|
Name |
Accession |
Description |
Interval |
E-value |
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
9-581 |
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: 1154.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 9 TQGVLKRISGPVVTAVGL-DAHMYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGLLT 87
Cdd:COG1155 3 TKGKIVKINGPLVTAEGMgGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 88 SIYDGIQRPLEVLMDKMGSFIKRGVSAPGLSHEKKWEFVPTVKAGDVVGPGDILGTVQETN-IVHKIMVPPNLKGgKIKK 166
Cdd:COG1155 83 NIFDGIQRPLDKIAEKSGDFIPRGVDVPALDREKKWDFTPTVKVGDKVSAGDILGTVQETPlIEHKIMVPPGVSG-TVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 167 ISG-GSFTIDETICVLEDGT----EITMLQRWPVRVPRPVKEKLNPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKT 241
Cdd:COG1155 162 IAPeGEYTVEDTIAVLEDEDgeehELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 242 VTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPELEDPKTGRPLMERTVLIANTSNMPVAAREASVYTGITIAEYFRD 321
Cdd:COG1155 242 VTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYRD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 322 MGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAISLNGASGSVSVIGAVSPPGGDFSEPV 401
Cdd:COG1155 322 MGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGGDFSEPV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 402 TQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLDSLGEWYDKEVSPEWNTLRSWAMGVLQKEAELQEIVQLVGSDA 481
Cdd:COG1155 402 TQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDENVDPDWSELRNEAMDLLQEEAELQEIVRLVGEDA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 482 LPDEEQITIEVARMIREIFLQQNAYDAVDTFCPMSKQYDMMKAIKHYADLARTAQAGGATPQQIVGARSKNELPQIKFIK 561
Cdd:COG1155 482 LPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLSEIKELPLREKIARMKYSP 561
|
570 580
....*....|....*....|..
gi 1055291904 562 --DYEPVLEKILKDMDAEFEAM 581
Cdd:COG1155 562 enELLEKFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
8-583 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 1142.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 8 RTQGVLKRISGPVVTAVGLD-AHMYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGLL 86
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGgARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 87 TSIYDGIQRPLEVLMDKMGSFIKRGVSAPGLSHEKKWEFVPTVKAGDVVGPGDILGTVQET-NIVHKIMVPPNLKGgKIK 165
Cdd:PRK04192 82 GSIFDGIQRPLDELAEKSGDFLERGVYVPALDREKKWEFTPTVKVGDKVEAGDILGTVQETpSIEHKIMVPPGVSG-TVK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 166 KISG-GSFTIDETICVLED----GTEITMLQRWPVRVPRPVKEKLNPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGK 240
Cdd:PRK04192 161 EIVSeGDYTVDDTIAVLEDedgeGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 241 TVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPELEDPKTGRPLMERTVLIANTSNMPVAAREASVYTGITIAEYFR 320
Cdd:PRK04192 241 TVTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELIDPKTGRPLMERTVLIANTSNMPVAAREASIYTGITIAEYYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 321 DMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAISLNGASGSVSVIGAVSPPGGDFSEP 400
Cdd:PRK04192 321 DMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEEGSVTIIGAVSPPGGDFSEP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 401 VTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLDSLGEWYDKEVSPEWNTLRSWAMGVLQKEAELQEIVQLVGSD 480
Cdd:PRK04192 401 VTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 481 ALPDEEQITIEVARMIREIFLQQNAYDAVDTFCPMSKQYDMMKAIKHYADLARTAQAGGATPQQIVGARSKNELPQIKFI 560
Cdd:PRK04192 481 ALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGVPVSEILELEVRDRIARLKYI 560
|
570 580
....*....|....*....|....*
gi 1055291904 561 K--DYEPVLEKILKDMDAEFEAMRA 583
Cdd:PRK04192 561 PenEYLEKIDEIFEKLEEELEELIA 585
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
11-579 |
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: 1041.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 11 GVLKRISGPVVTAVGLD-AHMYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGLLTSI 89
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKgAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 90 YDGIQRPLEVLMDKMGSFIKRGVSAPGLSHEKKWEFVPTVKAGDVVGPGDILGTVQET-NIVHKIMVPPNLKGgKIKKI- 167
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGDFIARGVDAPGLDRDKKWHFKPTVKEGDKVEGGDIIGVVPETsLIEHKILVPPNVEG-EIVEIa 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 168 SGGSFTIDETICVLE-DG-TEITMLQRWPVRVPRPVKEKLNPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQ 245
Cdd:TIGR01043 161 EEGDYTVEDTIAVVDtDGdEEIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTVTQH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 246 QLAKWSDAEIVVYIGCGERGNEMTEVLTEFPELEDPKTGRPLMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYD 325
Cdd:TIGR01043 241 QLAKWSDADIVVYIGCGERGNEMTDVLEEFPELKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 326 VSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAISLNG--ASGSVSVIGAVSPPGGDFSEPVTQ 403
Cdd:TIGR01043 321 VALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGeeRVGSVTVIGAVSPPGGDFSEPVTQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 404 NTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLDSLGEWYDKEVSPEWNTLRSWAMGVLQKEAELQEIVQLVGSDALP 483
Cdd:TIGR01043 401 NTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVQDWWHENVDPDWREMRDEAMDLLQKESELQEIVQLVGPDALP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 484 DEEQITIEVARMIREIFLQQNAYDAVDTFCPMSKQYDMMKAIKHYADLARTAQAGGATPQQIVGARSKNELPQIKFIKD- 562
Cdd:TIGR01043 481 ERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVEEILKLEVKEEIGRMKYEPDn 560
|
570
....*....|....*...
gi 1055291904 563 -YEPVLEKILKDMDAEFE 579
Cdd:TIGR01043 561 dILAKIDEILEKIEKEFK 578
|
|
| V-ATPase_V1_A |
TIGR01042 |
V-type (H+)-ATPase V1, A subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
11-582 |
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: 739.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 11 GVLKRISGPVVTAVGL-DAHMYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGLLTSI 89
Cdd:TIGR01042 3 GYIYKVSGPVVVAENMaGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILGNI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 90 YDGIQRPLEVLMDKMGS-FIKRGVSAPGLSHEKKWEFVP-TVKAGDVVGPGDILGTVQETNIV-HKIMVPPNLKGgKIKK 166
Cdd:TIGR01042 83 FDGIQRPLKAIAEQSQSiYIPRGVNVPALDRDKKWEFTPkKLRVGDHITGGDIYGTVFENSLIkHKIMLPPRARG-TITY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 167 IS-GGSFTIDETICVLE-DG--TEITMLQRWPVRVPRPVKEKLNPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTV 242
Cdd:TIGR01042 162 IApAGNYTVDDTVLEVEfQGvkKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 243 TQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPELEDPKTGR--PLMERTVLIANTSNMPVAAREASVYTGITIAEYFR 320
Cdd:TIGR01042 242 ISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEVDGReeSIMKRTTLVANTSNMPVAAREASIYTGITLAEYFR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 321 DMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAISLNGAS--GSVSVIGAVSPPGGDFS 398
Cdd:TIGR01042 322 DMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEreGSVSIVGAVSPPGGDFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 399 EPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLDSLGEWYDKEVsPEWNTLRSWAMGVLQKEAELQEIVQLVG 478
Cdd:TIGR01042 402 DPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFY-PEFVPLRTKAKEILQEEEDLNEIVQLVG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 479 SDALPDEEQITIEVARMIREIFLQQNAYDAVDTFCPMSKQYDMMKAIKHYADLARTAQAGGATPQQ-----IVGARSKNE 553
Cdd:TIGR01042 481 KDALAETDKITLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQDDNkitwsIIKESLGDL 560
|
570 580 590
....*....|....*....|....*....|.
gi 1055291904 554 LPQIKFIKDYEPV--LEKILKDMDAEFEAMR 582
Cdd:TIGR01042 561 LYRLSSMKFEDPSdgEAKIKADYEKLNEDMQ 591
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
76-437 |
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: 602.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 76 PLAVELGPGLLTSIYDGIQRPLEVLMDKMGSFIKRGVsapglshekkwefvptvkagdvvgpgdilgtvqetnivhkimv 155
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGSIFIPRGV------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 156 ppnlkggkikkisggsftideticvledgteitMLQRWPVRVPRPVKEKLNPDVPLITGQRILDGLFPIAKGGTAAIPGP 235
Cdd:cd01134 38 ---------------------------------NVQRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGP 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 236 FGSGKTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPELEDPKTGRPLMERTVLIANTSNMPVAAREASVYTGITI 315
Cdd:cd01134 85 FGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 316 AEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAISLN--GASGSVSVIGAVSPP 393
Cdd:cd01134 165 AEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGspGREGSVTIVGAVSPP 244
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1055291904 394 GGDFSEPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLY 437
Cdd:cd01134 245 GGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
241-579 |
1.02e-160 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 485.68 E-value: 1.02e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 241 TVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPELEDPKTGRPLMERTVLIANTSNMPVAAREASVYTGITIAEYFR 320
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 321 DMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAISLNG--ASGSVSVIGAVSPPGGDFS 398
Cdd:PRK14698 750 DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSdyRVGSVSVIGAVSPPGGDFS 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 399 EPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLDSLGEWYDKEVSPEWNTLRSWAMGVLQKEAELQEIVQLVG 478
Cdd:PRK14698 830 EPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDPEWKAMRDKAMELLQKEAELQEIVRIVG 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 479 SDALPDEEQITIEVARMIREIFLQQNAYDAVDTFCPMSKQYDMMKAIKHYADLARTAQAGGATPQQIVGARSKNELPQIK 558
Cdd:PRK14698 910 PDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPLEEIAKLPVREEIGRMK 989
|
330 340
....*....|....*....|.
gi 1055291904 559 FikdyEPVLEKILKDMDAEFE 579
Cdd:PRK14698 990 F----EPDIEKIKALIDKTNE 1006
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
214-435 |
7.98e-110 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 327.39 E-value: 7.98e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 214 GQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPELEdpktgrpLMERTVL 293
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSG-------ALKRTVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 294 IANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGR 373
Cdd:pfam00006 74 VVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055291904 374 aisLNGASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYS 435
Cdd:pfam00006 154 ---VKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
181-437 |
5.15e-107 |
|
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: 322.48 E-value: 5.15e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 181 LEDGTEITMLQRWPVRVPRPVK-EKLNPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWS---DAEIV 256
Cdd:cd19476 20 LDGLPPIKTKQRRPIHLKAPNPiERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQakaHAGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 257 VYIGCGERGNEMTEVLTEFPELEDpktgrplMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRW 336
Cdd:cd19476 100 VFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 337 AEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRaisLNGASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALD 416
Cdd:cd19476 173 AEALREMSALLGEPPGREGYPPYLFTKLATLYERAGK---VKDGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLS 249
|
250 260
....*....|....*....|.
gi 1055291904 417 AKLSQRRHFPAINWLNSYSLY 437
Cdd:cd19476 250 RELARKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
10-283 |
1.89e-88 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 294.62 E-value: 1.89e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 10 QGVLKRISGPVVTAVGLD-AHMYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGLLTS 88
Cdd:PRK14698 4 KGRIIRVTGPLVIADGMKgAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 89 IYDGIQRPLEVLMDKMGSFIKRGVSAPGLSHEKKWEFVPTVKAGDVVGPGDILGTVQETN-IVHKIMVPPNLKGGKIKKI 167
Cdd:PRK14698 84 IYDGIQRPLEVIREKSGDFIARGISAPALPRDKKWHFIPKVKVGDKVVGGDIIGEVPETSiITHKIMVPPGIEGEIVEIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 168 SGGSFTIDETICVLEDGT----EITMLQRWPVRVPRPVKEKLNPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVT 243
Cdd:PRK14698 164 DEGEYTIEEVIAKVKTPSgeikELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVD 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1055291904 244 QQQLAKWSDAEIV----VYIGCGERGNEMTEVLTEFPELEDPKT 283
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 ... |
90-205 |
6.34e-68 |
|
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: 215.72 E-value: 6.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 90 YDGIQRPLEVLMDKMGSFIKRGVSAPGLSHEKKWEFVPTVKAGDVVGPGDILGTVQETN-IVHKIMVPPNLKgGKIKKIS 168
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGSFIPRGVDVPALDREKKWEFTPTVKVGDKVSGGDILGTVQETSlIEHKIMVPPGVS-GTVTEIA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1055291904 169 G-GSFTIDETICVLEDG---TEITMLQRWPVRVPRPVKEKL 205
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 ... |
453-554 |
1.03e-50 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 169.88 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 453 WNTLRSWAMGVLQKEAELQEIVQLVGSDALPDEEQITIEVARMIREIFLQQNAYDAVDTFCPMSKQYDMMKAIKHYADLA 532
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|..
gi 1055291904 533 RTAQAGGATPQQIVGARSKNEL 554
Cdd:cd18111 81 LEALEKGVPLSKILELPVREKI 102
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
8-510 |
1.44e-50 |
|
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: 180.23 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 8 RTQGVLKRISGPVVTAVGLDAHMYDVVKV---GNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPG 84
Cdd:COG1157 18 RVSGRVTRVVGLLIEAVGPDASIGELCEIetaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 85 LLTSIYDGIQRPLevlmDKMGSfIKRGVSAPglshekkwefvptvkagdVVGPgdilgtvqetnivhkimvPPNlkggki 164
Cdd:COG1157 98 LLGRVLDGLGRPL----DGKGP-LPGEERRP------------------LDAP------------------PPN------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 165 kkisggsftideticvledgteitMLQRwpvrvpRPVKEklnpdvPLITGQRILDGLFPIAKG---GTAAipGPfGSGKT 241
Cdd:COG1157 131 ------------------------PLER------ARITE------PLDTGVRAIDGLLTVGRGqriGIFA--GS-GVGKS 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 242 VTQQQLAKWSDAEIVVyIG-CGERGNEmtevLTEFpeLEDPKtGRPLMERTVLIANTSNMPVAAREASVYTGITIAEYFR 320
Cdd:COG1157 172 TLLGMIARNTEADVNV-IAlIGERGRE----VREF--IEDDL-GEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFR 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 321 DMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGraislNGASGSVSVIGAVSPPGGDFSEP 400
Cdd:COG1157 244 DQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAG-----NGGKGSITAFYTVLVEGDDMNDP 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 401 VTqNTLR------IVkvfwaLDAKLSQRRHFPAINWLNSYSLYLDSLgewydkeVSPEWNTLRSWAMGVLQKEAELQEIV 474
Cdd:COG1157 319 IA-DAVRgildghIV-----LSRKLAERGHYPAIDVLASISRVMPDI-------VSPEHRALARRLRRLLARYEENEDLI 385
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1055291904 475 QL----VGSDALPDEeqiTIEVARMIREiFLQQNAYDAVD 510
Cdd:COG1157 386 RIgayqPGSDPELDE---AIALIPAIEA-FLRQGMDERVS 421
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
11-510 |
7.04e-48 |
|
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: 172.94 E-value: 7.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 11 GVLKRISGPVVTAVGLDAHMYDVVKV----GNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGLL 86
Cdd:TIGR01026 25 GRVTKVKGLLIEAVGPQASVGDLCLIerrgSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSIKVGDGLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 87 TSIYDGIQRPLEvlmdkmgsfikrgvsapglshekkwefvptvkagdvvGPGDILGTVQETNIvhkIMVPPN-LKGGKIK 165
Cdd:TIGR01026 105 GRVLDGLGKPID-------------------------------------GKGKFLDNVETEGL---ITAPINpLKRAPIR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 166 KIsggsftideticvledgteitmlqrwpvrvprpvkeklnpdvpLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQ 245
Cdd:TIGR01026 145 EI-------------------------------------------LSTGVRSIDGLLTVGKGQRIGIFAGSGVGKSTLLG 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 246 QLAKWSDAEIVVYIGCGERGNEmtevLTEFPELEDPKTGrplMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYD 325
Cdd:TIGR01026 182 MIARNTEADVNVIALIGERGRE----VREFIEHDLGEEG---LKRSVVVVATSDQSPLLRLKGAYVATAIAEYFRDQGKD 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 326 VSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAislngASGSVSVIGAVSPPGGDFSEPVTQNT 405
Cdd:TIGR01026 255 VLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGAS-----GKGSITAFYTVLVEGDDMNEPIADSV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 406 LRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLDSLgewydkeVSPEWNTLRSWAMGVLQKEAELQEIVQ----LVGSDA 481
Cdd:TIGR01026 330 RGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAI-------VSEEHRRAARKFRELLSKYKDNEDLIRigayQRGSDR 402
|
490 500 510
....*....|....*....|....*....|
gi 1055291904 482 LPDEeqiTIE-VARMIReiFLQQNAYDAVD 510
Cdd:TIGR01026 403 ELDF---AIAkYPKLER--FLKQGINEKVN 427
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
11-510 |
5.65e-42 |
|
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: 156.10 E-value: 5.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 11 GVLKRISGPVVTAVGLDAHMYDVVKV---GNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGLLT 87
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPVGSRCEIessDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 88 SIYDGIQRPLevlmDKMGSfIKRGVSAPglshekkwefvptvkagdvvgpgdilgtvqetnivhkIMVPPnlkggkikki 167
Cdd:TIGR03496 81 RVIDGLGRPL----DGKGP-LDAGERVP-------------------------------------LYAPP---------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 168 sggsftideticvledgteITMLQRwpvrvpRPVKEklnpdvPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQL 247
Cdd:TIGR03496 109 -------------------INPLKR------APIDE------PLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTLLGMM 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 248 AKWSDAEIVVyIG-CGERGNEmtevLTEFPELEDPKTGrplMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDV 326
Cdd:TIGR03496 158 ARYTEADVVV-VGlIGERGRE----VKEFIEDILGEEG---LARSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDV 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 327 SLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGraislNGA--SGSVSVIGAVSPPGGDFSEPVTqN 404
Cdd:TIGR03496 230 LLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAG-----NGEegKGSITAFYTVLVEGDDQQDPIA-D 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 405 TLR------IVkvfwaLDAKLSQRRHFPAINWLNSYSLYLDSLgewydkeVSPEWntlRSWAMGVLQKEAELQEIVQLV- 477
Cdd:TIGR03496 304 AARaildghIV-----LSRELAEQGHYPAIDILASISRVMPDV-------VSPEH---RQAARRFKQLLSRYQENRDLIs 368
|
490 500 510
....*....|....*....|....*....|....*....
gi 1055291904 478 ------GSDALPDEeqiTIEVARMIREiFLQQNAYDAVD 510
Cdd:TIGR03496 369 igayqaGSDPELDQ---AIALYPRIEA-FLQQGMRERAS 403
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
191-435 |
7.69e-42 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 151.56 E-value: 7.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 191 QRWPVRVPRPvkeklNP------DVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVYIGCGER 264
Cdd:cd01136 30 ERRPLIAAPP-----NPlkrapiEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGER 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 265 GNEmtevLTEFPELEDPKTGrplMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREIS 344
Cdd:cd01136 105 GRE----VREFIEKDLGEEG---LKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 345 SRLEEMPGEEGYPAYLSARLSEFYERAGraislNGASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRH 424
Cdd:cd01136 178 LAAGEPPTRRGYPPSVFALLPRLLERAG-----NGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGH 252
|
250
....*....|.
gi 1055291904 425 FPAINWLNSYS 435
Cdd:cd01136 253 YPAIDVLASIS 263
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
11-435 |
2.48e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 146.41 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 11 GVLKRISGPVVTAVGLDAHMYDVVKV-----GNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGL 85
Cdd:PRK07721 20 GKVSRVIGLMIESKGPESSIGDVCYIhtkggGDKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 86 LTSIYDGIQRPLEvlmdkmGSFIKRGVSapglshekkweFVPTVKAgdvvgpgdilgtvqetnivhkimvPPNlkggkik 165
Cdd:PRK07721 100 IGQVLDALGEPLD------GSALPKGLA-----------PVSTDQD------------------------PPN------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 166 kisggsftideticvledgteitmlqrwPVRVPrPVKEKLNpdvpliTGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQ 245
Cdd:PRK07721 132 ----------------------------PLKRP-PIREPME------VGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMG 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 246 QLAKWSDAEIVVYIGCGERGNEmtevLTEFPELEDPKTGrplMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYD 325
Cdd:PRK07721 177 MIARNTSADLNVIALIGERGRE----VREFIERDLGPEG---LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLN 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 326 VSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGraislNGASGSVSVIGAVSPPGGDFSEPVTQNT 405
Cdd:PRK07721 250 VMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG-----TNASGSITAFYTVLVDGDDMNEPIADTV 324
|
410 420 430
....*....|....*....|....*....|
gi 1055291904 406 LRIVKVFWALDAKLSQRRHFPAINWLNSYS 435
Cdd:PRK07721 325 RGILDGHFVLDRQLANKGQYPAINVLKSVS 354
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
18-525 |
8.65e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 144.96 E-value: 8.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 18 GPVVTAVGL-DAHMYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGLLTSIYDGIQRP 96
Cdd:PRK06820 37 GPTLLRASLpGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 97 LEvlmdkmgsfikrgvsapglshekkwefvptvkagdvvgpGDilgtvqetnivhkimvPPnlkggkikkisggsftide 176
Cdd:PRK06820 117 ID---------------------------------------GG----------------PP------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 177 ticvleDGTEITMLQRWPvrvPRPVKEKLnPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIV 256
Cdd:PRK06820 123 ------LTGQWRELDCPP---PSPLTRQP-IEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAADVM 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 257 VYIGCGERGNEMTE----VLTefPELEdpktgrplmERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADS 332
Cdd:PRK06820 193 VLALIGERGREVREfleqVLT--PEAR---------ARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADS 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 333 TSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGraislNGASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVF 412
Cdd:PRK06820 262 LTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG-----NSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGH 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 413 WALDAKLSQRRHFPAINWLNSYSLYLDSLgewydkeVSPEWntlRSWAMGVLQKEAELQEIVQLV-------GSDALPDE 485
Cdd:PRK06820 337 IVLSRRLAGAGHYPAIDIAASVSRIMPQI-------VSAGQ---LAMAQKLRRMLACYQEIELLVrvgeyqaGEDLQADE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1055291904 486 eqiTIEVARMIREiFLQQNaydaVDTFCPMSKQYDMMKAI 525
Cdd:PRK06820 407 ---ALQRYPAICA-FLQQD----HSETAHLETTLEHLAQV 438
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
183-503 |
8.76e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 136.42 E-value: 8.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 183 DGTEITMLQRW-PV--RVPRPVKEKLnPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVYI 259
Cdd:PRK06936 116 DGGHPPEPAAWyPVyaDAPAPMSRRL-IETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 260 GCGERGNEmtevLTEFPELEDPKTGrplMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEA 339
Cdd:PRK06936 195 LIGERGRE----VREFIESDLGEEG---LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 340 MREISSRLEEMPGEEGYPAYLSARLSEFYERAGraislNGASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKL 419
Cdd:PRK06936 268 QREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-----QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 420 SQRRHFPAINWLNSYSLYLDSLgewYDKEVSPEWNTLRSWamgvLQKEAELQEIVQL----VGSDALPDEeqiTIEVARM 495
Cdd:PRK06936 343 AAANHYPAIDVLRSASRVMNQI---VSKEHKTWAGRLREL----LAKYEEVELLLQIgeyqKGQDKEADQ---AIERIGA 412
|
....*...
gi 1055291904 496 IREiFLQQ 503
Cdd:PRK06936 413 IRG-FLRQ 419
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
192-504 |
1.50e-34 |
|
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: 136.39 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 192 RWPVRVPRPVKEKLNPDVPLI-TGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQL----AKwSDAEIVVYIGCGERGN 266
Cdd:TIGR01039 107 RWPIHRKAPSFEEQSTKVEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELinniAK-EHGGYSVFAGVGERTR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 267 EMTEVLTEFPEledpkTGrpLMERTVLIANTSNMPVAAREASVYTGITIAEYFRDM-GYDVSLMADSTSRWAEAMREISS 345
Cdd:TIGR01039 186 EGNDLYHEMKE-----SG--VIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDNIFRFTQAGSEVSA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 346 RLEEMPGEEGYPAYLSARLSEFYERagraISlNGASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRHF 425
Cdd:TIGR01039 259 LLGRMPSAVGYQPTLATEMGELQER----IT-STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIY 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 426 PAINWLNSYSLYLDSL---GEWYDKevspewntlrswAMGV---LQKEAELQEIVQLVGSDALPDEEQITIEVARMIREi 499
Cdd:TIGR01039 334 PAVDPLDSTSRLLDPSvvgEEHYDV------------ARGVqqiLQRYKELQDIIAILGMDELSEEDKLTVERARRIQR- 400
|
....*
gi 1055291904 500 FLQQN 504
Cdd:TIGR01039 401 FLSQP 405
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
15-435 |
6.65e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 128.19 E-value: 6.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 15 RISGPVvtavgLDAHMYDVvKVG----------NEELMGE--VIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELG 82
Cdd:PRK08149 12 RIQGPI-----IEAELPDV-AIGeiceiragwhSNEVIARaqVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 83 PGLLTSIYDgiqrplevlmdkmgsfikrgvsapglshekkwefvPTvkagdvvgpGDILGTVQETnivhkimVPPNlkgg 162
Cdd:PRK08149 86 EALLGAVLD-----------------------------------PT---------GKIVERFDAP-------PTVG---- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 163 kikkisggsfTIDETICVleDGTEITMLQRWPVRVPrpvkeklnpdvpLITGQRILDGLFPIAKGGTAAIPGPFGSGKTV 242
Cdd:PRK08149 111 ----------PISEERVI--DVAPPSYAERRPIREP------------LITGVRAIDGLLTCGVGQRMGIFASAGCGKTS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 243 TQQQLAKWSDAEIVVyIG-CGERGNEmtevLTEFPElEDPKTGRplMERTVLIANTSNMPVAAREASVYTGITIAEYFRD 321
Cdd:PRK08149 167 LMNMLIEHSEADVFV-IGlIGERGRE----VTEFVE-SLRASSR--REKCVLVYATSDFSSVDRCNAALVATTVAEYFRD 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 322 MGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAIslngaSGSVSVIGAVSPPGGDFSEPV 401
Cdd:PRK08149 239 QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATL-----AGSITAFYTVLLESEEEPDPI 313
|
410 420 430
....*....|....*....|....*....|....
gi 1055291904 402 TQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYS 435
Cdd:PRK08149 314 GDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVS 347
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
8-510 |
2.15e-29 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 121.03 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 8 RTQGVLKRISGPVVTAVGLDAHMYDV--VKVGNEELM--GEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGP 83
Cdd:PRK09099 23 RRTGKVVEVIGTLLRVSGLDVTLGELceLRQRDGTLLqrAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 84 GLLTSIYDGIQRPLEvlmdkmgsfikrgvsapglshekkwefvptvkagdvvgpgdilgtvqetnivhkimvppnlkggk 163
Cdd:PRK09099 103 ALLGRVIDGLGEPID----------------------------------------------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 164 ikkiSGGSFTIDETICVLEDGteitmlqrwpvrvPRPVKEKLnPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVT 243
Cdd:PRK09099 118 ----GGGPLDCDELVPVIAAP-------------PDPMSRRM-VEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 244 QQQLAKWSDAEIVVYIGCGERGNEmtevLTEFPELedpKTGRPLMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMG 323
Cdd:PRK09099 180 MGMFARGTQCDVNVIALIGERGRE----VREFIEL---ILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 324 YDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRaislnGASGSVSVIGAVSPPGGDFSEPVTQ 403
Cdd:PRK09099 253 LRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM-----GETGSITALYTVLAEDESGSDPIAE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 404 NTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLDSLgewYDKEVSPEWNTLRSwamgVLQKEAELQEIVQL----VGS 479
Cdd:PRK09099 328 EVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQV---VPREHVQAAGRLRQ----LLAKHREVETLLQVgeyrAGS 400
|
490 500 510
....*....|....*....|....*....|.
gi 1055291904 480 DALPDEeqiTIEVARMIREiFLQQNAYDAVD 510
Cdd:PRK09099 401 DPVADE---AIAKIDAIRD-FLSQRTDEYSD 427
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
8-435 |
3.97e-28 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 117.36 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 8 RTQGVLKRISGPVVTAVGLDAHMYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLPLAVELGPGLLT 87
Cdd:PRK07594 20 CRWGRIQDVSATLLNAWLPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 88 SIYDGIQRPLEVLMDKMGSFikRGVSAPglshekkwefvptvkagdvvgpgdilgtvqetnivhkimvPPnlkggkikki 167
Cdd:PRK07594 100 RVIDGFGRPLDGRELPDVCW--KDYDAM----------------------------------------PP---------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 168 sggsftideticvledgteitmlqrwPVRVPRPVKEklnpdvPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQL 247
Cdd:PRK07594 128 --------------------------PAMVRQPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAML 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 248 AKWSDAEIVVYIGCGERGNEMTEVLtEFPELEDPKtgrplmERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVS 327
Cdd:PRK07594 176 CNAPDADSNVLVLIGERGREVREFI-DFTLSEETR------KRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVV 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 328 LMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRaislnGASGSVSVIGAVSPPGGDFSEPVTQNTLR 407
Cdd:PRK07594 249 LLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM-----GEKGSITAFYTVLVEGDDMNEPLADEVRS 323
|
410 420
....*....|....*....|....*...
gi 1055291904 408 IVKVFWALDAKLSQRRHFPAINWLNSYS 435
Cdd:PRK07594 324 LLDGHIVLSRRLAERGHYPAIDVLATLS 351
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
210-525 |
1.06e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 115.85 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 210 PLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVyIG-CGERGNEMTEVLTEfpeledpKTGRPLM 288
Cdd:PRK08927 141 PLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSV-IGlIGERGREVQEFLQD-------DLGPEGL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 289 ERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFY 368
Cdd:PRK08927 213 ARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 369 ERAGRAISlngASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLdslgewyDKE 448
Cdd:PRK08927 293 ERAGPGPI---GEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-------PGC 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 449 VSPEWNTLRSWAMGVLQKEAELQEIVQL----VGSDAlpdeeqitiEVARMIR-----EIFLQQNAYDAvdtfCPMSKQY 519
Cdd:PRK08927 363 NDPEENPLVRRARQLMATYADMEELIRLgayrAGSDP---------EVDEAIRlnpalEAFLRQGKDEA----TSLAEGY 429
|
....*.
gi 1055291904 520 DMMKAI 525
Cdd:PRK08927 430 ARLAQI 435
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
10-504 |
1.16e-27 |
|
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: 116.34 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 10 QGVLKRISGPVVTAVGLDAHM---YDVVKVGNE---ELMGEVIKIQGENVIIQV-YEDTDGIRPGEPVVNTGLPLAVELG 82
Cdd:COG0055 5 TGKIVQVIGPVVDVEFPEGELpaiYNALEVENEgggELVLEVAQHLGDNTVRCIaMDSTDGLVRGMEVIDTGAPISVPVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 83 PGLLTSIYDgiqrplevlmdkmgsfikrgvsapglshekkwefvptvkagdVVG-PGDILGTVQETnivhkimvppnlkg 161
Cdd:COG0055 85 EATLGRIFN------------------------------------------VLGePIDGKGPIEAK-------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 162 gkikkisggsftideticvledgteitmlQRWPVRVPRPVKEKLNPDV-PLITGQRILDGLFPIAKGGTAAIPGPFGSGK 240
Cdd:COG0055 109 -----------------------------ERRPIHRPAPPFEEQSTKTeILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 241 TVTQQQL----AKWSDAeIVVYIGCGERGNEMTEVLTEFPEledpkTGrpLMERTVLIANTSNMPVAAREASVYTGITIA 316
Cdd:COG0055 160 TVLIMELihniAKEHGG-VSVFAGVGERTREGNDLYREMKE-----SG--VLDKTALVFGQMNEPPGARLRVALTALTMA 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 317 EYFRD-MGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERagraISlNGASGSVSVIGAVSPPGG 395
Cdd:COG0055 232 EYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQER----IT-STKKGSITSVQAVYVPAD 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 396 DFSEPVTQNTlrivkvFWALDAK--LSQRRH----FPAINWLNSYSLYLDSL--G-EWYDKevspewntlrswAMGV--- 463
Cdd:COG0055 307 DLTDPAPATT------FAHLDATtvLSRKIAelgiYPAVDPLDSTSRILDPLivGeEHYRV------------AREVqri 368
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1055291904 464 LQKEAELQEIVQLVGSDALPDEEQITIEVARMIrEIFLQQN 504
Cdd:COG0055 369 LQRYKELQDIIAILGMDELSEEDKLTVARARKI-QRFLSQP 408
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
11-429 |
1.83e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 115.18 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 11 GVLKRISGPVVTAVGLDAHMYDVVKVG--NEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVV----NTGLPLavelGPG 84
Cdd:PRK08972 27 GKLVRVVGLTLEATGCRAPVGSLCSIEtmAGELEAEVVGFDGDLLYLMPIEELRGVLPGARVTplgeQSGLPV----GMS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 85 LLTSIYDGIQRPLevlmdkmgsfikrgvsapglshekkwefvptvkagdvvgpgDILGTVQETNIVHKimvppnlkggki 164
Cdd:PRK08972 103 LLGRVIDGVGNPL-----------------------------------------DGLGPIYTDQRASR------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 165 kkisggsftideticvleDGTEITMLQRwpvrvpRPVKEklnpdvPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQ 244
Cdd:PRK08972 130 ------------------HSPPINPLSR------RPITE------PLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 245 QQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPELEdpktGRplmERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGY 324
Cdd:PRK08972 180 GMMTRGTTADVIVVGLVGERGREVKEFIEEILGEE----GR---ARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGL 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 325 DVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGraislNGAS--GSVSVIGAVSPPGGDFSEPVT 402
Cdd:PRK08972 253 NVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG-----NGGPgqGSITAFYTVLTEGDDLQDPIA 327
|
410 420
....*....|....*....|....*..
gi 1055291904 403 QNTLRIVKVFWALDAKLSQRRHFPAIN 429
Cdd:PRK08972 328 DASRAILDGHIVLSRELADSGHYPAID 354
|
|
| 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 ... |
10-74 |
1.08e-26 |
|
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: 102.99 E-value: 1.08e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1055291904 10 QGVLKRISGPVVTAVGL-DAHMYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTG 74
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMsGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTG 66
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
13-507 |
3.70e-26 |
|
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: 111.78 E-value: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 13 LKRISGPV-----VTAVGLDaHMYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVN-TGLPLAVELGPGLL 86
Cdd:COG1156 9 ISEIAGPLlfvegVEGVGYG-ELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSEDML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 87 TSIYDGIQRPL--------EVLMDKMGSFIKrgvsaPgLSHEKKWEFVPTvkagdvvgpgdilgtvqetnivhkimvppn 158
Cdd:COG1156 88 GRVFNGLGRPIdggppiipEKRLDINGSPIN-----P-VAREYPREFIQT------------------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 159 lkgGkikkISggsfTIDeticvledgteitmlqrwpvrvprpvkeKLNPdvpLITGQRIldglfPIakggtaaipgpF-G 237
Cdd:COG1156 132 ---G----IS----AID----------------------------GLNT---LVRGQKL-----PI-----------FsG 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 238 SG--------KTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPEledpkTGRplMERTVLIANTSNMPVAAREASV 309
Cdd:COG1156 154 SGlphnelaaQIARQAKVRGEEEKFAVVFAAMGITHDEANFFREEFEE-----TGA--LDRVVMFLNLADDPAIERIITP 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 310 YTGITIAEYFR-DMGYDV-SLMADSTSrWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRaisLNGASGSVSVI 387
Cdd:COG1156 227 RMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGR---IKGRKGSITQI 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 388 GAVSPPGGDFSEPV-------TQNtlRIVkvfwaLDAKLSQRRHFPAINWLNSYS-LYLDSLGEWYDKEVSPEW-NTL-R 457
Cdd:COG1156 303 PILTMPNDDITHPIpdltgyiTEG--QIV-----LSRDLHRKGIYPPIDVLPSLSrLMKDGIGEGKTREDHADVaNQLyA 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1055291904 458 SWAMGVlqkeaELQEIVQLVGSDALPDEEQITIEVARMIREIFLQQNAYD 507
Cdd:COG1156 376 AYARGQ-----EVRELAAIVGEEALSETDKKYLKFADAFERRFVNQGFDE 420
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
13-503 |
3.99e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 108.76 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 13 LKRISGPVVTAVGLDAHMYD-VVKV---GNEELMGEVIKIQGENVIIQVYEDTDGIRPGE-PVVNTGLPLAVELGPGLLT 87
Cdd:PRK04196 7 VSEIKGPLLFVEGVEGVAYGeIVEIelpNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDtKVRFTGEPLKLPVSEDMLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 88 SIYDGIQRPLevlmDKMGSFIKrgvsapglshEKKWefvptvkagdvvgpgDILGTvqetnivhkimvPPNlkggkikki 167
Cdd:PRK04196 87 RIFDGLGRPI----DGGPEIIP----------EKRL---------------DINGA------------PIN--------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 168 sggsftideticvledgteitmlqrwpvrvprPVKeKLNPDVPLITGQRILDGLFPIAKGGTAAIpgpF-GSG------- 239
Cdd:PRK04196 117 --------------------------------PVA-REYPEEFIQTGISAIDGLNTLVRGQKLPI---FsGSGlphnela 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 240 -KTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPEledpkTGrpLMERTVLIANTSNMPVAAREASVYTGITIAEY 318
Cdd:PRK04196 161 aQIARQAKVLGEEENFAVVFAAMGITFEEANFFMEDFEE-----TG--ALERSVVFLNLADDPAIERILTPRMALTAAEY 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 319 FR-DMGYDV-SLMADSTSrWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRaisLNGASGSVSVIGAVSPPGGD 396
Cdd:PRK04196 234 LAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGR---IKGKKGSITQIPILTMPDDD 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 397 FSEPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYS-LYLDSLGEWYDKEVSPEW-NTL-RSWAMGVlqkeaELQEI 473
Cdd:PRK04196 310 ITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSrLMKDGIGEGKTREDHKDVaNQLyAAYARGK-----DLREL 384
|
490 500 510
....*....|....*....|....*....|
gi 1055291904 474 VQLVGSDALPDEEQITIEVARMIREIFLQQ 503
Cdd:PRK04196 385 AAIVGEEALSERDRKYLKFADAFEREFVNQ 414
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
191-439 |
1.10e-24 |
|
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: 103.84 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 191 QRWPVRVPRPVKEKLNPDV-PLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQL----AKWSDAeIVVYIGCGERG 265
Cdd:cd01133 30 ERWPIHREAPEFVELSTEQeILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinniAKAHGG-YSVFAGVGERT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 266 NEMTEVLTEFPELEDPKTGRplMERTVLIANTSNMPVAAREASVYTGITIAEYFRDM-GYDVSLMADSTSRWAEAMREIS 344
Cdd:cd01133 109 REGNDLYHEMKESGVINLDG--LSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEVS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 345 SRLEEMPGEEGYPAYLSARLSEFYERagraISlNGASGSVSVIGAVSPPGGDFSEPVTQNTlrivkvFWALDAKLSQRRH 424
Cdd:cd01133 187 ALLGRIPSAVGYQPTLATEMGSLQER----IT-STKKGSITSVQAVYVPADDLTDPAPATT------FAHLDATTVLSRG 255
|
250 260
....*....|....*....|.
gi 1055291904 425 ------FPAINWLNSYSLYLD 439
Cdd:cd01133 256 iaelgiYPAVDPLDSTSRILD 276
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
10-429 |
1.23e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 107.12 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 10 QGVLKRISGPVVTAVGLDAHMYDVVKVGNE------ELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVntglPLA----V 79
Cdd:PRK05688 28 EGRLLRMVGLTLEAEGLRAAVGSRCLVINDdsyhpvQVEAEVMGFSGDKVFLMPVGSVAGIAPGARVV----PLAdtgrL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 80 ELGPGLLTSIYDGIQRPLEvlmdkmgsfikrgvsapGLSHEKKWEFVPTvkagdvvgpgdilgtvqetnivhkimvppnl 159
Cdd:PRK05688 104 PMGMSMLGRVLDGAGRALD-----------------GKGPMKAEDWVPM------------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 160 kggkikkisggsftideticvleDGTEITMLQRWPVRVPRPVkeklnpdvplitGQRILDGLFPIAKGGTAAIPGPFGSG 239
Cdd:PRK05688 136 -----------------------DGPTINPLNRHPISEPLDV------------GIRSINGLLTVGRGQRLGLFAGTGVG 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 240 KTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFpeledpkTGRPLMERTVLIANTSN-MPVAAREASVYTgITIAEY 318
Cdd:PRK05688 181 KSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHI-------LGEEGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEY 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 319 FRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAislNGASGSVSVIGAVSPPGGDFS 398
Cdd:PRK05688 253 FRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNA---EPGGGSITAFYTVLSEGDDQQ 329
|
410 420 430
....*....|....*....|....*....|.
gi 1055291904 399 EPVTQNTLRIVKVFWALDAKLSQRRHFPAIN 429
Cdd:PRK05688 330 DPIADSARGVLDGHIVLSRRLAEEGHYPAID 360
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
213-435 |
4.72e-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: 102.30 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 213 TGQRILDGLFPIAKGgtAAIPGPFGSG--------KTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPEledpkTG 284
Cdd:cd01135 55 TGISAIDVMNTLVRG--QKLPIFSGSGlphnelaaQIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEE-----TG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 285 rpLMERTVLIANTSNMPVAAREASVYTGITIAEYFR-DMGYDV-SLMADSTSrWAEAMREISSRLEEMPGEEGYPAYLSA 362
Cdd:cd01135 128 --ALERVVLFLNLANDPTIERIITPRMALTTAEYLAyEKGKHVlVILTDMTN-YAEALREVSAAREEVPGRRGYPGYMYT 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1055291904 363 RLSEFYERAGRaisLNGASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYS 435
Cdd:cd01135 205 DLATIYERAGR---VEGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLS 274
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
11-435 |
6.20e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 104.77 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 11 GVLKRISGPVVTAVGLDAHMYDVVKV----GNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVV--NTGLPLAVelGPG 84
Cdd:PRK08472 20 GSITKISPTIIEADGLNPSVGDIVKIessdNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFisKEGLNIPV--GRN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 85 LLTSIYDGIQRPLEvlmdkmgsfikrgvsapglshekkwefvptvkagdvvGPGDILGTvqETNIVHKIMVPPnLKGGki 164
Cdd:PRK08472 98 LLGRVVDPLGRPID-------------------------------------GKGAIDYE--RYAPIMKAPIAA-MKRG-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 165 kkisggsfTIDETICVledgteitmlqrwpvrvprpvkeklnpdvplitGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQ 244
Cdd:PRK08472 136 --------LIDEVFSV---------------------------------GVKSIDGLLTCGKGQKLGIFAGSGVGKSTLM 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 245 QQLAKWSDAEIVVYIGCGERGNEMtevltefPELEDPKTGRPLmERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGY 324
Cdd:PRK08472 175 GMIVKGCLAPIKVVALIGERGREI-------PEFIEKNLGGDL-ENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 325 DVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRaislNGASGSVSVIGAVSPPGGDFSEPVTQN 404
Cdd:PRK08472 247 DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK----EEGKGSITAFFTVLVEGDDMSDPIADQ 322
|
410 420 430
....*....|....*....|....*....|.
gi 1055291904 405 TLRIVKVFWALDAKLSQRRHFPAINWLNSYS 435
Cdd:PRK08472 323 SRSILDGHIVLSRELTDFGIYPPINILNSAS 353
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-503 |
2.54e-23 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 103.58 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 2 KKNTEKRTQgvlkrISGPVVTAVGLDAHM---YDVVKVGNEELMGEVIKIQ-------GENVIIQV-YEDTDGIRPGEPV 70
Cdd:CHL00060 13 EKNLGRITQ-----IIGPVLDVAFPPGKMpniYNALVVKGRDTAGQEINVTcevqqllGNNRVRAVaMSATDGLMRGMEV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 71 VNTGLPLAVELGPGLLTSIYDgiqrplevlmdkmgsfikrgvsapglshekkwefvptvkagdVVG-PGDILGTVQ--ET 147
Cdd:CHL00060 88 IDTGAPLSVPVGGATLGRIFN------------------------------------------VLGePVDNLGPVDtrTT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 148 NIVHKimvppnlkggkikkiSGGSFTI-DETICVLEdgteitmlqrwpvrvprpvkeklnpdvpliTGQRILDGLFPIAK 226
Cdd:CHL00060 126 SPIHR---------------SAPAFIQlDTKLSIFE------------------------------TGIKVVDLLAPYRR 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 227 GGTAAIPGPFGSGKTVTQQQL----AKwSDAEIVVYIGCGERGNEMTEVLTEFPELEDPKTGRPLMERTVLIANTSNMPV 302
Cdd:CHL00060 161 GGKIGLFGGAGVGKTVLIMELinniAK-AHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPP 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 303 AAREASVYTGITIAEYFRDMGY-DVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERagraISlNGAS 381
Cdd:CHL00060 240 GARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER----IT-STKE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 382 GSVSVIGAVSPPGGDFSEPVTQNTlrivkvFWALDAK------LSQRRHFPAINWLNSYSLYLDslgEWYdkeVSPEWNT 455
Cdd:CHL00060 315 GSITSIQAVYVPADDLTDPAPATT------FAHLDATtvlsrgLAAKGIYPAVDPLDSTSTMLQ---PRI---VGEEHYE 382
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1055291904 456 LRSWAMGVLQKEAELQEIVQLVGSDALPDEEQITIEVARMIrEIFLQQ 503
Cdd:CHL00060 383 TAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 429
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
1-441 |
4.22e-23 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 102.55 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 1 MKKNTEKRTQGVLKRISGPVVTAVGLdaHM----------YDVVKVgnEELMGEVIKIQGENVIIQVYEDTDGIRPGEPV 70
Cdd:PRK07960 19 MAQLPAVRRYGRLTRATGLVLEATGL--QLplgatcvierQNGSET--HEVESEVVGFNGQRLFLMPLEEVEGILPGARV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 71 VNTGLPLA-------VELGPGLLTSIYDGIQRPLEvlmdkmgsfikrGVSAPglshekkwefvptvkagdvvgpgdilgt 143
Cdd:PRK07960 95 YARNISGEglqsgkqLPLGPALLGRVLDGSGKPLD------------GLPAP---------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 144 vqETNIVHKIMVPPnlkggkikkisggsftideticvledgteITMLQRWPVRvprpvkeklnpDVpLITGQRILDGLFP 223
Cdd:PRK07960 135 --DTGETGALITPP-----------------------------FNPLQRTPIE-----------HV-LDTGVRAINALLT 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 224 IAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVYIGCGERGNEmtevLTEFPELEDPKTGRplmERTVLIANTSNMPVA 303
Cdd:PRK07960 172 VGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGRE----VKDFIENILGAEGR---ARSVVIAAPADVSPL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 304 AREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAGRAISlngASGS 383
Cdd:PRK07960 245 LRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS---GGGS 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1055291904 384 VSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLDSL 441
Cdd:PRK07960 322 ITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAL 379
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
208-435 |
7.60e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 101.61 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 208 DVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLtefpelEDPKTGRpl 287
Cdd:PRK06002 146 ETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFL------EDTLADN-- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 288 MERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEF 367
Cdd:PRK06002 218 LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRL 297
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1055291904 368 YERAGRAISlngASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYS 435
Cdd:PRK06002 298 LERAGPGAE---GGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASIS 362
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
188-435 |
1.35e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 100.74 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 188 TMLQRWPVRVpRPVKEKlNPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVYIGCGERGNE 267
Cdd:PRK07196 118 TPLQQQLPQI-HPLQRR-AVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGRE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 268 MTEVLtefpeleDPKTGRPLMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRL 347
Cdd:PRK07196 196 VKEFI-------EHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 348 EEMPGEEGYPAYLSARLSEFYERAGraislNG-ASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRHFP 426
Cdd:PRK07196 269 GEPPATKGYPPSAFSIIPRLAESAG-----NSsGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYP 343
|
....*....
gi 1055291904 427 AINWLNSYS 435
Cdd:PRK07196 344 AIDISQSIS 352
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
213-390 |
2.47e-21 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 96.90 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 213 TGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEIVVYIGCGERGNEMTEVLtefpelEDPKTGRPlMERTV 292
Cdd:PRK05922 143 TGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYI------EQHKEGLA-AQRTI 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 293 LIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYERAG 372
Cdd:PRK05922 216 IIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG 295
|
170
....*....|....*...
gi 1055291904 373 raislNGASGSVSVIGAV 390
Cdd:PRK05922 296 -----NNDKGSITALYAI 308
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
180-470 |
2.70e-20 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 93.50 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 180 VLEDGTEITMLQRWPVRVPrPV----KEKLNpDVpLITGQRILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAKWSDAEI 255
Cdd:PRK06793 108 VLNEEAENIPLQKIKLDAP-PIhafeREEIT-DV-FETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADI 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 256 VVYIGCGERGNEMTEVLTEfpeledpKTGRPLMERTVLIANTSNMP--VAAREASVYTgiTIAEYFRDMGYDVSLMADST 333
Cdd:PRK06793 185 NVISLVGERGREVKDFIRK-------ELGEEGMRKSVVVVATSDEShlMQLRAAKLAT--SIAEYFRDQGNNVLLMMDSV 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 334 SRWAEAMREISSRLEEMPgEEGYPAYLSARLSEFYERAGRAislngASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFW 413
Cdd:PRK06793 256 TRFADARRSVDIAVKELP-IGGKTLLMESYMKKLLERSGKT-----QKGSITGIYTVLVDGDDLNGPVPDLARGILDGHI 329
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055291904 414 ALDAKLSQRRHFPAINWLNSYSLYLDSLgewydkeVSP-EW---NTLRSWAMgvLQKEAEL 470
Cdd:PRK06793 330 VLKRELATLSHYPAISVLDSVSRIMEEI-------VSPnHWqlaNEMRKILS--IYKENEL 381
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
288-523 |
3.31e-20 |
|
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: 93.63 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 288 MERTVLIANTSNMPVAAREASVYTGITIAEYFR-DMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPAYLSARLSE 366
Cdd:TIGR01040 210 MERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLAT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 367 FYERAGRaisLNGASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRHFPAINWLNSYSLYLDS-LGEWY 445
Cdd:TIGR01040 290 IYERAGR---VEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSaIGEGM 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 446 DKE----VSpewNTLRS-WAMGvlqkeAELQEIVQLVGSDALPDEEQITIEVARMIREIFLQQNAYDAVDTFCPMSKQYD 520
Cdd:TIGR01040 367 TRKdhsdVS---NQLYAcYAIG-----KDVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQ 438
|
...
gi 1055291904 521 MMK 523
Cdd:TIGR01040 439 LLR 441
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
199-429 |
2.52e-17 |
|
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: 82.22 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 199 RPVKEklnpdvPLITGQRILDGLFPIAKGGTAAIPGPFGSGKT------VTQQQLAKWsdaeIVVYIGCGERGNEMTEVL 272
Cdd:cd01132 47 QSVNE------PLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaiaidtIINQKGKKV----YCIYVAIGQKRSTVAQIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 273 TEFPEledpktgRPLMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPG 352
Cdd:cd01132 117 KTLEE-------HGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 353 EEGYPA---YLSARLsefYERAGRAISLNGAsGSVSVIGAVSPPGGDFSEPVTQNTLRIV--KVFwaLDAKLSQRRHFPA 427
Cdd:cd01132 190 REAYPGdvfYLHSRL---LERAAKLSDELGG-GSLTALPIIETQAGDVSAYIPTNVISITdgQIF--LESELFNKGIRPA 263
|
..
gi 1055291904 428 IN 429
Cdd:cd01132 264 IN 265
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
210-429 |
1.43e-16 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 82.70 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 210 PLITGQRILDGLFPIAKGGTAAIPGPFGSGKT--VTQQQLAKWSDAEIVVYIGCGERGNEMTEVLTEFPEledpktgRPL 287
Cdd:CHL00059 124 PLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTavATDTILNQKGQNVICVYVAIGQKASSVAQVVTTLQE-------RGA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 288 MERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPA---YLSARL 364
Cdd:CHL00059 197 MEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL 276
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055291904 365 SEfyeragRAISLNGA--SGSVSVIGAVSPPGGDFSEPVTQNTLRIV--KVFWALDAKLSQRRhfPAIN 429
Cdd:CHL00059 277 LE------RAAKLSSQlgEGSMTALPIVETQAGDVSAYIPTNVISITdgQIFLSADLFNAGIR--PAIN 337
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
181-385 |
2.71e-16 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 81.89 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 181 LEDGTEITMLQRWPVRVPRP-VKEKLNPDVPLITGQRILDGLFPIAKGGTAAIPGPFGSGKTvtqqQLA-------KWSD 252
Cdd:PRK13343 115 LDGGGPLQATARRPLERPAPaIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKT----AIAidaiinqKDSD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 253 AeIVVYIGCGERGNEMTEVLTEFPEledpktgRPLMERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADS 332
Cdd:PRK13343 191 V-ICVYVAIGQKASAVARVIETLRE-------HGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDD 262
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055291904 333 TSRWAEAMREISSRLEEMPGEEGYPA---YLSARLSEfyeragRAISLNGASGSVS 385
Cdd:PRK13343 263 LSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRLLE------RAAKLSPELGGGS 312
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
1-405 |
6.32e-15 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 77.00 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 1 MKKNTEKRTQgvlkrISGPVVT----AVGLDAhmYDVVKVGNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTGLP 76
Cdd:PRK02118 1 MQKIYTKITD-----ITGNVITveaeGVGYGE--LATVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 77 LAVELGPGLLTSIYDGIQRPlevlmdkmgsfIKRGvsapglshekkwefvptvkagdvvgpgdilgtvqetnivhkimvp 156
Cdd:PRK02118 74 MQVTYSESLLGRRFNGSGKP-----------IDGG--------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 157 PNLKGGKIKkISGGSFTideticvledgteitmlqrwPVR--VPRpvkEKLNPDVP-------LITGQRIldglfPIAkg 227
Cdd:PRK02118 98 PELEGEPIE-IGGPSVN--------------------PVKriVPR---EMIRTGIPmidvfntLVESQKI-----PIF-- 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 228 gtaAIPG-PFgsgktvtQQQLAK---WSDAEIVVYIGCGERGNEMTEVLTEFPELEdpktgrpLMERTVLIANTSNMPVA 303
Cdd:PRK02118 147 ---SVSGePY-------NALLARialQAEADIIILGGMGLTFDDYLFFKDTFENAG-------ALDRTVMFIHTASDPPV 209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 304 AREASVYTGITIAEYFRDMGYD--VSLMADSTSrWAEAMREISSRLEEMPGEEGYPAYLSARLSEFYEragRAISLNGAs 381
Cdd:PRK02118 210 ECLLVPDMALAVAEKFALEGKKkvLVLLTDMTN-FADALKEISITMDQIPSNRGYPGSLYSDLASRYE---KAVDFEDG- 284
|
410 420
....*....|....*....|....
gi 1055291904 382 GSVSVIGAVSPPGGDFSEPVTQNT 405
Cdd:PRK02118 285 GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
211-429 |
1.36e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 73.54 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 211 LITGQRILDGLFPIAKGGTAAIPGPFGSGKT------------VTQQQLAKwsDAEIVVYIGCGERGNEMTEV---LTEF 275
Cdd:PTZ00185 173 LLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsiavstiinqvrINQQILSK--NAVISIYVSIGQRCSNVARIhrlLRSY 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 276 PELEdpktgrplmeRTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEG 355
Cdd:PTZ00185 251 GALR----------YTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055291904 356 YPA---YLSARLsefYERAGrAISLNGASGSVSVIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAKLSQRRHFPAIN 429
Cdd:PTZ00185 321 YPGdvfYLHSRL---LERAA-MLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
15-74 |
9.47e-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: 60.64 E-value: 9.47e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055291904 15 RISGPVVTAVGLDAH---MYDVVKVGNEE----LMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTG 74
Cdd:pfam02874 3 QVIGPVVDVEFGIGRlpgLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
10-74 |
7.44e-11 |
|
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: 58.09 E-value: 7.44e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1055291904 10 QGVLKRISGPVVTAVGL-DAHMYDVVKV----GNEE--LMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTG 74
Cdd:cd01426 1 KGRVIRVNGPLVEAELEgEVAIGEVCEIergdGNNEtvLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTG 72
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
288-383 |
1.00e-08 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 57.77 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 288 MERTVLIANTSNMPVAAREASVYTGITIAEYFRDMGYDVSLMADSTSRWAEAMREISSRLEEMPGEEGYPA---YLSARL 364
Cdd:PRK09281 218 MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL 297
|
90
....*....|....*....
gi 1055291904 365 sefYERAGRAISLNGAsGS 383
Cdd:PRK09281 298 ---LERAAKLSDELGG-GS 312
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
464-510 |
9.07e-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: 9.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1055291904 464 LQKEAELQEIVQLVGSDALPDEEQITIEVARMIREiFLQQNAYDAVD 510
Cdd:cd01429 12 LAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPET 57
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
11-74 |
1.42e-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: 40.20 E-value: 1.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1055291904 11 GVLKRISGPVVTAVGLDAHMYDVVKV---GNEELMGEVIKIQGENVIIQVYEDTDGIRPGEPVVNTG 74
Cdd:cd18117 3 GRVVRVVGLLLEAVGPQAPIGELCLIetaDGLSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLG 69
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
216-339 |
2.39e-04 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 42.96 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 216 RILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAK-----WSDAE-IVVYIgcGERGNEMTEvltefpeledpktgrplME 289
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANaiaknHPEVElIVLLI--DERPEEVTD-----------------MR 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1055291904 290 RTV---LIANTSNMPvAAREASV-YTGITIAEYFRDMGYDVSLMADSTSRWAEA 339
Cdd:cd01128 66 RSVkgeVVASTFDEP-PERHVQVaEMVIEKAKRLVEHGKDVVILLDSITRLARA 118
|
|
| 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 ... |
13-64 |
3.31e-04 |
|
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: 39.33 E-value: 3.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1055291904 13 LKRISGPVVTAVGLDAHMYD-VVKV---GNEELMGEVIKIQGENVIIQVYEDTDGI 64
Cdd:cd18118 5 VSEINGPLVIVEGVKGVKYGeIVEItlpDGEVRRGQVLEVSGDKAVVQVFEGTSGL 60
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
216-433 |
7.33e-04 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 42.37 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 216 RILDGLFPIAKGGTAAIPGPFGSGKTVTQQQLAK-----WSDAE-IVVYIgcGERGNEMTEvltefpeledpktgrplME 289
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQaitrnHPEVElIVLLI--DERPEEVTD-----------------MQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055291904 290 RTV---LIANTSNMPvAAREASVyTGITIAEYFR--DMGYDVSLMADSTSRWAEAMREI---SSRLeeMPGeeGYPAYLS 361
Cdd:TIGR00767 218 RSVkgeVVASTFDEP-ASRHVQV-AEMVIEKAKRlvEHKKDVVILLDSITRLARAYNTVtpaSGKV--LSG--GVDANAL 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1055291904 362 ARLSEFYErAGRAISlNGasGSVSVIG-AVSPPGGDFSEPV------TQNtLRIVkvfwaLDAKLSQRRHFPAINWLNS 433
Cdd:TIGR00767 292 HRPKRFFG-AARNIE-EG--GSLTIIAtALIDTGSRMDEVIfeefkgTGN-MELH-----LDRKLADRRIFPAIDIKKS 360
|
|
| |
