|
Name |
Accession |
Description |
Interval |
E-value |
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
1-582 |
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: 1230.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 1 MVAKGRIIRVTGPLVVADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRL 80
Cdd:COG1155 1 MMTKGKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 81 LTSIYDGIQRPLEVIREKTGDFIARGVTAPALPRDKKWHFIPKAKVGDKVVGGDIIGEVPETSIIVHKIMVPPGIEGEIV 160
Cdd:COG1155 81 LGNIFDGIQRPLDKIAEKSGDFIPRGVDVPALDREKKWDFTPTVKVGDKVSAGDILGTVQETPLIEHKIMVPPGVSGTVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 161 EIAEEGDYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGK 240
Cdd:COG1155 161 EIAPEGEYTVEDTIAVLEDEDGEEHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 241 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 320
Cdd:COG1155 241 TVTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 321 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDyrVGSVSVIGAVSPPGGDFS 400
Cdd:COG1155 321 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGDFS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 401 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNIDPEWKAMRDKAMALLQKESELQEIVRIVG 480
Cdd:COG1155 399 EPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDENVDPDWSELRNEAMDLLQEEAELQEIVRLVG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 481 PDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMEAINRGVPLEEIAKLPVREEIGRMK 560
Cdd:COG1155 479 EDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLSEIKELPLREKIARMK 558
|
570 580
....*....|....*....|....*
3P20_A 561 F---ERDVSKIRSLIDKTNEQFEEL 582
Cdd:COG1155 559 YspeNELLEKFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-585 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 1198.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 1 MVAKGRIIRVTGPLVVADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRL 80
Cdd:PRK04192 1 MMTKGKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 81 LTSIYDGIQRPLEVIREKTGDFIARGVTAPALPRDKKWHFIPKAKVGDKVVGGDIIGEVPETSIIVHKIMVPPGIEGEIV 160
Cdd:PRK04192 81 LGSIFDGIQRPLDELAEKSGDFLERGVYVPALDREKKWEFTPTVKVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 161 EIAEEGDYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGK 240
Cdd:PRK04192 161 EIVSEGDYTVDDTIAVLEDEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 241 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 320
Cdd:PRK04192 241 TVTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 321 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDyrVGSVSVIGAVSPPGGDFS 400
Cdd:PRK04192 321 DMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGDFS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 401 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNIDPEWKAMRDKAMALLQKESELQEIVRIVG 480
Cdd:PRK04192 399 EPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEENVDPDWRELRDEAMDLLQREAELQEIVRLVG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 481 PDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMEAINRGVPLEEIAKLPVREEIGRMK 560
Cdd:PRK04192 479 PDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGVPVSEILELEVRDRIARLK 558
|
570 580
....*....|....*....|....*...
3P20_A 561 F---ERDVSKIRSLIDKTNEQFEELFKK 585
Cdd:PRK04192 559 YipeNEYLEKIDEIFEKLEEELEELIAE 586
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
4-584 |
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: 1174.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 4 KGRIIRVTGPLVVADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRLLTS 83
Cdd:TIGR01043 1 KGRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 84 IYDGIQRPLEVIREKTGDFIARGVTAPALPRDKKWHFIPKAKVGDKVVGGDIIGEVPETSIIVHKIMVPPGIEGEIVEIA 163
Cdd:TIGR01043 81 IYDGVQRPLDVLKEKTGDFIARGVDAPGLDRDKKWHFKPTVKEGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 164 EEGDYTIEEVIAKVKTPSGEikELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVT 243
Cdd:TIGR01043 161 EEGDYTVEDTIAVVDTDGDE--EIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 244 QHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG 323
Cdd:TIGR01043 239 QHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPELKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 324 YDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPV 403
Cdd:TIGR01043 319 YDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDFSEPV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 404 VQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNIDPEWKAMRDKAMALLQKESELQEIVRIVGPDA 483
Cdd:TIGR01043 399 TQNTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVQDWWHENVDPDWREMRDEAMDLLQKESELQEIVQLVGPDA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 484 LPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMEAINRGVPLEEIAKLPVREEIGRMKFER 563
Cdd:TIGR01043 479 LPERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVEEILKLEVKEEIGRMKYEP 558
|
570 580
....*....|....*....|.
3P20_A 564 DVsKIRSLIDKTNEQFEELFK 584
Cdd:TIGR01043 559 DN-DILAKIDEILEKIEKEFK 578
|
|
| V-ATPase_V1_A |
TIGR01042 |
V-type (H+)-ATPase V1, A subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
5-585 |
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: 763.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 5 GRIIRVTGPLVVADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRLLTSI 84
Cdd:TIGR01042 3 GYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILGNI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 85 YDGIQRPLEVIREKTGD-FIARGVTAPALPRDKKWHFIPKA-KVGDKVVGGDIIGEVPETSIIVHKIMVPPGIEGEIVEI 162
Cdd:TIGR01042 83 FDGIQRPLKAIAEQSQSiYIPRGVNVPALDRDKKWEFTPKKlRVGDHITGGDIYGTVFENSLIKHKIMLPPRARGTITYI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 163 AEEGDYTIEEVIAKVKTpSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTV 242
Cdd:TIGR01042 163 APAGNYTVDDTVLEVEF-QGVKKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 243 TQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGK--PLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 320
Cdd:TIGR01042 242 ISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEVDGReeSIMKRTTLVANTSNMPVAAREASIYTGITLAEYFR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 321 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGDFS 400
Cdd:TIGR01042 322 DMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGDFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 401 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNiDPEWKAMRDKAMALLQKESELQEIVRIVG 480
Cdd:TIGR01042 402 DPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKF-YPEFVPLRTKAKEILQEEEDLNEIVQLVG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 481 PDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMEAINRG-VPLEEIAKLPVREEIGRM 559
Cdd:TIGR01042 481 KDALAETDKITLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTaQDDNKITWSIIKESLGDL 560
|
570 580
....*....|....*....|....*....
3P20_A 560 KFERDVSKIRSLID---KTNEQFEELFKK 585
Cdd:TIGR01042 561 LYRLSSMKFEDPSDgeaKIKADYEKLNED 589
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
241-588 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 708.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 241 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 320
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 321 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGDFS 400
Cdd:PRK14698 750 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGDFS 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 401 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNIDPEWKAMRDKAMALLQKESELQEIVRIVG 480
Cdd:PRK14698 830 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDPEWKAMRDKAMELLQKEAELQEIVRIVG 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 481 PDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMEAINRGVPLEEIAKLPVREEIGRMK 560
Cdd:PRK14698 910 PDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPLEEIAKLPVREEIGRMK 989
|
330 340
....*....|....*....|....*...
3P20_A 561 FERDVSKIRSLIDKTNEQFEELFKKYGA 588
Cdd:PRK14698 990 FEPDIEKIKALIDKTNEQFDELFKKYGA 1017
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
72-439 |
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: 604.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 72 LSVELGPRLLTSIYDGIQRPLEVIREKTGDFIARGVtapalprdkkwhfipkakvgdkvvggdiigevpetsiivhkimv 151
Cdd:cd01134 2 LSVELGPGLLGSIFDGIQRPLEVIAETGSIFIPRGV-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 152 ppgiegeiveiaeegdytieeviakvktpsgeikelkMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAA 231
Cdd:cd01134 38 -------------------------------------NVQRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAA 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 232 IPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYT 311
Cdd:cd01134 81 IPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGESLMERTVLIANTSNMPVAAREASIYT 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 312 GITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGA 391
Cdd:cd01134 161 GITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSVTIVGA 240
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
3P20_A 392 VSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLY 439
Cdd:cd01134 241 VSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
1-283 |
9.24e-160 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 483.37 E-value: 9.24e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 1 MVAKGRIIRVTGPLVVADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRL 80
Cdd:PRK14698 1 MPAKGRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 81 LTSIYDGIQRPLEVIREKTGDFIARGVTAPALPRDKKWHFIPKAKVGDKVVGGDIIGEVPETSIIVHKIMVPPGIEGEIV 160
Cdd:PRK14698 81 LTSIYDGIQRPLEVIREKSGDFIARGISAPALPRDKKWHFIPKVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 161 EIAEEGDYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGK 240
Cdd:PRK14698 161 EIADEGEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
3P20_A 241 TVTQHQLAKWSDAQVV----IYIGCGERGNEMTDVLEEFPKLKDPKT 283
Cdd:PRK14698 241 CVDGDTLILTKEFGLIkikdLYEILDGKGKKTVEGNEEWTELEEPIT 287
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
180-439 |
1.11e-120 |
|
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: 357.54 E-value: 1.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 180 PSGEIKELKMYQRWPVRVKRPYK-EKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWS---DAQV 255
Cdd:cd19476 19 PLDGLPPIKTKQRRPIHLKAPNPiERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQakaHAGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 256 VIYIGCGERGNEMTDVLEEFPKLKDpktgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSR 335
Cdd:cd19476 99 VVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 336 WAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFW 415
Cdd:cd19476 172 YAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD-----GGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQI 246
|
250 260
....*....|....*....|....
3P20_A 416 ALDADLARRRHFPAINWLTSYSLY 439
Cdd:cd19476 247 VLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
214-437 |
4.45e-107 |
|
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: 320.46 E-value: 4.45e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 214 GQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPklkdpktGKPLMERTVL 293
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELL-------GSGALKRTVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 294 IANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGR 373
Cdd:pfam00006 74 VVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3P20_A 374 VvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 437
Cdd:pfam00006 154 V-----KGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
85-205 |
2.93e-76 |
|
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: 237.68 E-value: 2.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 85 YDGIQRPLEVIREKTGDFIARGVTAPALPRDKKWHFIPKAKVGDKVVGGDIIGEVPETSIIVHKIMVPPGIEGEIVEIAE 164
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGSFIPRGVDVPALDREKKWEFTPTVKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTEIAP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
3P20_A 165 EGDYTIEEVIAKVKTPsGEIKELKMYQRWPVRVKRPYKEKL 205
Cdd:pfam16886 81 EGEYTVEDTIAEVEDE-GKEKELTMMQKWPVRRPRPYKEKL 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 ... |
455-559 |
3.55e-62 |
|
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: 200.31 E-value: 3.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 455 WKAMRDKAMALLQKESELQEIVRIVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKT 534
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....*
3P20_A 535 MEAINRGVPLEEIAKLPVREEIGRM 559
Cdd:cd18111 81 LEALEKGVPLSKILELPVREKIARM 105
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
5-512 |
1.19e-45 |
|
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: 167.16 E-value: 1.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 5 GRIIRVTGPLVVADGMKgAKMYEVVRV----GELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRL 80
Cdd:TIGR01026 25 GRVTKVKGLLIEAVGPQ-ASVGDLCLIerrgSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSIKVGDGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 81 LTSIYDGIQRPLEVirektgdfiargvtapalprdkkwhfipkakvgdkvvGGDIIGEVPETSIIvhkimvppgiegeiv 160
Cdd:TIGR01026 104 LGRVLDGLGKPIDG-------------------------------------KGKFLDNVETEGLI--------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 161 eiaeegdytieeviakvKTPSGEIKelkmyqRWPVRVKrpykeklppevpLITGQRVIDTFFPQAKGGTAAIPGPFGSGK 240
Cdd:TIGR01026 132 -----------------TAPINPLK------RAPIREI------------LSTGVRSIDGLLTVGKGQRIGIFAGSGVGK 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 241 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEfpklkdpKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 320
Cdd:TIGR01026 177 STLLGMIARNTEADVNVIALIGERGREVREFIEH-------DLGEEGLKRSVVVVATSDQSPLLRLKGAYVATAIAEYFR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 321 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGrvvtlgsDYRVGSVSVIGAVSPPGGDFS 400
Cdd:TIGR01026 250 DQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAG-------ASGKGSITAFYTVLVEGDDMN 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 401 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVdavkdwwHKNIDPEWKAMRDKAMALLQKESELQEIVRI-- 478
Cdd:TIGR01026 323 EPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLM-------TAIVSEEHRRAARKFRELLSKYKDNEDLIRIga 395
|
490 500 510
....*....|....*....|....*....|....*.
3P20_A 479 --VGPDalPERERAILLVARMlrEDYLQQDAFDEVD 512
Cdd:TIGR01026 396 yqRGSD--RELDFAIAKYPKL--ERFLKQGINEKVN 427
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
5-512 |
1.10e-39 |
|
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: 150.18 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 5 GRIIRVTGPLVVADGMKgakmyevVRVGELGLI---------GEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVE 75
Cdd:COG1157 21 GRVTRVVGLLIEAVGPD-------ASIGELCEIetadgrpvlAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 76 LGPRLLTSIYDGIQRPLEvirektgdfiargvTAPALPRDKKWhfipkakvgdkvvggDIIGEVPetsiivhkimvPPgi 155
Cdd:COG1157 94 VGDGLLGRVLDGLGRPLD--------------GKGPLPGEERR---------------PLDAPPP-----------NP-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 156 egeiveiaeegdytieeviakvktpsgeikelkmYQRWPVRVkrpykeklppevPLITGQRVIDTFFPQAKG---GTAAi 232
Cdd:COG1157 132 ----------------------------------LERARITE------------PLDTGVRAIDGLLTVGRGqriGIFA- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 233 pGPfGSGKTVTQHQLAKWSDAQVVIyIG-CGERGNEMTDVLEEfpKLkdpktGKPLMERTVLIANTSNMPVAAREASIYT 311
Cdd:COG1157 165 -GS-GVGKSTLLGMIARNTEADVNV-IAlIGERGREVREFIED--DL-----GEEGLARSVVVVATSDEPPLMRLRAAYT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 312 GITIAEYFRDMGYDVALMADSTSRWAEALREI---SGrleEMPGEEGYPAYLASKLAEFYERAGRVvtlgsdyRVGSVSV 388
Cdd:COG1157 235 ATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIglaAG---EPPATRGYPPSVFALLPRLLERAGNG-------GKGSITA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 389 IGAVSPPGGDFSEPVVqNTLR------VVkvfwaLDADLARRRHFPAINWLTSYSLYVDAVkdwwhknIDPEWKAMRDKA 462
Cdd:COG1157 305 FYTVLVEGDDMNDPIA-DAVRgildghIV-----LSRKLAERGHYPAIDVLASISRVMPDI-------VSPEHRALARRL 371
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
3P20_A 463 MALLQKESELQEIVRI----VGPDalPERERAILLVARMlrEDYLQQDAFDEVD 512
Cdd:COG1157 372 RRLLARYEENEDLIRIgayqPGSD--PELDEAIALIPAI--EAFLRQGMDERVS 421
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
191-437 |
4.55e-37 |
|
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: 138.46 E-value: 4.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 191 QRWPVRVKRP-YKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMT 269
Cdd:cd01136 30 ERRPLIAAPPnPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGREVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 270 DVLEEfpklkdpKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEE 349
Cdd:cd01136 110 EFIEK-------DLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 350 MPGEEGYPAYLASKLAEFYERAGRVVTlgsdyrvGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPA 429
Cdd:cd01136 183 PPTRRGYPPSVFALLPRLLERAGNGEK-------GSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPA 255
|
....*...
3P20_A 430 INWLTSYS 437
Cdd:cd01136 256 IDVLASIS 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 ... |
4-70 |
5.46e-37 |
|
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: 131.49 E-value: 5.46e-37
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3P20_A 4 KGRIIRVTGPLVVADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGA 70
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
5-512 |
1.10e-35 |
|
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: 138.38 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 5 GRIIRVTGPLVVADGMKgakmyevVRVGELGLI---------GEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVE 75
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLR-------APVGSRCEIessdgdpieAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 76 LGPRLLTSIYDGIQRPLEvirektgdfiargvTAPALPRDKKWHFIPKAkvgdkvvggdiigevpetsiivhkimVPPgi 155
Cdd:TIGR03496 74 VGDSLLGRVIDGLGRPLD--------------GKGPLDAGERVPLYAPP--------------------------INP-- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 156 egeiveiaeegdytieeviakvktpsgeikelkmYQRWPVRVkrpykeklppevPLITGQRVIDTFFPQAKGGTAAIPGP 235
Cdd:TIGR03496 112 ----------------------------------LKRAPIDE------------PLDVGVRAINGLLTVGRGQRMGIFAG 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 236 FGSGKTVTQHQLAKWSDAQVVIyIG-CGERGNEMTDVLEEfpklkdpKTGKPLMERTVLIANTSNMPVAAREASIYTGIT 314
Cdd:TIGR03496 146 SGVGKSTLLGMMARYTEADVVV-VGlIGERGREVKEFIED-------ILGEEGLARSVVVAATADESPLMRLRAAFYATA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 315 IAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGsdyrvGSVSVIGAVSP 394
Cdd:TIGR03496 218 IAEYFRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGNGEEGK-----GSITAFYTVLV 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 395 PGGDFSEPVVqNTLR------VVkvfwaLDADLARRRHFPAINWLTSYSLYVDAVkdwwhknIDPEWKAMRDKAMALLQK 468
Cdd:TIGR03496 293 EGDDQQDPIA-DAARaildghIV-----LSRELAEQGHYPAIDILASISRVMPDV-------VSPEHRQAARRFKQLLSR 359
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
3P20_A 469 ESELQEIVRI----VGPDalPERERAILLVARMlrEDYLQQDAFDEVD 512
Cdd:TIGR03496 360 YQENRDLISIgayqAGSD--PELDQAIALYPRI--EAFLQQGMRERAS 403
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
5-478 |
2.49e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 132.63 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 5 GRIIRVtGPLVVADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRLLTSI 84
Cdd:PRK06820 31 GPIVEI-GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 85 YDGIQRPLEvirektgdfiargvtapalprdkkwhfipkakvgdkvvGGDIIGevpetsiivhkimvppgiegeiveiae 164
Cdd:PRK06820 110 LDGLGAPID--------------------------------------GGPPLT--------------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 165 egdytieeviakvktpsGEIKELkmYQRWPVRVKRPykeklPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQ 244
Cdd:PRK06820 125 -----------------GQWREL--DCPPPSPLTRQ-----PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 245 HQLAKWSDAQVVIYIGCGERGNEMTDVLEEF--PKLKdpktgkplmERTVLIANTSNMPVAAREASIYTGITIAEYFRDM 322
Cdd:PRK06820 181 GMLCADSAADVMVLALIGERGREVREFLEQVltPEAR---------ARTVVVVATSDRPALERLKGLSTATTIAEYFRDR 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 323 GYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyrvGSVSVIGAVSPPGGDFSEP 402
Cdd:PRK06820 252 GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR-------GSITAFYTVLVEGDDMNEP 324
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3P20_A 403 VVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHknidpewKAMRDKAMALLQKESELQEIVRI 478
Cdd:PRK06820 325 VADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQ-------LAMAQKLRRMLACYQEIELLVRV 393
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
199-510 |
2.51e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 129.34 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 199 RPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIyIG-CGERGNEMTDVLEEFPK 277
Cdd:PRK08149 123 PSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFV-IGlIGERGREVTEFVESLRA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 278 lkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYP 357
Cdd:PRK08149 202 -------SSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 358 AYLASKLAEFYERAGRVVTlgsdyrvGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 437
Cdd:PRK08149 275 ASVFDSLPRLLERPGATLA-------GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVS 347
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3P20_A 438 LYVDAVKDWWHKNIDpewKAMRDkamaLLQKESELQEIVRI----VGPDAlpERERAILLVARMlrEDYLQQDaFDE 510
Cdd:PRK08149 348 RVFGQVTDPKHRQLA---AAFRK----LLTRLEELQLFIDLgeyrRGENA--DNDRAMDKRPAL--EAFLKQD-VAE 412
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
166-508 |
2.20e-30 |
|
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: 124.06 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 166 GDYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQ 244
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 245 ----HQLAKwSDAQVVIYIGCGERGNEMTDVLEEfpkLKDPKtgkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 320
Cdd:TIGR01039 161 qeliNNIAK-EHGGYSVFAGVGERTREGNDLYHE---MKESG----VIDKTALVYGQMNEPPGARMRVALTGLTMAEYFR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 321 DM-GYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDF 399
Cdd:TIGR01039 233 DEqGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI-------TSTKTGSITSVQAVYVPADDL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 400 SEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNIDPEWKAMRDKAMALLQKESELQEIVRIV 479
Cdd:TIGR01039 306 TDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDP------SVVGEEHYDVARGVQQILQRYKELQDIIAIL 379
|
330 340
....*....|....*....|....*....
3P20_A 480 GPDALPERERAILLVARMLrEDYLQQDAF 508
Cdd:TIGR01039 380 GMDELSEEDKLTVERARRI-QRFLSQPFF 407
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
4-478 |
8.14e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 122.17 E-value: 8.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 4 KGRIIRVTGPLVVAdgmkgakMYEVVRVGEL----------GLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLS 73
Cdd:PRK06936 24 RGRVTQVTGTILKA-------VVPGVRIGELcylrnpdnslSLQAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 74 VELGPRLLTSIYDGIQRPLEVirektgdfiargvtaPALPRDKKWHFIpkakvgdkvvggdiigevpetsiivhkimvpp 153
Cdd:PRK06936 97 VGVGEHLLGRVLDGLGQPFDG---------------GHPPEPAAWYPV-------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 154 giegeiveiaeegdytieeviakvktpsgeikelkmYQRWPVRVKRPYKEKlppevPLITGQRVIDTFFPQAKGGTAAIP 233
Cdd:PRK06936 130 ------------------------------------YADAPAPMSRRLIET-----PLSLGVRVIDGLLTCGEGQRMGIF 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 234 GPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEfpklkdpKTGKPLMERTVLIANTSNMPVAAREASIYTGI 313
Cdd:PRK06936 169 AAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIES-------DLGEEGLRKAVLVVATSDRPSMERAKAGFVAT 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 314 TIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRvvtlgSDYrvGSVSVIGAVS 393
Cdd:PRK06936 242 SIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-----SDK--GSITALYTVL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 394 PPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVkdwwhknIDPEWKAMRDKAMALLQKESELQ 473
Cdd:PRK06936 315 VEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQI-------VSKEHKTWAGRLRELLAKYEEVE 387
|
....*
3P20_A 474 EIVRI 478
Cdd:PRK06936 388 LLLQI 392
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
210-506 |
1.80e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 118.16 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 210 PLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIyIG-CGERGNEMTDVLEEfpklkdpKTGKPLM 288
Cdd:PRK08927 141 PLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSV-IGlIGERGREVQEFLQD-------DLGPEGL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 289 ERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFY 368
Cdd:PRK08927 213 ARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 369 ERAGRVVTlgsdyRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDavkdwwh 448
Cdd:PRK08927 293 ERAGPGPI-----GEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMP------- 360
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
3P20_A 449 KNIDPEWKAMRDKAMALLQKESELQEIVRI----VGPDalPERERAILLVARMlrEDYLQQD 506
Cdd:PRK08927 361 GCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSD--PEVDEAIRLNPAL--EAFLRQG 418
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
5-529 |
2.04e-28 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 118.13 E-value: 2.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 5 GRIIRVTGPLVVAdGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRLLTSI 84
Cdd:PRK07594 23 GRIQDVSATLLNA-WLPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 85 YDGIQRPLEVIrektgdfiargvtapalprdkkwhfipkakvgdkvvggdiigEVPETSIIVHKIMVPPGIegeiveiae 164
Cdd:PRK07594 102 IDGFGRPLDGR------------------------------------------ELPDVCWKDYDAMPPPAM--------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 165 egdytieeviakvktpsgeikelkmyqrwpvrVKRPYKEklppevPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQ 244
Cdd:PRK07594 131 --------------------------------VRQPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLL 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 245 HQLAKWSDAQVVIYIGCGERGNEMTDVLEEfpklkdpKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGY 324
Cdd:PRK07594 173 AMLCNAPDADSNVLVLIGERGREVREFIDF-------TLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 325 DVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGrvvtLGSdyrVGSVSVIGAVSPPGGDFSEPVV 404
Cdd:PRK07594 246 RVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG----MGE---KGSITAFYTVLVEGDDMNEPLA 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 405 QNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNIdpewKAMRDKAMALLQkesELQEIVRI----VG 480
Cdd:PRK07594 319 DEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQL----AAILRRCLALYQ---EVELLIRIgeyqRG 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
3P20_A 481 PDalPERERAILLVARMLRedYLQQDAfdevDTYCPPEK-QVTMMRVLLN 529
Cdd:PRK07594 392 VD--TDTDKAIDTYPDICT--FLRQSK----DEVCGPELlIEKLHQILTE 433
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
7-510 |
5.28e-28 |
|
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: 117.17 E-value: 5.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 7 IIRVTGPLVVADGMKGAKMYEVVRV----GELGLiGEIIRLEGDKAVIQVYEETAGVRPGEPVVG-TGASLSVELGPRLL 81
Cdd:COG1156 9 ISEIAGPLLFVEGVEGVGYGELVEIelpdGERRR-GQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSEDML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 82 TSIYDGIQRPlevirektgdfiargvtapalpRDKkwhfipkakvgdkvvGGDIIgevPETSIivhkimvppGIEGEIVE 161
Cdd:COG1156 88 GRVFNGLGRP----------------------IDG---------------GPPII---PEKRL---------DINGSPIN 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 162 iaeegdytieeviakvktpsgeikelkmyqrwPVRvkRPYkeklpPEVPLITGQRVIDtffpqakGGTAAIPG---PFGS 238
Cdd:COG1156 119 --------------------------------PVA--REY-----PREFIQTGISAID-------GLNTLVRGqklPIFS 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 239 GKTVTQHQLAkwsdAQV--------------VIYIGCGERGNEMTDVLEEFPKlkdpkTGkpLMERTVLIANTSNMPVAA 304
Cdd:COG1156 153 GSGLPHNELA----AQIarqakvrgeeekfaVVFAAMGITHDEANFFREEFEE-----TG--ALDRVVMFLNLADDPAIE 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 305 REASIYTGITIAEYFR-DMGYDV-ALMADSTSrWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVvtLGsdyR 382
Cdd:COG1156 222 RIITPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRI--KG---R 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 383 VGSVSVIGAVSPPGGDFSEPVVQNT-----LRVVkvfwaLDADLARRRHFPAINWLTSYS-LYVDAV------KDwwHKN 450
Cdd:COG1156 296 KGSITQIPILTMPNDDITHPIPDLTgyiteGQIV-----LSRDLHRKGIYPPIDVLPSLSrLMKDGIgegktrED--HAD 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 451 IdpewkamRDKAMALLQKESELQEIVRIVGPDALPERERAILLVARMLREDYLQQDaFDE 510
Cdd:COG1156 369 V-------ANQLYAAYARGQEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQG-FDE 420
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
5-437 |
6.24e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 116.75 E-value: 6.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 5 GRIIRVTGPLVVADGMKGAkmyevvrVGELGLI-----------GEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLS 73
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESS-------IGDVCYIhtkgggdkaikAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 74 VELGPRLLTSIYDGIQRPLEvirektgdfiargvtAPALPRdkkwhfipkakvGDKVVGGDiigevpetsiivhkimvpp 153
Cdd:PRK07721 93 VKVGSGLIGQVLDALGEPLD---------------GSALPK------------GLAPVSTD------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 154 giegeiveiaeegdytieeviakvKTPsgeikelkmyqrwPVRVKRPykeklPPEVPLITGQRVIDTFFPQAKGGTAAIP 233
Cdd:PRK07721 127 ------------------------QDP-------------PNPLKRP-----PIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 234 GPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEefpklKDpkTGKPLMERTVLIANTSNMPVAAREASIYTGI 313
Cdd:PRK07721 165 AGSGVGKSTLMGMIARNTSADLNVIALIGERGREVREFIE-----RD--LGPEGLKRSIVVVATSDQPALMRIKGAYTAT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 314 TIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGrvvTLGSdyrvGSVSVIGAVS 393
Cdd:PRK07721 238 AIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG---TNAS----GSITAFYTVL 310
|
410 420 430 440
....*....|....*....|....*....|....*....|....
3P20_A 394 PPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 437
Cdd:PRK07721 311 VDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVS 354
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
7-510 |
4.77e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 114.54 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 7 IIRVTGPLVVADGMKGAKMYEVVRV----GELGLiGEIIRLEGDKAVIQVYEETAGVRPGE-PVVGTGASLSVELGPRLL 81
Cdd:PRK04196 7 VSEIKGPLLFVEGVEGVAYGEIVEIelpnGEKRR-GQVLEVSEDKAVVQVFEGTTGLDLKDtKVRFTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 82 TSIYDGIQRPlevirektgdfiargvtapalpRDKKWHFIPKAKVgdkvvggDIIGEVpetsiivhkiMVPpgiegeive 161
Cdd:PRK04196 86 GRIFDGLGRP----------------------IDGGPEIIPEKRL-------DINGAP----------INP--------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 162 iaeegdytieeviakvktpsgeikelkmyqrwpvrVKRPYkeklpPEVPLITGQRVIDTFFPQAKGGTAAIpgpF-GSG- 239
Cdd:PRK04196 118 -----------------------------------VAREY-----PEEFIQTGISAIDGLNTLVRGQKLPI---FsGSGl 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 240 -------KTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKlkdpkTGKplMERTVLIANTSNMPVAAREASIYTG 312
Cdd:PRK04196 155 phnelaaQIARQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEE-----TGA--LERSVVFLNLADDPAIERILTPRMA 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 313 ITIAEYFR-DMGYDV-ALMADSTSrWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyRVGSVSVIG 390
Cdd:PRK04196 228 LTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKG-----KKGSITQIP 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 391 AVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS-LYVDAV------KDwwHKNIdpewkamRDKAM 463
Cdd:PRK04196 302 ILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSrLMKDGIgegktrED--HKDV-------ANQLY 372
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
3P20_A 464 ALLQKESELQEIVRIVGPDALPERERAILLVARMLREDYLQQDaFDE 510
Cdd:PRK04196 373 AAYARGKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQG-FDE 418
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
200-437 |
2.57e-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: 103.07 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 200 PYKEKLPPEvPLITGQRVIDTFFPQAKGgtAAIPGPFGSG--------KTVTQHQLAKWSDAQVVIYIGCGergneMTDV 271
Cdd:cd01135 43 PVARIYPEE-MIQTGISAIDVMNTLVRG--QKLPIFSGSGlphnelaaQIARQAGVVGSEENFAIVFAAMG-----VTME 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 272 LEEFPKLKDPKTGKplMERTVLIANTSNMPVAAReasIYT---GITIAEYFR-DMGYDV-ALMADSTSrWAEALREISGR 346
Cdd:cd01135 115 EARFFKDDFEETGA--LERVVLFLNLANDPTIER---IITprmALTTAEYLAyEKGKHVlVILTDMTN-YAEALREVSAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 347 LEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRH 426
Cdd:cd01135 189 REEVPGRRGYPGYMYTDLATIYERAGRVEG-----RKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGI 263
|
250
....*....|.
3P20_A 427 FPAINWLTSYS 437
Cdd:cd01135 264 YPPIDVLPSLS 274
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
198-529 |
2.82e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 105.94 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 198 KRPYKEklppevPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFpk 277
Cdd:PRK08972 139 RRPITE------PLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEI-- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 278 lkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYP 357
Cdd:PRK08972 211 -----LGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYP 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 358 AYLASKLAEFYERAGRvvtlGSDYRvGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 437
Cdd:PRK08972 286 PSVFAKLPALVERAGN----GGPGQ-GSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASIS 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 438 LYVDAVkdwwhknIDPE-WKAMR--DKAMALLQKESELQEI-VRIVGPDalPERERAILLVARMlrEDYLQQdAFDEVDT 513
Cdd:PRK08972 361 RVMPMV-------ISEEhLEAMRrvKQVYSLYQQNRDLISIgAYKQGSD--PRIDNAIRLQPAM--NAFLQQ-TMKEAVP 428
|
330
....*....|....*.
3P20_A 514 YcppEKQVTMMRVLLN 529
Cdd:PRK08972 429 Y---DMSVNMLKQLAA 441
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
208-510 |
3.09e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 105.85 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 208 EVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEfpklkdpktgkPL 287
Cdd:PRK06002 146 ETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLED-----------TL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 288 ---MERTVLIANTSN-MPVAAREASIyTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASK 363
Cdd:PRK06002 215 adnLKKAVAVVATSDeSPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 364 LAEFYERAGRvvtlGSDYRvGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDav 443
Cdd:PRK06002 294 LPRLLERAGP----GAEGG-GSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLAR-- 366
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3P20_A 444 KDWwhkniDPEWKAMRDKAMALLQKESELQEIvRIVG---PDALPERERAILLVARM---LR---EDYLQQDAFDE 510
Cdd:PRK06002 367 HAW-----TPEQRKLVSRLKSMIARFEETRDL-RLIGgyrAGSDPDLDQAVDLVPRIyeaLRqspGDPPSDDAFAD 436
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
180-441 |
4.87e-23 |
|
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: 99.22 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 180 PSGEIKELKMYQRWPVRVKRPYKEKLPPEV-PLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQ----HQLAKWSDAQ 254
Cdd:cd01133 19 PIDERGPIKAKERWPIHREAPEFVELSTEQeILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLImeliNNIAKAHGGY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 255 VViYIGCGERGNEMTDVLEEfpkLKDPKTGKPL-MERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMADS 332
Cdd:cd01133 99 SV-FAGVGERTREGNDLYHE---MKESGVINLDgLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 333 TSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVvtlgsdyRVGSVSVIGAVSPPGGDFSEPVVQNTlrvvk 412
Cdd:cd01133 175 IFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST-------KKGSITSVQAVYVPADDLTDPAPATT----- 242
|
250 260 270
....*....|....*....|....*....|....*
3P20_A 413 vFWALDADLARRRH------FPAINWLTSYSLYVD 441
Cdd:cd01133 243 -FAHLDATTVLSRGiaelgiYPAVDPLDSTSRILD 276
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
120-511 |
1.17e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 100.92 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 120 FIPKAKVGDKV----------VGGDIIGEVpetsiiVHKIMVPpgiegeiveIAEEGDYTIEEVIAKVKTPSGEIKELKM 189
Cdd:PRK08472 73 FIEGFKIGDKVfiskeglnipVGRNLLGRV------VDPLGRP---------IDGKGAIDYERYAPIMKAPIAAMKRGLI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 190 YQRWPVRVKrpykeklppevplitgqrVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMT 269
Cdd:PRK08472 138 DEVFSVGVK------------------SIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 270 DVLEefpklkdpKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEE 349
Cdd:PRK08472 200 EFIE--------KNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 350 MPGEEGYPAYLASKLAEFYERAGRvvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPA 429
Cdd:PRK08472 272 PPTSKGYPPSVLSLLPQLMERAGK------EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 430 INWLTSYSLYVDAVKDWWHKNidpewKAMRDKAMALLQKESELqeIVRI----VGPDalPERERAILLVARMlrEDYLQQ 505
Cdd:PRK08472 346 INILNSASRVMNDIISPEHKL-----AARKFKRLYSLLKENEV--LIRIgayqKGND--KELDEAISKKEFM--EQFLKQ 414
|
410
....*....|.
3P20_A 506 DA-----FDEV 511
Cdd:PRK08472 415 NPnelfpFEQT 425
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
203-509 |
2.21e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 99.97 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 203 EKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEfpklkdpK 282
Cdd:PRK07196 131 QRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFIEH-------S 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 283 TGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLAS 362
Cdd:PRK07196 204 LQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 363 KLAEFYERAgrvvtlGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDA 442
Cdd:PRK07196 284 IIPRLAESA------GNSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQ 357
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3P20_A 443 VKDWWHKNIDPEWKAMRDKAMallqkesELQEIVRIVG--PDALPERERAILLVARMlrEDYLQQDAFD 509
Cdd:PRK07196 358 VIGSQQAKAASLLKQCYADYM-------AIKPLIPLGGyvAGADPMADQAVHYYPAI--TQFLRQEVGH 417
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
5-527 |
3.97e-22 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 99.46 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 5 GRIIRVTGPLVVADGMKgAKMYEVVRV----GELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRL 80
Cdd:PRK09099 26 GKVVEVIGTLLRVSGLD-VTLGELCELrqrdGTLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 81 LTSIYDGIQRPLEvirektgdfiargvtapalprdkkwhfipkakvgdkvvGGdiigevpetsiivhkimvpPGIEGEiv 160
Cdd:PRK09099 105 LGRVIDGLGEPID--------------------------------------GG-------------------GPLDCD-- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 161 eiaeegdyTIEEVIAKVKTPsgeikelkmyqrwpvrVKRPYKEKlppevPLITGQRVIDTFFPQAKGGTAAIPGPFGSGK 240
Cdd:PRK09099 126 --------ELVPVIAAPPDP----------------MSRRMVEA-----PLPTGVRIVDGLMTLGEGQRMGIFAPAGVGK 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 241 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 320
Cdd:PRK09099 177 STLMGMFARGTQCDVNVIALIGERGREVREFIELI-------LGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 321 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyrvGSVSVIGAVSPPGGDFS 400
Cdd:PRK09099 250 DRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET-------GSITALYTVLAEDESGS 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 401 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVkdwwhknIDPEWKAMRDKAMALLQKESELQEIVRI-- 478
Cdd:PRK09099 323 DPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQV-------VPREHVQAAGRLRQLLAKHREVETLLQVge 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
3P20_A 479 --VGPDALPerERAILLVARMlrEDYLQQdafdEVDTYCPPEKQVTMMRVL 527
Cdd:PRK09099 396 yrAGSDPVA--DEAIAKIDAI--RDFLSQ----RTDEYSDPDATLAALAEL 438
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
206-505 |
3.16e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 96.72 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 206 PPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGK 285
Cdd:PRK05688 147 PISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHI-------LGE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 286 PLMERTVLIANTSN-MPVAAREASIYTgITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKL 364
Cdd:PRK05688 220 EGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 365 AEFYERAGRVVTLGsdyrvGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVk 444
Cdd:PRK05688 299 PKLVERAGNAEPGG-----GSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQV- 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
3P20_A 445 dwwhknIDPEWKAMRDKAMALLQKESELQEIVRIVG--PDALPERERAILLVARMLRedYLQQ 505
Cdd:PRK05688 373 ------VDPEHLRRAQRFKQLWSRYQQSRDLISVGAyvAGGDPETDLAIARFPHLVQ--FLRQ 427
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
198-372 |
5.45e-21 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 95.74 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 198 KRPYKEKLPpevpliTGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPK 277
Cdd:PRK05922 134 RQPIQEIFP------TGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 278 -LKDpktgkplmERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGY 356
Cdd:PRK05922 208 gLAA--------QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHY 279
|
170
....*....|....*.
3P20_A 357 PAYLASKLAEFYERAG 372
Cdd:PRK05922 280 AASVFHHVSEFTERAG 295
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
203-509 |
6.55e-21 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 95.62 E-value: 6.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 203 EKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFpklkdpk 282
Cdd:PRK07960 151 QRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENI------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 283 TGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLAS 362
Cdd:PRK07960 224 LGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 363 KLAEFYERAGRVVTLGsdyrvGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDA 442
Cdd:PRK07960 304 KLPALVERAGNGISGG-----GSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTA 378
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3P20_A 443 VKDWWHKNIDPEWKAMrdkaMALLQKESELQEI-VRIVGPDalPERERAILLVARMlrEDYLQQDAFD 509
Cdd:PRK07960 379 LIDEQHYARVRQFKQL----LSSFQRNRDLVSVgAYAKGSD--PMLDKAIALWPQL--EAFLQQGIFE 438
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
213-516 |
8.02e-21 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 95.88 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 213 TGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQL----AKwSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLM 288
Cdd:CHL00060 147 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELinniAK-AHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 289 ERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGY-DVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEF 367
Cdd:CHL00060 226 SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 368 YERagrvVTLGSDyrvGSVSVIGAVSPPGGDFSEPVVQNTlrvvkvFWALDA------DLARRRHFPAINWLTSYSLyvd 441
Cdd:CHL00060 306 QER----ITSTKE---GSITSIQAVYVPADDLTDPAPATT------FAHLDAttvlsrGLAAKGIYPAVDPLDSTST--- 369
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3P20_A 442 AVKDWWhknIDPEWKAMRDKAMALLQKESELQEIVRIVGPDALPERERaiLLVARMLR-EDYLQQDAF-DEVDTYCP 516
Cdd:CHL00060 370 MLQPRI---VGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR--LTVARARKiERFLSQPFFvAEVFTGSP 441
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
191-496 |
1.62e-20 |
|
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: 94.77 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 191 QRWPVRVKRPYKEKLPPEV-PLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTV----------TQHQlakwsdaQVVIYI 259
Cdd:COG0055 109 ERRPIHRPAPPFEEQSTKTeILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVlimelihniaKEHG-------GVSVFA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 260 GCGERGNEMTDVLEEFpklKDpkTGkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYDVALMADSTSRWAE 338
Cdd:COG0055 182 GVGERTREGNDLYREM---KE--SG--VLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 339 ALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTlgsdyrvGSVSVIGAVSPPGGDFSEPVVQNTlrvvkvFWALD 418
Cdd:COG0055 255 AGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKK-------GSITSVQAVYVPADDLTDPAPATT------FAHLD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 419 AD--LARRRH----FPAINWLTSYSLYVDA--VKDwWHKNIdpewkAMRDKamALLQKESELQEIVRIVGPDALPERERa 490
Cdd:COG0055 322 ATtvLSRKIAelgiYPAVDPLDSTSRILDPliVGE-EHYRV-----AREVQ--RILQRYKELQDIIAILGMDELSEEDK- 392
|
....*.
3P20_A 491 iLLVAR 496
Cdd:COG0055 393 -LTVAR 397
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
122-437 |
7.30e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 89.27 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 122 PKAKVGDKVVGGD--IIGEVpeTSIIVHKIMVPPGIE------GEIVEIAEEgDYTI---EEVIAKVKTPSGEI--KELK 188
Cdd:PRK06793 38 PKAKIGDVCFVGEhnVLCEV--IAIEKENNMLLPFEQtekvcyGDSVTLIAE-DVVIprgNHLLGKVLSANGEVlnEEAE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 189 MYQRWPVRVKRP----YKEKLPPEVpLITGQRVIDTFFPQAKGGTAAIPGPFGSGKTVTQHQLAKWSDAQVVIYIGCGER 264
Cdd:PRK06793 115 NIPLQKIKLDAPpihaFEREEITDV-FETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGER 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 265 GNEMTDVLEEfpklkdpKTGKPLMERTVLIANTSNMP--VAAREASIYTgiTIAEYFRDMGYDVALMADSTSRWAEALRE 342
Cdd:PRK06793 194 GREVKDFIRK-------ELGEEGMRKSVVVVATSDEShlMQLRAAKLAT--SIAEYFRDQGNNVLLMMDSVTRFADARRS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 343 ISGRLEEMPgEEGYPAYLASKLAEFYERAGRVvtlgsdyRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLA 422
Cdd:PRK06793 265 VDIAVKELP-IGGKTLLMESYMKKLLERSGKT-------QKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELA 336
|
330
....*....|....*
3P20_A 423 RRRHFPAINWLTSYS 437
Cdd:PRK06793 337 TLSHYPAISVLDSVS 351
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
288-437 |
5.40e-17 |
|
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: 83.62 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 288 MERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAE 366
Cdd:TIGR01040 210 MERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLAT 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3P20_A 367 FYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 437
Cdd:TIGR01040 290 IYERAGRV-----EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLS 355
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-70 |
5.42e-16 |
|
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: 72.73 E-value: 5.42e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3P20_A 4 KGRIIRVTGPLVVADGMKGAKMYEVVRVG------ELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGA 70
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIErgdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
27-407 |
1.29e-15 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 79.31 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 27 EVVRVGELGLI--------GEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRLLTSIYDGiqrplevirek 98
Cdd:PRK02118 21 EGVGYGELATVerkdgsslAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNG----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 99 TGDfiargvtapalPRDkkwhfipkakvgdkvvGGdiigevpetsiivhkimvpPGIEGEIVEIAeegdytieeviakvk 178
Cdd:PRK02118 90 SGK-----------PID----------------GG-------------------PELEGEPIEIG--------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 179 TPSgeikelkmyqrwpvrvKRPYKEKLPPEvpLI-TGQRVIDTFFPQAKGgtAAIPGPFGSGKTVTQ--HQLAKWSDAQV 255
Cdd:PRK02118 109 GPS----------------VNPVKRIVPRE--MIrTGIPMIDVFNTLVES--QKIPIFSVSGEPYNAllARIALQAEADI 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 256 VIYIGCGERGNEMTDVLEEFPKLKdpktgkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYD--VALMADST 333
Cdd:PRK02118 169 IILGGMGLTFDDYLFFKDTFENAG-------ALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKkvLVLLTDMT 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3P20_A 334 SrWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYR-VGSVSVIGAVSPPGGDFSEPVVQNT 407
Cdd:PRK02118 242 N-FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA-------VDFEdGGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
5-588 |
7.41e-15 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 77.26 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 5 GRIIRVTGPLVVADGMKGAKMYEVVRVGElGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTGASLSVELGPRLLTSI 84
Cdd:PRK13343 29 GRVESVGDGIAFVSGLPDAALDELLRFEG-GSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 85 YDGIQRPLEvirektgdfiargvtapalprdkkwhfipkakvgdkvvggdiiGEVPETSIIVHKIMVP-PGIegeiveia 163
Cdd:PRK13343 108 IDPLGRPLD-------------------------------------------GGGPLQATARRPLERPaPAI-------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 164 eegdytIEeviakvktpsgeikelkmyqRWPVRVkrpykeklppevPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKT-- 241
Cdd:PRK13343 137 ------IE--------------------RDFVTE------------PLQTGIKVVDALIPIGRGQRELIIGDRQTGKTai 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 242 -----VTQHqlakwsDAQVV-IYIGCGERGNEMTDVLEefpKLKdpKTGKplMERTVLIANTSNMPVAAREASIYTGITI 315
Cdd:PRK13343 179 aidaiINQK------DSDVIcVYVAIGQKASAVARVIE---TLR--EHGA--LEYTTVVVAEASDPPGLQYLAPFAGCAI 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 316 AEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAV 392
Cdd:PRK13343 246 AEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRLLE------RAAKLSPELGGGSLTALPII 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 393 SPPGGDFSEPVVQNTLRVV--KVFwaLDADLARRRHFPAINWLTSYSLYVDAVKdwwHKNIDPEWKAMRdkaMALLQKEs 470
Cdd:PRK13343 320 ETLAGELSAYIPTNLISITdgQIY--LDSDLFAAGQRPAVDVGLSVSRVGGKAQ---HPAIRKESGRLR---LDYAQFL- 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 471 ELQEIVRIVGpdALPERERAILLVARMLREdYLQQDAFDEVdtycPPEKQVTMMRVLLN-FYDKtmeainrgVPLEEIA- 548
Cdd:PRK13343 391 ELEAFTRFGG--LLDAGTQKQITRGRRLRE-LLKQPRFSPL----SVEEQIALLYALNEgLLDA--------VPLANIQa 455
|
570 580 590 600
....*....|....*....|....*....|....*....|...
3P20_A 549 ---KLPVREEIGRMKFERDVSKIRSLIDKTNEQFEELFKKYGA 588
Cdd:PRK13343 456 feeRLLEKLDARFAALSLALESPRELDEAWLAALEEILREAGE 498
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
210-431 |
4.01e-14 |
|
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: 72.98 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 210 PLITGQRVIDTFFPQAKGGTAAIPGPFGSGKT-------VTQHqlakwsDAQVV-IYIGCGERGNEMTDVLEefpKLKDP 281
Cdd:cd01132 52 PLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaiaidtiINQK------GKKVYcIYVAIGQKRSTVAQIVK---TLEEH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 282 KTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA--- 358
Cdd:cd01132 123 GA----MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvf 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3P20_A 359 YLASKLaefYERAGRvvtLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV--KVFwaLDADLARRRHFPAIN 431
Cdd:cd01132 199 YLHSRL---LERAAK---LSDELGGGSLTALPIIETQAGDVSAYIPTNVISITdgQIF--LESELFNKGIRPAIN 265
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
7-69 |
3.01e-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: 64.87 E-value: 3.01e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3P20_A 7 IIRVTGPLVVADGMKGA--KMYEVVRVGEL----GLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTG 69
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRlpGLLNALEVELVefgsLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
206-431 |
1.10e-12 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 70.84 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 206 PPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKT------------VTQHQLAKwsDAQVVIYIGCGERGNEMTDV-- 271
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiinqvrINQQILSK--NAVISIYVSIGQRCSNVARIhr 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 272 -LEEFPKLKdpktgkplmeRTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEM 350
Cdd:PTZ00185 246 lLRSYGALR----------YTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 351 PGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHF 427
Cdd:PTZ00185 316 PGREAYPGdvfYLHSRLLE------RAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQR 389
|
....
3P20_A 428 PAIN 431
Cdd:PTZ00185 390 PAVN 393
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
210-431 |
1.47e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 69.99 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 210 PLITGQRVIDTFFPQAKGGTAAIPGPFGSGKT--VTQHQLAKWSDAQVVIYIGCGERGN---EMTDVLEEfpklkdpktg 284
Cdd:CHL00059 124 PLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavATDTILNQKGQNVICVYVAIGQKASsvaQVVTTLQE---------- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 285 KPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLA 361
Cdd:CHL00059 194 RGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLH 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3P20_A 362 SKLaefYERAGRvvtLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV--KVFwaLDADLARRRHFPAIN 431
Cdd:CHL00059 274 SRL---LERAAK---LSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITdgQIF--LSADLFNAGIRPAIN 337
|
|
| 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 ... |
9-59 |
3.86e-09 |
|
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: 53.20 E-value: 3.86e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
3P20_A 9 RVTGPLVVADGMKGAKMYEVVRV----GELGLiGEIIRLEGDKAVIQVYEETAGV 59
Cdd:cd18118 7 EINGPLVIVEGVKGVKYGEIVEItlpdGEVRR-GQVLEVSGDKAVVQVFEGTSGL 60
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
288-374 |
1.41e-08 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 57.38 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3P20_A 288 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKL 364
Cdd:PRK09281 218 MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL 297
|
90
....*....|
3P20_A 365 aefYERAGRV 374
Cdd:PRK09281 298 ---LERAAKL 304
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
456-529 |
6.68e-08 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 49.75 E-value: 6.68e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3P20_A 456 KAMRDKAMALLQKESELQEIVRIVGPDALPERERAILLVARMLREdYLQQDAFdevdTYCPPEKQVTMMRVLLN 529
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQF----EPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
5-69 |
3.27e-04 |
|
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the 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 FliI ATPase is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of F1-ATP synthase. Although they both are proton driven rotary molecular devices, 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: 349741 [Multi-domain] Cd Length: 70 Bit Score: 39.43 E-value: 3.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3P20_A 5 GRIIRVTGPLVVADGMKgAKMYEVVRV---GELGLIGEIIRLEGDKAVIQVYEETAGVRPGEPVVGTG 69
Cdd:cd18117 3 GRVVRVVGLLLEAVGPQ-APIGELCLIetaDGLSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLG 69
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