|
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 ... |
66-658 |
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: 1268.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 66 EYGYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILG 145
Cdd:TIGR01042 1 EYGYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 146 NIFDGIQRPLKTIAKRSGDVYIPRGVSVPALDKDTLWEFQPKKIGEGDLLTGGDLYATVFENSLMQHHIALPPDNMGKIT 225
Cdd:TIGR01042 81 NIFDGIQRPLKAIAEQSQSIYIPRGVNVPALDRDKKWEFTPKKLRVGDHITGGDIYGTVFENSLIKHKIMLPPRARGTIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 226 YIAPPGQYSLQDTVLELEFQGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKT 305
Cdd:TIGR01042 161 YIAPAGNYTVDDTVLEVEFQGVKKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 306 VISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLpDGREESVMKRTTLVANTSNMPVAAREASIYTGITLAEY 385
Cdd:TIGR01042 241 VISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEV-DGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 386 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERTGSVTIVGAVSPPGGD 465
Cdd:TIGR01042 320 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 466 FSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALETFYEQFDPDFINIRTKAREVLQREDDLNEIVQLV 545
Cdd:TIGR01042 400 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 546 GKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGsDGQKISYTLIKHRMG 625
Cdd:TIGR01042 480 GKDALAETDKITLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQ-DDNKITWSIIKESLG 558
|
570 580 590
....*....|....*....|....*....|...
gi 2113159344 626 DLFYRLVSQKFEDPAEGEAALVAKFQKLHEDLT 658
Cdd:TIGR01042 559 DLLYRLSSMKFEDPSDGEAKIKADYEKLNEDMQ 591
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
68-664 |
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: 942.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 68 GYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 147
Cdd:COG1155 5 GKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLLGNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 148 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDTLWEFQPKKiGEGDLLTGGDLYATVFENSLMQHHIALPPDNMGKITYI 227
Cdd:COG1155 85 FDGIQRPLDKIAEKSGD-FIPRGVDVPALDREKKWDFTPTV-KVGDKVSAGDILGTVQETPLIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 228 APPGQYSLQDTVLELE-FQGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 306
Cdd:COG1155 163 APEGEYTVEDTIAVLEdEDGEEHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 307 ISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTmtlpD---GReeSVMKRTTLVANTSNMPVAAREASIYTGITLA 383
Cdd:COG1155 243 TQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELI----DpktGR--PLMERTVLIANTSNMPVAAREASIYTGITIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 384 EYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPErtGSVTIVGAVSPPG 463
Cdd:COG1155 317 EYYRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 464 GDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALETFY-EQFDPDFINIRTKAREVLQREDDLNEIV 542
Cdd:COG1155 395 GDFSEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYdENVDPDWSELRNEAMDLLQEEAELQEIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 543 QLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGagsdgqkISYTLIKH 622
Cdd:COG1155 475 RLVGEDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKG-------VPLSEIKE 547
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2113159344 623 rmGDLFYRLVSQKFEDPAEgeaaLVAKFQKLHEDLTNGFRNL 664
Cdd:COG1155 548 --LPLREKIARMKYSPENE----LLEKFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
68-667 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 899.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 68 GYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 147
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 148 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDTLWEFQPKKiGEGDLLTGGDLYATVFENSLMQHHIALPPDNMGKITYI 227
Cdd:PRK04192 85 FDGIQRPLDELAEKSGD-FLERGVYVPALDREKKWEFTPTV-KVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 228 APPGQYSLQDTVLELE-FQGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 306
Cdd:PRK04192 163 VSEGDYTVDDTIAVLEdEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 307 ISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTmtlpD---GReeSVMKRTTLVANTSNMPVAAREASIYTGITLA 383
Cdd:PRK04192 243 TQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELI----DpktGR--PLMERTVLIANTSNMPVAAREASIYTGITIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 384 EYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPErtGSVTIVGAVSPPG 463
Cdd:PRK04192 317 EYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 464 GDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALETFY-EQFDPDFINIRTKAREVLQREDDLNEIV 542
Cdd:PRK04192 395 GDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWeENVDPDWRELRDEAMDLLQREAELQEIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 543 QLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAgsdgqkisyTLIKH 622
Cdd:PRK04192 475 RLVGPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGV---------PVSEI 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 2113159344 623 RMGDLFYRLVSQKFEDPAEGEaalvAKFQKLHEDLTNGFRNLEDE 667
Cdd:PRK04192 546 LELEVRDRIARLKYIPENEYL----EKIDEIFEKLEEELEELIAE 586
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
68-657 |
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: 825.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 68 GYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 147
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 148 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDTLWEFQPKkIGEGDLLTGGDLYATVFENSLMQHHIALPPDNMGKITYI 227
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGD-FIARGVDAPGLDRDKKWHFKPT-VKEGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 228 APPGQYSLQDTVLELEFQGvKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVI 307
Cdd:TIGR01043 160 AEEGDYTVEDTIAVVDTDG-DEEIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 308 SQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLtmtlPDGRE-ESVMKRTTLVANTSNMPVAAREASIYTGITLAEYF 386
Cdd:TIGR01043 239 QHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPEL----KDPKTgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 387 RDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERTGSVTIVGAVSPPGGDF 466
Cdd:TIGR01043 315 RDMGYDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 467 SDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTAL-ETFYEQFDPDFINIRTKAREVLQREDDLNEIVQLV 545
Cdd:TIGR01043 395 SEPVTQNTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVqDWWHENVDPDWREMRDEAMDLLQKESELQEIVQLV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 546 GKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGSDgqKISYTLIKHRMG 625
Cdd:TIGR01043 475 GPDALPERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVE--EILKLEVKEEIG 552
|
570 580 590
....*....|....*....|....*....|..
gi 2113159344 626 DLfyrlvsqKFEDPAEGEAALVAKFQKLHEDL 657
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 ... |
134-506 |
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: 620.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 134 PLSVELGPGILGNIFDGIQRPLKTIAKrSGDVYIPRGVSVpaldkdtlwefqpkkigegdlltggdlyatvfenslmqhh 213
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAE-TGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 214 ialppdnmgkityiappgqyslqdtvlelefqgvkkkftmlQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGT 293
Cdd:cd01134 40 -----------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 294 CAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLpdgREESVMKRTTLVANTSNMPVAARE 373
Cdd:cd01134 79 AAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPI---TGESLMERTVLIANTSNMPVAARE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 374 ASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERTGSV 453
Cdd:cd01134 156 ASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSV 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2113159344 454 TIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKY 506
Cdd:cd01134 236 TIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
305-657 |
1.38e-123 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 391.69 E-value: 1.38e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 305 TVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTmtlPDGREESVMKRTTLVANTSNMPVAAREASIYTGITLAE 384
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLK---DPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 385 YFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERTGSVTIVGAVSPPGG 464
Cdd:PRK14698 747 YFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGG 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 465 DFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALETFYEQ-FDPDFINIRTKAREVLQREDDLNEIVQ 543
Cdd:PRK14698 827 DFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKnVDPEWKAMRDKAMELLQKEAELQEIVR 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 544 LVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERGAGSdgQKISYTLIKHR 623
Cdd:PRK14698 907 IVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPL--EEIAKLPVREE 984
|
330 340 350
....*....|....*....|....*....|....
gi 2113159344 624 MGDLfyrlvsqKFEDPAEGEAALVAKFQKLHEDL 657
Cdd:PRK14698 985 IGRM-------KFEPDIEKIKALIDKTNEQFDEL 1011
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
278-504 |
4.44e-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: 315.06 E-value: 4.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 278 GQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPqltmtlpdgrEESVMKR 357
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELL----------GSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 358 TTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYER 437
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113159344 438 AGKVKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYS 504
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 ... |
253-506 |
6.49e-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: 280.88 E-value: 6.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 253 MLQTWPVRTPRP-VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNS---DAVVYVGCGER 328
Cdd:cd19476 28 TKQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKahaGVVVFAGIGER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 329 GNEMAEVLMDFPqltmtlpdgrEESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALR 408
Cdd:cd19476 108 GREVNDLYEEFT----------KSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 409 EISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKL 488
Cdd:cd19476 178 EMSALLGEPPGREGYPPYLFTKLATLYERAGKVK-----DGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSREL 252
|
250
....*....|....*...
gi 2113159344 489 AQRKHFPSVNWLISYSKY 506
Cdd:cd19476 253 ARKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
68-306 |
3.55e-75 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 260.72 E-value: 3.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 68 GYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNI 147
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 148 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDTLWEFQPkKIGEGDLLTGGDLYATVFENSLMQHHIALPPDNMGKITYI 227
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFIP-KVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 228 APPGQYSLQDTVLELEF-QGVKKKFTMLQTWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 306
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 ... |
148-269 |
6.94e-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: 199.16 E-value: 6.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 148 FDGIQRPLKTIAKRSGDvYIPRGVSVPALDKDTLWEFQPKkIGEGDLLTGGDLYATVFENSLMQHHIALPPDNMGKITYI 227
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTPT-VKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTEI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2113159344 228 APPGQYSLQDTVLELEFQGVKKKFTMLQTWPVRTPRPVASKL 269
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 ... |
521-627 |
8.83e-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: 171.42 E-value: 8.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 521 FINIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLA 600
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....*..
gi 2113159344 601 NQAVERGAgsDGQKISYTLIKHRMGDL 627
Cdd:cd18111 81 LEALEKGV--PLSKILELPVREKIARM 105
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
54-578 |
1.00e-41 |
|
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: 157.15 E-value: 1.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 54 RLTTFEDSEKESEYGYVRKVSGPVVVADGMAgAAMYELVRV----GHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVL 129
Cdd:TIGR01026 11 RLCQEMDLRLVKRVGRVTKVKGLLIEAVGPQ-ASVGDLCLIerrgSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 130 RTHKPLSVELGPGILGNIFDGIQRPLKTiakrsgdvyiprgvsvpaldkdtlwefqpkkigegdlltGGDLYATVFENSL 209
Cdd:TIGR01026 90 ATGEGLSIKVGDGLLGRVLDGLGKPIDG---------------------------------------KGKFLDNVETEGL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 210 MQHHIAlpPDNMGKITYIappgqyslqdtvlelefqgvkkkftmlqtwpvrtprpvasklaadtpLLTGQRVLDALFPSV 289
Cdd:TIGR01026 131 ITAPIN--PLKRAPIREI-----------------------------------------------LSTGVRSIDGLLTVG 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 290 LGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEmaevLMDFPQltmtlPDGREESvMKRTTLVANTSNMPV 369
Cdd:TIGR01026 162 KGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGRE----VREFIE-----HDLGEEG-LKRSVVVVATSDQSP 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 370 AAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpER 449
Cdd:TIGR01026 232 LLRLKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGA-------SG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 450 TGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALETfYEQFDpdfinIRTKAR 529
Cdd:TIGR01026 305 KGSITAFYTVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVS-EEHRR-----AARKFR 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2113159344 530 EVL---QREDDLNEI-VQLVGKDalAEGDKITLETAKLlrEDYLAQNAFTPYD 578
Cdd:TIGR01026 379 ELLskyKDNEDLIRIgAYQRGSD--RELDFAIAKYPKL--ERFLKQGINEKVN 427
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
67-505 |
4.16e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 152.66 E-value: 4.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 67 YGYVRKVsGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGN 146
Cdd:PRK06820 30 RGPIVEI-GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 147 IFDGIQRPLktiakrsgdvyiprgvsvpaldkdtlwefqpkkigEGDLLTGGDLYatvfenslmqhhialPPDNmgkity 226
Cdd:PRK06820 109 ILDGLGAPI-----------------------------------DGGPPLTGQWR---------------ELDC------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 227 iaPPgqyslqdtvlelefqgvkkkftmlqtwpvrtPRPVASKLAaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 306
Cdd:PRK06820 133 --PP-------------------------------PSPLTRQPI-EQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKST 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 307 ISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQLTMTlPDGREesvmkRTTLVANTSNMPVAAREASIYTGITLAEYF 386
Cdd:PRK06820 179 LLGMLCADSAADVMVLALIGERGREVRE----FLEQVLT-PEARA-----RTVVVVATSDRPALERLKGLSTATTIAEYF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 387 RDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAgkvkclgGPERTGSVTIVGAVSPPGGDF 466
Cdd:PRK06820 249 RDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERT-------GNSDRGSITAFYTVLVEGDDM 321
|
410 420 430
....*....|....*....|....*....|....*....
gi 2113159344 467 SDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 505
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 ... |
67-133 |
5.28e-40 |
|
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: 140.74 E-value: 5.28e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113159344 67 YGYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHK 133
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
255-505 |
6.32e-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: 141.93 E-value: 6.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 255 QTWPVRTPRPVASKLAA-DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEma 333
Cdd:cd01136 30 ERRPLIAAPPNPLKRAPiEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 334 evLMDFPQLTMtlpdgrEESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGR 413
Cdd:cd01136 108 --VREFIEKDL------GEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 414 LAEMPADSGYPAYLAARLASFYERAgkvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKH 493
Cdd:cd01136 180 AGEPPTRRGYPPSVFALLPRLLERA-------GNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGH 252
|
250
....*....|..
gi 2113159344 494 FPSVNWLISYSK 505
Cdd:cd01136 253 YPAIDVLASISR 264
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
67-498 |
2.66e-37 |
|
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: 144.40 E-value: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 67 YGYVRKVSGPVVVADGMaGAAMYELVRV---GHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGI 143
Cdd:COG1157 20 SGRVTRVVGLLIEAVGP-DASIGELCEIetaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 144 LGNIFDGIQRPLktiakrsgdvyiprgvsvpaldkDtlwefqpkkiGEGdLLTGGDLYATvfenslmqhhIALPPDNMGK 223
Cdd:COG1157 99 LGRVLDGLGRPL-----------------------D----------GKG-PLPGEERRPL----------DAPPPNPLER 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 224 ityiappgqyslqdtvlelefqgvkkkftmlqtwpvrtpRPVasklaaDTPLLTGQRVLDALFPSVLG---GTCAipGAf 300
Cdd:COG1157 135 ---------------------------------------ARI------TEPLDTGVRAIDGLLTVGRGqriGIFA--GS- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 301 GCGKTVISQALSKYSNSDAVVyVG-CGERGNEmaevLMDFpqLTMTL-PDGreesvMKRTTLVANTSNMPVAAREASIYT 378
Cdd:COG1157 167 GVGKSTLLGMIARNTEADVNV-IAlIGERGRE----VREF--IEDDLgEEG-----LARSVVVVATSDEPPLMRLRAAYT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 379 GITLAEYFRDMGYNVSMMADSTSRWAEALREISgrLA--EMPADSGYPAYLAARLASFYERAgkvkclgGPERTGSVTIV 456
Cdd:COG1157 235 ATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIG--LAagEPPATRGYPPSVFALLPRLLERA-------GNGGKGSITAF 305
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2113159344 457 GAVSPPGGDFSDPVTSATLS-----IVqvfwgLDKKLAQRKHFPSVN 498
Cdd:COG1157 306 YTVLVEGDDMNDPIADAVRGildghIV-----LSRKLAERGHYPAID 347
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
256-574 |
3.37e-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: 144.86 E-value: 3.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 256 TWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSK---YSNSDAVVYVGCGER--- 328
Cdd:TIGR01039 107 RWPIHRKAPSFEEQSTKVEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINniaKEHGGYSVFAGVGERtre 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 329 GN----EMAEvlmdfpqltmtlpdgreESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDM-GYNVSMMADSTSRW 403
Cdd:TIGR01039 187 GNdlyhEMKE-----------------SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDNIFRF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 404 AEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWG 483
Cdd:TIGR01039 250 TQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTK-------TGSITSVQAVYVPADDLTDPAPATTFAHLDATTV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 484 LDKKLAQRKHFPSVNWLISYSKYSTALETFYEQFDpdfinIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKL 563
Cdd:TIGR01039 323 LSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYD-----VARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARR 397
|
330
....*....|.
gi 2113159344 564 LrEDYLAQNAF 574
Cdd:TIGR01039 398 I-QRFLSQPFF 407
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
262-544 |
5.52e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 128.96 E-value: 5.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 262 PRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQ 341
Cdd:PRK08149 122 PPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTE----FVE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 342 lTMTLPDGREesvmkRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADS 421
Cdd:PRK08149 198 -SLRASSRRE-----KCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 422 GYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLI 501
Cdd:PRK08149 272 GYPASVFDSLPRLLERPGATL-------AGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLK 344
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2113159344 502 SYSKystaleTFYEQFDPDFINIRTKAREVLQREDDLNEIVQL 544
Cdd:PRK08149 345 SVSR------VFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDL 381
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
68-504 |
8.48e-32 |
|
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: 127.98 E-value: 8.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 68 GYVRKVSGPVVVADGMAGA--AMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILG 145
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPvgSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 146 NIFDGIQRPLKTIakrsgdvyiprgvsvPALDKDTLWEFQPKKIgegdlltggdlyatvfeNSLMQHHIalppdnmgkit 225
Cdd:TIGR03496 81 RVIDGLGRPLDGK---------------GPLDAGERVPLYAPPI-----------------NPLKRAPI----------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 226 yiappgqyslqdtvlelefqgvkkkftmlqtwpvrtprpvasklaaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKT 305
Cdd:TIGR03496 118 ----------------------------------------------DEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKS 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 306 VISQALSKYSNSDAVVyVG-CGERGNEMAEVLMDfpqltmTLPdgreESVMKRTTLVANTSNMPVAAREASIYTGITLAE 384
Cdd:TIGR03496 152 TLLGMMARYTEADVVV-VGlIGERGREVKEFIED------ILG----EEGLARSVVVAATADESPLMRLRAAFYATAIAE 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 385 YFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclgGPERTGSVTIVGAVSPPGG 464
Cdd:TIGR03496 221 YFRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGN-----GEEGKGSITAFYTVLVEGD 295
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2113159344 465 DFSDPVTSATLSIVQvfwG---LDKKLAQRKHFPSVNWLISYS 504
Cdd:TIGR03496 296 DQQDPIADAARAILD---GhivLSRELAEQGHYPAIDILASIS 335
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
262-552 |
2.33e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 127.56 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 262 PRPVASKLAaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDfpq 341
Cdd:PRK06936 134 PAPMSRRLI-ETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIES--- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 342 ltmtlpDGREESvMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADS 421
Cdd:PRK06936 210 ------DLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 422 GYPAYLAARLASFYERAgkvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLI 501
Cdd:PRK06936 283 GYPPSVFAALPRLMERA-------GQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLR 355
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2113159344 502 SYSKYSTALetfyeqFDPDFINIRTKAREVLQREDDLNEIVQL----VGKDALAE 552
Cdd:PRK06936 356 SASRVMNQI------VSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEAD 404
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
258-544 |
3.46e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 127.02 E-value: 3.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 258 PVRTPRPVA-SKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVL 336
Cdd:PRK08927 124 PLRAPPPPAhSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 337 MDfpqltmTL-PDGreesvMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLA 415
Cdd:PRK08927 204 QD------DLgPEG-----LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 416 EMPADSGYPAYLAARLASFYERAGKvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFP 495
Cdd:PRK08927 273 EPPTTKGYTPTVFAELPRLLERAGP-----GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYP 347
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2113159344 496 SVNWLISYSKystaleTFYEQFDPDFINIRTKAREVLQREDDLNEIVQL 544
Cdd:PRK08927 348 AINVLKSVSR------TMPGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
83-505 |
1.04e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 125.45 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 83 MAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKtiakrs 162
Cdd:PRK07594 37 LPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD------ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 163 gDVYIPRGvsvPALDKDtlwefqpkkigegdlltggdlyatvfenslmqhhiALPPdnmgkityiappgqyslqdtvlel 242
Cdd:PRK07594 111 -GRELPDV---CWKDYD-----------------------------------AMPP------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 243 efqgvkkkftmlqtwPVRTPRPVASklaadtPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVY 322
Cdd:PRK07594 128 ---------------PAMVRQPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 323 VGCGERGNEMAEvlmdFPQLTMTlpdgreESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSR 402
Cdd:PRK07594 187 VLIGERGREVRE----FIDFTLS------EETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 403 WAEALREISGRLAEMPADSGYPAYLAARLASFYERAGkvkcLGgpeRTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFW 482
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG----MG---EKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHI 329
|
410 420
....*....|....*....|...
gi 2113159344 483 GLDKKLAQRKHFPSVNWLISYSK 505
Cdd:PRK07594 330 VLSRRLAERGHYPAIDVLATLSR 352
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
261-505 |
1.67e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 122.03 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 261 TPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDfp 340
Cdd:PRK06002 135 TAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLED-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 341 qltmTLPDGREESVmkrtTLVANTSNMPVAAREASIyTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPAD 420
Cdd:PRK06002 213 ----TLADNLKKAV----AVVATSDESPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 421 SGYPAYLAARLASFYERAGKvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWL 500
Cdd:PRK06002 284 RGYPPSVFSELPRLLERAGP-----GAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPL 358
|
....*
gi 2113159344 501 ISYSK 505
Cdd:PRK06002 359 ASISR 363
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
66-571 |
3.88e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 118.00 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 66 EYGYVRKVSGPVVVADGMAGAAMYELVRVGHDN---LIGEIIRLEGDSATIQVYEETAGLMVNDPVLR-THKPLSVELGP 141
Cdd:PRK04196 3 EYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNgekRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 142 GILGNIFDGIQRPL----KTIAKRSGDV---------------YIPRGVSvpALDkdtlwefqpkkiGEGDLLTGGDLya 202
Cdd:PRK04196 83 DMLGRIFDGLGRPIdggpEIIPEKRLDIngapinpvareypeeFIQTGIS--AID------------GLNTLVRGQKL-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 203 TVFENSLMQHhialppdnmgkityiappgqyslqdtvlelefqgvkkkftmlqtwpvrtprpvaSKLAAdtplltgQRVL 282
Cdd:PRK04196 147 PIFSGSGLPH------------------------------------------------------NELAA-------QIAR 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 283 DAlfpSVLGGTcaipgafgcgktvisqalSKYsnsdAVVYVGCGERgNEMAEVLMDfpqltmtlpDGREESVMKRTTLVA 362
Cdd:PRK04196 166 QA---KVLGEE------------------ENF----AVVFAAMGIT-FEEANFFME---------DFEETGALERSVVFL 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 363 NTSNMPVAAREASIYTGITLAEYFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGK 440
Cdd:PRK04196 211 NLADDPAIERILTPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGR 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 441 VKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSkystaletfyeqfd 518
Cdd:PRK04196 290 IK-----GKKGSITQIPILTMPDDDITHPIPDLTGYITegQIV--LSRELHRKGIYPPIDVLPSLS-------------- 348
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113159344 519 pdfiniRTKAR---EVLQRED----------------DLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQ 571
Cdd:PRK04196 349 ------RLMKDgigEGKTREDhkdvanqlyaayargkDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQ 414
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
66-571 |
4.16e-28 |
|
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 440770 [Multi-domain] Cd Length: 462 Bit Score: 117.94 E-value: 4.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 66 EYGYVRKVSGPVVVADGMAGAAMYELVRV-GHDNLI--GEIIRLEGDSATIQVYEETAGLMVNDPVLR-THKPLSVELGP 141
Cdd:COG1156 5 EYRTISEIAGPLLFVEGVEGVGYGELVEIeLPDGERrrGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 142 GILGNIFDGIQRPL----KTIAKRSGDV---------------YIPRGVSvpALDkdtlwefqpkkiGEGDLLTGGDLya 202
Cdd:COG1156 85 DMLGRVFNGLGRPIdggpPIIPEKRLDIngspinpvareypreFIQTGIS--AID------------GLNTLVRGQKL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 203 TVFENSLMQHhialppdnmgkityiappgqyslqdtvlelefqgvkkkftmlqtwpvrtprpvaSKLAAdtplltgQRVL 282
Cdd:COG1156 149 PIFSGSGLPH------------------------------------------------------NELAA-------QIAR 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 283 DAlfpSVLGGTcaipGAFgcgktvisqalskysnsdAVVYVGCGERGNEMAEVLMDFpqltmtlpdgrEES-VMKRTTLV 361
Cdd:COG1156 168 QA---KVRGEE----EKF------------------AVVFAAMGITHDEANFFREEF-----------EETgALDRVVMF 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 362 ANTSNMPVAAREASIYTGITLAEYFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAG 439
Cdd:COG1156 212 LNLADDPAIERIITPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAG 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 440 KVKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSkystaletfyeqf 517
Cdd:COG1156 291 RIK-----GRKGSITQIPILTMPNDDITHPIPDLTGYITegQIV--LSRDLHRKGIYPPIDVLPSLS------------- 350
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113159344 518 dpdfiniRTKAR---EVLQRED----------------DLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQ 571
Cdd:COG1156 351 -------RLMKDgigEGKTREDhadvanqlyaayargqEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQ 416
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
273-505 |
7.82e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 116.75 E-value: 7.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 273 TPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVL-MDFPqltmtlPDGre 351
Cdd:PRK07721 140 EPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIALIGERGREVREFIeRDLG------PEG-- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 352 esvMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARL 431
Cdd:PRK07721 212 ---LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAIL 288
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113159344 432 ASFYERAGKvkclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 505
Cdd:PRK07721 289 PKLLERTGT-------NASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSR 355
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
255-575 |
2.21e-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: 112.88 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 255 QTWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQAL--------SKYSnsdavVYVGC 325
Cdd:COG0055 109 ERRPIHRPAPPFEEQSTKTEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELihniakehGGVS-----VFAGV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 326 GER---GNEMaevlmdfpQLTMtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRD-MGYNVSMMADSTS 401
Cdd:COG0055 184 GERtreGNDL--------YREM-----KESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFIDNIF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 402 RWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLS----- 476
Cdd:COG0055 251 RFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAhldat 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 477 IVqvfwgLDKKLAQRKHFPSVNWLISYSKystaletfyeQFDPDFI-----NIRTKAREVLQREDDLNEIVQLVGKDALA 551
Cdd:COG0055 324 TV-----LSRKIAELGIYPAVDPLDSTSR----------ILDPLIVgeehyRVAREVQRILQRYKELQDIIAILGMDELS 388
|
330 340
....*....|....*....|....*
gi 2113159344 552 EGDKITLETA-KLLRedYLAQNAFT 575
Cdd:COG0055 389 EEDKLTVARArKIQR--FLSQPFFV 411
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
301-498 |
9.31e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 110.95 E-value: 9.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 301 GCGKTVISQALSKYSNSDAVVyVG-CGERGNEMAEVLMDfpqltMTLPDGREESVmkrttLVANTSNMPVAAREASIYTG 379
Cdd:PRK08972 172 GVGKSVLLGMMTRGTTADVIV-VGlVGERGREVKEFIEE-----ILGEEGRARSV-----VVAAPADTSPLMRLKGCETA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 380 ITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclgGPERTGSVTIVGAV 459
Cdd:PRK08972 241 TTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGN-----GGPGQGSITAFYTV 315
|
170 180 190
....*....|....*....|....*....|....*....
gi 2113159344 460 SPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVN 498
Cdd:PRK08972 316 LTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAID 354
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
67-594 |
9.68e-26 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 110.63 E-value: 9.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 67 YGYVRKVSGPVVVADGMAgAAMYEL--VRVGHDNLI--GEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPG 142
Cdd:PRK09099 25 TGKVVEVIGTLLRVSGLD-VTLGELceLRQRDGTLLqrAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 143 ILGNIFDGIQRPLKtiakrsgdvyiprgvSVPALDKDtlwEFQPKkigegdlltggdlyatvfenslmqhhIALPPDNMg 222
Cdd:PRK09099 104 LLGRVIDGLGEPID---------------GGGPLDCD---ELVPV--------------------------IAAPPDPM- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 223 kityiappgqyslqdtvlelefqgvkkkftmlqtwpvrtprpvaSKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGC 302
Cdd:PRK09099 139 --------------------------------------------SRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 303 GKTVISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQLTMTlPDGreesvMKRTTLVANTSNMPVAAREASIYTGITL 382
Cdd:PRK09099 175 GKSTLMGMFARGTQCDVNVIALIGERGREVRE----FIELILG-EDG-----MARSVVVCATSDRSSIERAKAAYVATAI 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 383 AEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpERTGSVTIVGAVSPP 462
Cdd:PRK09099 245 AEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM-------GETGSITALYTVLAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 463 GGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALetfyeqFDPDFINIRTKAREVLQREDDLNEIV 542
Cdd:PRK09099 318 DESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQV------VPREHVQAAGRLRQLLAKHREVETLL 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2113159344 543 QL----VGKDALAEGdkiTLETAKLLReDYLAQnaftPYDKFCPFYKSVWMMRNII 594
Cdd:PRK09099 392 QVgeyrAGSDPVADE---AIAKIDAIR-DFLSQ----RTDEYSDPDATLAALAELS 439
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
255-505 |
3.59e-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: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 255 QTWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQAL----SKySNSDAVVYVGCGERG 329
Cdd:cd01133 30 ERWPIHREAPEFVELSTEQEILeTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinniAK-AHGGYSVFAGVGERT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 330 NEMAEVLMDfpqltMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDM-GYNVSMMADSTSRWAEALR 408
Cdd:cd01133 109 REGNDLYHE-----MKESGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 409 EISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKL 488
Cdd:cd01133 184 EVSALLGRIPSAVGYQPTLATEMGSLQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGI 256
|
250
....*....|....*..
gi 2113159344 489 AQRKHFPSVNWLISYSK 505
Cdd:cd01133 257 AELGIYPAVDPLDSTSR 273
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
255-574 |
1.07e-22 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 102.04 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 255 QTWPVRTPRPVASKLaaDTPLL---TGQRVLDALFPSVLGGTCAIPGAFGCGKTV--------ISQALSKYSnsdavVYV 323
Cdd:CHL00060 124 TTSPIHRSAPAFIQL--DTKLSifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVlimelinnIAKAHGGVS-----VFG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 324 GCGERGNEMAEVLMDFPQLTMTLPDGREESvmkRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGY-NVSMMADSTSR 402
Cdd:CHL00060 197 GVGERTREGNDLYMEMKESGVINEQNIAES---KVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFR 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 403 WAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFW 482
Cdd:CHL00060 274 FVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-------EGSITSIQAVYVPADDLTDPAPATTFAHLDATT 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 483 GLDKKLAQRKHFPSVNWLISyskYSTAL------ETFYEqfdpdfinIRTKAREVLQREDDLNEIVQLVGKDALAEGDKI 556
Cdd:CHL00060 347 VLSRGLAAKGIYPAVDPLDS---TSTMLqprivgEEHYE--------TAQRVKQTLQRYKELQDIIAILGLDELSEEDRL 415
|
330
....*....|....*...
gi 2113159344 557 TLETAKLLrEDYLAQNAF 574
Cdd:CHL00060 416 TVARARKI-ERFLSQPFF 432
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
272-505 |
6.15e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 99.42 E-value: 6.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 272 DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFpqltmtlpdgRE 351
Cdd:PRK05688 149 SEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHI----------LG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 352 ESVMKRTTLVANTSN-MPVAAREASIYTgITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAAR 430
Cdd:PRK05688 219 EEGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAK 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113159344 431 LASFYERAGKVKClGGpertGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 505
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 ... |
309-505 |
1.04e-21 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 95.75 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 309 QA-LSKYSNSDAVVYVGCGERgNEMAEVLMDfpqltmtlpDGREESVMKRTTLVANTSNMPVAAReasIYT---GITLAE 384
Cdd:cd01135 92 QAgVVGSEENFAIVFAAMGVT-MEEARFFKD---------DFEETGALERVVLFLNLANDPTIER---IITprmALTTAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 385 YFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggpERTGSVTIVGAVSPP 462
Cdd:cd01135 159 YLAyEKGKHVlVILTDMTN-YAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVE-----GRKGSITQIPILTMP 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2113159344 463 GGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSK 505
Cdd:cd01135 233 NDDITHPIPDLTGYITegQIY--LDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
275-581 |
4.07e-21 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 96.78 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 275 LLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAevlmDFPQLTMTlPDGREESV 354
Cdd:PRK07960 159 LDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVK----DFIENILG-AEGRARSV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 355 MkrttLVANTSNMPVAAREASIYtGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASF 434
Cdd:PRK07960 234 V----IAAPADVSPLLRMQGAAY-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPAL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 435 YERAGKvkclgGPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTAL--ET 512
Cdd:PRK07960 309 VERAGN-----GISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALidEQ 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113159344 513 FYEQfdpdfinIRTkAREVL---QREDDlneivqLVGKDALAEGDKITLETAKLL---REDYLAQNAFTP--YDKFC 581
Cdd:PRK07960 384 HYAR-------VRQ-FKQLLssfQRNRD------LVSVGAYAKGSDPMLDKAIALwpqLEAFLQQGIFERadWEDSL 446
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
268-505 |
8.14e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 95.73 E-value: 8.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 268 KLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLmdfpqltmtlP 347
Cdd:PRK07196 132 RRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFI----------E 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 348 DGREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYL 427
Cdd:PRK07196 202 HSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSA 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113159344 428 AARLASFYERAGKvkclggPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 505
Cdd:PRK07196 282 FSIIPRLAESAGN------SSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISR 353
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
272-594 |
7.61e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 89.74 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 272 DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQLTMtlpDGRE 351
Cdd:PRK08472 138 DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPE----FIEKNL---GGDL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 352 ESvmkrTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARL 431
Cdd:PRK08472 211 EN----TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 432 ASFYERAGKvkclggPERTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALE 511
Cdd:PRK08472 287 PQLMERAGK------EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDII 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 512 TfyeqfdPDFINIRTKAREV--LQREddlNEIVQLVGkdALAEGDKITLETA---KLLREDYLAQNaftPYDKFcPFYKS 586
Cdd:PRK08472 361 S------PEHKLAARKFKRLysLLKE---NEVLIRIG--AYQKGNDKELDEAiskKEFMEQFLKQN---PNELF-PFEQT 425
|
....*...
gi 2113159344 587 VWMMRNII 594
Cdd:PRK08472 426 FEQLEEIL 433
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
185-538 |
1.38e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 88.88 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 185 QPKKIGEGDLLTggdlyatvfensLMQHHIALPPDN--MGKItyiappgqYSLQDTVLELEFQGVKkkftmLQTWPVRTP 262
Cdd:PRK06793 72 QTEKVCYGDSVT------------LIAEDVVIPRGNhlLGKV--------LSANGEVLNEEAENIP-----LQKIKLDAP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 263 RPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAevlmDFPQ 341
Cdd:PRK06793 127 PIHAFEREEITDVFeTGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVK----DFIR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 342 LTMTlpdgreESVMKRTTLVANTSNMP--VAAREASIYTGItlAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPA 419
Cdd:PRK06793 203 KELG------EEGMRKSVVVVATSDEShlMQLRAAKLATSI--AEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 420 dSGYPAYLAARLASFYERAGKVKclggperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNW 499
Cdd:PRK06793 275 -GGKTLLMESYMKKLLERSGKTQ-------KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISV 346
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2113159344 500 LISYSKystaleTFYEQFDPDFINIRTKAREVLQ--REDDL 538
Cdd:PRK06793 347 LDSVSR------IMEEIVSPNHWQLANEMRKILSiyKENEL 381
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
53-454 |
6.73e-18 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 87.28 E-value: 6.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 53 ARLTTFEDSEKESEYGYVRKVSGPVVVADGMAGAAMYELVRVGhDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTH 132
Cdd:PRK13343 14 QRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFE-GGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 133 KPLSVELGPGILGNIFDGIQRPLKtiakrsgdvyiprgvsvpaldkdtlwefqpkkiGEGdlltggdlyatvfenslmqh 212
Cdd:PRK13343 93 RVLEVPVGDGLLGRVIDPLGRPLD---------------------------------GGG-------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 213 hiALPPDNMGKITYIAPPgqyslqdtVLELEFqgvkkkftmlqtwpvrtprpvasklaADTPLLTGQRVLDALFPSVLGG 292
Cdd:PRK13343 120 --PLQATARRPLERPAPA--------IIERDF--------------------------VTEPLQTGIKVVDALIPIGRGQ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 293 TCAIPGAFGCGKTVIS-QALSKYSNSDAV-VYVGCGERGNEMAEVLMdfpqltmTLpdgREESVMKRTTLVANTSNMPVA 370
Cdd:PRK13343 164 RELIIGDRQTGKTAIAiDAIINQKDSDVIcVYVAIGQKASAVARVIE-------TL---REHGALEYTTVVVAEASDPPG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 371 AREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPA---YLAARLasfYERAGKV-KCLGG 446
Cdd:PRK13343 234 LQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRL---LERAAKLsPELGG 310
|
....*...
gi 2113159344 447 pertGSVT 454
Cdd:PRK13343 311 ----GSLT 314
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
348-574 |
6.99e-17 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 83.62 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 348 DGREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFR-DMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAY 426
Cdd:TIGR01040 203 DFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGY 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 427 LAARLASFYERAGKVKclggpERTGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYS 504
Cdd:TIGR01040 283 MYTDLATIYERAGRVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPINVLPSLS 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113159344 505 KY--STALETFYEQFDPDFINiRTKAREVLQRedDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAF 574
Cdd:TIGR01040 356 RLmkSAIGEGMTRKDHSDVSN-QLYACYAIGK--DVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPY 424
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
258-581 |
4.47e-16 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 81.10 E-value: 4.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 258 PVRTPRPVA-SKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVL 336
Cdd:PRK05922 123 PLFSSPPSPmSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 337 MDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAE 416
Cdd:PRK05922 203 EQH----------KEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 417 MPADSGYPAYLAARLASFYERAGKvkclggpERTGSVTIVGAV--SPPGGD-FSDPVTSAtlsivqvfwgLDKKL---AQ 490
Cdd:PRK05922 273 TLSAHHYAASVFHHVSEFTERAGN-------NDKGSITALYAIlhYPNHPDiFTDYLKSL----------LDGHFfltPQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 491 RKHF--PSVNWLISYSKYSTALETfyeqfdPDFINIRTKAREVLQREDDLNEIVQLvgkDALAEGDKITLETA-KLLR-- 565
Cdd:PRK05922 336 GKALasPPIDILTSLSRSARQLAL------PHHYAAAEELRSLLKAYHEALDIIQL---GAYVPGQDAHLDRAvKLLPsi 406
|
330
....*....|....*.
gi 2113159344 566 EDYLAQnaftPYDKFC 581
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 ... |
274-505 |
9.03e-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: 77.98 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 274 PLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIsqALSKYSNSDA----VVYVGCGERGNEMAevlmdfpQLTMTLpdg 349
Cdd:cd01132 52 PLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAI--AIDTIINQKGkkvyCIYVAIGQKRSTVA-------QIVKTL--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 350 REESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPA---Y 426
Cdd:cd01132 120 EEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 427 LAARLasfYERAGKVK-CLGGpertGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISY 503
Cdd:cd01132 200 LHSRL---LERAAKLSdELGG----GSLTALPIIETQAGDVSAYIPTNVISITdgQIF--LESELFNKGIRPAINVGLSV 270
|
..
gi 2113159344 504 SK 505
Cdd:cd01132 271 SR 272
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
261-509 |
7.19e-14 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 74.61 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 261 TPRP-VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIsqALSKYSN---SDAV-VYVGCGERGNEMAEV 335
Cdd:CHL00059 110 SPAPgIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAV--ATDTILNqkgQNVIcVYVAIGQKASSVAQV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 336 LMDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISGRLA 415
Cdd:CHL00059 188 VTTL----------QERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 416 EMPADSGYPA---YLAARLasfYERAGKV-KCLGGpertGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLA 489
Cdd:CHL00059 258 RPPGREAYPGdvfYLHSRL---LERAAKLsSQLGE----GSMTALPIVETQAGDVSAYIPTNVISITdgQIF--LSADLF 328
|
250 260
....*....|....*....|
gi 2113159344 490 QRKHFPSVNWLISYSKYSTA 509
Cdd:CHL00059 329 NAGIRPAINVGISVSRVGSA 348
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
70-131 |
5.94e-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: 64.10 E-value: 5.94e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113159344 70 VRKVSGPVVVADGMAGAA--MYELVRVGHDN----LIGEIIRLEGDSATIQVYEETAGLMVNDPVLRT 131
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, ... |
67-128 |
1.53e-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: 63.10 E-value: 1.53e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113159344 67 YGYVRKVSGPVVVADGMAGAAMYELVRVGHDN------LIGEIIRLEGDSATIQVYEETAGLMVNDPV 128
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDgnnetvLKAEVIGFRGDRAILQLFESTRGLSRGALV 68
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
265-511 |
2.65e-11 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 66.60 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 265 VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIS------------QALSKysNSDAVVYVGCGERGNEM 332
Cdd:PTZ00185 163 IVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvstiinqvrinqQILSK--NAVISIYVSIGQRCSNV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 333 AEVLMDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREISG 412
Cdd:PTZ00185 241 ARIHRLL----------RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 413 RLAEMPADSGYPA---YLAARLasfYERAGKVKCLGGperTGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLA 489
Cdd:PTZ00185 311 LLRRPPGREAYPGdvfYLHSRL---LERAAMLSPGKG---GGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLF 384
|
250 260
....*....|....*....|..
gi 2113159344 490 QRKHFPSVNWLISYSKYSTALE 511
Cdd:PTZ00185 385 TGGQRPAVNIGLSVSRVGSSAQ 406
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
85-474 |
2.99e-11 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 65.83 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 85 GAAMYELVRV--GHDNLIGEIIRLEGDSATIQVYEETAGLMVNDPVLRTHKPLSVELGPGILGNIFDGIQRPlktiakrs 162
Cdd:PRK02118 22 GVGYGELATVerKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKP-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 163 gdvyIPRGvsvPALdkdtlwefqpkkigEGDLLTggdlyatvfenslmqhhIALPPDNmgkityiappgqyslqdtvlel 242
Cdd:PRK02118 94 ----IDGG---PEL--------------EGEPIE-----------------IGGPSVN---------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 243 efqgvkkkftmlqtwPVRtpRPVASKLAAdtpllTGqrvldalfpsvlggtcaIPG--AFGCgkTVISQALSKYSNSdav 320
Cdd:PRK02118 114 ---------------PVK--RIVPREMIR-----TG-----------------IPMidVFNT--LVESQKIPIFSVS--- 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 321 vyvgcGERGNE-MAEVLM-----------------DFPQLTMTLPDGreeSVMKRTTLVANTSNMPVAAREASIYTGITL 382
Cdd:PRK02118 150 -----GEPYNAlLARIALqaeadiiilggmgltfdDYLFFKDTFENA---GALDRTVMFIHTASDPPVECLLVPDMALAV 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 383 AEYFR-DMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAgkVKCLGGpertGSVTIVGAVSP 461
Cdd:PRK02118 222 AEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA--VDFEDG----GSITIIAVTTM 295
|
410
....*....|...
gi 2113159344 462 PGGDFSDPVTSAT 474
Cdd:PRK02118 296 PGDDVTHPVPDNT 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 ... |
66-122 |
5.15e-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: 50.12 E-value: 5.15e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 66 EYGYVRKVSGPVVVADGMAGAAMYELVRVGHDN---LIGEIIRLEGDSATIQVYEETAGL 122
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDgevRRGQVLEVSGDKAVVQVFEGTSGL 60
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
272-454 |
2.66e-07 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 53.53 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 272 DTPLLTGQRVLDALFPS-------VLG----GTCAIpgafgCGKTVISQalsKYSNsdaV--VYVGCGERGNEMAevlmd 338
Cdd:PRK09281 143 HEPLQTGIKAIDAMIPIgrgqrelIIGdrqtGKTAI-----AIDTIINQ---KGKD---VicIYVAIGQKASTVA----- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113159344 339 fpQLTMTLpdgREESVMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDMGYNVSMMADSTSRWAEALREIS------- 411
Cdd:PRK09281 207 --QVVRKL---EEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSlllrrpp 281
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2113159344 412 GRLAempadsgYPA---YLAARLasfYERAGKV-KCLGGpertGSVT 454
Cdd:PRK09281 282 GREA-------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, ... |
522-576 |
4.93e-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: 4.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2113159344 522 INIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREdYLAQNAFTP 576
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEP 55
|
|
| |
