|
Name |
Accession |
Description |
Interval |
E-value |
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
3-580 |
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: 1046.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 3 GTLSKITGPVVVADGMIGIKMYDVVRVGAAGLMGEVIRLEGTHATIQVYEDTSGLKVGEPVESTEGPLKLELGPGLLSSI 82
Cdd:COG1155 5 GKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLLGNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 83 YDGIQRPLPVIASQTGsDFIARGTTVSALDHEKLWEYTPVIEVGQELVEGDVVGTVPESPTVLHKVMVPPGIKGKVTNVI 162
Cdd:COG1155 85 FDGIQRPLDKIAEKSG-DFIPRGVDVPALDREKKWDFTPTVKVGDKVSAGDILGTVQETPLIEHKIMVPPGVSGTVKEIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 163 APGSYTVDAVVAVL---DGD-KEIRMSQWWPVRQGRPYARKLDPTTPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVT 238
Cdd:COG1155 164 PEGEYTVEDTIAVLedeDGEeHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKTVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 239 QQSLAKWADVDIIVYVGCGERGNEMTEVLKEFPELEDPRTGSKLMDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMG 318
Cdd:COG1155 244 QHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDMG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 319 YNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRCASLGAEErvGSVTMVGAVSPPGGDMSEPM 398
Cdd:COG1155 324 YDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPGGDFSEPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 399 TQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLFLGQVRPWFEEEVAQDWADVRERAMFLLQKETELQEIVQLVGPDA 478
Cdd:COG1155 402 TQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDENVDPDWSELRNEAMDLLQEEAELQEIVRLVGEDA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 479 LPETEKIILEVARMLREDFLQQFAFDAVDAYCPPKKAYWLLRSILAFYDAATQAMSRGVSLRQIMQLPMREEIATLKTTD 558
Cdd:COG1155 482 LPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLSEIKELPLREKIARMKYSP 561
|
570 580
....*....|....*....|..
gi 1309179977 559 HERAITRMQEMVAQISDEIAGI 580
Cdd:COG1155 562 ENELLEKFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
3-581 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 1021.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 3 GTLSKITGPVVVADGMIGIKMYDVVRVGAAGLMGEVIRLEGTHATIQVYEDTSGLKVGEPVESTEGPLKLELGPGLLSSI 82
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 83 YDGIQRPLPVIASQTGsDFIARGTTVSALDHEKLWEYTPVIEVGQELVEGDVVGTVPESPTVLHKVMVPPGIKGKVTNVI 162
Cdd:PRK04192 85 FDGIQRPLDELAEKSG-DFLERGVYVPALDREKKWEFTPTVKVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKEIV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 163 APGSYTVDAVVAVLD----GDKEIRMSQWWPVRQGRPYARKLDPTTPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVT 238
Cdd:PRK04192 164 SEGDYTVDDTIAVLEdedgEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 239 QQSLAKWADVDIIVYVGCGERGNEMTEVLKEFPELEDPRTGSKLMDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMG 318
Cdd:PRK04192 244 QHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRDMG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 319 YNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRCASLGAEErvGSVTMVGAVSPPGGDMSEPM 398
Cdd:PRK04192 324 YDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPGGDFSEPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 399 TQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLFLGQVRPWFEEEVAQDWADVRERAMFLLQKETELQEIVQLVGPDA 478
Cdd:PRK04192 402 TQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 479 LPETEKIILEVARMLREDFLQQFAFDAVDAYCPPKKAYWLLRSILAFYDAATQAMSRGVSLRQIMQLPMREEIATLKTTD 558
Cdd:PRK04192 482 LPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGVPVSEILELEVRDRIARLKYIP 561
|
570 580
....*....|....*....|...
gi 1309179977 559 HERAITRMQEMVAQISDEIAGIE 581
Cdd:PRK04192 562 ENEYLEKIDEIFEKLEEELEELI 584
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
3-578 |
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: 943.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 3 GTLSKITGPVVVADGMIGIKMYDVVRVGAAGLMGEVIRLEGTHATIQVYEDTSGLKVGEPVESTEGPLKLELGPGLLSSI 82
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 83 YDGIQRPLPVIASQTGsDFIARGTTVSALDHEKLWEYTPVIEVGQELVEGDVVGTVPESPTVLHKVMVPPGIKGKVTNVI 162
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTG-DFIARGVDAPGLDRDKKWHFKPTVKEGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 163 APGSYTVDAVVAVLD--GDKEIRMSQWWPVRQGRPYARKLDPTTPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQ 240
Cdd:TIGR01043 161 EEGDYTVEDTIAVVDtdGDEEIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTVTQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 241 SLAKWADVDIIVYVGCGERGNEMTEVLKEFPELEDPRTGSKLMDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYN 320
Cdd:TIGR01043 241 QLAKWSDADIVVYIGCGERGNEMTDVLEEFPELKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 321 VAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRCASLGAEERVGSVTMVGAVSPPGGDMSEPMTQ 400
Cdd:TIGR01043 321 VALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDFSEPVTQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 401 NSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLFLGQVRPWFEEEVAQDWADVRERAMFLLQKETELQEIVQLVGPDALP 480
Cdd:TIGR01043 401 NTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVQDWWHENVDPDWREMRDEAMDLLQKESELQEIVQLVGPDALP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 481 ETEKIILEVARMLREDFLQQFAFDAVDAYCPPKKAYWLLRSILAFYDAATQAMSRGVSLRQIMQLPMREEIATLKTTDHE 560
Cdd:TIGR01043 481 ERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVEEILKLEVKEEIGRMKYEPDN 560
|
570
....*....|....*...
gi 1309179977 561 RAITRMQEMVAQISDEIA 578
Cdd:TIGR01043 561 DILAKIDEILEKIEKEFK 578
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
69-434 |
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: 549.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 69 PLKLELGPGLLSSIYDGIQRPLPVIAsQTGSDFIARGTTVsaldheklweytpvievgqelvegdvvgtvpesptvlhkv 148
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIA-ETGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 149 mvppgikgkvtnviapgsytvdavvavldgdkeirmsQWWPVRQGRPYARKLDPTTPFLTGMRILDTFFPIALGGNAIIP 228
Cdd:cd01134 40 -------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIP 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 229 GGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEMTEVLKEFPELEDPRTGSKLMDRTVLVANTSNMPVAAREASIYTGV 308
Cdd:cd01134 83 GPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGESLMERTVLIANTSNMPVAAREASIYTGI 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 309 TLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRCASLGAEERVGSVTMVGAVS 388
Cdd:cd01134 163 TIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSVTIVGAVS 242
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1309179977 389 PPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLF 434
Cdd:cd01134 243 PPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
236-555 |
1.08e-160 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 485.30 E-value: 1.08e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 236 TVTQQSLAKWADVDIIVYVGCGERGNEMTEVLKEFPELEDPRTGSKLMDRTVLVANTSNMPVAAREASIYTGVTLAEFYR 315
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 316 DMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRCASLGAEERVGSVTMVGAVSPPGGDMS 395
Cdd:PRK14698 750 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGDFS 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 396 EPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLFLGQVRPWFEEEVAQDWADVRERAMFLLQKETELQEIVQLVG 475
Cdd:PRK14698 830 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDPEWKAMRDKAMELLQKEAELQEIVRIVG 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 476 PDALPETEKIILEVARMLREDFLQQFAFDAVDAYCPPKKAYWLLRSILAFYDAATQAMSRGVSLRQIMQLPMREEIATLK 555
Cdd:PRK14698 910 PDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPLEEIAKLPVREEIGRMK 989
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
209-431 |
7.61e-99 |
|
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: 299.27 E-value: 7.61e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 209 GMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEMTEVLKEFPEledprtgSKLMDRTVL 288
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLG-------SGALKRTVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 289 VANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGR 368
Cdd:pfam00006 74 VVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179977 369 caslgAEERVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSY 431
Cdd:pfam00006 154 -----VKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASV 211
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
147-433 |
6.13e-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: 275.87 E-value: 6.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 147 KVMVPPGIKGKVTNVIApgsytvdavvAVLDGDKEIRMSQWWPVRQGRPY-ARKLDPTTPFLTGMRILDTFFPIALGGNA 225
Cdd:cd19476 1 SVPVGPELLGRILDGLG----------EPLDGLPPIKTKQRRPIHLKAPNpIERLPPEEPLQTGIKVIDLLAPYGRGQKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 226 IIPGGFGTGKTVTQQSLAKW---ADVDIIVYVGCGERGNEMTEVLKEFPELEDprtgsklMDRTVLVANTSNMPVAAREA 302
Cdd:cd19476 71 GIFGGSGVGKTVLAMQLARNqakAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 303 SIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRcaslgAEERVGSVT 382
Cdd:cd19476 144 VPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGK-----VKDGGGSIT 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1309179977 383 MVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTL 433
Cdd:cd19476 219 AIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSR 269
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
3-278 |
1.76e-87 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 292.31 E-value: 1.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 3 GTLSKITGPVVVADGMIGIKMYDVVRVGAAGLMGEVIRLEGTHATIQVYEDTSGLKVGEPVESTEGPLKLELGPGLLSSI 82
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 83 YDGIQRPLPVIASQTGsDFIARGTTVSALDHEKLWEYTPVIEVGQELVEGDVVGTVPESPTVLHKVMVPPGIKGKVTNVI 162
Cdd:PRK14698 85 YDGIQRPLEVIREKSG-DFIARGISAPALPRDKKWHFIPKVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVEIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 163 APGSYTVDAVVAVL---DGD-KEIRMSQWWPVRQGRPYARKLDPTTPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVT 238
Cdd:PRK14698 164 DEGEYTIEEVIAKVktpSGEiKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVD 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1309179977 239 QQSLAKWADVDII----VYVGCGERGNEMTEVLKEFPELEDPRT 278
Cdd:PRK14698 244 GDTLILTKEFGLIkikdLYEILDGKGKKTVEGNEEWTELEEPIT 287
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
83-200 |
3.79e-59 |
|
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: 192.61 E-value: 3.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 83 YDGIQRPLPVIASQTGSdFIARGTTVSALDHEKLWEYTPVIEVGQELVEGDVVGTVPESPTVLHKVMVPPGIKGKVTNVI 162
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTPTVKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTEIA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1309179977 163 APGSYTVDAVVAVLD---GDKEIRMSQWWPVRQGRPYARKL 200
Cdd:pfam16886 80 PEGEYTVEDTIAEVEdegKEKELTMMQKWPVRRPRPYKEKL 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 ... |
450-554 |
1.15e-57 |
|
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: 188.37 E-value: 1.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 450 WADVRERAMFLLQKETELQEIVQLVGPDALPETEKIILEVARMLREDFLQQFAFDAVDAYCPPKKAYWLLRSILAFYDAA 529
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....*
gi 1309179977 530 TQAMSRGVSLRQIMQLPMREEIATL 554
Cdd:cd18111 81 LEALEKGVPLSKILELPVREKIARM 105
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
147-425 |
6.76e-35 |
|
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: 132.68 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 147 KVMVPPGIKGKVtnviapgsytVDAVVAVLDGDKEIRMSQWWPVrqgrpYARKLDP------TTPFLTGMRILDTFFPIA 220
Cdd:cd01136 1 SIPVGDGLLGRV----------IDALGEPLDGKGLPDEPERRPL-----IAAPPNPlkrapiEQPLPTGVRAIDGLLTCG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 221 LGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEmtevLKEFPELEdprTGSKLMDRTVLVANTSNMPVAAR 300
Cdd:cd01136 66 EGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE----VREFIEKD---LGEEGLKRSVLVVATSDESPLLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 301 EASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRcaslGAEervGS 380
Cdd:cd01136 139 VRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN----GEK---GS 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1309179977 381 VTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAI 425
Cdd:cd01136 212 ITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAI 256
|
|
| 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 ... |
3-66 |
1.12e-31 |
|
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: 116.86 E-value: 1.12e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179977 3 GTLSKITGPVVVADGMIGIKMYDVVRVGAAGLMGEVIRLEGTHATIQVYEDTSGLKVGEPVEST 66
Cdd:cd18119 2 GKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERT 65
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
10-467 |
1.88e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 126.85 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 10 GPVVVADGMIGIKMYDVVRVGAAGLMGEVIRLEGTHATIQVYEDTSGLKVGEPVESTEGPLKLELGPGLLSSIYDGIQRP 89
Cdd:PRK06820 37 GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 90 Lpviasqtgsdfiargttvsaldheklweytpvievgqelvegdvvgtvpesptvlhkvmvppgikgkvtnviapgsytv 169
Cdd:PRK06820 117 I------------------------------------------------------------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 170 davvavlDGDkEIRMSQWWPVRQGRPYARKLDP-TTPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADV 248
Cdd:PRK06820 118 -------DGG-PPLTGQWRELDCPPPSPLTRQPiEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 249 DIIVYVGCGERGNEMTEVLkEFPELEDPRTgsklmdRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADST 328
Cdd:PRK06820 190 DVMVLALIGERGREVREFL-EQVLTPEARA------RTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 329 SRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRCASlgaeervGSVTMVGAVSPPGGDMSEPMTQNSLRVTGA 408
Cdd:PRK06820 263 TRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR-------GSITAFYTVLVEGDDMNEPVADEVRSLLDG 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179977 409 FWALDTSLAHRRHFPAISWTKSYTLFLGQVRPWFEEEVAQdwadvRERAMFLLQKETEL 467
Cdd:PRK06820 336 HIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQ-----KLRRMLACYQEIEL 389
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-425 |
2.10e-31 |
|
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: 126.68 E-value: 2.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 3 GTLSKITGPVVVADGM---IGikmyDVVRVGAAG---LMGEVIRLEGTHATIQVYEDTSGLKVGEPVESTEGPLKLELGP 76
Cdd:COG1157 21 GRVTRVVGLLIEAVGPdasIG----ELCEIETADgrpVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 77 GLLSSIYDGIQRPLpviasqtgsdfiargttvsaldheklweytpvievgqelvegdvvgtvpesptvlhkvmvppgikg 156
Cdd:COG1157 97 GLLGRVLDGLGRPL------------------------------------------------------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 157 kvtnviapgsytvdavvavlDGDKEIRMSQWWPVrqgrpYARKLDP------TTPFLTGMRILDTFFPIALG---GnaiI 227
Cdd:COG1157 111 --------------------DGKGPLPGEERRPL-----DAPPPNPlerariTEPLDTGVRAIDGLLTVGRGqriG---I 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 228 PGGFGTGKTVTQQSLAKWADVDIIVyVG-CGERGNEmtevLKEFpeLEDPRtGSKLMDRTVLVANTSNMPVAAREASIYT 306
Cdd:COG1157 163 FAGSGVGKSTLLGMIARNTEADVNV-IAlIGERGRE----VREF--IEDDL-GEEGLARSVVVVATSDEPPLMRLRAAYT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 307 GVTLAEFYRDMGYNVAMMADSTSRWGEALREV---SGrleEMPGEEGYPAYLATRLAAFYERSGRCASlgaeervGSVTM 383
Cdd:COG1157 235 ATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIglaAG---EPPATRGYPPSVFALLPRLLERAGNGGK-------GSITA 304
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1309179977 384 VGAVSPPGGDMSEPMTqNSLR-------VtgafwaLDTSLAHRRHFPAI 425
Cdd:COG1157 305 FYTVLVEGDDMNDPIA-DAVRgildghiV------LSRKLAERGHYPAI 346
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
141-473 |
1.33e-28 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 118.70 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 141 SPT-VLHKVMVPPGIKGKVtnviapgsytVDAVVAVLDGDKEIRMSQWWPVRQG--RPYARKLdPTTPFLTGMRILDTFF 217
Cdd:PRK06936 89 SPTgTMHQVGVGEHLLGRV----------LDGLGQPFDGGHPPEPAAWYPVYADapAPMSRRL-IETPLSLGVRVIDGLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 218 PIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEmtevLKEFPELEdprTGSKLMDRTVLVANTSNMPV 297
Cdd:PRK06936 158 TCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGRE----VREFIESD---LGEEGLRKAVLVVATSDRPS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 298 AAREASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRCASlgaeer 377
Cdd:PRK06936 231 MERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDK------ 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 378 vGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLFLGQVrpwFEEEVAQDWADVREra 457
Cdd:PRK06936 305 -GSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQI---VSKEHKTWAGRLRE-- 378
|
330
....*....|....*.
gi 1309179977 458 mfLLQKETELQEIVQL 473
Cdd:PRK06936 379 --LLAKYEEVELLLQI 392
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
194-473 |
4.21e-26 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 111.24 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 194 RPYARKLDPTTPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEMTEVLKEFpel 273
Cdd:PRK08149 123 PSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVESL--- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 274 edprTGSKLMDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPA 353
Cdd:PRK08149 200 ----RASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 354 YLATRLAAFYERSGRCaslgaeeRVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTL 433
Cdd:PRK08149 276 SVFDSLPRLLERPGAT-------LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR 348
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1309179977 434 FLGQVRpwfEEEVAQDWADVREramfLLQKETELQEIVQL 473
Cdd:PRK08149 349 VFGQVT---DPKHRQLAAAFRK----LLTRLEELQLFIDL 381
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
147-430 |
9.17e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 110.20 E-value: 9.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 147 KVMVPPGIKGKVtnviapgsytVDAVVAVLDGDKEIRMSQWWPVRQGRPYARKLDP-TTPFLTGMRILDTFFPIALGGNA 225
Cdd:PRK07721 92 EVKVGSGLIGQV----------LDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPiREPMEVGVRAIDSLLTVGKGQRV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 226 IIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEmtevLKEFPELEdprTGSKLMDRTVLVANTSNMPVAAREASIY 305
Cdd:PRK07721 162 GIFAGSGVGKSTLMGMIARNTSADLNVIALIGERGRE----VREFIERD---LGPEGLKRSIVVVATSDQPALMRIKGAY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 306 TGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRCASlgaeervGSVTMVG 385
Cdd:PRK07721 235 TATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS-------GSITAFY 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1309179977 386 AVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKS 430
Cdd:PRK07721 308 TVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKS 352
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
20-425 |
1.17e-25 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 110.04 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 20 GIKMYDVVRVGAAGLMGEVIRLEGTHATIQVYEDTSGLKVGEPVESTEGPLKLELGPGLLSSIYDGIQRPLPviasqtgs 99
Cdd:PRK07594 39 GVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD-------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 100 dfiargttvsaldheklweytpvievGQELvegdvvgtvPESPTVLHKVMVPPGIkgkvtnviapgsytvdavvavldgd 179
Cdd:PRK07594 111 --------------------------GREL---------PDVCWKDYDAMPPPAM------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 180 keirmsqwwpVRQgrPYARkldpttPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGER 259
Cdd:PRK07594 131 ----------VRQ--PITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVLVLIGER 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 260 GNEMTEVLkEFPELEDPRtgsklmDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVS 339
Cdd:PRK07594 193 GREVREFI-DFTLSEETR------KRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 340 GRLEEMPGEEGYPAYLATRLAAFYERSGrcasLGaeeRVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHR 419
Cdd:PRK07594 266 LAAGETAVSGEYPPGVFSALPRLLERTG----MG---EKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAER 338
|
....*.
gi 1309179977 420 RHFPAI 425
Cdd:PRK07594 339 GHYPAI 344
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
204-426 |
1.48e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 109.70 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 204 TPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEmtevLKEFpeLEDPRTGSklM 283
Cdd:PRK06002 147 TGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGRE----VREF--LEDTLADN--L 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 284 DRTVLVANTSN-MPVAAREASIyTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAF 362
Cdd:PRK06002 219 KKAVAVVATSDeSPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRL 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179977 363 YERSGRcaslGAEERvGSVTMVGAVSPPGGDMSEPMTqNSLRVT-GAFWALDTSLAHRRHFPAIS 426
Cdd:PRK06002 298 LERAGP----GAEGG-GSITGIFSVLVDGDDHNDPVA-DSIRGTlDGHIVLDRAIAEQGRYPAVD 356
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
147-397 |
4.23e-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: 4.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 147 KVMVPPGIKGKVTNVIApgsytvdavvAVLDGDKEIRMSQWWPVRQGRPYARKLDPTT-PFLTGMRILDTFFPIALGGNA 225
Cdd:cd01133 1 SVPVGEETLGRIFNVLG----------EPIDERGPIKAKERWPIHREAPEFVELSTEQeILETGIKVVDLLAPYAKGGKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 226 IIPGGFGTGKTVTQQSL----AKWADVdIIVYVGCGERGNEMTEVLKEFPELEDPRTGSklMDRTVLVANTSNMPVAARE 301
Cdd:cd01133 71 GLFGGAGVGKTVLIMELinniAKAHGG-YSVFAGVGERTREGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 302 ASIYTGVTLAEFYRDM-GYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSgrcaslgAEERVGS 380
Cdd:cd01133 148 RVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERI-------TSTKKGS 220
|
250
....*....|....*..
gi 1309179977 381 VTMVGAVSPPGGDMSEP 397
Cdd:cd01133 221 ITSVQAVYVPADDLTDP 237
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
4-500 |
5.08e-22 |
|
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: 99.06 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 4 TLSKITGPVVVADGMIGIKMYDVVRV-GAAG--LMGEVIRLEGTHATIQVYEDTSGLKVGEP-VESTEGPLKLELGPGLL 79
Cdd:COG1156 8 TISEIAGPLLFVEGVEGVGYGELVEIeLPDGerRRGQVLEVSEDKAVVQVFEGTTGLSLKNTkVRFLGEPLELPVSEDML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 80 SSIYDGIQRPL----PVIASQ----TG-----------SDFIARGttVSALDHeklweYTPVIEvGQELvegdvvgtvpe 140
Cdd:COG1156 88 GRVFNGLGRPIdggpPIIPEKrldiNGspinpvareypREFIQTG--ISAIDG-----LNTLVR-GQKL----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 141 sptvlhkvmvpPgikgkvtnvIAPGSYTVDAVVAVldgdkEIrmsqwwpVRQgrpyARKLDPTTPFLtgmrildtffpia 220
Cdd:COG1156 149 -----------P---------IFSGSGLPHNELAA-----QI-------ARQ----AKVRGEEEKFA------------- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 221 lggnaiipggfgtgktvtqqslakwadvdiIVYVGCGERGNEMTEVLKEFPEledprTGSklMDRTVLVANTSNMPVAAR 300
Cdd:COG1156 180 ------------------------------VVFAAMGITHDEANFFREEFEE-----TGA--LDRVVMFLNLADDPAIER 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 301 EASIYTGVTLAEF--YrDMGYNV-AMMADSTSrWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRcaslgAEER 377
Cdd:COG1156 223 IITPRMALTAAEYlaF-EKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGR-----IKGR 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 378 VGSVTMVGAVSPPGGDMSEP-------MTQNSLrvtgafwALDTSLAHRRHFPAISWTKS------------YTlflgqv 438
Cdd:COG1156 296 KGSITQIPILTMPNDDITHPipdltgyITEGQI-------VLSRDLHRKGIYPPIDVLPSlsrlmkdgigegKT------ 362
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179977 439 RpwfeeevaQDWADVRERAMFLLQKETELQEIVQLVGPDALPETEKIILEVARMLREDFLQQ 500
Cdd:COG1156 363 R--------EDHADVANQLYAAYARGQEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQ 416
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
4-500 |
5.73e-22 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 99.13 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 4 TLSKITGPVVVADGMIGIKMYDVVRV-GAAG--LMGEVIRLEGTHATIQVYEDTSGLKVGE-PVESTEGPLKLELGPGLL 79
Cdd:PRK04196 6 TVSEIKGPLLFVEGVEGVAYGEIVEIeLPNGekRRGQVLEVSEDKAVVQVFEGTTGLDLKDtKVRFTGEPLKLPVSEDML 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 80 SSIYDGIQRPL----PVIASQ----TG-----------SDFIARGttVSALDHEklweYTPVieVGQELvegdvvgtvpe 140
Cdd:PRK04196 86 GRIFDGLGRPIdggpEIIPEKrldiNGapinpvareypEEFIQTG--ISAIDGL----NTLV--RGQKL----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 141 sptvlhkvmvpPgikgkvtnvIAPGSytvdavvavldgdkeirmsqwwpvrqGRPYARkldpttpfltgmrildtffpIA 220
Cdd:PRK04196 147 -----------P---------IFSGS--------------------------GLPHNE--------------------LA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 221 LggnaiipggfgtgKTVTQQSLAKWADVDIIVYVGCGERGNEMTEVLKEFPeledpRTGSklMDRTVLVANTSNMPVAAR 300
Cdd:PRK04196 161 A-------------QIARQAKVLGEEENFAVVFAAMGITFEEANFFMEDFE-----ETGA--LERSVVFLNLADDPAIER 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 301 EASIYTGVTLAEFYR-DMGYNV-AMMADSTSrWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRcaslgAEERV 378
Cdd:PRK04196 221 ILTPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGR-----IKGKK 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 379 GSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLFL------GQVRpwfeeevaQDWAD 452
Cdd:PRK04196 295 GSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMkdgigeGKTR--------EDHKD 366
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1309179977 453 VRERAMFLLQKETELQEIVQLVGPDALPETEKIILEVARMLREDFLQQ 500
Cdd:PRK04196 367 VANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQ 414
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
203-467 |
1.03e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 98.13 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 203 TTPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEMTEVLKEfpELedprtGSKL 282
Cdd:PRK06793 137 TDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRK--EL-----GEEG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 283 MDRTVLVANTSNMP--VAAREASIYTgvTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPgEEGYPAYLATRLA 360
Cdd:PRK06793 210 MRKSVVVVATSDEShlMQLRAAKLAT--SIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP-IGGKTLLMESYMK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 361 AFYERSGRCASlgaeervGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISwtksytlFLGQVRP 440
Cdd:PRK06793 287 KLLERSGKTQK-------GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAIS-------VLDSVSR 352
|
250 260
....*....|....*....|....*....
gi 1309179977 441 WFEEEVAQD-WADVRE-RAMFLLQKETEL 467
Cdd:PRK06793 353 IMEEIVSPNhWQLANEmRKILSIYKENEL 381
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
169-430 |
2.83e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 96.69 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 169 VDAVVAVLDGDKEIRMSQWWPVRQGR--PYARKldPTT-PFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKW 245
Cdd:PRK08972 108 IDGVGNPLDGLGPIYTDQRASRHSPPinPLSRR--PITePLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 246 ADVDIIVyVG-CGERGNEMTEVLKEFpeledprTGSKLMDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMM 324
Cdd:PRK08972 186 TTADVIV-VGlVGERGREVKEFIEEI-------LGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 325 ADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRcaslGAEERvGSVTMVGAVSPPGGDMSEPMTQNSLR 404
Cdd:PRK08972 258 MDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGN----GGPGQ-GSITAFYTVLTEGDDLQDPIADASRA 332
|
250 260
....*....|....*....|....*.
gi 1309179977 405 VTGAFWALDTSLAHRRHFPAISWTKS 430
Cdd:PRK08972 333 ILDGHIVLSRELADSGHYPAIDIEAS 358
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
195-425 |
4.83e-21 |
|
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: 93.44 E-value: 4.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 195 PYARKLdPTTPFLTGMRILDTFFPIALGGNaiIPGGFGTG--------KTVTQQSLAKWADVDIIVYVGCGERGNEMTEV 266
Cdd:cd01135 43 PVARIY-PEEMIQTGISAIDVMNTLVRGQK--LPIFSGSGlphnelaaQIARQAGVVGSEENFAIVFAAMGVTMEEARFF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 267 LKEFPEledprTGSklMDRTVLVANTSNMPVAAReasIYT---GVTLAEFYR-DMGYNV-AMMADSTSrWGEALREVSGR 341
Cdd:cd01135 120 KDDFEE-----TGA--LERVVLFLNLANDPTIER---IITprmALTTAEYLAyEKGKHVlVILTDMTN-YAEALREVSAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 342 LEEMPGEEGYPAYLATRLAAFYERSGRcaslgAEERVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRH 421
Cdd:cd01135 189 REEVPGRRGYPGYMYTDLATIYERAGR-----VEGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGI 263
|
....
gi 1309179977 422 FPAI 425
Cdd:cd01135 264 YPPI 267
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
189-505 |
1.31e-20 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 95.11 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 189 PVRQGRPYARKLDpTTP--FLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSL----AKwADVDIIVYVGCGER--- 259
Cdd:CHL00060 127 PIHRSAPAFIQLD-TKLsiFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELinniAK-AHGGVSVFGGVGERtre 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 260 GNEMTEVLKEfpeledprtgSKLMD-------RTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGY-NVAMMADSTSRW 331
Cdd:CHL00060 205 GNDLYMEMKE----------SGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRF 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 332 GEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSgrcaslgAEERVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWA 411
Cdd:CHL00060 275 VQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 412 LDTSLAHRRHFPAISWTKSYTLFLgqvRPWF--EE--EVAQdwaDVREramfLLQKETELQEIVQLVGPDALPETEKIIL 487
Cdd:CHL00060 348 LSRGLAAKGIYPAVDPLDSTSTML---QPRIvgEEhyETAQ---RVKQ----TLQRYKELQDIIAILGLDELSEEDRLTV 417
|
330
....*....|....*...
gi 1309179977 488 EVARMLrEDFLQQFAFDA 505
Cdd:CHL00060 418 ARARKI-ERFLSQPFFVA 434
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
148-522 |
2.22e-20 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 94.06 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 148 VMVPPGIKGKVtnviapgsytVDAVVAVLDGDKEIRMSQWWPVrqgrpYARKLDPT------TPFLTGMRILDTFFPIAL 221
Cdd:PRK09099 98 VPVGPALLGRV----------IDGLGEPIDGGGPLDCDELVPV-----IAAPPDPMsrrmveAPLPTGVRIVDGLMTLGE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 222 GGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEmtevLKEFPELedpRTGSKLMDRTVLVANTSNMPVAARE 301
Cdd:PRK09099 163 GQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGRE----VREFIEL---ILGEDGMARSVVVCATSDRSSIERA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 302 ASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRCASlgaeervGSV 381
Cdd:PRK09099 236 KAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGET-------GSI 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 382 TMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLFLGQVRPwfeEEVAQDWADVREramfLL 461
Cdd:PRK09099 309 TALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVP---REHVQAAGRLRQ----LL 381
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179977 462 QKETELQEIVQL----VGPDALPEtekiilevARMLREDFLQQFAFDAVDAYCPPKKAYWLLRSI 522
Cdd:PRK09099 382 AKHREVETLLQVgeyrAGSDPVAD--------EAIAKIDAIRDFLSQRTDEYSDPDATLAALAEL 438
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
209-430 |
4.84e-20 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 93.12 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 209 GMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEmtevLKEFpeLEDPrTGSKLMDRTVL 288
Cdd:PRK08927 145 GVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGRE----VQEF--LQDD-LGPEGLARSVV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 289 VANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGR 368
Cdd:PRK08927 218 VVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGP 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179977 369 caslgAEERVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKS 430
Cdd:PRK08927 298 -----GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKS 354
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
176-425 |
3.90e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 87.09 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 176 LDGDKEIRMSQWWPVRQGRPYARKLDPTT-PFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYV 254
Cdd:PRK05688 121 LDGKGPMKAEDWVPMDGPTINPLNRHPISePLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 255 GCGERGNEMTEVLKEFpeledprTGSKLMDRTVLVANTSN-MPVAAREASIYTgVTLAEFYRDMGYNVAMMADSTSRWGE 333
Cdd:PRK05688 201 LIGERGREVKEFIEHI-------LGEEGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQ 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 334 ALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGrcaslGAEERVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALD 413
Cdd:PRK05688 273 AQREIALAIGEPPATKGYPPSVFAKLPKLVERAG-----NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLS 347
|
250
....*....|..
gi 1309179977 414 TSLAHRRHFPAI 425
Cdd:PRK05688 348 RRLAEEGHYPAI 359
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
204-505 |
6.74e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 86.48 E-value: 6.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 204 TPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEMTEVLkefpeleDPRTGSKLM 283
Cdd:PRK07196 137 TPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFI-------EHSLQAAGM 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 284 DRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFY 363
Cdd:PRK07196 210 AKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 364 ErsgrcaSLGAEERVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLFLGQVrpwfe 443
Cdd:PRK07196 290 E------SAGNSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQV----- 358
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179977 444 eeVAQDWADVRERAMFLLQKETELQEIVQLVG--PDALPETEKIILEVARM---LREDFLQQFAFDA 505
Cdd:PRK07196 359 --IGSQQAKAASLLKQCYADYMAIKPLIPLGGyvAGADPMADQAVHYYPAItqfLRQEVGHPALFSA 423
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
169-402 |
2.37e-17 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 84.74 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 169 VDAVVAVLDGDKEIRMSQWWPVRQG--RPYARKLdPTTPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWA 246
Cdd:PRK08472 103 VDPLGRPIDGKGAIDYERYAPIMKApiAAMKRGL-IDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGC 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 247 DVDIIVYVGCGERGnemtevlKEFPELEDPRTGSKLmDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMAD 326
Cdd:PRK08472 182 LAPIKVVALIGERG-------REIPEFIEKNLGGDL-ENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMD 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179977 327 STSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSGRcaslgaEERVGSVTMVGAVSPPGGDMSEPMTQNS 402
Cdd:PRK08472 254 SVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK------EEGKGSITAFFTVLVEGDDMSDPIADQS 323
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
283-520 |
7.79e-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: 83.23 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 283 MDRTVLVANTSNMPVAAREASIYTGVTLAEFYR-DMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAA 361
Cdd:TIGR01040 210 MERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLAT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 362 FYERSGRcaslgAEERVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAISWTKSYTLFL------ 435
Cdd:TIGR01040 290 IYERAGR-----VEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMksaige 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 436 GQVRpwfeeevaQDWADVRER--AMFLLQKetELQEIVQLVGPDALPETEKIILEVARMLREDFLQQFAFDAVDAYCPPK 513
Cdd:TIGR01040 365 GMTR--------KDHSDVSNQlyACYAIGK--DVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLD 434
|
....*..
gi 1309179977 514 KAYWLLR 520
Cdd:TIGR01040 435 IAWQLLR 441
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
208-425 |
3.14e-16 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 81.37 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 208 TGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWADVDIIVYVGCGERGNEmtevLKEFPEledPRTGSKLMDRTV 287
Cdd:PRK07960 161 TGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGRE----VKDFIE---NILGAEGRARSV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 288 LVANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSG 367
Cdd:PRK07960 234 VIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179977 368 RCASLGaeervGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAI 425
Cdd:PRK07960 314 NGISGG-----GSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAI 366
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
176-430 |
9.14e-16 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 79.96 E-value: 9.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 176 LDGDKEIRMSQWWPVRQGRPYARKLDPTT-PFLTGMRILDTFFPIALGGNAIIPGGFGTGKTvtqqSLAkwadVDII--- 251
Cdd:PRK13343 115 LDGGGPLQATARRPLERPAPAIIERDFVTePLQTGIKVVDALIPIGRGQRELIIGDRQTGKT----AIA----IDAIinq 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 252 -------VYVGCGERGN---EMTEVLKEFpeledprtGSklMDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYNV 321
Cdd:PRK13343 187 kdsdvicVYVAIGQKASavaRVIETLREH--------GA--LEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 322 AMMADSTSRWGEALREVSGRLEEMPGEEGYPA---YLATRLaafYERSgrcASLGAEERVGSVTMVGAVSPPGGDMSEPM 398
Cdd:PRK13343 257 LIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRL---LERA---AKLSPELGGGSLTALPIIETLAGELSAYI 330
|
250 260 270
....*....|....*....|....*....|..
gi 1309179977 399 TQNSLRVTGAFWALDTSLAHRRHFPAISWTKS 430
Cdd:PRK13343 331 PTNLISITDGQIYLDSDLFAAGQRPAVDVGLS 362
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
169-367 |
1.39e-15 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 79.18 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 169 VDAVVAVLDGDKEIRMSQWWPVRQGRPYARKLDPTTP-FLTGMRILDTFFPIALGGNAIIPGGFGTGKTVTQQSLAKWAD 247
Cdd:PRK05922 103 LDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEiFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 248 VDIIVYVGCGERGNEMTEVLKEFPEledprtGSKlMDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADS 327
Cdd:PRK05922 183 STINVIALIGERGREVREYIEQHKE------GLA-AQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDS 255
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1309179977 328 TSRWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSG 367
Cdd:PRK05922 256 LSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG 295
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
204-395 |
4.41e-14 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 74.61 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 204 TPFLTGMRILDTFFPIALGGNAIIPGGFGTGKTvtqqSLA-------KWADVdIIVYVGCGERGNEMTEVLKEFPEledp 276
Cdd:CHL00059 123 EPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKT----AVAtdtilnqKGQNV-ICVYVAIGQKASSVAQVVTTLQE---- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 277 rTGSklMDRTVLVANTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPA--- 353
Cdd:CHL00059 194 -RGA--MEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvf 270
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1309179977 354 YLATRLaafYERSgrcASLGAEERVGSVTMVGAVSPPGGDMS 395
Cdd:CHL00059 271 YLHSRL---LERA---AKLSSQLGEGSMTALPIVETQAGDVS 306
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
206-426 |
5.52e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 71.61 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 206 FLTGMRILDTFFPIALGGNAIIPGGFGTGKT------------VTQQSLAKWADVDIivYVGCGERGNEMTEVLKEFpel 273
Cdd:PTZ00185 173 LLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiinqvrINQQILSKNAVISI--YVSIGQRCSNVARIHRLL--- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 274 edpRTGSKLMDRTVLVAnTSNMPVAAREASIYTGVTLAEFYRDMGYNVAMMADSTSRWGEALREVSGRLEEMPGEEGYPA 353
Cdd:PTZ00185 248 ---RSYGALRYTTVMAA-TAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPG 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179977 354 ---YLATRLAAfyersgRCASLGAEERVGSVTMVGAVSPPGGDMSEPMTQNSLRVTGAFWALDTSLAHRRHFPAIS 426
Cdd:PTZ00185 324 dvfYLHSRLLE------RAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-66 |
1.54e-12 |
|
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: 62.95 E-value: 1.54e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179977 6 SKITGPVVVADGMIG--IKMYDVVRVGA----AGLMGEVIRLEGTHATIQVYEDTSGLKVGEPVEST 66
Cdd:pfam02874 2 VQVIGPVVDVEFGIGrlPGLLNALEVELvefgSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
8-410 |
3.84e-10 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 62.36 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 8 ITGPV--VVADGmIGIKMYDVVRVGAAGLMGEVIRLEGTHATIQVYEDTSGLKVGEPVESTEGPLKLELGPGLLSSIYDG 85
Cdd:PRK02118 11 ITGNVitVEAEG-VGYGELATVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 86 IQRPlpviasqtgsdfiargttvsaldheklweytpvIEVGQELVEGDV-VGTVPESPTvlhKVMVPpgikgkvTNVIAP 164
Cdd:PRK02118 90 SGKP---------------------------------IDGGPELEGEPIeIGGPSVNPV---KRIVP-------REMIRT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 165 GsytvdavVAVLDGDKEIRMSQWWPV--RQGRPYARKLdpttpfltgMRIldtffpialggnaiipggfgtgktvtqqsl 242
Cdd:PRK02118 127 G-------IPMIDVFNTLVESQKIPIfsVSGEPYNALL---------ARI------------------------------ 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 243 AKWADVDIIVYVGCGERGNEMTEVLKEFPELedprtGSklMDRTVLVANTSNMPVAAREASIYTGVTLAE-FYRDMGYNV 321
Cdd:PRK02118 161 ALQAEADIIILGGMGLTFDDYLFFKDTFENA-----GA--LDRTVMFIHTASDPPVECLLVPDMALAVAEkFALEGKKKV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179977 322 -AMMADSTSrWGEALREVSGRLEEMPGEEGYPAYLATRLAAFYERSgrCASLGAeervGSVTMVGAVSPPGGDMSEPMTQ 400
Cdd:PRK02118 234 lVLLTDMTN-FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA--VDFEDG----GSITIIAVTTMPGDDVTHPVPD 306
|
410
....*....|.
gi 1309179977 401 NSLRVT-GAFW 410
Cdd:PRK02118 307 NTGYITeGQFY 317
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
2-66 |
7.31e-10 |
|
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: 55.40 E-value: 7.31e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179977 2 LGTLSKITGPVVVADGMIGIKMYDVVRVGAA------GLMGEVIRLEGTHATIQVYEDTSGLKVGEPVEST 66
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGdgnnetVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPT 71
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
452-507 |
8.29e-07 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 46.67 E-value: 8.29e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179977 452 DVRERAMFLLQKETELQEIVQLVGPDALPETEKIILEVARMLREdFLQQFAFDAVD 507
Cdd:cd01429 3 AVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPET 57
|
|
| 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 ... |
4-57 |
5.69e-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: 5.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179977 4 TLSKITGPVVVADGMIGIKMYDVVRV-GAAG--LMGEVIRLEGTHATIQVYEDTSGL 57
Cdd:cd18118 4 TVSEINGPLVIVEGVKGVKYGEIVEItLPDGevRRGQVLEVSGDKAVVQVFEGTSGL 60
|
|
| |
