|
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 ... |
20-611 |
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: 1258.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 20 EYGYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILG 99
Cdd:TIGR01042 1 EYGYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 100 NIFDGIQRPLKTIARISGDVYIPRGVSVPALDKDCLWEFQPNKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKIT 179
Cdd:TIGR01042 81 NIFDGIQRPLKAIAEQSQSIYIPRGVNVPALDRDKKWEFTPKKLRVGDHITGGDIYGTVFENSLIKHKIMLPPRARGTIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 180 YIAPAGQYSLKDTVIELEFQGIKKSYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKT 259
Cdd:TIGR01042 161 YIAPAGNYTVDDTVLEVEFQGVKKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 260 VISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLpDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEY 339
Cdd:TIGR01042 241 VISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEV-DGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 340 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGD 419
Cdd:TIGR01042 320 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 420 FSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEKFDPDFINIRTKAREVLQREDDLNEIVQLV 499
Cdd:TIGR01042 400 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 500 GKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERAAGmDGQKITYTLIKHRLG 579
Cdd:TIGR01042 480 GKDALAETDKITLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQ-DDNKITWSIIKESLG 558
|
570 580 590
....*....|....*....|....*....|..
gi 15219234 580 DLFYRLVSQKFEDPAEGEDTLVEKFKKLYDDL 611
Cdd:TIGR01042 559 DLLYRLSSMKFEDPSDGEAKIKADYEKLNEDM 590
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
22-618 |
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: 935.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 22 GYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNI 101
Cdd:COG1155 5 GKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLLGNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 102 FDGIQRPLKTIARISGDvYIPRGVSVPALDKDCLWEFQPNKFVeGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYI 181
Cdd:COG1155 85 FDGIQRPLDKIAEKSGD-FIPRGVDVPALDREKKWDFTPTVKV-GDKVSAGDILGTVQETPLIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 182 APAGQYSLKDTVIELE-FQGIKKSYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 260
Cdd:COG1155 163 APEGEYTVEDTIAVLEdEDGEEHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 261 ISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTmtlpD---GReeSVMKRTTLVANTSNMPVAAREASIYTGITIA 337
Cdd:COG1155 243 TQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELI----DpktGR--PLMERTVLIANTSNMPVAAREASIYTGITIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 338 EYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPErnGSVTIVGAVSPPG 417
Cdd:COG1155 317 EYYRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 418 GDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEK-FDPDFINIRTKAREVLQREDDLNEIV 496
Cdd:COG1155 395 GDFSEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDEnVDPDWSELRNEAMDLLQEEAELQEIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 497 QLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERAAGMDgqkityTLIKH 576
Cdd:COG1155 475 RLVGEDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLS------EIKEL 548
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 15219234 577 RLGDLFYRLvsqKFEDpaegEDTLVEKFKKLYDDLNAGFRAL 618
Cdd:COG1155 549 PLREKIARM---KYSP----ENELLEKFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
22-621 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 898.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 22 GYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNI 101
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 102 FDGIQRPLKTIARISGDvYIPRGVSVPALDKDCLWEFQPnKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYI 181
Cdd:PRK04192 85 FDGIQRPLDELAEKSGD-FLERGVYVPALDREKKWEFTP-TVKVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 182 APAGQYSLKDTVIELE-FQGIKKSYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 260
Cdd:PRK04192 163 VSEGDYTVDDTIAVLEdEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 261 ISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTmtlpD---GReeSVMKRTTLVANTSNMPVAAREASIYTGITIA 337
Cdd:PRK04192 243 TQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELI----DpktGR--PLMERTVLIANTSNMPVAAREASIYTGITIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 338 EYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPErnGSVTIVGAVSPPG 417
Cdd:PRK04192 317 EYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEE--GSVTIIGAVSPPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 418 GDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEK-FDPDFINIRTKAREVLQREDDLNEIV 496
Cdd:PRK04192 395 GDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEEnVDPDWRELRDEAMDLLQREAELQEIV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 497 QLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVEraAGMDGQKITYTLIKH 576
Cdd:PRK04192 475 RLVGPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALE--KGVPVSEILELEVRD 552
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 15219234 577 RLGDLFYrlvsqkfedpaEGEDTLVEKFKKLYDDLNAGFRALEDE 621
Cdd:PRK04192 553 RIARLKY-----------IPENEYLEKIDEIFEKLEEELEELIAE 586
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
22-609 |
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: 818.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 22 GYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNI 101
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 102 FDGIQRPLKTIARISGDvYIPRGVSVPALDKDCLWEFQPnKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYI 181
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGD-FIARGVDAPGLDRDKKWHFKP-TVKEGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 182 APAGQYSLKDTVIELEFQGIKKsYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVI 261
Cdd:TIGR01043 160 AEEGDYTVEDTIAVVDTDGDEE-IKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 262 SQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLtmtlPDGRE-ESVMKRTTLVANTSNMPVAAREASIYTGITIAEYF 340
Cdd:TIGR01043 239 QHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPEL----KDPKTgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 341 RDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGGDF 420
Cdd:TIGR01043 315 RDMGYDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 421 SDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTAL-ESFYEKFDPDFINIRTKAREVLQREDDLNEIVQLV 499
Cdd:TIGR01043 395 SEPVTQNTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVqDWWHENVDPDWREMRDEAMDLLQKESELQEIVQLV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 500 GKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERaaGMDGQKITYTLIKHRLG 579
Cdd:TIGR01043 475 GPDALPERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALER--GVPVEEILKLEVKEEIG 552
|
570 580 590
....*....|....*....|....*....|
gi 15219234 580 dlfyRLVSQKFEDPAEGEDTLVEKFKKLYD 609
Cdd:TIGR01043 553 ----RMKYEPDNDILAKIDEILEKIEKEFK 578
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
88-460 |
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: 619.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 88 PLSVELGPGILGNIFDGIQRPLKTIARiSGDVYIPRGVSVpaldkdclwefqpnkfvegdtitggdlyatvfentlmnhl 167
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAE-TGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 168 valppdamgkityiapagqyslkdtvielefqgikksytmlQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGT 247
Cdd:cd01134 40 -----------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 248 CAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTMTLpdgREESVMKRTTLVANTSNMPVAARE 327
Cdd:cd01134 79 AAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPI---TGESLMERTVLIANTSNMPVAARE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 328 ASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSV 407
Cdd:cd01134 156 ASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSV 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15219234 408 TIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKY 460
Cdd:cd01134 236 TIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
259-611 |
4.53e-125 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 394.00 E-value: 4.53e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 259 TVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQLTmtlPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAE 338
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLK---DPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 339 YFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKCLGGPERNGSVTIVGAVSPPGG 418
Cdd:PRK14698 747 YFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGG 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 419 DFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESFYEK-FDPDFINIRTKAREVLQREDDLNEIVQ 497
Cdd:PRK14698 827 DFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKnVDPEWKAMRDKAMELLQKEAELQEIVR 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 498 LVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLANQAVERaaGMDGQKITYTLIKHR 577
Cdd:PRK14698 907 IVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISR--GVPLEEIAKLPVREE 984
|
330 340 350
....*....|....*....|....*....|....
gi 15219234 578 LGDLfyrlvsqKFEDPAEGEDTLVEKFKKLYDDL 611
Cdd:PRK14698 985 IGRM-------KFEPDIEKIKALIDKTNEQFDEL 1011
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
232-458 |
2.64e-105 |
|
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: 316.99 E-value: 2.64e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 232 GQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPqltmtlpdgrEESVMKR 311
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELL----------GSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 312 TTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYER 391
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219234 392 AGKVKclggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYS 458
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 ... |
207-460 |
4.56e-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: 280.11 E-value: 4.56e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 207 MLQSWPVRTPRP-VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNS---DAVVYVGCGER 282
Cdd:cd19476 28 TKQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKahaGVVVFAGIGER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 283 GNEMAEVLMDFPqltmtlpdgrEESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALR 362
Cdd:cd19476 108 GREVNDLYEEFT----------KSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 363 EISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKL 442
Cdd:cd19476 178 EMSALLGEPPGREGYPPYLFTKLATLYERAGKVK-----DGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSREL 252
|
250
....*....|....*...
gi 15219234 443 AQRKHFPSVNWLISYSKY 460
Cdd:cd19476 253 ARKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
22-260 |
4.46e-73 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 253.79 E-value: 4.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 22 GYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNI 101
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 102 FDGIQRPLKTIARISGDvYIPRGVSVPALDKDCLWEFQPnKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYI 181
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFIP-KVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 182 APAGQYSLKDTVIELEF-QGIKKSYTMLQSWPVRTPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 260
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 ... |
102-223 |
8.31e-59 |
|
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the alpha-beta catalytic subunit of VATA or V-type proton ATPase catalytic subunit at the N-terminal end. It is found from bacteria to humans, and was not modelled in family ATP-synt_ab, pfam00006.
Pssm-ID: 465299 [Multi-domain] Cd Length: 120 Bit Score: 192.61 E-value: 8.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 102 FDGIQRPLKTIARISGDvYIPRGVSVPALDKDCLWEFQPnKFVEGDTITGGDLYATVFENTLMNHLVALPPDAMGKITYI 181
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTP-TVKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTEI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15219234 182 APAGQYSLKDTVIELEFQGIKKSYTMLQSWPVRTPRPVASKL 223
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 ... |
475-581 |
3.60e-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: 171.80 E-value: 3.60e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 475 FINIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAFTPYDKFCPFYKSVWMMRNIIHFYNLA 554
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....*..
gi 15219234 555 NQAVERaaGMDGQKITYTLIKHRLGDL 581
Cdd:cd18111 81 LEALEK--GVPLSKILELPVREKIARM 105
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
21-532 |
2.88e-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: 158.30 E-value: 2.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 21 YGYVRKVSGPVVVADGMAgAAMYELVRV----GHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPG 96
Cdd:TIGR01026 24 VGRVTKVKGLLIEAVGPQ-ASVGDLCLIerrgSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSIKVGDG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 97 ILGNIFDGIQRPLKTiarisgdvyiprgvsvpaldkdclwefqpnkfvegdtitGGDLYATVFENTLMnhlvaLPPdamg 176
Cdd:TIGR01026 103 LLGRVLDGLGKPIDG---------------------------------------KGKFLDNVETEGLI-----TAP---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 177 kityIAPagqysLKDTVIElefqgikksytmlqswpvrtprpvasklaadTPLLTGQRVLDALFPSVLGGTCAIPGAFGC 256
Cdd:TIGR01026 135 ----INP-----LKRAPIR-------------------------------EILSTGVRSIDGLLTVGKGQRIGIFAGSGV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 257 GKTVISQALSKYSNSDAVVYVGCGERGNEmaevLMDFPQltmtlPDGREESvMKRTTLVANTSNMPVAAREASIYTGITI 336
Cdd:TIGR01026 175 GKSTLLGMIARNTEADVNVIALIGERGRE----VREFIE-----HDLGEEG-LKRSVVVVATSDQSPLLRLKGAYVATAI 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 337 AEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpERNGSVTIVGAVSPP 416
Cdd:TIGR01026 245 AEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGA-------SGKGSITAFYTVLVE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 417 GGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESfYEKFDpdfinIRTKAREVL---QREDDLN 493
Cdd:TIGR01026 318 GDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIVS-EEHRR-----AARKFRELLskyKDNEDLI 391
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15219234 494 EI-VQLVGKDalAEGDKITLETAKLlrEDYLAQNAFTPYD 532
Cdd:TIGR01026 392 RIgAYQRGSD--RELDFAIAKYPKL--ERFLKQGINEKVN 427
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
21-452 |
4.08e-41 |
|
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: 154.80 E-value: 4.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 21 YGYVRKVSGPVVVADGMaGAAMYELVRV---GHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGI 97
Cdd:COG1157 20 SGRVTRVVGLLIEAVGP-DASIGELCEIetaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 98 LGNIFDGIQRPLKTIARISGDVYIPrgvsvpaldkdclwefqpnkfvegdtitggdlyatvfentlmnhLVALPPDAMGK 177
Cdd:COG1157 99 LGRVLDGLGRPLDGKGPLPGEERRP--------------------------------------------LDAPPPNPLER 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 178 ityiapagqyslkdtvielefqgikksytmlqswpvrtpRPVasklaaDTPLLTGQRVLDALFPSVLG---GTCAipGAf 254
Cdd:COG1157 135 ---------------------------------------ARI------TEPLDTGVRAIDGLLTVGRGqriGIFA--GS- 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 255 GCGKTVISQALSKYSNSDAVVyVG-CGERGNEmaevLMDFpqLTMTL-PDGreesvMKRTTLVANTSNMPVAAREASIYT 332
Cdd:COG1157 167 GVGKSTLLGMIARNTEADVNV-IAlIGERGRE----VREF--IEDDLgEEG-----LARSVVVVATSDEPPLMRLRAAYT 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 333 GITIAEYFRDMGYNVSMMADSTSRWAEALREISgrLA--EMPADSGYPAYLAARLASFYERAgkvkclgGPERNGSVTIV 410
Cdd:COG1157 235 ATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIG--LAagEPPATRGYPPSVFALLPRLLERA-------GNGGKGSITAF 305
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15219234 411 GAVSPPGGDFSDPVTSATLSI-----VqvfwgLDKKLAQRKHFPSVN 452
Cdd:COG1157 306 YTVLVEGDDMNDPIADAVRGIldghiV-----LSRKLAERGHYPAID 347
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
21-459 |
8.09e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 154.20 E-value: 8.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 21 YGYVRKVsGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGN 100
Cdd:PRK06820 30 RGPIVEI-GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 101 IFDGIQRPLktiarisgDVYIPRGVSVPALDKdclwefqpnkfvegdtitggdlyatvfentlmnhlvalPPdamgkity 180
Cdd:PRK06820 109 ILDGLGAPI--------DGGPPLTGQWRELDC--------------------------------------PP-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 181 iapagqyslkdtvielefqgikksytmlqswpvrtPRPVASKLAaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTV 260
Cdd:PRK06820 135 -----------------------------------PSPLTRQPI-EQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKST 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 261 ISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQLTMTlPDGREesvmkRTTLVANTSNMPVAAREASIYTGITIAEYF 340
Cdd:PRK06820 179 LLGMLCADSAADVMVLALIGERGREVRE----FLEQVLT-PEARA-----RTVVVVATSDRPALERLKGLSTATTIAEYF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 341 RDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAgkvkclgGPERNGSVTIVGAVSPPGGDF 420
Cdd:PRK06820 249 RDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERT-------GNSDRGSITAFYTVLVEGDDM 321
|
410 420 430
....*....|....*....|....*....|....*....
gi 15219234 421 SDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 459
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 ... |
21-87 |
4.90e-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: 140.35 E-value: 4.90e-40
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219234 21 YGYVRKVSGPVVVADGMAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHK 87
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
209-459 |
1.45e-39 |
|
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: 145.78 E-value: 1.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 209 QSWPVRTPRPVASKLAA-DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEma 287
Cdd:cd01136 30 ERRPLIAAPPNPLKRAPiEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 288 evLMDFPQLTMtlpdgrEESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGR 367
Cdd:cd01136 108 --VREFIEKDL------GEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 368 LAEMPADSGYPAYLAARLASFYERAgkvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKH 447
Cdd:cd01136 180 AGEPPTRRGYPPSVFALLPRLLERA-------GNGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGH 252
|
250
....*....|..
gi 15219234 448 FPSVNWLISYSK 459
Cdd:cd01136 253 YPAIDVLASISR 264
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
211-528 |
1.11e-36 |
|
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: 142.94 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 211 WPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSK---YSNSDAVVYVGCGER---G 283
Cdd:TIGR01039 108 WPIHRKAPSFEEQSTKVEILeTGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINniaKEHGGYSVFAGVGERtreG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 284 N----EMAEvlmdfpqltmtlpdgreESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSMMADSTSRWA 358
Cdd:TIGR01039 188 NdlyhEMKE-----------------SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEqGQDVLLFIDNIFRFT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 359 EALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGL 438
Cdd:TIGR01039 251 QAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTK-------TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 439 DKKLAQRKHFPSVNWLISYSKYstalesfyekFDPDFINIR-----TKAREVLQREDDLNEIVQLVGKDALAEGDKITLE 513
Cdd:TIGR01039 324 SRKIAELGIYPAVDPLDSTSRL----------LDPSVVGEEhydvaRGVQQILQRYKELQDIIAILGMDELSEEDKLTVE 393
|
330
....*....|....*
gi 15219234 514 TAKLLrEDYLAQNAF 528
Cdd:TIGR01039 394 RARRI-QRFLSQPFF 407
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
22-458 |
2.14e-34 |
|
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: 135.30 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 22 GYVRKVSGPVVVADGMAGA--AMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILG 99
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPvgSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 100 NIFDGIQRPLKTIARISGDVYIPrgvsvpaldkdclwefqpnkfvegdtitggdlyatvfentlmnhLVALPPDAMGKit 179
Cdd:TIGR03496 81 RVIDGLGRPLDGKGPLDAGERVP--------------------------------------------LYAPPINPLKR-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 180 yiapagqyslkdtvielefqgikksytmlqswpvrtpRPVasklaaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKT 259
Cdd:TIGR03496 115 -------------------------------------API------DEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKS 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 260 VISQALSKYSNSDAVVyVG-CGERGNEMAEVLMDfpqltmTLPdgreESVMKRTTLVANTSNMPVAAREASIYTGITIAE 338
Cdd:TIGR03496 152 TLLGMMARYTEADVVV-VGlIGERGREVKEFIED------ILG----EEGLARSVVVAATADESPLMRLRAAFYATAIAE 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 339 YFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclgGPERNGSVTIVGAVSPPGG 418
Cdd:TIGR03496 221 YFRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGN-----GEEGKGSITAFYTVLVEGD 295
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 15219234 419 DFSDPVTSATLSIVQvfwG---LDKKLAQRKHFPSVNWLISYS 458
Cdd:TIGR03496 296 DQQDPIADAARAILD---GhivLSRELAEQGHYPAIDILASIS 335
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
37-506 |
5.84e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 131.61 E-value: 5.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 37 MAGAAMYELVRVGHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKtiaris 116
Cdd:PRK07594 37 LPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD------ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 117 gDVYIPRGvsvPALDKDclwefqpnkfvegdtitggdlyatvfentlmnhlvALPPDAMgkityiapagqyslkdtviel 196
Cdd:PRK07594 111 -GRELPDV---CWKDYD-----------------------------------AMPPPAM--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 197 efqgikksytmlqswpvrTPRPVASklaadtPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVY 276
Cdd:PRK07594 131 ------------------VRQPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 277 VGCGERGNEMAEvlmdFPQLTMTlpdgreESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSR 356
Cdd:PRK07594 187 VLIGERGREVRE----FIDFTLS------EETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 357 WAEALREISGRLAEMPADSGYPAYLAARLASFYERAGkvkcLGgpeRNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFW 436
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG----MG---EKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHI 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15219234 437 GLDKKLAQRKHFPSVNWLISYSKYSTALESfyekfdPDFINIRTKAREVLQREDDLNEIVQL----VGKDALAE 506
Cdd:PRK07594 330 VLSRRLAERGHYPAIDVLATLSRVFPVVTS------HEHRQLAAILRRCLALYQEVELLIRIgeyqRGVDTDTD 397
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
216-498 |
1.82e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 130.11 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 216 PRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQ 295
Cdd:PRK08149 122 PPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTE----FVE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 296 lTMTLPDGREesvmkRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADS 375
Cdd:PRK08149 198 -SLRASSRRE-----KCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 376 GYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLI 455
Cdd:PRK08149 272 GYPASVFDSLPRLLERPGATL-------AGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLK 344
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 15219234 456 SYSKYstalesFYEKFDPDFINIRTKAREVLQREDDLNEIVQL 498
Cdd:PRK08149 345 SVSRV------FGQVTDPKHRQLAAAFRKLLTRLEELQLFIDL 381
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
216-506 |
3.07e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 129.49 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 216 PRPVASKLAaDTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDfpq 295
Cdd:PRK06936 134 PAPMSRRLI-ETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIES--- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 296 ltmtlpDGREESvMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADS 375
Cdd:PRK06936 210 ------DLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRR 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 376 GYPAYLAARLASFYERAgkvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLI 455
Cdd:PRK06936 283 GYPPSVFAALPRLMERA-------GQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLR 355
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 15219234 456 SYSKYSTALesfyekFDPDFINIRTKAREVLQREDDLNEIVQL----VGKDALAE 506
Cdd:PRK06936 356 SASRVMNQI------VSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEAD 404
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
209-498 |
2.37e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 127.02 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 209 QSWPVRTPRPVA-SKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMA 287
Cdd:PRK08927 121 VPYPLRAPPPPAhSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 288 EVLMDfpqltmTL-PDGreesvMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISG 366
Cdd:PRK08927 201 EFLQD------DLgPEG-----LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 367 RLAEMPADSGYPAYLAARLASFYERAGKvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRK 446
Cdd:PRK08927 270 SAGEPPTTKGYTPTVFAELPRLLERAGP-----GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERG 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15219234 447 HFPSVNWLISYSKysTALESfyekFDPDFINIRTKAREVLQREDDLNEIVQL 498
Cdd:PRK08927 345 RYPAINVLKSVSR--TMPGC----NDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
215-459 |
5.09e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 123.18 E-value: 5.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 215 TPRPVASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDfp 294
Cdd:PRK06002 135 TAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGREVREFLED-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 295 qltmTLPDGREESVmkrtTLVANTSNMPVAAREASIyTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPAD 374
Cdd:PRK06002 213 ----TLADNLKKAV----AVVATSDESPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 375 SGYPAYLAARLASFYERAGKvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWL 454
Cdd:PRK06002 284 RGYPPSVFSELPRLLERAGP-----GAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPL 358
|
....*
gi 15219234 455 ISYSK 459
Cdd:PRK06002 359 ASISR 363
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
20-525 |
1.50e-29 |
|
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: 122.18 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 20 EYGYVRKVSGPVVVADGMAGAAMYELVRV-GHDNLI--GEIIRLEGDSATIQVYEETAGLTVNDPVLR-THKPLSVELGP 95
Cdd:COG1156 5 EYRTISEIAGPLLFVEGVEGVGYGELVEIeLPDGERrrGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 96 GILGNIFDGIQRP-------------------LKTIARISGDVYIPRGVSvpaldkdclwefqpnkfvegdTITGgdlya 156
Cdd:COG1156 85 DMLGRVFNGLGRPidggppiipekrldingspINPVAREYPREFIQTGIS---------------------AIDG----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 157 tvfentlMNHLVAlppdamgkityiapaGQyslkdtviELefqgikksytmlqswpvrtprPVAS-------KLAAdtpl 229
Cdd:COG1156 139 -------LNTLVR---------------GQ--------KL---------------------PIFSgsglphnELAA---- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 230 ltgQRVLDAlfpSVLGGTcaipGAFgcgktvisqalskysnsdAVVYVGCGERGNEMAEVLMDFpqltmtlpdgREESVM 309
Cdd:COG1156 164 ---QIARQA---KVRGEE----EKF------------------AVVFAAMGITHDEANFFREEF----------EETGAL 205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 310 KRTTLVANTSNMPVAAREASIYTGITIAEYFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLAS 387
Cdd:COG1156 206 DRVVMFLNLADDPAIERIITPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLAS 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 388 FYERAGKVKclggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSkystale 465
Cdd:COG1156 285 LYERAGRIK-----GRKGSITQIPILTMPNDDITHPIPDLTGYITegQIV--LSRDLHRKGIYPPIDVLPSLS------- 350
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15219234 466 sfyekfdpdfiniRTKAR---EVLQRED----------------DLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQ 525
Cdd:COG1156 351 -------------RLMKDgigEGKTREDhadvanqlyaayargqEVRELAAIVGEEALSETDKKYLKFADAFERRFVNQ 416
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
20-525 |
1.71e-29 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 121.86 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 20 EYGYVRKVSGPVVVADGMAGAAMYELVRVGHDN---LIGEIIRLEGDSATIQVYEETAGLTVNDPVLR-THKPLSVELGP 95
Cdd:PRK04196 3 EYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNgekRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 96 GILGNIFDGIQRPLktiarisgdvyiprgvsvpaldkDCLWEFQPNKFVEgdtITGGDlyatvfentlMNHLVALPPDAM 175
Cdd:PRK04196 83 DMLGRIFDGLGRPI-----------------------DGGPEIIPEKRLD---INGAP----------INPVAREYPEEF 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 176 gkityiapagqyslkdtvIELEFQGIKKSYTML--QSWPVRTprpvASKLAADtpLLTGQRVLDAlfpSVLGGTcaipga 253
Cdd:PRK04196 127 ------------------IQTGISAIDGLNTLVrgQKLPIFS----GSGLPHN--ELAAQIARQA---KVLGEE------ 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 254 fgcgktvisqalSKYsnsdAVVYVGCGERgNEMAEVLMDfpqltmtlpDGREESVMKRTTLVANTSNMPVAAREASIYTG 333
Cdd:PRK04196 174 ------------ENF----AVVFAAMGIT-FEEANFFME---------DFEETGALERSVVFLNLADDPAIERILTPRMA 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 334 ITIAEYFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggpERNGSVTIVG 411
Cdd:PRK04196 228 LTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIK-----GKKGSITQIP 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 412 AVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSkystalesfyekfdpdfiniRTKAR---EVL 486
Cdd:PRK04196 302 ILTMPDDDITHPIPDLTGYITegQIV--LSRELHRKGIYPPIDVLPSLS--------------------RLMKDgigEGK 359
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15219234 487 QRED----------------DLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQ 525
Cdd:PRK04196 360 TREDhkdvanqlyaayargkDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQ 414
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
21-459 |
6.28e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 119.83 E-value: 6.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 21 YGYVRKVSGPVVVADGMA---GAAMYELVRVGHDNLI-GEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPG 96
Cdd:PRK07721 19 YGKVSRVIGLMIESKGPEssiGDVCYIHTKGGGDKAIkAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 97 ILGNIFDGIQRPLKTIArisgdvyIPRGVSVPALDKDclwefqpnkfvegdtitggdlyatvfentlmnhlvalPPDAMG 176
Cdd:PRK07721 99 LIGQVLDALGEPLDGSA-------LPKGLAPVSTDQD-------------------------------------PPNPLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 177 KityiaPagqyslkdtvielefqgikksytmlqswPVRTPRPVasklaadtplltGQRVLDALFPSVLGGTCAIPGAFGC 256
Cdd:PRK07721 135 R-----P----------------------------PIREPMEV------------GVRAIDSLLTVGKGQRVGIFAGSGV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 257 GKTVISQALSKYSNSDAVVYVGCGERGNEMAEVL-MDFPqltmtlPDGreesvMKRTTLVANTSNMPVAAREASIYTGIT 335
Cdd:PRK07721 170 GKSTLMGMIARNTSADLNVIALIGERGREVREFIeRDLG------PEG-----LKRSIVVVATSDQPALMRIKGAYTATA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 336 IAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpERNGSVTIVGAVSP 415
Cdd:PRK07721 239 IAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT-------NASGSITAFYTVLV 311
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15219234 416 PGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 459
Cdd:PRK07721 312 DGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSR 355
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
22-529 |
1.27e-27 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 116.34 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 22 GYVRKVSGPVVVADGMAGA--AMYELVRV---GHDNLIGEIIRLEGDSA--TIQVyEETAGLTVNDPVLRTHKPLSVELG 94
Cdd:COG0055 6 GKIVQVIGPVVDVEFPEGElpAIYNALEVeneGGGELVLEVAQHLGDNTvrCIAM-DSTDGLVRGMEVIDTGAPISVPVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 95 PGILGNIFDgiqrplktiarisgdvyiprgvsvpaldkdclwefqpnkfVEGDTItggdlyatvfentlmnhlvalppDA 174
Cdd:COG0055 85 EATLGRIFN----------------------------------------VLGEPI-----------------------DG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 175 MGKItyiaPAGQYslkdtvielefqgikksytmlqsWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGA 253
Cdd:COG0055 102 KGPI----EAKER-----------------------RPIHRPAPPFEEQSTKTEILeTGIKVIDLLAPYAKGGKIGLFGG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 254 FGCGKTVISQAL--------SKYSnsdavVYVGCGER---GNEMaevlmdfpQLTMtlpdgREESVMKRTTLVANTSNMP 322
Cdd:COG0055 155 AGVGKTVLIMELihniakehGGVS-----VFAGVGERtreGNDL--------YREM-----KESGVLDKTALVFGQMNEP 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 323 VAAREASIYTGITIAEYFRD-MGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggp 401
Cdd:COG0055 217 PGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTK----- 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 402 erNGSVTIVGAVSPPGGDFSDPVTSATLS-----IVqvfwgLDKKLAQRKHFPSVNWLISYSKystALesfyekfDPDFI 476
Cdd:COG0055 292 --KGSITSVQAVYVPADDLTDPAPATTFAhldatTV-----LSRKIAELGIYPAVDPLDSTSR---IL-------DPLIV 354
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15219234 477 -----NIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETA-KLLRedYLAQNAFT 529
Cdd:COG0055 355 geehyRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARArKIQR--FLSQPFFV 411
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
21-548 |
1.53e-27 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 115.64 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 21 YGYVRKVSGPVVVADGMAgAAMYEL--VRVGHDNLI--GEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPG 96
Cdd:PRK09099 25 TGKVVEVIGTLLRVSGLD-VTLGELceLRQRDGTLLqrAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 97 ILGNIFDGIQRPlktiarISGDvyiprgvsvPALDKDclwEFQPnkfvegdtitggdlyatvfentlmnhLVALPPDAMg 176
Cdd:PRK09099 104 LLGRVIDGLGEP------IDGG---------GPLDCD---ELVP--------------------------VIAAPPDPM- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 177 kityiapagqyslkdtvielefqgikksytmlqswpvrtprpvaSKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGC 256
Cdd:PRK09099 139 --------------------------------------------SRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 257 GKTVISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQLTMTlPDGreesvMKRTTLVANTSNMPVAAREASIYTGITI 336
Cdd:PRK09099 175 GKSTLMGMFARGTQCDVNVIALIGERGREVRE----FIELILG-EDG-----MARSVVVCATSDRSSIERAKAAYVATAI 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 337 AEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpERNGSVTIVGAVSPP 416
Cdd:PRK09099 245 AEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM-------GETGSITALYTVLAE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 417 GGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALesfyekFDPDFINIRTKAREVLQREDDLNEIV 496
Cdd:PRK09099 318 DESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQV------VPREHVQAAGRLRQLLAKHREVETLL 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15219234 497 QL----VGKDALAEGdkiTLETAKLLReDYLAQnaftPYDKFCPFYKSVWMMRNII 548
Cdd:PRK09099 392 QVgeyrAGSDPVADE---AIAKIDAIR-DFLSQ----RTDEYSDPDATLAALAELS 439
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
255-452 |
7.02e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 114.03 E-value: 7.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 255 GCGKTVISQALSKYSNSDAVVyVG-CGERGNEMAEVLMDFpqLTmtlPDGREESVmkrttLVANTSNMPVAAREASIYTG 333
Cdd:PRK08972 172 GVGKSVLLGMMTRGTTADVIV-VGlVGERGREVKEFIEEI--LG---EEGRARSV-----VVAAPADTSPLMRLKGCETA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 334 ITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclgGPERNGSVTIVGAV 413
Cdd:PRK08972 241 TTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGN-----GGPGQGSITAFYTV 315
|
170 180 190
....*....|....*....|....*....|....*....
gi 15219234 414 SPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVN 452
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 ... |
211-459 |
3.31e-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: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 211 WPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQAL----SKySNSDAVVYVGCGERGNE 285
Cdd:cd01133 32 WPIHREAPEFVELSTEQEILeTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinniAK-AHGGYSVFAGVGERTRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 286 MAEVLMDfpqltMTLPDGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSMMADSTSRWAEALREI 364
Cdd:cd01133 111 GNDLYHE-----MKESGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSEV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 365 SGRLAEMPADSGYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQ 444
Cdd:cd01133 186 SALLGRIPSAVGYQPTLATEMGSLQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAE 258
|
250
....*....|....*
gi 15219234 445 RKHFPSVNWLISYSK 459
Cdd:cd01133 259 LGIYPAVDPLDSTSR 273
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
226-459 |
6.36e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 102.12 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 226 DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFpqltmtlpdgRE 305
Cdd:PRK05688 149 SEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEHI----------LG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 306 ESVMKRTTLVANTSN-MPVAAREASIYTgITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAAR 384
Cdd:PRK05688 219 EEGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAK 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219234 385 LASFYERAGKvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 459
Cdd:PRK05688 298 LPKLVERAGN-----AEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISR 367
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
231-528 |
1.63e-22 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 101.27 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 231 TGQRVLDALFPSVLGGTCAIPGAFGCGKTV--------ISQALSKYSnsdavVYVGCGERGNEMAEVLMDFPQLTMTLPD 302
Cdd:CHL00060 147 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVlimelinnIAKAHGGVS-----VFGGVGERTREGNDLYMEMKESGVINEQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 303 GREESvmkRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGY-NVSMMADSTSRWAEALREISGRLAEMPADSGYPAYL 381
Cdd:CHL00060 222 NIAES---KVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 382 AARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISyskYS 461
Cdd:CHL00060 299 STEMGSLQERITSTK-------EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDS---TS 368
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15219234 462 TAL------ESFYEkfdpdfinIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLrEDYLAQNAF 528
Cdd:CHL00060 369 TMLqprivgEEHYE--------TAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQPFF 432
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
263-459 |
1.93e-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: 97.68 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 263 QA-LSKYSNSDAVVYVGCGERgNEMAEVLMDfpqltmtlpDGREESVMKRTTLVANTSNMPVAAReasIYT---GITIAE 338
Cdd:cd01135 92 QAgVVGSEENFAIVFAAMGVT-MEEARFFKD---------DFEETGALERVVLFLNLANDPTIER---IITprmALTTAE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 339 YFR-DMGYNV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKVKclggpERNGSVTIVGAVSPP 416
Cdd:cd01135 159 YLAyEKGKHVlVILTDMTN-YAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVE-----GRKGSITQIPILTMP 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15219234 417 GGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYSK 459
Cdd:cd01135 233 NDDITHPIPDLTGYITegQIY--LDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
229-535 |
7.46e-22 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 98.70 E-value: 7.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 229 LLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAevlmDFPQLTMTlPDGREESV 308
Cdd:PRK07960 159 LDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVK----DFIENILG-AEGRARSV 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 309 MkrttLVANTSNMPVAAREASIYtGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASF 388
Cdd:PRK07960 234 V----IAAPADVSPLLRMQGAAY-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPAL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 389 YERAGKvkclgGPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALESfy 468
Cdd:PRK07960 309 VERAGN-----GISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALID-- 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219234 469 ekfDPDFINIRTkAREVL---QREDDlneivqLVGKDALAEGDKITLETAKLL---REDYLAQNAFTP--YDKFC 535
Cdd:PRK07960 382 ---EQHYARVRQ-FKQLLssfQRNRD------LVSVGAYAKGSDPMLDKAIALwpqLEAFLQQGIFERadWEDSL 446
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
222-459 |
1.43e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 97.65 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 222 KLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFPQltmtlp 301
Cdd:PRK07196 132 RRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKEFIEHSLQ------ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 302 dgrEESVMKRTTLVANTSNMPVAAREASIYTGiTIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYL 381
Cdd:PRK07196 206 ---AAGMAKSVVVAAPADESPLMRIKATELCH-AIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSA 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219234 382 AARLASFYERAGKvkclggPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSK 459
Cdd:PRK07196 282 FSIIPRLAESAGN------SSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISR 353
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
226-548 |
2.11e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 91.29 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 226 DTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEMAEvlmdFPQLTMtlpDGRE 305
Cdd:PRK08472 138 DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPE----FIEKNL---GGDL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 306 ESvmkrTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARL 385
Cdd:PRK08472 211 EN----TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 386 ASFYERAGKvkclggPERNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALE 465
Cdd:PRK08472 287 PQLMERAGK------EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDII 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 466 SfyekfdPDFINIRTKAREV--LQREddlNEIVQLVGkdALAEGDKITLETA---KLLREDYLAQNaftPYDKFcPFYKS 540
Cdd:PRK08472 361 S------PEHKLAARKFKRLysLLKE---NEVLIRIG--AYQKGNDKELDEAiskKEFMEQFLKQN---PNELF-PFEQT 425
|
....*...
gi 15219234 541 VWMMRNII 548
Cdd:PRK08472 426 FEQLEEIL 433
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
208-492 |
2.77e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 90.81 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 208 LQSWPVRTPRPVASKLAADTPLL-TGQRVLDALFPSVLGGTCAIPGAFGCGKTVISQALSKYSNSDAVVYVGCGERGNEM 286
Cdd:PRK06793 118 LQKIKLDAPPIHAFEREEITDVFeTGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 287 AevlmDFPQLTMTlpdgreESVMKRTTLVANTSNMP--VAAREASIYTgiTIAEYFRDMGYNVSMMADSTSRWAEALREI 364
Cdd:PRK06793 198 K----DFIRKELG------EEGMRKSVVVVATSDEShlMQLRAAKLAT--SIAEYFRDQGNNVLLMMDSVTRFADARRSV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 365 SGRLAEMPAdSGYPAYLAARLASFYERAGKVKclggperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQ 444
Cdd:PRK06793 266 DIAVKELPI-GGKTLLMESYMKKLLERSGKTQ-------KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELAT 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15219234 445 RKHFPSVNWLISYSKYstalesFYEKFDPDFINIRTKAREVLQ--REDDL 492
Cdd:PRK06793 338 LSHYPAISVLDSVSRI------MEEIVSPNHWQLANEMRKILSiyKENEL 381
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
19-408 |
1.11e-18 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 89.59 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 19 SEYGYVRKVSGPVVVADGMAGAAMYELVRVGhDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGIL 98
Cdd:PRK13343 26 REIGRVESVGDGIAFVSGLPDAALDELLRFE-GGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 99 GNIFDGIQRPLKtiarisgdvyiprgvsvpaldkdclwefqpnkfvegdtitGGDlyatvfentlmnhlvALPPDAMGKI 178
Cdd:PRK13343 105 GRVIDPLGRPLD----------------------------------------GGG---------------PLQATARRPL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 179 TYIAPAgqyslkdtVIELEFqgikksytmlqswpvrtprpvasklaADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGK 258
Cdd:PRK13343 130 ERPAPA--------IIERDF--------------------------VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGK 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 259 T------VISQalskySNSDAV-VYVGCGERGNEMAEVLMdfpqltmTLpdgREESVMKRTTLVANTSNMPVAAREASIY 331
Cdd:PRK13343 176 TaiaidaIINQ-----KDSDVIcVYVAIGQKASAVARVIE-------TL---REHGALEYTTVVVAEASDPPGLQYLAPF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 332 TGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPA---YLAARLasfYERAGKV-KCLGGpernGSV 407
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRL---LERAAKLsPELGG----GSL 313
|
.
gi 15219234 408 T 408
Cdd:PRK13343 314 T 314
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
302-528 |
1.86e-18 |
|
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: 88.63 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 302 DGREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFR-DMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAY 380
Cdd:TIGR01040 203 DFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGY 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 381 LAARLASFYERAGKVKclggpERNGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISYS 458
Cdd:TIGR01040 283 MYTDLATIYERAGRVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPINVLPSLS 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219234 459 KY--STALESFYEKFDPDFINiRTKAREVLQRedDLNEIVQLVGKDALAEGDKITLETAKLLREDYLAQNAF 528
Cdd:TIGR01040 356 RLmkSAIGEGMTRKDHSDVSN-QLYACYAIGK--DVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPY 424
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
20-535 |
3.35e-17 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 84.19 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 20 EYGYVRKVSGPVVVADGMAgAAMYELVRVG---HDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPG 96
Cdd:PRK05922 19 ECGLLSRVSGNLLEAQGLS-ACLGELCQISlskSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 97 ILGNIFDGIQRPLKtiarisgdvyiprgvSVPALDKdclwefqpnkfvegdtitggdlyatvfenTLMNHLVALPPDAMG 176
Cdd:PRK05922 98 LLGRVLDGFGNPLD---------------GKEQLPK-----------------------------THLKPLFSSPPSPMS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 177 kityiapagqyslkdtvielefqgikksytmlqswpvRTPrpvasklaADTPLLTGQRVLDALFPSVLGGTCAIPGAFGC 256
Cdd:PRK05922 134 -------------------------------------RQP--------IQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGS 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 257 GKTVISQALSKYSNSDAVVYVGCGERGNEMAEVLMDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITI 336
Cdd:PRK05922 169 GKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQH----------KEGLAAQRTIIIASPAHETAPTKVIAGRAAMTI 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 337 AEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAGKvkclggpERNGSVTIVGAV--S 414
Cdd:PRK05922 239 AEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-------NDKGSITALYAIlhY 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 415 PPGGD-FSDPVTSAtlsivqvfwgLDKKL---AQRKHF--PSVNWLISYSKYSTALESfyekfdPDFINIRTKAREVLQR 488
Cdd:PRK05922 312 PNHPDiFTDYLKSL----------LDGHFfltPQGKALasPPIDILTSLSRSARQLAL------PHHYAAAEELRSLLKA 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15219234 489 EDDLNEIVQLvgkDALAEGDKITLETA-KLLR--EDYLAQnaftPYDKFC 535
Cdd:PRK05922 376 YHEALDIIQL---GAYVPGQDAHLDRAvKLLPsiKQFLSQ----PLSSYC 418
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
228-459 |
6.00e-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: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 228 PLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIsqALSKYSNSDA----VVYVGCGERGNEMAevlmdfpQLTMTLpdg 303
Cdd:cd01132 52 PLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAI--AIDTIINQKGkkvyCIYVAIGQKRSTVA-------QIVKTL--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 304 REESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPA---Y 380
Cdd:cd01132 120 EEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfY 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 381 LAARLasfYERAGKVK-CLGGpernGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLAQRKHFPSVNWLISY 457
Cdd:cd01132 200 LHSRL---LERAAKLSdELGG----GSLTALPIIETQAGDVSAYIPTNVISITdgQIF--LESELFNKGIRPAINVGLSV 270
|
..
gi 15219234 458 SK 459
Cdd:cd01132 271 SR 272
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
215-463 |
1.07e-13 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 73.84 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 215 TPRP-VASKLAADTPLLTGQRVLDALFPSVLGGTCAIPGAFGCGKTVIsqALSKYSN---SDAV-VYVGCGERGNEMAEV 289
Cdd:CHL00059 110 SPAPgIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAV--ATDTILNqkgQNVIcVYVAIGQKASSVAQV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 290 LMDFpqltmtlpdgREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLA 369
Cdd:CHL00059 188 VTTL----------QERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 370 EMPADSGYPA---YLAARLasfYERAGKV-KCLGGpernGSVTIVGAVSPPGGDFSDPVTSATLSIV--QVFwgLDKKLA 443
Cdd:CHL00059 258 RPPGREAYPGdvfYLHSRL---LERAAKLsSQLGE----GSMTALPIVETQAGDVSAYIPTNVISITdgQIF--LSADLF 328
|
250 260
....*....|....*....|
gi 15219234 444 QRKHFPSVNWLISYSKYSTA 463
Cdd:CHL00059 329 NAGIRPAINVGISVSRVGSA 348
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
21-82 |
3.23e-13 |
|
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: 65.03 E-value: 3.23e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219234 21 YGYVRKVSGPVVVADGMAGAAMYELVRVGHDN------LIGEIIRLEGDSATIQVYEETAGLTVNDPV 82
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDgnnetvLKAEVIGFRGDRAILQLFESTRGLSRGALV 68
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
24-85 |
9.91e-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: 63.33 E-value: 9.91e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15219234 24 VRKVSGPVVVADGMAGAA--MYELVRVGHDN----LIGEIIRLEGDSATIQVYEETAGLTVNDPVLRT 85
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLpgLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
39-428 |
5.76e-12 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 68.14 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 39 GAAMYELVRV--GHDNLIGEIIRLEGDSATIQVYEETAGLTVNDPVLRTHKPLSVELGPGILGNIFDGIQRPLKTIARIS 116
Cdd:PRK02118 22 GVGYGELATVerKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 117 GDVYIPRGVSV-PALDKdclwefQPNKFVEGDtITGGDLYATVFENTlmnhlvalppdamgKITYIAPAGQyslkdtvie 195
Cdd:PRK02118 102 GEPIEIGGPSVnPVKRI------VPREMIRTG-IPMIDVFNTLVESQ--------------KIPIFSVSGE--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 196 lefqgikksytmlqswpvrtprPVASKLAadtplltgqRVldALfpsvlggtcaipgafgcgktvisQAlskysNSDAVV 275
Cdd:PRK02118 152 ----------------------PYNALLA---------RI--AL-----------------------QA-----EADIII 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 276 YVGCGERGNemaevlmDFPQLTMTLPDGreeSVMKRTTLVANTSNMPVAAREASIYTGITIAEYFR-DMGYNVSMMADST 354
Cdd:PRK02118 171 LGGMGLTFD-------DYLFFKDTFENA---GALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDM 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15219234 355 SRWAEALREISGRLAEMPADSGYPAYLAARLASFYERAgkVKCLGGpernGSVTIVGAVSPPGGDFSDPVTSAT 428
Cdd:PRK02118 241 TNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA--VDFEDG----GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
174-466 |
1.65e-11 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 66.99 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 174 AMGKITYIaPAGQYSLKDTVI----ELEFQGIKKSYTMLQSWP----VRTPRP-VASKLAADTPLLTGQRVLDALFPSVL 244
Cdd:PTZ00185 110 ATGKLLYI-PVGAGVLGKVVNplghEVPVGLLTRSRALLESEQtlgkVDAGAPnIVSRSPVNYNLLTGFKAVDTMIPIGR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 245 GGTCAIPGAFGCGKTVIS------------QALSKysNSDAVVYVGCGERGNEMAEVLMDFpqltmtlpdgREESVMKRT 312
Cdd:PTZ00185 189 GQRELIVGDRQTGKTSIAvstiinqvrinqQILSK--NAVISIYVSIGQRCSNVARIHRLL----------RSYGALRYT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 313 TLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPA---YLAARLasfY 389
Cdd:PTZ00185 257 TVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGdvfYLHSRL---L 333
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219234 390 ERAGKVKCLGGperNGSVTIVGAVSPPGGDFSDPVTSATLSIVQVFWGLDKKLAQRKHFPSVNWLISYSKYSTALES 466
Cdd:PTZ00185 334 ERAAMLSPGKG---GGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQN 407
|
|
| 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 ... |
20-78 |
4.87e-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: 4.87e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219234 20 EYGYVRKVSGPVVVADGMAGAAMYELVRVGHDN---LIGEIIRLEGDSATIQVYEETAGLTV 78
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDgevRRGQVLEVSGDKAVVQVFEGTSGLDL 62
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
226-408 |
7.12e-08 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 55.46 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 226 DTPLLTGQRVLDALFPS-------VLG----GTCAIpgafgCGKTVISQalsKYSNsdaV--VYVGCGERGNEMAevlmd 292
Cdd:PRK09281 143 HEPLQTGIKAIDAMIPIgrgqrelIIGdrqtGKTAI-----AIDTIINQ---KGKD---VicIYVAIGQKASTVA----- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219234 293 fpQLTMTLpdgREESVMKRTTLVANTSNMPVAAREASIYTGITIAEYFRDMGYNVSMMADSTSRWAEALREIS------- 365
Cdd:PRK09281 207 --QVVRKL---EEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSlllrrpp 281
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15219234 366 GRLAempadsgYPA---YLAARLasfYERAGKV-KCLGGpernGSVT 408
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, ... |
476-530 |
3.87e-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: 42.05 E-value: 3.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 15219234 476 INIRTKAREVLQREDDLNEIVQLVGKDALAEGDKITLETAKLLREdYLAQNAFTP 530
Cdd:cd01429 2 KAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEP 55
|
|
| |
