFSgsglP---HNELAA-------QIARQA----------KVLG---- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 244 gktvisqSLSKYsnsdAIIYVGCGERGNEMSEVLRDFPEltmevegvtTSIMKRTALVANTSNMPVAAREASIYTGITLA 323
Cdd:PRK04196 172 -------EEENF----AVVFAAMGITFEEANFFMEDFEE---------TGALERSVVFLNLADDPAIERILTPRMALTAA 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 324 EYFR-DMGLNV-AMMADSTSrWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKclgspEREGSVTIVGAVSP 401
Cdd:PRK04196 232 EYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIK-----GKKGSITQIPILTM 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 402 PGGDFADPVTSATLGIV--QVFwgLDKKLAQRKHFPSINWLISYSEYMR--ALEEFYEKNYPEFVSlrtkckeilQ---- 473
Cdd:PRK04196 306 PDDDITHPIPDLTGYITegQIV--LSRELHRKGIYPPIDVLPSLSRLMKdgIGEGKTREDHKDVAN---------Qlyaa 374
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 17565854 474 --EEEDLSEIVQLVGKASLAESDKVTLEVAKIIKDDFLQQNGYT 515
Cdd:PRK04196 375 yaRGKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQGFDE 418
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
215-484 |
3.65e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 129.33 E-value: 3.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 215 PLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEMSEVLRDfpelTMEVEGvttsi 294
Cdd:PRK08927 141 PLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQD----DLGPEG----- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 295 MKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASF 374
Cdd:PRK08927 212 LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 375 YERAGRvkclgSPEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRALeefy 454
Cdd:PRK08927 292 LERAGP-----GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGC---- 362
|
250 260 270
....*....|....*....|....*....|
gi 17565854 455 ekNYPEFVSLRTKCKEILQEEEDLSEIVQL 484
Cdd:PRK08927 363 --NDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
7-515 |
2.03e-31 |
|
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: 127.57 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 7 YGFVYGVSGPVVTAEKMAGSAMYELVRV---GHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLR-TGKPLSVELGPG 82
Cdd:COG1156 6 YRTISEIAGPLLFVEGVEGVGYGELVEIelpDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 83 IMGSIFDGIQRPLKDIADITQSIYIP-KGVSTNALSREARWDFVVskdlrvgghvTGgdiIGTVDenllikhkillppsa 161
Cdd:COG1156 86 MLGRVFNGLGRPIDGGPPIIPEKRLDiNGSPINPVAREYPREFIQ----------TG---ISAID--------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 162 cGTITFVapsgqytvedtllelefagRKQKFsmlqiwPVRS----PRpvtEKLAAnnpllcgQRVLDAlfpcvqggttAI 237
Cdd:COG1156 138 -GLNTLV-------------------RGQKL------PIFSgsglPH---NELAA-------QIARQA----------KV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 238 PGafgcgktvisqslskySNSD-AIIYVGCGERGNEMSEVLRDFPEltmevegvtTSIMKRTALVANTSNMPVAAREASI 316
Cdd:COG1156 172 RG----------------EEEKfAVVFAAMGITHDEANFFREEFEE---------TGALDRVVMFLNLADDPAIERIITP 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 317 YTGITLAEYF---RDMGLNVaMMADSTSrWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKclgspEREGSV 393
Cdd:COG1156 227 RMALTAAEYLafeKGMHVLV-ILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIK-----GRKGSI 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 394 TIVGAVSPPGGDFADPVTSATLGIV--QVFwgLDKKLAQRKHFPSINWLISYSEYMR--ALEEFYEKNYPE-----FVSL 464
Cdd:COG1156 300 TQIPILTMPNDDITHPIPDLTGYITegQIV--LSRDLHRKGIYPPIDVLPSLSRLMKdgIGEGKTREDHADvanqlYAAY 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 17565854 465 -RTKckeilqeeeDLSEIVQLVGKASLAESDKVTLEVAKIIKDDFLQQNGYT 515
Cdd:COG1156 378 aRGQ---------EVRELAAIVGEEALSETDKKYLKFADAFERRFVNQGFDE 420
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
202-454 |
1.91e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 118.26 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 202 SPRPVTEklaannPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDaIIYVG-CGERGNEMSEvlrdF 280
Cdd:PRK08972 138 SRRPITE------PLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD-VIVVGlVGERGREVKE----F 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 281 PELTMEVEGvttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPAD 360
Cdd:PRK08972 207 IEEILGEEG-----RARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPAT 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 361 SGYPAYLAARLASFYERAGRvkclGSPeREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWL 440
Cdd:PRK08972 282 KGYPPSVFAKLPALVERAGN----GGP-GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIE 356
|
250 260
....*....|....*....|....*.
gi 17565854 441 ISYS------------EYMRALEEFY 454
Cdd:PRK08972 357 ASISrvmpmviseehlEAMRRVKQVY 382
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
203-535 |
1.93e-27 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 115.25 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 203 PRPVTEKLAaNNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEmsevLRDFPE 282
Cdd:PRK09099 135 PDPMSRRMV-EAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGRE----VREFIE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 283 LTMEVEGvttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSG 362
Cdd:PRK09099 210 LILGEDG-----MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 363 YPAYLAARLASFYERAGRvkclgspEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLIS 442
Cdd:PRK09099 285 FPPSVFAELPRLLERAGM-------GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 443 YSEYMRALEEfyeknyPEFVSLRTKCKEILQEEEDLSEIVQlVGKASlAESDKVTLE-VAKI--IKdDFLQQngytKYDR 519
Cdd:PRK09099 358 LSRVMPQVVP------REHVQAAGRLRQLLAKHREVETLLQ-VGEYR-AGSDPVADEaIAKIdaIR-DFLSQ----RTDE 424
|
330
....*....|....*.
gi 17565854 520 FCPFYKTVGMLKNMIG 535
Cdd:PRK09099 425 YSDPDATLAALAELSG 440
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
215-478 |
1.24e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 113.29 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 215 PLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDaIIYVG-CGERGNEMSEvlrdFPELTMEVEGvtts 293
Cdd:PRK05688 151 PLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD-IIVVGlIGERGREVKE----FIEHILGEEG---- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 294 iMKRTALVANTSN-MPVAAREASIYTgITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLA 372
Cdd:PRK05688 222 -LKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLP 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 373 SFYERAGRVKCLGspereGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRALEE 452
Cdd:PRK05688 300 KLVERAGNAEPGG-----GSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVD 374
|
250 260
....*....|....*....|....*....
gi 17565854 453 fyeknyPEFVSLRTKCKEIL---QEEEDL 478
Cdd:PRK05688 375 ------PEHLRRAQRFKQLWsryQQSRDL 397
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
196-447 |
3.90e-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: 108.08 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 196 QIWPVRSPRPVTEKLAANNPLL-CGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSL--------SKYSnsdaiIYVGC 266
Cdd:cd01133 30 ERWPIHREAPEFVELSTEQEILeTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinniakahGGYS-----VFAGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 267 GERGNEMSEVLRDfpeltMEVEGV-TTSIMKRTALVANTSNMPVAAREASIYTGITLAEYFRDM-GLNVAMMADSTSRWA 344
Cdd:cd01133 105 GERTREGNDLYHE-----MKESGViNLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 345 EALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKclgsperEGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGL 424
Cdd:cd01133 180 QAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVL 252
|
250 260
....*....|....*....|...
gi 17565854 425 DKKLAQRKHFPSINWLISYSEYM 447
Cdd:cd01133 253 SRGIAELGIYPAVDPLDSTSRIL 275
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
214-444 |
2.79e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 108.93 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 214 NPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEMSEVLrdfpeltmevEGVTTS 293
Cdd:PRK06002 147 TGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFL----------EDTLAD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 294 IMKRTALVANTSN-MPVAAREASIyTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLA 372
Cdd:PRK06002 217 NLKKAVAVVATSDeSPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELP 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17565854 373 SFYERAGrvkclgsPEREGSVTIVG--AVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYS 444
Cdd:PRK06002 296 RLLERAG-------PGAEGGGSITGifSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASIS 362
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
3-512 |
7.53e-25 |
|
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: 107.87 E-value: 7.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 3 AESSYGFVYGVSGPVVTAEKMAGS--AMYELVRV---GHQELVGEIIRLEGDYA--TIQVyEETSGVTIGDPVLRTGKPL 75
Cdd:COG0055 1 MAMNTGKIVQVIGPVVDVEFPEGElpAIYNALEVeneGGGELVLEVAQHLGDNTvrCIAM-DSTDGLVRGMEVIDTGAPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 76 SVELGPGIMGSIFDgiqrplkdiaditqsiyipkgvstnalsrearwdfvvskdlrvgghVTGGdiigTVDEnllikhki 155
Cdd:COG0055 80 SVPVGEATLGRIFN----------------------------------------------VLGE----PIDG-------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 156 lLPPsacgtitfvapsgqytVEDTllelefagrkqkfsmlQIWPV-RSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGT 234
Cdd:COG0055 102 -KGP----------------IEAK----------------ERRPIhRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGK 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 235 TAIPGAFGCGKTVISQSL--------SKYSnsdaiIYVGCGER---GNEMsevLRDfpeltMEVEGVttsiMKRTALVAN 303
Cdd:COG0055 149 IGLFGGAGVGKTVLIMELihniakehGGVS-----VFAGVGERtreGNDL---YRE-----MKESGV----LDKTALVFG 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 304 TSNMPVAAREASIYTGITLAEYFRD-MGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVK 382
Cdd:COG0055 212 QMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTK 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 383 clgsperEGSVTIVGAVSPPGGDFADPVTSATLG-----IVqvfwgLDKKLAQRKHFPSINWLISYSeymRALEefyekn 457
Cdd:COG0055 292 -------KGSITSVQAVYVPADDLTDPAPATTFAhldatTV-----LSRKIAELGIYPAVDPLDSTS---RILD------ 350
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17565854 458 yPEFVSLR-----TKCKEILQEEEDLSEIVQLVGKASLAESDKVTLEVA-KIIKddFLQQN 512
Cdd:COG0055 351 -PLIVGEEhyrvaREVQRILQRYKELQDIIAILGMDELSEEDKLTVARArKIQR--FLSQP 408
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
251-448 |
8.61e-24 |
|
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: 101.53 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 251 SLSKYSNSDAIIYVGCGERGNEMSEVLRDFPEltmevegvtTSIMKRTALVANTSNMPVAAReasIYT---GITLAEYFR 327
Cdd:cd01135 94 GVVGSEENFAIVFAAMGVTMEEARFFKDDFEE---------TGALERVVLFLNLANDPTIER---IITprmALTTAEYLA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 328 -DMGLNV-AMMADSTSrWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVKclgspEREGSVTIVGAVSPPGGD 405
Cdd:cd01135 162 yEKGKHVlVILTDMTN-YAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVE-----GRKGSITQIPILTMPNDD 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17565854 406 FADPVTSATLGIV--QVFwgLDKKLAQRKHFPSINWLISYSEYMR 448
Cdd:cd01135 236 ITHPIPDLTGYITegQIY--LDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
219-456 |
1.76e-23 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 103.71 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 219 GQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEmsevLRDFPELTMEVEGVTTSIMkrT 298
Cdd:PRK07960 162 GVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGRE----VKDFIENILGAEGRARSVV--I 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 299 ALVANTSNMpVAAREASIYTGItlAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERA 378
Cdd:PRK07960 236 AAPADVSPL-LRMQGAAYATRI--AEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 379 GRVKCLGspereGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSEYMRAL--EEFYEK 456
Cdd:PRK07960 313 GNGISGG-----GSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALidEQHYAR 387
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
196-450 |
7.35e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 101.51 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 196 QIWPVRSpRPVteklaaNNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEmse 275
Cdd:PRK07196 126 QIHPLQR-RAV------DTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGRE--- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 276 vLRDFPELTMEVEGvttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLG 355
Cdd:PRK07196 196 -VKEFIEHSLQAAG-----MAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 356 EMPADSGYPAYLAARLASFYERAgrvkclGSPEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFP 435
Cdd:PRK07196 270 EPPATKGYPPSAFSIIPRLAESA------GNSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYP 343
|
250
....*....|....*
gi 17565854 436 SINWLISYSEYMRAL 450
Cdd:PRK07196 344 AIDISQSISRCMSQV 358
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
219-536 |
6.83e-21 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 96.26 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 219 GQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSkysNSDA------IIYVGCGER---GN----EMSE----VLRDFP 281
Cdd:CHL00060 148 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELI---NNIAkahggvSVFGGVGERtreGNdlymEMKEsgviNEQNIA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 282 EltmevegvttsimKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGL-NVAMMADSTSRWAEALREISGRLGEMPAD 360
Cdd:CHL00060 225 E-------------SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 361 SGYPAYLAARLASFYERAGRVKclgsperEGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWL 440
Cdd:CHL00060 292 VGYQPTLSTEMGSLQERITSTK-------EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 441 ISYSEYMRAL---EEFYEknypefvsLRTKCKEILQEEEDLSEIVQLVGKASLAESDKVTLEVAKIIkDDFLQQngytky 517
Cdd:CHL00060 365 DSTSTMLQPRivgEEHYE--------TAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ------ 429
|
330 340
....*....|....*....|....*....
gi 17565854 518 drfcPFY----------KTVGMLKNMIGF 536
Cdd:CHL00060 430 ----PFFvaevftgspgKYVGLAETIRGF 454
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
219-476 |
1.54e-20 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 94.66 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 219 GQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEmsevLRDFPELTMEVEGvttsiMKRT 298
Cdd:PRK06793 143 GIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGRE----VKDFIRKELGEEG-----MRKS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 299 ALVANTSNMP--VAAREASIYTGItlAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPAdSGYPAYLAARLASFYE 376
Cdd:PRK06793 214 VVVVATSDEShlMQLRAAKLATSI--AEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 377 RAGRVKclgsperEGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSeymRALEEFYEK 456
Cdd:PRK06793 291 RSGKTQ-------KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVS---RIMEEIVSP 360
|
250 260
....*....|....*....|
gi 17565854 457 NYPEFVSLRTKCKEILQEEE 476
Cdd:PRK06793 361 NHWQLANEMRKILSIYKENE 380
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
295-520 |
1.85e-19 |
|
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: 91.71 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 295 MKRTALVANTSNMPVAAREASIYTGITLAEYFR-DMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLAS 373
Cdd:TIGR01040 210 MERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLAT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 374 FYERAGRVKclgspEREGSVTIVGAVSPPGGDFADPVTSATLGIV--QVFwgLDKKLAQRKHFPSINWLISYSEYMRAL- 450
Cdd:TIGR01040 290 IYERAGRVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPINVLPSLSRLMKSAi 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17565854 451 -EEFYEKNYPEFVSLRTKCKEILQeeeDLSEIVQLVGKASLAESDKVTLEVAKIIKDDFLQQNGYTKYDRF 520
Cdd:TIGR01040 363 gEGMTRKDHSDVSNQLYACYAIGK---DVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPYENRTIF 430
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
200-535 |
4.01e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 90.13 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 200 VRSPRPVTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEMSEVLRD 279
Cdd:PRK08472 125 MKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPEFIEK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 280 fpELTMEVEGvttsimkrTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPA 359
Cdd:PRK08472 205 --NLGGDLEN--------TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 360 DSGYPAYLAARLASFYERAGRvkclgsPEREGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLAQRKHFPSINW 439
Cdd:PRK08472 275 SKGYPPSVLSLLPQLMERAGK------EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 440 LISYSEYM-RALEEFYEKNYPEFVSLRTKCKEilqeeedlSEIVQLVG---KASLAESDKVTLEVAKIikDDFLQQNGYT 515
Cdd:PRK08472 349 LNSASRVMnDIISPEHKLAARKFKRLYSLLKE--------NEVLIRIGayqKGNDKELDEAISKKEFM--EQFLKQNPNE 418
|
330 340
....*....|....*....|
gi 17565854 516 KYdrfcPFYKTVGMLKNMIG 535
Cdd:PRK08472 419 LF----PFEQTFEQLEEILR 434
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
219-484 |
1.02e-16 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 82.64 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 219 GQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDAIIYVGCGERGNEmsevLRDFPEltMEVEGVTTsimKRT 298
Cdd:PRK05922 144 GIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGRE----VREYIE--QHKEGLAA---QRT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 299 ALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPADSGYPAYLAARLASFYERA 378
Cdd:PRK05922 215 IIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 379 GRvkclgspEREGSVTIVGAV--SPPGGD-FADPVTSATLGivQVFWGldkklAQRKHF--PSINWLISYSEYMRALEef 453
Cdd:PRK05922 295 GN-------NDKGSITALYAIlhYPNHPDiFTDYLKSLLDG--HFFLT-----PQGKALasPPIDILTSLSRSARQLA-- 358
|
250 260 270
....*....|....*....|....*....|.
gi 17565854 454 yeknYPEFVSLRTKCKEILQEEEDLSEIVQL 484
Cdd:PRK05922 359 ----LPHHYAAAEELRSLLKAYHEALDIIQL 385
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
10-72 |
1.61e-13 |
|
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: 65.64 E-value: 1.61e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17565854 10 VYGVSGPVVTAEKMAGSA--MYELVRVGHQE----LVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTG 72
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLpgLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
204-444 |
3.84e-13 |
|
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: 69.89 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 204 RPVTEklaannPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKT------VISQSLSKYsnsdAIIYVGCGERGNEMSEVL 277
Cdd:cd01132 47 QSVNE------PLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaiaidtIINQKGKKV----YCIYVAIGQKRSTVAQIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 278 RdfpelTMEVEGVttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEM 357
Cdd:cd01132 117 K-----TLEEHGA----MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 358 PADSGYPA---YLAARLasfYERAGRvkcLGSPEREGSVTIVGAVSPPGGD----FADPVTSATLGivQVFwgLDKKLAQ 430
Cdd:cd01132 188 PGREAYPGdvfYLHSRL---LERAAK---LSDELGGGSLTALPIIETQAGDvsayIPTNVISITDG--QIF--LESELFN 257
|
250
....*....|....
gi 17565854 431 RKHFPSINWLISYS 444
Cdd:cd01132 258 KGIRPAINVGLSVS 271
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
199-394 |
5.55e-13 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 71.49 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 199 PVRSPRP-VTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKT------VISQSlskysNSDAI-IYVGCGERG 270
Cdd:PRK13343 128 PLERPAPaIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTaiaidaIINQK-----DSDVIcVYVAIGQKA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 271 NEMSEVLRdfpelTMEVEGVttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREI 350
Cdd:PRK13343 203 SAVARVIE-----TLREHGA----LEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYREL 273
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17565854 351 SGRLGEMPADSGYPA---YLAARLasfYERAGRVkclgSPERE-GSVT 394
Cdd:PRK13343 274 SLLLRRPPGREAYPGdifYLHSRL---LERAAKL----SPELGgGSLT 314
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
18-414 |
3.20e-12 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 68.91 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 18 VTAEkmaGSAMYELVRV--GHQELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGKPLSVELGPGIMGSIFDGIQRPL 95
Cdd:PRK02118 18 VEAE---GVGYGELATVerKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 96 KDiaditqsiyipkgvstnalsrearwdfvvskdlrvGGHVTGGDI-IGTvdenllikhkillpPSacgtitfVAPsgqy 174
Cdd:PRK02118 95 DG-----------------------------------GPELEGEPIeIGG--------------PS-------VNP---- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 175 tvedtllelefAGRKQKFSMlqiwpVRSPRPVTEklaANNPLLCGQRVldALFpcvqggttAIPGafgcgkTVISQSLSK 254
Cdd:PRK02118 115 -----------VKRIVPREM-----IRTGIPMID---VFNTLVESQKI--PIF--------SVSG------EPYNALLAR 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 255 YSN---SDAIIYVGCGERGNEMSEVLRDFPELtmeveGVttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFR-DMG 330
Cdd:PRK02118 160 IALqaeADIIILGGMGLTFDDYLFFKDTFENA-----GA----LDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGK 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 331 LNV-AMMADSTSrWAEALREISGRLGEMPADSGYPAYLAARLASFYERAGRVkclgspEREGSVTIVGAVSPPGGDFADP 409
Cdd:PRK02118 231 KKVlVLLTDMTN-FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDF------EDGGSITIIAVTTMPGDDVTHP 303
|
....*
gi 17565854 410 VTSAT 414
Cdd:PRK02118 304 VPDNT 308
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
7-73 |
9.20e-12 |
|
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: 60.79 E-value: 9.20e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17565854 7 YGFVYGVSGPVVTAEKMAGSAMYELVRVGHQ------ELVGEIIRLEGDYATIQVYEETSGVTIGDPVLRTGK 73
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGdgnnetVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
202-444 |
1.44e-10 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 63.83 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 202 SPRPVTEklaannPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVIS-QSLSKYSNSDAI-IYVGCGERGNEMSEVLRD 279
Cdd:CHL00059 117 SRRSVYE------PLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVAtDTILNQKGQNVIcVYVAIGQKASSVAQVVTT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 280 FPEltmevegvtTSIMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGRLGEMPA 359
Cdd:CHL00059 191 LQE---------RGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 360 DSGYPA---YLAARLasfYERAGRvkcLGSPEREGSVTIVGAVSPPGGDFAD--P--VTSATLGivQVFwgLDKKLAQRK 432
Cdd:CHL00059 262 REAYPGdvfYLHSRL---LERAAK---LSSQLGEGSMTALPIVETQAGDVSAyiPtnVISITDG--QIF--LSADLFNAG 331
|
250
....*....|..
gi 17565854 433 HFPSINWLISYS 444
Cdd:CHL00059 332 IRPAINVGISVS 343
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
206-444 |
1.40e-09 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 60.82 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 206 VTEKLAANNPLLCGQRVLDALFPCVQGGTTAIPGAFGCGKTVIS------------QSLSKysNSDAIIYVGCGERGNEM 273
Cdd:PTZ00185 163 IVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvstiinqvrinqQILSK--NAVISIYVSIGQRCSNV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 274 SEVLRDFPeltmevegvTTSIMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISGR 353
Cdd:PTZ00185 241 ARIHRLLR---------SYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 354 LGEMPADSGYPA---YLAARLasfYERAGRVkclgSPER-EGSVTIVGAVSPPGGDFADPVTSATLGIVQVFWGLDKKLA 429
Cdd:PTZ00185 312 LRRPPGREAYPGdvfYLHSRL---LERAAML----SPGKgGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLF 384
|
250
....*....|....*
gi 17565854 430 QRKHFPSINWLISYS 444
Cdd:PTZ00185 385 TGGQRPAVNIGLSVS 399
|
|
| 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 ... |
12-73 |
6.40e-06 |
|
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: 44.34 E-value: 6.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17565854 12 GVSGPVVTAEKMAGSAMYELVRV----GHQELvGEIIRLEGDYATIQVYEETSGVTIGDPVLR-TGK 73
Cdd:cd18118 7 EINGPLVIVEGVKGVKYGEIVEItlpdGEVRR-GQVLEVSGDKAVVQVFEGTSGLDLKGTKVRfTGE 72
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
469-511 |
5.31e-05 |
|
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: 41.66 E-value: 5.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 17565854 469 KEILQEEEDLSEIVQLVGKASLAESDKVTLEVAKIIKdDFLQQ 511
Cdd:cd01429 9 KAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLE-EFLQQ 50
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
205-394 |
6.83e-05 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 45.83 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 205 PVTEklaannPLLCGQRVLDALFPCVQG-----------GTTAIpgafgCGKTVISQSlskysNSDAI-IYVGCGERGNE 272
Cdd:PRK09281 141 SVHE------PLQTGIKAIDAMIPIGRGqreliigdrqtGKTAI-----AIDTIINQK-----GKDVIcIYVAIGQKAST 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565854 273 MSEVLRdfpelTMEVEGVttsiMKRTALVANTSNMPVAAREASIYTGITLAEYFRDMGLNVAMMADSTSRWAEALREISG 352
Cdd:PRK09281 205 VAQVVR-----KLEEHGA----MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSL 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17565854 353 RLGEMPADSGYPA---YLAARLasfYERAGRVkclgSPER-EGSVT 394
Cdd:PRK09281 276 LLRRPPGREAYPGdvfYLHSRL---LERAAKL----SDELgGGSLT 314
|
|
| |
