|
Name |
Accession |
Description |
Interval |
E-value |
| V-ATPase_V1_A |
TIGR01042 |
V-type (H+)-ATPase V1, A subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
52-644 |
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: 1268.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 52 EYGYVRKVSGPVVVADGMAGAAMYELVRVGRDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILG 131
Cdd:TIGR01042 1 EYGYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 132 NIFDGIQRPLKTIAKRSGDVYIPRGVSVPALDKDILWEFQPKKIGEGDLLTGGDLYASVFENTLMQHHIALPPDAMGKIT 211
Cdd:TIGR01042 81 NIFDGIQRPLKAIAEQSQSIYIPRGVNVPALDRDKKWEFTPKKLRVGDHITGGDIYGTVFENSLIKHKIMLPPRARGTIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 212 YIAPPGQYSLKDTVLELEFQGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKT 291
Cdd:TIGR01042 161 YIAPAGNYTVDDTVLEVEFQGVKKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 292 VISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLpDGREESVMKRTTLVANTSNMPVAAREASIYTGITLAEY 371
Cdd:TIGR01042 241 VISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEV-DGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 372 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERTGSVTIVGAVSPPGGD 451
Cdd:TIGR01042 320 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 452 FSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEQFDPDFINIRTKAREVLQREDDLNEIVQLV 531
Cdd:TIGR01042 400 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 532 GKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGtDGQKITYTLIKHRMG 611
Cdd:TIGR01042 480 GKDALAETDKITLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQ-DDNKITWSIIKESLG 558
|
570 580 590
....*....|....*....|....*....|...
gi 1785461406 612 DLFYRLVSQKFEDPAEGEAALVAKFKQLHEDLT 644
Cdd:TIGR01042 559 DLLYRLSSMKFEDPSDGEAKIKADYEKLNEDMQ 591
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
54-650 |
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: 939.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 54 GYVRKVSGPVVVADGMAGAAMYELVRVGRDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 133
Cdd:COG1155 5 GKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLLGNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 134 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPKKiGEGDLLTGGDLYASVFENTLMQHHIALPPDAMGKITYI 213
Cdd:COG1155 85 FDGIQRPLDKIAEKSGD-FIPRGVDVPALDREKKWDFTPTV-KVGDKVSAGDILGTVQETPLIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 214 APPGQYSLKDTVLELE-FQGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 292
Cdd:COG1155 163 APEGEYTVEDTIAVLEdEDGEEHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 293 ISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTmtlpD---GReeSVMKRTTLVANTSNMPVAAREASIYTGITLA 369
Cdd:COG1155 243 TQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELI----DpktGR--PLMERTVLIANTSNMPVAAREASIYTGITIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 370 EYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPErtGSVTIVGAVSPPG 449
Cdd:COG1155 317 EYYRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 450 GDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFY-EQFDPDFINIRTKAREVLQREDDLNEIV 528
Cdd:COG1155 395 GDFSEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYdENVDPDWSELRNEAMDLLQEEAELQEIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 529 QLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGTDgqkityTLIKH 608
Cdd:COG1155 475 RLVGEDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLS------EIKEL 548
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1785461406 609 RMGDLFYRLvsqKFEDPAEgeaaLVAKFKQLHEDLTSGFRNL 650
Cdd:COG1155 549 PLREKIARM---KYSPENE----LLEKFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
54-653 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 896.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 54 GYVRKVSGPVVVADGMAGAAMYELVRVGRDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 133
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 134 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPKKiGEGDLLTGGDLYASVFENTLMQHHIALPPDAMGKITYI 213
Cdd:PRK04192 85 FDGIQRPLDELAEKSGD-FLERGVYVPALDREKKWEFTPTV-KVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 214 APPGQYSLKDTVLELE-FQGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 292
Cdd:PRK04192 163 VSEGDYTVDDTIAVLEdEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 293 ISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTmtlpD---GReeSVMKRTTLVANTSNMPVAAREASIYTGITLA 369
Cdd:PRK04192 243 TQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELI----DpktGR--PLMERTVLIANTSNMPVAAREASIYTGITIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 370 EYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPErtGSVTIVGAVSPPG 449
Cdd:PRK04192 317 EYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 450 GDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFY-EQFDPDFINIRTKAREVLQREDDLNEIV 528
Cdd:PRK04192 395 GDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWeENVDPDWRELRDEAMDLLQREAELQEIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 529 QLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAgtdgqkityTLIKH 608
Cdd:PRK04192 475 RLVGPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGV---------PVSEI 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1785461406 609 RMGDLFYRLVSQKFEDPAEGEaalvAKFKQLHEDLTSGFRNLEDE 653
Cdd:PRK04192 546 LELEVRDRIARLKYIPENEYL----EKIDEIFEKLEEELEELIAE 586
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
54-643 |
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: 825.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 54 GYVRKVSGPVVVADGMAGAAMYELVRVGRDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 133
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 134 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPKkIGEGDLLTGGDLYASVFENTLMQHHIALPPDAMGKITYI 213
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGD-FIARGVDAPGLDRDKKWHFKPT-VKEGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 214 APPGQYSLKDTVLELEFQGvKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVI 293
Cdd:TIGR01043 160 AEEGDYTVEDTIAVVDTDG-DEEIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 294 SQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLtmtlPDGRE-ESVMKRTTLVANTSNMPVAAREASIYTGITLAEYF 372
Cdd:TIGR01043 239 QHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPEL----KDPKTgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 373 RDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERTGSVTIVGAVSPPGGDF 452
Cdd:TIGR01043 315 RDMGYDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 453 SDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTAL-ESFYEQFDPDFINIRTKAREVLQREDDLNEIVQLV 531
Cdd:TIGR01043 395 SEPVTQNTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVqDWWHENVDPDWREMRDEAMDLLQKESELQEIVQLV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 532 GKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGTDgqKITYTLIKHRMG 611
Cdd:TIGR01043 475 GPDALPERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVE--EILKLEVKEEIG 552
|
570 580 590
....*....|....*....|....*....|..
gi 1785461406 612 DLfyrlvsqKFEDPAEGEAALVAKFKQLHEDL 643
Cdd:TIGR01043 553 RM-------KYEPDNDILAKIDEILEKIEKEF 577
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
120-492 |
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: 621.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 120 PLSVELGPGILGNIFDGIQRPLKTIAKrSGDVYIPRGVSVpaldkdilwefqpkkigegdlltggdlyasvfentlmqhh 199
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAE-TGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 200 ialppdamgkityiappgqyslkdtvlelefqgvkkkftmlQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGT 279
Cdd:cd01134 40 -----------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 280 CAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLpdgREESVMKRTTLVANTSNMPVAARE 359
Cdd:cd01134 79 AAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPI---TGESLMERTVLIANTSNMPVAARE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 360 ASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERTGSV 439
Cdd:cd01134 156 ASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSV 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1785461406 440 TIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKY 492
Cdd:cd01134 236 TIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
291-643 |
2.24e-124 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 393.23 E-value: 2.24e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 291 TVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTmtlPDGREESVMKRTTLVANTSNMPVAAREASIYTGITLAE 370
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLK---DPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 371 YFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERTGSVTIVGAVSPPGG 450
Cdd:PRK14698 747 YFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGG 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 451 DFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEQ-FDPDFINIRTKAREVLQREDDLNEIVQ 529
Cdd:PRK14698 827 DFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKnVDPEWKAMRDKAMELLQKEAELQEIVR 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 530 LVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGTdgQKITYTLIKHR 609
Cdd:PRK14698 907 IVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPL--EEIAKLPVREE 984
|
330 340 350
....*....|....*....|....*....|....
gi 1785461406 610 MGDLfyrlvsqKFEDPAEGEAALVAKFKQLHEDL 643
Cdd:PRK14698 985 IGRM-------KFEPDIEKIKALIDKTNEQFDEL 1011
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
264-490 |
2.53e-104 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 315.45 E-value: 2.53e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 264 GQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPqltmtlpdgrEESVMKR 343
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELL----------GSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 344 TTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYER 423
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785461406 424 AGKVKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYS 490
Cdd:pfam00006 151 AGRVK-----GKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
239-492 |
1.28e-90 |
|
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: 282.42 E-value: 1.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 239 MLQTWPVRTPRP-VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNS---DAVVYVGCGER 314
Cdd:cd19476 28 TKQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKahaGVVVFAGIGER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 315 GNEMAEVLMDFPqltmtlpdgrEESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALR 394
Cdd:cd19476 108 GREVNDLYEEFT----------KSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 395 EISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKL 474
Cdd:cd19476 178 EMSALLGEPPGREGYPPYLFTKLATLYERAGKVK-----DGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSREL 252
|
250
....*....|....*...
gi 1785461406 475 AQRKHFPSVNWLISYSKY 492
Cdd:cd19476 253 ARKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
54-292 |
5.50e-75 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 259.95 E-value: 5.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 54 GYVRKVSGPVVVADGMAGAAMYELVRVGRDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 133
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 134 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPkKIGEGDLLTGGDLYASVFENTLMQHHIALPPDAMGKITYI 213
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFIP-KVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 214 APPGQYSLKDTVLELEF-QGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 292
Cdd:PRK14698 163 ADEGEYTIEEVIAKVKTpSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCV 242
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
134-255 |
3.88e-61 |
|
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: 199.55 E-value: 3.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 134 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDILWEFQPKkIGEGDLLTGGDLYASVFENTLMQHHIALPPDAMGKITYI 213
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTPT-VKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTEI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1785461406 214 APPGQYSLKDTVLELEFQGVKKKFTMLQTWPVRTPRPVASKL 255
Cdd:pfam16886 79 APEGEYTVEDTIAEVEDEGKEKELTMMQKWPVRRPRPYKEKL 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 ... |
507-613 |
2.51e-51 |
|
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: 172.57 E-value: 2.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 507 FINIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLA 586
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....*..
gi 1785461406 587 NQAVERGAGTDgqKITYTLIKHRMGDL 613
Cdd:cd18111 81 LEALEKGVPLS--KILELPVREKIARM 105
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
40-564 |
2.07e-42 |
|
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: 159.07 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 40 RLTTFEDSEKESEYGYVRKVSGPVVVADGMAgAAMYELVRVGRDN----LIGEIIRLEGDSATIQVYEETAGLMVNDPVL 115
Cdd:TIGR01026 11 RLCQEMDLRLVKRVGRVTKVKGLLIEAVGPQ-ASVGDLCLIERRGsegrLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 116 RTHKPLSVELGPGILGNIFDGIQRPLKtiakrsgdvyiprgvsvpaldkdilwefqpkkiGEGDLLtggdlyasvfeNTL 195
Cdd:TIGR01026 90 ATGEGLSIKVGDGLLGRVLDGLGKPID---------------------------------GKGKFL-----------DNV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 196 MQHHIALPPdamgkityIAPpgqyslkdtvlelefqgvkkkftmLQTWPVRTPrpvasklaadtpLLTGQRVLDALFPSV 275
Cdd:TIGR01026 126 ETEGLITAP--------INP------------------------LKRAPIREI------------LSTGVRSIDGLLTVG 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 276 LGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEmaevLMDFPQltmtlPDGREESvMKRTTLVANTSNMPV 355
Cdd:TIGR01026 162 KGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGRE----VREFIE-----HDLGEEG-LKRSVVVVATSDQSP 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 356 AAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpER 435
Cdd:TIGR01026 232 LLRLKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGA-------SG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 436 TGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESfYEQFDpdfinIRTKAR 515
Cdd:TIGR01026 305 KGSITAFYTVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVS-EEHRR-----AARKFR 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1785461406 516 EVL---QREDDLNEI-VQLVGKDalAEGDKITLETAKLlrEDYLAQNAFTPYD 564
Cdd:TIGR01026 379 ELLskyKDNEDLIRIgAYQRGSD--RELDFAIAKYPKL--ERFLKQGINEKVN 427
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
53-484 |
1.56e-39 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 150.57 E-value: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 53 YGYVRKVSGPVVVADGMaGAAMYELVRVGRDN---LIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGI 129
Cdd:COG1157 20 SGRVTRVVGLLIEAVGP-DASIGELCEIETADgrpVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 130 LGNIFDGIQRPLktiakrSGDVYIPRGVSVPaldkdilwefqpkkigegdlltggdLYASvfentlmqhhialPPDAMGK 209
Cdd:COG1157 99 LGRVLDGLGRPL------DGKGPLPGEERRP-------------------------LDAP-------------PPNPLER 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 210 ityiappgqyslkdtvlelefqgvkkkftmlqtwpvrtpRPVasklaaDTPLLTGQRVLDALFPSVLG---GTCAipGAf 286
Cdd:COG1157 135 ---------------------------------------ARI------TEPLDTGVRAIDGLLTVGRGqriGIFA--GS- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 287 GCGKTVISQALSKYSNSDAVVyVG-CGERGNEmaevLMDFpqLTMTL-PDGreesvMKRTTLVANTSNMPVAAREASIYT 364
Cdd:COG1157 167 GVGKSTLLGMIARNTEADVNV-IAlIGERGRE----VREF--IEDDLgEEG-----LARSVVVVATSDEPPLMRLRAAYT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 365 GITLAEYFRDMGYNVSMMADSTSRWAEALREISgrLA--EMPADSGYPAYLAARLASFYERAgkvkclgGPERTGSVTIV 442
Cdd:COG1157 235 ATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIG--LAagEPPATRGYPPSVFALLPRLLERA-------GNGGKGSITAF 305
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1785461406 443 GAVSPPGGDFSDPVTSATLS-----IVqvfwgLDKKLAQRKHFPSVN 484
Cdd:COG1157 306 YTVLVEGDDMNDPIADAVRGildghIV-----LSRKLAERGHYPAID 347
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
53-491 |
2.96e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 149.96 E-value: 2.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 53 YGYVRKVsGPVVVADGMAGAAMYELVRVGRDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGN 132
Cdd:PRK06820 30 RGPIVEI-GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 133 IFDGIQRPLktiakrsgDVYIPRGVSVPALDkdilwefqpkkigegdlltggdlyasvfentlmqhhialppdamgkity 212
Cdd:PRK06820 109 ILDGLGAPI--------DGGPPLTGQWRELD------------------------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 213 iAPPgqyslkdtvlelefqgvkkkftmlqtwpvrtPRPVASKLAaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 292
Cdd:PRK06820 132 -CPP-------------------------------PSPLTRQPI-EQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKST 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 293 ISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQLTMTlPDGREesvmkRTTLVANTSNMPVAAREASIYTGITLAEYF 372
Cdd:PRK06820 179 LLGMLCADSAADVMVLALIGERGREVRE----FLEQVLT-PEARA-----RTVVVVATSDRPALERLKGLSTATTIAEYF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 373 RDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAgkvkclgGPERTGSVTIVGAVSPPGGDF 452
Cdd:PRK06820 249 RDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERT-------GNSDRGSITAFYTVLVEGDDM 321
|
410 420 430
....*....|....*....|....*....|....*....
gi 1785461406 453 SDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 491
Cdd:PRK06820 322 NEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSR 360
|
|
| 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 ... |
53-119 |
3.23e-39 |
|
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349743 [Multi-domain] Cd Length: 67 Bit Score: 138.43 E-value: 3.23e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785461406 53 YGYVRKVSGPVVVADGMAGAAMYELVRVGRDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHK 119
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
241-491 |
3.89e-38 |
|
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: 142.31 E-value: 3.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 241 QTWPVRTPRPVASKLAA-DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEma 319
Cdd:cd01136 30 ERRPLIAAPPNPLKRAPiEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 320 evLMDFPQLTMtlpdgrEESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGR 399
Cdd:cd01136 108 --VREFIEKDL------GEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 400 LAEMPADSGYPAYLAARLASFYERAgkvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKH 479
Cdd:cd01136 180 AGEPPTRRGYPPSVFALLPRLLERA-------GNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGH 252
|
250
....*....|..
gi 1785461406 480 FPSVNWLISYSK 491
Cdd:cd01136 253 YPAIDVLASISR 264
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
242-560 |
4.44e-37 |
|
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: 144.48 E-value: 4.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 242 TWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSK---YSNSDAVVYVGCGER--- 314
Cdd:TIGR01039 107 RWPIHRKAPSFEEQSTKVEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINniaKEHGGYSVFAGVGERtre 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 315 GN----EMAEvlmdfpqltmtlpdgreESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDM-GYNVSMMADSTSRW 389
Cdd:TIGR01039 187 GNdlyhEMKE-----------------SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDNIFRF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 390 AEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWG 469
Cdd:TIGR01039 250 TQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTK-------TGSITSVQAVYVPADDLTDPAPATTFAHLDATTV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 470 LDKKLAQRKHFPSVNWLISYSKystalesfyeQFDPDFINIR-----TKAREVLQREDDLNEIVQLVGKDALAEGDKITL 544
Cdd:TIGR01039 323 LSRKIAELGIYPAVDPLDSTSR----------LLDPSVVGEEhydvaRGVQQILQRYKELQDIIAILGMDELSEEDKLTV 392
|
330
....*....|....*.
gi 1785461406 545 ETAKLLrEDYLAQNAF 560
Cdd:TIGR01039 393 ERARRI-QRFLSQPFF 407
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
54-490 |
1.36e-33 |
|
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: 133.37 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 54 GYVRKVSGPVVVADGMAgAAMYELVRVGR---DNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGIL 130
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLR-APVGSRCEIESsdgDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 131 GNIFDGIQRPLktiakrSGDVYIPRGVSVPAldkdilwefqpkkigegdlltggdlyasvfentlmqhhIALPPDAMGKi 210
Cdd:TIGR03496 80 GRVIDGLGRPL------DGKGPLDAGERVPL--------------------------------------YAPPINPLKR- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 211 tyiappgqyslkdtvlelefqgvkkkftmlqtwpvrtpRPVasklaaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGK 290
Cdd:TIGR03496 115 --------------------------------------API------DEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGK 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 291 TVISQALSKYSNSDAVVyVG-CGERGNEMAEVLMDfpqltmTLPdgreESVMKRTTLVANTSNMPVAAREASIYTGITLA 369
Cdd:TIGR03496 151 STLLGMMARYTEADVVV-VGlIGERGREVKEFIED------ILG----EEGLARSVVVAATADESPLMRLRAAFYATAIA 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 370 EYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclgGPERTGSVTIVGAVSPPG 449
Cdd:TIGR03496 220 EYFRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGN-----GEEGKGSITAFYTVLVEG 294
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1785461406 450 GDFSDPVTSATLSIVQvfwG---LDKKLAQRKHFPSVNWLISYS 490
Cdd:TIGR03496 295 DDQQDPIADAARAILD---GhivLSRELAEQGHYPAIDILASIS 335
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
69-538 |
4.43e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 129.30 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 69 MAGAAMYELVRVGRDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKtiakrs 148
Cdd:PRK07594 37 LPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD------ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 149 gdvyiprGVSVPaldkDILWefqpkkigegdlltggdlyasvfentlmQHHIALPPDAMgkityiappgqyslkdtvlel 228
Cdd:PRK07594 111 -------GRELP----DVCW----------------------------KDYDAMPPPAM--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 229 efqgvkkkftmlqtwpvrTPRPVASklaadtPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVY 308
Cdd:PRK07594 131 ------------------VRQPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 309 VGCGERGNEMAEvlmdFPQLTMTlpdgreESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSR 388
Cdd:PRK07594 187 VLIGERGREVRE----FIDFTLS------EETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 389 WAEALREISGRLAEMPADSGYPAYLAARLASFYERAGkvkcLGgpeRTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFW 468
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG----MG---EKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHI 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785461406 469 GLDKKLAQRKHFPSVNWLISYSKYSTALESfyeqfdPDFINIRTKAREVLQREDDLNEIVQL----VGKDALAE 538
Cdd:PRK07594 330 VLSRRLAERGHYPAIDVLATLSRVFPVVTS------HEHRQLAAILRRCLALYQEVELLIRIgeyqRGVDTDTD 397
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
248-530 |
5.17e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 128.96 E-value: 5.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 248 PRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQ 327
Cdd:PRK08149 122 PPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTE----FVE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 328 lTMTLPDGREesvmkRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADS 407
Cdd:PRK08149 198 -SLRASSRRE-----KCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 408 GYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLI 487
Cdd:PRK08149 272 GYPASVFDSLPRLLERPGATL-------AGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLK 344
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1785461406 488 SYSKYstalesFYEQFDPDFINIRTKAREVLQREDDLNEIVQL 530
Cdd:PRK08149 345 SVSRV------FGQVTDPKHRQLAAAFRKLLTRLEELQLFIDL 381
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
248-538 |
1.12e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 128.33 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 248 PRPVASKLAaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDfpq 327
Cdd:PRK06936 134 PAPMSRRLI-ETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIES--- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 328 ltmtlpDGREESvMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADS 407
Cdd:PRK06936 210 ------DLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 408 GYPAYLAARLASFYERAgkvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLI 487
Cdd:PRK06936 283 GYPPSVFAALPRLMERA-------GQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLR 355
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1785461406 488 SYSKYSTALesfyeqFDPDFINIRTKAREVLQREDDLNEIVQL----VGKDALAE 538
Cdd:PRK06936 356 SASRVMNQI------VSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEAD 404
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
244-530 |
3.71e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 126.63 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 244 PVRTPRPVA-SKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVL 322
Cdd:PRK08927 124 PLRAPPPPAhSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 323 MDfpqltmTL-PDGreesvMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLA 401
Cdd:PRK08927 204 QD------DLgPEG-----LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 402 EMPADSGYPAYLAARLASFYERAGKvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFP 481
Cdd:PRK08927 273 EPPTTKGYTPTVFAELPRLLERAGP-----GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYP 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1785461406 482 SVNWLISYSKysTALESfyeqFDPDFINIRTKAREVLQREDDLNEIVQL 530
Cdd:PRK08927 348 AINVLKSVSR--TMPGC----NDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
247-491 |
7.78e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 122.80 E-value: 7.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 247 TPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDfp 326
Cdd:PRK06002 135 TAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLED-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 327 qltmTLPDGREESVmkrtTLVANTSNMPVAAREASIyTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPAD 406
Cdd:PRK06002 213 ----TLADNLKKAV----AVVATSDESPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 407 SGYPAYLAARLASFYERAGKvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWL 486
Cdd:PRK06002 284 RGYPPSVFSELPRLLERAGP-----GAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPL 358
|
....*
gi 1785461406 487 ISYSK 491
Cdd:PRK06002 359 ASISR 363
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
52-557 |
1.09e-28 |
|
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 440770 [Multi-domain] Cd Length: 462 Bit Score: 119.86 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 52 EYGYVRKVSGPVVVADGMAGAAMYELVRVGRDN---LIGEIIRLEGDSATIQVYEETAGLMVNDPVLR-THKPLSVELGP 127
Cdd:COG1156 5 EYRTISEIAGPLLFVEGVEGVGYGELVEIELPDgerRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 128 GILGNIFDGIQRPL----KTIAKRSGDV---------------YIPRGVSVpaldkdilwefqpkkIgegDLLtggdlya 188
Cdd:COG1156 85 DMLGRVFNGLGRPIdggpPIIPEKRLDIngspinpvareypreFIQTGISA---------------I---DGL------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 189 svfeNTLMQhhialppdamgkityiappGQyslkdtvlelefqgvkkKFtmlqtwpvrtprPVAS-------KLAAdtpl 261
Cdd:COG1156 140 ----NTLVR-------------------GQ-----------------KL------------PIFSgsglphnELAA---- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 262 ltgQRVLDAlfpSVLGGTcaipGAFgcgktvisqalskysnsdAVVYVGCGERGNEMAEVLMDFpqltmtlpdgrEES-V 340
Cdd:COG1156 164 ---QIARQA---KVRGEE----EKF------------------AVVFAAMGITHDEANFFREEF-----------EETgA 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 341 MKRTTLVANTSNMPVAAREASIYTGITLAEYFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLA 418
Cdd:COG1156 205 LDRVVMFLNLADDPAIERIITPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLA 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 419 SFYERAGKVKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSkystal 496
Cdd:COG1156 284 SLYERAGRIK-----GRKGSITQIPILTMPNDDITHPIPDLTGYITegQIV--LSRDLHRKGIYPPIDVLPSLS------ 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 497 esfyeqfdpdfiniRTKAR---EVLQRED----------------DLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQ 557
Cdd:COG1156 351 --------------RLMKDgigEGKTREDhadvanqlyaayargqEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQ 416
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
53-491 |
3.39e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 117.90 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 53 YGYVRKVSGPVVVADGMA---GAAMYELVRVGRDNLI-GEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPG 128
Cdd:PRK07721 19 YGKVSRVIGLMIESKGPEssiGDVCYIHTKGGGDKAIkAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 129 ILGNIFDGIQRPLKTIAkrsgdvyIPRGVSVPALDKDilwefqpkkigegdlltggdlyasvfentlmqhhialPPDAMG 208
Cdd:PRK07721 99 LIGQVLDALGEPLDGSA-------LPKGLAPVSTDQD-------------------------------------PPNPLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 209 KityiapPgqyslkdtvlelefqgvkkkftmlqtwPVRTPRPVasklaadtplltGQRVLDALFPSVLGGTCAIPGAFGC 288
Cdd:PRK07721 135 R------P---------------------------PIREPMEV------------GVRAIDSLLTVGKGQRVGIFAGSGV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 289 GKTVISQALSKYSNSDAVVYVGCGERGNEMAEVL-MDFPqltmtlPDGreesvMKRTTLVANTSNMPVAAREASIYTGIT 367
Cdd:PRK07721 170 GKSTLMGMIARNTSADLNVIALIGERGREVREFIeRDLG------PEG-----LKRSIVVVATSDQPALMRIKGAYTATA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 368 LAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpERTGSVTIVGAVSP 447
Cdd:PRK07721 239 IAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT-------NASGSITAFYTVLV 311
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1785461406 448 PGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 491
Cdd:PRK07721 312 DGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSR 355
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
52-557 |
2.80e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 115.31 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 52 EYGYVRKVSGPVVVADGMAGAAMYELVRV---GRDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLR-THKPLSVELGP 127
Cdd:PRK04196 3 EYRTVSEIKGPLLFVEGVEGVAYGEIVEIelpNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 128 GILGNIFDGIQRPL----KTIAKRSGDV---------------YIPRGVSvpALDkdilwefqpkkiGEGDLLTGGDLya 188
Cdd:PRK04196 83 DMLGRIFDGLGRPIdggpEIIPEKRLDIngapinpvareypeeFIQTGIS--AID------------GLNTLVRGQKL-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 189 SVFENTLMQHhialppdamgkityiappgqyslkdtvlelefqgvkkkftmlqtwpvrtprpvaSKLAAdtplltgQRVL 268
Cdd:PRK04196 147 PIFSGSGLPH------------------------------------------------------NELAA-------QIAR 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 269 DAlfpSVLGGTcaipgafgcgktvisqalSKYsnsdAVVYVGCGERgNEMAEVLMDfpqltmtlpDGREESVMKRTTLVA 348
Cdd:PRK04196 166 QA---KVLGEE------------------ENF----AVVFAAMGIT-FEEANFFME---------DFEETGALERSVVFL 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 349 NTSNMPVAAREASIYTGITLAEYFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGK 426
Cdd:PRK04196 211 NLADDPAIERILTPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGR 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 427 VKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSkystalesfyeqfd 504
Cdd:PRK04196 290 IK-----GKKGSITQIPILTMPDDDITHPIPDLTGYITegQIV--LSRELHRKGIYPPIDVLPSLS-------------- 348
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785461406 505 pdfiniRTKAR---EVLQRED----------------DLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQ 557
Cdd:PRK04196 349 ------RLMKDgigEGKTREDhkdvanqlyaayargkDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQ 414
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
53-580 |
3.88e-27 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 114.87 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 53 YGYVRKVSGPVVVADGMAgAAMYEL--VRVGRDNLI--GEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPG 128
Cdd:PRK09099 25 TGKVVEVIGTLLRVSGLD-VTLGELceLRQRDGTLLqrAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 129 ILGNIFDGIQRPLKtiakrsgdvyiprgvSVPALDKDilwEFQPKkigegdlltggdlyasvfentlmqhhIALPPDAMg 208
Cdd:PRK09099 104 LLGRVIDGLGEPID---------------GGGPLDCD---ELVPV--------------------------IAAPPDPM- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 209 kityiappgqyslkdtvlelefqgvkkkftmlqtwpvrtprpvaSKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGC 288
Cdd:PRK09099 139 --------------------------------------------SRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 289 GKTVISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQLTMTlPDGreesvMKRTTLVANTSNMPVAAREASIYTGITL 368
Cdd:PRK09099 175 GKSTLMGMFARGTQCDVNVIALIGERGREVRE----FIELILG-EDG-----MARSVVVCATSDRSSIERAKAAYVATAI 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 369 AEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpERTGSVTIVGAVSPP 448
Cdd:PRK09099 245 AEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM-------GETGSITALYTVLAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 449 GGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALesfyeqFDPDFINIRTKAREVLQREDDLNEIV 528
Cdd:PRK09099 318 DESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQV------VPREHVQAAGRLRQLLAKHREVETLL 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1785461406 529 QL----VGKDALAEGdkiTLETAKLLReDYLAQnaftPYDKFCPFYKSVWMMRNII 580
Cdd:PRK09099 392 QVgeyrAGSDPVADE---AIAKIDAIR-DFLSQ----RTDEYSDPDATLAALAELS 439
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
241-561 |
1.50e-26 |
|
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: 113.26 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 241 QTWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQAL--------SKYSnsdavVYVGC 311
Cdd:COG0055 109 ERRPIHRPAPPFEEQSTKTEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELihniakehGGVS-----VFAGV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 312 GER---GNEMaevlmdfpQLTMtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRD-MGYNVSMMADSTS 387
Cdd:COG0055 184 GERtreGNDL--------YREM-----KESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 388 RWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLS----- 462
Cdd:COG0055 251 RFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAhldat 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 463 IVqvfwgLDKKLAQRKHFPSVNWLISYSKystalesfyeQFDPDFI-----NIRTKAREVLQREDDLNEIVQLVGKDALA 537
Cdd:COG0055 324 TV-----LSRKIAELGIYPAVDPLDSTSR----------ILDPLIVgeehyRVAREVQRILQRYKELQDIIAILGMDELS 388
|
330 340
....*....|....*....|....*
gi 1785461406 538 EGDKITLETA-KLLRedYLAQNAFT 561
Cdd:COG0055 389 EEDKLTVARArKIQR--FLSQPFFV 411
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
287-484 |
5.49e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 111.33 E-value: 5.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 287 GCGKTVISQALSKYSNSDAVVyVG-CGERGNEMAEVLMDFpqLTmtlPDGREESVmkrttLVANTSNMPVAAREASIYTG 365
Cdd:PRK08972 172 GVGKSVLLGMMTRGTTADVIV-VGlVGERGREVKEFIEEI--LG---EEGRARSV-----VVAAPADTSPLMRLKGCETA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 366 ITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclgGPERTGSVTIVGAV 445
Cdd:PRK08972 241 TTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGN-----GGPGQGSITAFYTV 315
|
170 180 190
....*....|....*....|....*....|....*....
gi 1785461406 446 SPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVN 484
Cdd:PRK08972 316 LTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAID 354
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
241-491 |
3.18e-25 |
|
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: 105.76 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 241 QTWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQAL----SKySNSDAVVYVGCGERG 315
Cdd:cd01133 30 ERWPIHREAPEFVELSTEQEILeTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinniAK-AHGGYSVFAGVGERT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 316 NEMAEVLMDfpqltMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDM-GYNVSMMADSTSRWAEALR 394
Cdd:cd01133 109 REGNDLYHE-----MKESGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 395 EISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKL 474
Cdd:cd01133 184 EVSALLGRIPSAVGYQPTLATEMGSLQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGI 256
|
250
....*....|....*..
gi 1785461406 475 AQRKHFPSVNWLISYSK 491
Cdd:cd01133 257 AELGIYPAVDPLDSTSR 273
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
241-560 |
1.02e-22 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 102.04 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 241 QTWPVRTPRPVASKLaaDTPLL---TGQRVLDALFPSVLGGTCAIPGAFGCGKTV--------ISQALSKYSnsdavVYV 309
Cdd:CHL00060 124 TTSPIHRSAPAFIQL--DTKLSifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVlimelinnIAKAHGGVS-----VFG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 310 GCGERGNEMAEVLMDFPQLTMTLPDGREESvmkRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGY-NVSMMADSTSR 388
Cdd:CHL00060 197 GVGERTREGNDLYMEMKESGVINEQNIAES---KVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 389 WAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFW 468
Cdd:CHL00060 274 FVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-------EGSITSIQAVYVPADDLTDPAPATTFAHLDATT 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 469 GLDKKLAQRKHFPSVNWLISyskYSTAL------ESFYEqfdpdfinIRTKAREVLQREDDLNEIVQLVGKDALAEGDKI 542
Cdd:CHL00060 347 VLSRGLAAKGIYPAVDPLDS---TSTMLqprivgEEHYE--------TAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
330
....*....|....*...
gi 1785461406 543 TLETAKLLrEDYLAQNAF 560
Cdd:CHL00060 416 TVARARKI-ERFLSQPFF 432
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
258-491 |
3.33e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 100.19 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 258 DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFpqltmtlpdgRE 337
Cdd:PRK05688 149 SEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHI----------LG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 338 ESVMKRTTLVANTSN-MPVAAREASIYTgITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAAR 416
Cdd:PRK05688 219 EEGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAK 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785461406 417 LASFYERAGKVKClGGpertGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 491
Cdd:PRK05688 298 LPKLVERAGNAEP-GG----GSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISR 367
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
295-491 |
7.65e-22 |
|
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: 96.14 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 295 QA-LSKYSNSDAVVYVGCGERgNEMAEVLMDfpqltmtlpDGREESVMKRTTLVANTSNMPVAAReasIYT---GITLAE 370
Cdd:cd01135 92 QAgVVGSEENFAIVFAAMGVT-MEEARFFKD---------DFEETGALERVVLFLNLANDPTIER---IITprmALTTAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 371 YFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggpERTGSVTIVGAVSPP 448
Cdd:cd01135 159 YLAyEKGKHVlVILTDMTN-YAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVE-----GRKGSITQIPILTMP 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1785461406 449 GGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSK 491
Cdd:cd01135 233 NDDITHPIPDLTGYITegQIY--LDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
261-567 |
3.76e-21 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 96.78 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 261 LLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAevlmDFPQLTMTlPDGREESV 340
Cdd:PRK07960 159 LDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVK----DFIENILG-AEGRARSV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 341 MkrttLVANTSNMPVAAREASIYtGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASF 420
Cdd:PRK07960 234 V----IAAPADVSPLLRMQGAAY-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPAL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 421 YERAGKvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTAL--ES 498
Cdd:PRK07960 309 VERAGN-----GISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALidEQ 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785461406 499 FYEQfdpdfinIRTkAREVL---QREDDlneivqLVGKDALAEGDKITLETAKLL---REDYLAQNAFTP--YDKFC 567
Cdd:PRK07960 384 HYAR-------VRQ-FKQLLssfQRNRD------LVSVGAYAKGSDPMLDKAIALwpqLEAFLQQGIFERadWEDSL 446
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
254-491 |
4.58e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 96.50 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 254 KLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLmdfpqltmtlP 333
Cdd:PRK07196 132 RRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFI----------E 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 334 DGREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYL 413
Cdd:PRK07196 202 HSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSA 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785461406 414 AARLASFYERAGKvkclggPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 491
Cdd:PRK07196 282 FSIIPRLAESAGN------SSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISR 353
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
258-580 |
7.73e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 89.36 E-value: 7.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 258 DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQLTMtlpDGRE 337
Cdd:PRK08472 138 DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPE----FIEKNL---GGDL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 338 ESvmkrTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARL 417
Cdd:PRK08472 211 EN----TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 418 ASFYERAGKvkclggPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALE 497
Cdd:PRK08472 287 PQLMERAGK------EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDII 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 498 SfyeqfdPDFINIRTKAREV--LQREddlNEIVQLVGkdALAEGDKITLETA---KLLREDYLAQNaftPYDKFcPFYKS 572
Cdd:PRK08472 361 S------PEHKLAARKFKRLysLLKE---NEVLIRIG--AYQKGNDKELDEAiskKEFMEQFLKQN---PNELF-PFEQT 425
|
....*...
gi 1785461406 573 VWMMRNII 580
Cdd:PRK08472 426 FEQLEEIL 433
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
39-440 |
2.11e-18 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 88.82 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 39 ARLTTFEDSEKESEYGYVRKVSGPVVVADGMAGAAMYELVRVGrDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTH 118
Cdd:PRK13343 14 QRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFE-GGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 119 KPLSVELGPGILGNIFDGIQRPLKtiakrsgdvyiprgvsvpaldkdilwefqpkkiGEGdlltggdlyasvfentlmqh 198
Cdd:PRK13343 93 RVLEVPVGDGLLGRVIDPLGRPLD---------------------------------GGG-------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 199 hiALPPDAMGKITYIAPPgqyslkdtVLELEFqgvkkkftmlqtwpvrtprpvasklaADTPLLTGQRVLDALFPSVLGG 278
Cdd:PRK13343 120 --PLQATARRPLERPAPA--------IIERDF--------------------------VTEPLQTGIKVVDALIPIGRGQ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 279 TCAIPGAFGCGKT------VISQalskySNSDAV-VYVGCGERGNEMAEVLMdfpqltmTLpdgREESVMKRTTLVANTS 351
Cdd:PRK13343 164 RELIIGDRQTGKTaiaidaIINQ-----KDSDVIcVYVAIGQKASAVARVIE-------TL---REHGALEYTTVVVAEA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 352 NMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPA---YLAARLasfYERAGKV- 427
Cdd:PRK13343 229 SDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRL---LERAAKLs 305
|
410
....*....|...
gi 1785461406 428 KCLGGpertGSVT 440
Cdd:PRK13343 306 PELGG----GSLT 314
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
240-524 |
2.18e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 88.11 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 240 LQTWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEM 318
Cdd:PRK06793 118 LQKIKLDAPPIHAFEREEITDVFeTGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 319 AevlmDFPQLTMTlpdgreESVMKRTTLVANTSNMP--VAAREASIYTGItlAEYFRDMGYNVSMMADSTSRWAEALREI 396
Cdd:PRK06793 198 K----DFIRKELG------EEGMRKSVVVVATSDEShlMQLRAAKLATSI--AEYFRDQGNNVLLMMDSVTRFADARRSV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 397 SGRLAEMPAdSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQ 476
Cdd:PRK06793 266 DIAVKELPI-GGKTLLMESYMKKLLERSGKTQ-------KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELAT 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1785461406 477 RKHFPSVNWLISYSKYstalesFYEQFDPDFINIRTKAREVLQ--REDDL 524
Cdd:PRK06793 338 LSHYPAISVLDSVSRI------MEEIVSPNHWQLANEMRKILSiyKENEL 381
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
334-560 |
4.59e-17 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 84.39 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 334 DGREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFR-DMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAY 412
Cdd:TIGR01040 203 DFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGY 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 413 LAARLASFYERAGKVKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYS 490
Cdd:TIGR01040 283 MYTDLATIYERAGRVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPINVLPSLS 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785461406 491 KY--STALESFYEQFDPDFINiRTKAREVLQRedDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAF 560
Cdd:TIGR01040 356 RLmkSAIGEGMTRKDHSDVSN-QLYACYAIGK--DVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPY 424
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
244-567 |
6.39e-16 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 80.72 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 244 PVRTPRPVA-SKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVL 322
Cdd:PRK05922 123 PLFSSPPSPmSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 323 MDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAE 402
Cdd:PRK05922 203 EQH----------KEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 403 MPADSGYPAYLAARLASFYERAGKvkclggpERTGSVTIVGAV--SPPGGD-FSDPVTSAtlsivqvfwgLDKKL---AQ 476
Cdd:PRK05922 273 TLSAHHYAASVFHHVSEFTERAGN-------NDKGSITALYAIlhYPNHPDiFTDYLKSL----------LDGHFfltPQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 477 RKHF--PSVNWLISYSKYSTALESfyeqfdPDFINIRTKAREVLQREDDLNEIVQLvgkDALAEGDKITLETA-KLLR-- 551
Cdd:PRK05922 336 GKALasPPIDILTSLSRSARQLAL------PHHYAAAEELRSLLKAYHEALDIIQL---GAYVPGQDAHLDRAvKLLPsi 406
|
330
....*....|....*.
gi 1785461406 552 EDYLAQnaftPYDKFC 567
Cdd:PRK05922 407 KQFLSQ----PLSSYC 418
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
260-491 |
6.44e-16 |
|
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: 78.37 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 260 PLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIsqALSKYSNSDA----VVYVGCGERGNEMAevlmdfpQLTMTLpdg 335
Cdd:cd01132 52 PLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAI--AIDTIINQKGkkvyCIYVAIGQKRSTVA-------QIVKTL--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 336 REESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPA---Y 412
Cdd:cd01132 120 EEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 413 LAARLasfYERAGKVK-CLGGpertGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISY 489
Cdd:cd01132 200 LHSRL---LERAAKLSdELGG----GSLTALPIIETQAGDVSAYIPTNVISITdgQIF--LESELFNKGIRPAINVGLSV 270
|
..
gi 1785461406 490 SK 491
Cdd:cd01132 271 SR 272
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
247-495 |
6.46e-14 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 74.61 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 247 TPRP-VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIsqALSKYSN---SDAV-VYVGCGERGNEMAEV 321
Cdd:CHL00059 110 SPAPgIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAV--ATDTILNqkgQNVIcVYVAIGQKASSVAQV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 322 LMDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLA 401
Cdd:CHL00059 188 VTTL----------QERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 402 EMPADSGYPA---YLAARLasfYERAGKV-KCLGGpertGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLA 475
Cdd:CHL00059 258 RPPGREAYPGdvfYLHSRL---LERAAKLsSQLGE----GSMTALPIVETQAGDVSAYIPTNVISITdgQIF--LSADLF 328
|
250 260
....*....|....*....|
gi 1785461406 476 QRKHFPSVNWLISYSKYSTA 495
Cdd:CHL00059 329 NAGIRPAINVGISVSRVGSA 348
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
56-117 |
4.73e-13 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 64.49 E-value: 4.73e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785461406 56 VRKVSGPVVVADGMAGAA--MYELVRVGRDN----LIGEIIRLEGDSATIQVYEETAGLMVNDPVLRT 117
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLpgLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
53-114 |
1.01e-12 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 63.49 E-value: 1.01e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785461406 53 YGYVRKVSGPVVVADGMAGAAMYELVRVGRDN------LIGEIIRLEGDSATIQVYEETAGLMVNDPV 114
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDgnnetvLKAEVIGFRGDRAILQLFESTRGLSRGALV 68
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
251-498 |
2.23e-11 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 66.60 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 251 VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIS------------QALSKysNSDAVVYVGCGERGNEM 318
Cdd:PTZ00185 163 IVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvstiinqvrinqQILSK--NAVISIYVSIGQRCSNV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 319 AEVLMDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISG 398
Cdd:PTZ00185 241 ARIHRLL----------RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 399 RLAEMPADSGYPA---YLAARLasfYERAGKVKCLGGperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLA 475
Cdd:PTZ00185 311 LLRRPPGREAYPGdvfYLHSRL---LERAAMLSPGKG---GGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLF 384
|
250 260
....*....|....*....|...
gi 1785461406 476 QRKHFPSVNWLISYSKYSTALES 498
Cdd:PTZ00185 385 TGGQRPAVNIGLSVSRVGSSAQN 407
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
71-460 |
4.01e-11 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 65.44 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 71 GAAMYELVRVGRDN--LIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIAKRS 148
Cdd:PRK02118 22 GVGYGELATVERKDgsSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 149 GDVYIPRGVSV-PAldkdilwefqpKKIGEGDLLTGGDLYASVFeNTLMQHHialppdamgKITYIAPPGQyslkdtvle 227
Cdd:PRK02118 102 GEPIEIGGPSVnPV-----------KRIVPREMIRTGIPMIDVF-NTLVESQ---------KIPIFSVSGE--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 228 lefqgvkkkftmlqtwpvrtprPVASKLAadtplltgqRVldALfpsvlggtcaipgafgcgktvisQAlskysNSDAVV 307
Cdd:PRK02118 152 ----------------------PYNALLA---------RI--AL-----------------------QA-----EADIII 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 308 YVGCGERGNemaevlmDFPQLTMTLPDGreeSVMKRTTLVANTSNMPVAAREASIYTGITLAEYFR-DMGYNVSMMADST 386
Cdd:PRK02118 171 LGGMGLTFD-------DYLFFKDTFENA---GALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDM 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785461406 387 SRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAgkVKCLGGpertGSVTIVGAVSPPGGDFSDPVTSAT 460
Cdd:PRK02118 241 TNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA--VDFEDG----GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| 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 ... |
52-108 |
9.51e-08 |
|
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: 49.35 E-value: 9.51e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 52 EYGYVRKVSGPVVVADGMAGAAMYELVRVGRDN---LIGEIIRLEGDSATIQVYEETAGL 108
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDgevRRGQVLEVSGDKAVVQVFEGTSGL 60
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
29-440 |
1.26e-07 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 54.69 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 29 RSSTMSSVYGARLTTFEDSEKESEYGYVRKVSGPVVVADGMAGAAMYELVRVgRDNLIGEIIRLEGDSATIQVYEETAGL 108
Cdd:PRK09281 4 NPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEF-PGGVYGIALNLEEDNVGAVILGDYEDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 109 MVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLktiakrsgdvyiprgvsvpaldkDilwefqpkkiGEGDLLTggdlya 188
Cdd:PRK09281 83 KEGDTVKRTGRILEVPVGEALLGRVVNPLGQPI-----------------------D----------GKGPIEA------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 189 svfentlmqhhialppDAMGKITYIAPpgqyslkdtvlelefqGVkkkftmlqtwpvrTPR-PVasklaaDTPLLTGQRV 267
Cdd:PRK09281 124 ----------------TETRPVERKAP----------------GV-------------IDRkSV------HEPLQTGIKA 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 268 LDALFPS-------VLG----GTCAIpgafgCGKTVISQalsKYSNsdaV--VYVGCGERGNEMAevlmdfpQLTMTLpd 334
Cdd:PRK09281 153 IDAMIPIgrgqrelIIGdrqtGKTAI-----AIDTIINQ---KGKD---VicIYVAIGQKASTVA-------QVVRKL-- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785461406 335 gREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREIS-------GRLAempads 407
Cdd:PRK09281 213 -EEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSlllrrppGREA------ 285
|
410 420 430
....*....|....*....|....*....|....*..
gi 1785461406 408 gYPA---YLAARLasfYERAGKV-KCLGGpertGSVT 440
Cdd:PRK09281 286 -YPGdvfYLHSRL---LERAAKLsDELGG----GSLT 314
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
508-562 |
4.92e-05 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 41.66 E-value: 4.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1785461406 508 INIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREdYLAQNAFTP 562
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEP 55
|
|
| |
