|
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 ... |
15-606 |
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: 1242.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 15 EYGRVYAVSGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMG 94
Cdd:TIGR01042 1 EYGYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 95 SIFDGIQRPLRDIGVMTNSIYIPKGVNTTALSRSEMWEFNPLNVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVR 174
Cdd:TIGR01042 81 NIFDGIQRPLKAIAEQSQSIYIPRGVNVPALDRDKKWEFTPKKLRVGDHITGGDIYGTVFENSLIKHKIMLPPRARGTIT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 175 YIAPAGNYNLEDIVLETEFDGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKT 254
Cdd:TIGR01042 161 YIAPAGNYTVDDTVLEVEFQGVKKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 255 VISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTCEIDGVTESIMKRTALVANTSNMPVAAREASIYTGITLSEYF 334
Cdd:TIGR01042 241 VISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEVDGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEYF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 335 RDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDF 414
Cdd:TIGR01042 321 RDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGDF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 415 SDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDEYYDKNYPEFVPLRTKVKEILQEEEDLSEIVQLVG 494
Cdd:TIGR01042 401 SDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLVG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 495 KASLAETDKVTLEVAKLLKDDFLQQNSYSPYDRVCPFYKTVGMLRNIMAFYETARHAVESTAQSDNKITWNTIRESMGGI 574
Cdd:TIGR01042 481 KDALAETDKITLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQDDNKITWSIIKESLGDL 560
|
570 580 590
....*....|....*....|....*....|..
gi 12643429 575 MYQLSSMKFKDPVkDGEQKIKADYDQLYEDLQ 606
Cdd:TIGR01042 561 LYRLSSMKFEDPS-DGEAKIKADYEKLNEDMQ 591
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
17-612 |
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: 906.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 17 GRVYAVSGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSI 96
Cdd:COG1155 5 GKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLLGNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 97 FDGIQRPLRDIGVMTNSiYIPKGVNTTALSRSEMWEFNPLnVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYI 176
Cdd:COG1155 85 FDGIQRPLDKIAEKSGD-FIPRGVDVPALDREKKWDFTPT-VKVGDKVSAGDILGTVQETPLIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 177 APAGNYNLEDIV--LETEfDGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKT 254
Cdd:COG1155 163 APEGEYTVEDTIavLEDE-DGEEHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 255 VISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPELtceIDGVT-ESIMKRTALVANTSNMPVAAREASIYTGITLSEY 333
Cdd:COG1155 242 VTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPEL---IDPKTgRPLMERTVLIANTSNMPVAAREASIYTGITIAEY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 334 FRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKCLGNPerEGSVSIVGAVSPPGGD 413
Cdd:COG1155 319 YRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 414 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDEYYDKNY-PEFVPLRTKVKEILQEEEDLSEIVQL 492
Cdd:COG1155 397 FSEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDENVdPDWSELRNEAMDLLQEEAELQEIVRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 493 VGKASLAETDKVTLEVAKLLKDDFLQQNSYSPYDRVCPFYKTVGMLRNIMAFYETARHAVESTAQSDnKITWNTIREsmg 572
Cdd:COG1155 477 VGEDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALEKGVPLS-EIKELPLRE--- 552
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 12643429 573 gimyQLSSMKFkdpvkDGEQKIKADYDQLYEDLQQAFRNL 612
Cdd:COG1155 553 ----KIARMKY-----SPENELLEKFDELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
17-603 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 872.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 17 GRVYAVSGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSI 96
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 97 FDGIQRPLRDIGVMTnSIYIPKGVNTTALSRSEMWEFNPLnVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYI 176
Cdd:PRK04192 85 FDGIQRPLDELAEKS-GDFLERGVYVPALDREKKWEFTPT-VKVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 177 APAGNYNLEDIV--LETEfDGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKT 254
Cdd:PRK04192 163 VSEGDYTVDDTIavLEDE-DGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 255 VISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPELtceIDGVT-ESIMKRTALVANTSNMPVAAREASIYTGITLSEY 333
Cdd:PRK04192 242 VTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPEL---IDPKTgRPLMERTVLIANTSNMPVAAREASIYTGITIAEY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 334 FRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKCLGNPerEGSVSIVGAVSPPGGD 413
Cdd:PRK04192 319 YRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 414 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDEYYDKN-YPEFVPLRTKVKEILQEEEDLSEIVQL 492
Cdd:PRK04192 397 FSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEENvDPDWRELRDEAMDLLQREAELQEIVRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 493 VGKASLAETDKVTLEVAKLLKDDFLQQNSYSPYDRVCPFYKTVGMLRNIMAFYETARHAVESTAqSDNKITWNTIRESMG 572
Cdd:PRK04192 477 VGPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGV-PVSEILELEVRDRIA 555
|
570 580 590
....*....|....*....|....*....|.
gi 12643429 573 GIMYQLSSMkFKDPVKDGEQKIKADYDQLYE 603
Cdd:PRK04192 556 RLKYIPENE-YLEKIDEIFEKLEEELEELIA 585
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
17-599 |
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: 804.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 17 GRVYAVSGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSI 96
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 97 FDGIQRPLRDIGVMTNSiYIPKGVNTTALSRSEMWEFNPLnVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYI 176
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGD-FIARGVDAPGLDRDKKWHFKPT-VKEGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 177 APAGNYNLEDIVLETEFDGEItKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVI 256
Cdd:TIGR01043 160 AEEGDYTVEDTIAVVDTDGDE-EIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 257 SQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTceiDGVT-ESIMKRTALVANTSNMPVAAREASIYTGITLSEYFR 335
Cdd:TIGR01043 239 QHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPELK---DPKTgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 336 DMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFS 415
Cdd:TIGR01043 316 DMGYDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDFS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 416 DPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDEYYDKNY-PEFVPLRTKVKEILQEEEDLSEIVQLVG 494
Cdd:TIGR01043 396 EPVTQNTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVQDWWHENVdPDWREMRDEAMDLLQKESELQEIVQLVG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 495 KASLAETDKVTLEVAKLLKDDFLQQNSYSPYDRVCPFYKTVGMLRNIMAFYETARHAVESTAQSDnKITWNTIRESMGGI 574
Cdd:TIGR01043 476 PDALPERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVE-EILKLEVKEEIGRM 554
|
570 580
....*....|....*....|....*
gi 12643429 575 MYQLSSmKFKDPVKDGEQKIKADYD 599
Cdd:TIGR01043 555 KYEPDN-DILAKIDEILEKIEKEFK 578
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
83-454 |
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: 617.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 83 PLSVELGPGIMGSIFDGIQRPLRDIgVMTNSIYIPKGVNTtalsrsemwefnplnvrvgshitggdlygvvhentlvkqr 162
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVI-AETGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 163 mivaprakgtvryiapagnynledivletefdgeitkhtmlQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGT 242
Cdd:cd01134 40 -----------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 243 TAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTCEIDGvtESIMKRTALVANTSNMPVAAREA 322
Cdd:cd01134 79 AAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITG--ESLMERTVLIANTSNMPVAAREA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 323 SIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKCLGNPEREGSVS 402
Cdd:cd01134 157 SIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSVT 236
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 12643429 403 IVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKY 454
Cdd:cd01134 237 IVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
254-610 |
1.13e-122 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 387.46 E-value: 1.13e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 254 TVISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTCEIDGvtESIMKRTALVANTSNMPVAAREASIYTGITLSEY 333
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTG--KPLMERTVLIANTSNMPVAAREASIYTGITIAEY 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 334 FRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKCLGNPEREGSVSIVGAVSPPGGD 413
Cdd:PRK14698 748 FRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGD 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 414 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDEYYDKNY-PEFVPLRTKVKEILQEEEDLSEIVQL 492
Cdd:PRK14698 828 FSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVdPEWKAMRDKAMELLQKEAELQEIVRI 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 493 VGKASLAETDKVTLEVAKLLKDDFLQQNSYSPYDRVCPFYKTVGMLRNIMAFYETARHAVeSTAQSDNKITWNTIRESMG 572
Cdd:PRK14698 908 VGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAI-SRGVPLEEIAKLPVREEIG 986
|
330 340 350
....*....|....*....|....*....|....*...
gi 12643429 573 gimyqlsSMKFKDPVkdgeQKIKADYDQLYEDLQQAFR 610
Cdd:PRK14698 987 -------RMKFEPDI----EKIKALIDKTNEQFDELFK 1013
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
227-452 |
9.72e-103 |
|
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: 310.06 E-value: 9.72e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 227 GQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPEltceidgvtESIMKRT 306
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLG---------SGALKRT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 307 ALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERA 386
Cdd:pfam00006 72 VVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643429 387 GRVKclgnpEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYS 452
Cdd:pfam00006 152 GRVK-----GKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
202-454 |
1.47e-91 |
|
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: 283.58 E-value: 1.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 202 MLQVWPVRQPRP-VTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNS---DVIIYVGCGER 277
Cdd:cd19476 28 TKQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKahaGVVVFAGIGER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 278 GNEMSEVLRDFPELtceidgvteSIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALRE 357
Cdd:cd19476 108 GREVNDLYEEFTKS---------GAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALRE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 358 ISGRLAEMPADSGYPAYLGARLATFYERAGRVKclgnpEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLA 437
Cdd:cd19476 179 MSALLGEPPGREGYPPYLFTKLATLYERAGKVK-----DGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELA 253
|
250
....*....|....*..
gi 12643429 438 QRKHFPSINWLISYSKY 454
Cdd:cd19476 254 RKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
17-255 |
2.14e-70 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 245.70 E-value: 2.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 17 GRVYAVSGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGSI 96
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 97 FDGIQRPLRDIGVMTNSiYIPKGVNTTALSRSEMWEFNPlNVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYI 176
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFIP-KVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 177 APAGNYNLEDIVLETEF-DGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTV 255
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 ... |
97-218 |
1.38e-58 |
|
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: 191.84 E-value: 1.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 97 FDGIQRPLRDIGVMTNSiYIPKGVNTTALSRSEMWEFNPlNVRVGSHITGGDLYGVVHENTLVKQRMIVAPRAKGTVRYI 176
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTP-TVKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTEI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 12643429 177 APAGNYNLEDIVLETEFDGEITKHTMLQVWPVRQPRPVTEKL 218
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 ... |
469-572 |
1.18e-49 |
|
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: 167.57 E-value: 1.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 469 FVPLRTKVKEILQEEEDLSEIVQLVGKASLAETDKVTLEVAKLLKDDFLQQNSYSPYDRVCPFYKTVGMLRNIMAFYETA 548
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....
gi 12643429 549 RHAVEStAQSDNKITWNTIRESMG 572
Cdd:cd18111 81 LEALEK-GVPLSKILELPVREKIA 103
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
4-526 |
4.13e-45 |
|
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: 166.01 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 4 LRKFKDEERESEYGRVYAVSGPVVTAEAMSgSAMYELVRV----GYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLR 79
Cdd:TIGR01026 12 LCQEMDLRLVKRVGRVTKVKGLLIEAVGPQ-ASVGDLCLIerrgSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 80 TGKPLSVELGPGIMGSIFDGIQRPLrdigvmTNSIYIPKGVNTTALSRSEmweFNPLNvrvgshitggdlygvvhentlv 159
Cdd:TIGR01026 91 TGEGLSIKVGDGLLGRVLDGLGKPI------DGKGKFLDNVETEGLITAP---INPLK---------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 160 kqrmivaprakgtvryiapagnynledivletefdgeitkhtmlqvwpvrqprpvteKLPANHPLFTGQRVLDSLFPCVQ 239
Cdd:TIGR01026 140 ---------------------------------------------------------RAPIREILSTGVRSIDGLLTVGK 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 240 GGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEmsevLRDFPEltcEIDGvtESIMKRTALVANTSNMPVAA 319
Cdd:TIGR01026 163 GQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGRE----VREFIE---HDLG--EEGLKRSVVVVATSDQSPLL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 320 REASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGrvkclgnPEREG 399
Cdd:TIGR01026 234 RLKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAG-------ASGKG 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 400 SVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRAL--DEYYDKnypefvplRTKVK 477
Cdd:TIGR01026 307 SITAFYTVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIvsEEHRRA--------ARKFR 378
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 12643429 478 EIL---QEEEDLSEIvQLVGKASLAETDKVTLEVAKLlkDDFLQQNSYSPYD 526
Cdd:TIGR01026 379 ELLskyKDNEDLIRI-GAYQRGSDRELDFAIAKYPKL--ERFLKQGINEKVN 427
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
16-526 |
1.93e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 158.44 E-value: 1.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 16 YGRVYAVsGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGS 95
Cdd:PRK06820 30 RGPIVEI-GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 96 IFDGIQRPLRDIGVMTNsiyipkgvnttalsrsemwEFNPLNvrvgshitggdlygvvhentlvkqrmivaprakgtvry 175
Cdd:PRK06820 109 ILDGLGAPIDGGPPLTG-------------------QWRELD-------------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 176 iAPAgnynledivletefdgeitkhtmlqvwpvrqPRPVTEKlPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTV 255
Cdd:PRK06820 132 -CPP-------------------------------PSPLTRQ-PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKST 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 256 ISQALSKYSNSDVIIYVGCGERGNEmsevLRDFPELTceidgVTESIMKRTALVANTSNMPVAAREASIYTGITLSEYFR 335
Cdd:PRK06820 179 LLGMLCADSAADVMVLALIGERGRE----VREFLEQV-----LTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 336 DMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGrvkclgnPEREGSVSIVGAVSPPGGDFS 415
Cdd:PRK06820 250 DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG-------NSDRGSITAFYTVLVEGDDMN 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 416 DPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDEyydknyPEFVPLRTKVKEILQEEEDLSEIVQlVGK 495
Cdd:PRK06820 323 EPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVS------AGQLAMAQKLRRMLACYQEIELLVR-VGE 395
|
490 500 510
....*....|....*....|....*....|....*
gi 12643429 496 ASLAEtDKVTLEVAKLLKD--DFLQQ--NSYSPYD 526
Cdd:PRK06820 396 YQAGE-DLQADEALQRYPAicAFLQQdhSETAHLE 429
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
16-542 |
4.36e-40 |
|
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: 151.72 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 16 YGRVYAVSGPVVTAEAMSGS--AMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIM 93
Cdd:COG1157 20 SGRVTRVVGLLIEAVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 94 GSIFDGIQRPLRDIGVMTNSIYIPkgVNTTALsrsemwefNPLnvrvgshitggdlygvvhentlvkQRmivaprakgtv 173
Cdd:COG1157 100 GRVLDGLGRPLDGKGPLPGEERRP--LDAPPP--------NPL------------------------ER----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 174 ryiapagnynledivletefdgeitkhtmlqvwpvrqpRPVTEKLPanhplfTGQRVLDSLFPCVQG---GTTAipGAfG 250
Cdd:COG1157 135 --------------------------------------ARITEPLD------TGVRAIDGLLTVGRGqriGIFA--GS-G 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 251 CGKTVISQALSKYSNSDVIIyVG-CGERGNEmsevLRDFPELTCEIDGvtesiMKRTALVANTSNMPVAAREASIYTGIT 329
Cdd:COG1157 168 VGKSTLLGMIARNTEADVNV-IAlIGERGRE----VREFIEDDLGEEG-----LARSVVVVATSDEPPLMRLRAAYTATA 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 330 LSEYFRDMGYNVAMMADSTSRWAEALREISgrLA--EMPADSGYPAYLGARLATFYERAGrvkclgnPEREGSVSIVGAV 407
Cdd:COG1157 238 IAEYFRDQGKNVLLLMDSLTRFAMAQREIG--LAagEPPATRGYPPSVFALLPRLLERAG-------NGGKGSITAFYTV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 408 SPPGGDFSDPVTSATLGI-----VqvfwgLDKKLAQRKHFPSINWLISYSKYMRALdeyydkNYPEFVPLRTKVKEIL-- 480
Cdd:COG1157 309 LVEGDDMNDPIADAVRGIldghiV-----LSRKLAERGHYPAIDVLASISRVMPDI------VSPEHRALARRLRRLLar 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12643429 481 -QEEEDLseIvqLVG---KASLAETDKVtleVAKLLK-DDFLQQnsysPYDRVCPFYKTVGMLRNIM 542
Cdd:COG1157 378 yEENEDL--I--RIGayqPGSDPELDEA---IALIPAiEAFLRQ----GMDERVSFEESLAQLAELL 433
|
|
| 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 ... |
16-82 |
6.16e-39 |
|
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349743 [Multi-domain] Cd Length: 67 Bit Score: 137.27 E-value: 6.16e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12643429 16 YGRVYAVSGPVVTAEAMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGK 82
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
206-453 |
8.95e-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: 143.47 E-value: 8.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 206 WPVRQPRP-VTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEmsev 284
Cdd:cd01136 32 RPLIAAPPnPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 285 LRDFPELTCEIDGvtesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAE 364
Cdd:cd01136 108 VREFIEKDLGEEG-----LKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 365 MPADSGYPAYLGARLATFYERAGrvkclgnPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPS 444
Cdd:cd01136 183 PPTRRGYPPSVFALLPRLLERAG-------NGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPA 255
|
....*....
gi 12643429 445 INWLISYSK 453
Cdd:cd01136 256 IDVLASISR 264
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
206-543 |
6.76e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 137.19 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 206 WPVRQ--PRPVTEKLpANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEmse 283
Cdd:PRK06936 127 YPVYAdaPAPMSRRL-IETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGRE--- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 284 vLRDFPELTCEIDGvtesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLA 363
Cdd:PRK06936 203 -VREFIESDLGEEG-----LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 364 EMPADSGYPAYLGARLATFYERAGrvkclgnPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFP 443
Cdd:PRK06936 277 EPPTRRGYPPSVFAALPRLMERAG-------QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 444 SINWLISYSKYMRALDEyydknyPEFVPLRTKVKEILQEEEDLSEIVQL--VGKASLAETDKVTLEVAKLlkDDFLQQNS 521
Cdd:PRK06936 350 AIDVLRSASRVMNQIVS------KEHKTWAGRLRELLAKYEEVELLLQIgeYQKGQDKEADQAIERIGAI--RGFLRQGT 421
|
330 340
....*....|....*....|..
gi 12643429 522 YSPydrvCPFYKTVGMLRNIMA 543
Cdd:PRK06936 422 HEL----SHFNETLNLLETLTQ 439
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
165-543 |
9.29e-35 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 136.66 E-value: 9.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 165 VAPRAKGTVryIAPAGNynledIVLEteFDGEITKHTMLQVWPV-RQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTT 243
Cdd:PRK08149 84 VGEALLGAV--LDPTGK-----IVER--FDAPPTVGPISEERVIdVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 244 AIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMSEVlrdfpeltceIDGVTESIMK-RTALVANTSNMPVAAREA 322
Cdd:PRK08149 155 GIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEF----------VESLRASSRReKCVLVYATSDFSSVDRCN 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 323 SIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKclgnperEGSVS 402
Cdd:PRK08149 225 AALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATL-------AGSIT 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 403 IVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSkymRALDEYYDKNYPEfvpLRTKVKEILQE 482
Cdd:PRK08149 298 AFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVS---RVFGQVTDPKHRQ---LAAAFRKLLTR 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12643429 483 EEDLSEIVQLvGKASL---AETDKVTLEVAKLlkDDFLQQnsysPYDRVCPFYKTVGMLRNIMA 543
Cdd:PRK08149 372 LEELQLFIDL-GEYRRgenADNDRAMDKRPAL--EAFLKQ----DVAEKSSFSDTLERLNEFAA 428
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
193-489 |
2.45e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 135.62 E-value: 2.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 193 FDGEITKHTMLQVWPVRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYV 272
Cdd:PRK07721 111 LDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 273 GCGERGNEmsevLRDFPELTCEIDGvtesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWA 352
Cdd:PRK07721 191 LIGERGRE----VREFIERDLGPEG-----LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 353 EALREISGRLAEMPADSGYPAYLGARLATFYERAGrvkclgnPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGL 432
Cdd:PRK07721 262 MAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG-------TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVL 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 433 DKKLAQRKHFPSINWLISYSKYMRALDEyydknyPEFVPLRTKVKEIL---QEEEDLSEI 489
Cdd:PRK07721 335 DRQLANKGQYPAINVLKSVSRVMNHIVS------PEHKEAANRFRELLstyQNSEDLINI 388
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
17-520 |
1.02e-33 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274607 [Multi-domain] Cd Length: 411 Bit Score: 133.37 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 17 GRVYAVSGPVVTAEAMSGS--AMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMG 94
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPvgSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 95 SIFDGIQRPLRDIGVmtnsiyiPKGVNTTALSRSEMwefNPLNvrvgshitggdlygvvhentlvkqrmivaprakgtvr 174
Cdd:TIGR03496 81 RVIDGLGRPLDGKGP-------LDAGERVPLYAPPI---NPLK------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 175 yiapagnynledivletefdgeitkhtmlqvwpvRqpRPVTEklpanhPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKT 254
Cdd:TIGR03496 114 ----------------------------------R--APIDE------PLDVGVRAINGLLTVGRGQRMGIFAGSGVGKS 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 255 VISQALSKYSNSDVIIyVG-CGERGNEmsevLRDFPEltcEIDGvtESIMKRTALVANTSNMPVAAREASIYTGITLSEY 333
Cdd:TIGR03496 152 TLLGMMARYTEADVVV-VGlIGERGRE----VKEFIE---DILG--EEGLARSVVVAATADESPLMRLRAAFYATAIAEY 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 334 FRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGrvkclgnPEREGSVSIVG--AVSPPG 411
Cdd:TIGR03496 222 FRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAG-------NGEEGKGSITAfyTVLVEG 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 412 GDFSDPVTSATLGIVQvfwG---LDKKLAQRKHFPSINWLISYSKYMRAL--DEYYDknypefvpLRTKVKEIL---QEE 483
Cdd:TIGR03496 295 DDQQDPIADAARAILD---GhivLSRELAEQGHYPAIDILASISRVMPDVvsPEHRQ--------AARRFKQLLsryQEN 363
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 12643429 484 EDLSEIvqlvG---KASLAETDKVTLEVAKLlkDDFLQQN 520
Cdd:TIGR03496 364 RDLISI----GayqAGSDPELDQAIALYPRI--EAFLQQG 397
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
16-492 |
3.65e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 132.00 E-value: 3.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 16 YGRVYAVSGPVVTAEaMSGSAMYELVRVGYYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIMGS 95
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 96 IFDGIQRPLRDIGvmtnsiyIPKGVnttalsrsemWEfnplnvrvgshitggdlygvvhentlvkqrmivaprakgtvry 175
Cdd:PRK07594 101 VIDGFGRPLDGRE-------LPDVC----------WK------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 176 iapagnynledivletEFDGeitkhtmlqvwpvrQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTV 255
Cdd:PRK07594 121 ----------------DYDA--------------MPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKST 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 256 ISQALSKYSNSDVIIYVGCGERGNEmsevLRDFPELTceidgVTESIMKRTALVANTSNMPVAAREASIYTGITLSEYFR 335
Cdd:PRK07594 171 LLAMLCNAPDADSNVLVLIGERGRE----VREFIDFT-----LSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFR 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 336 DMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGrvkcLGNperEGSVSIVGAVSPPGGDFS 415
Cdd:PRK07594 242 DNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG----MGE---KGSITAFYTVLVEGDDMN 314
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12643429 416 DPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMRALDEyydknyPEFVPLRTKVKEILQEEEDLSEIVQL 492
Cdd:PRK07594 315 EPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTS------HEHRQLAAILRRCLALYQEVELLIRI 385
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
210-548 |
1.40e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 130.48 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 210 QPRPVTEKLPANH-------PLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMS 282
Cdd:PRK08927 121 VPYPLRAPPPPAHsrarvgePLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 283 EVLRDfpelTCEIDGvtesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRL 362
Cdd:PRK08927 201 EFLQD----DLGPEG-----LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 363 AEMPADSGYPAYLGARLATFYERAGRvkclgNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHF 442
Cdd:PRK08927 272 GEPPTTKGYTPTVFAELPRLLERAGP-----GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRY 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 443 PSINWLISYSKYMRALdeyydkNYPEFVPLRTKVKEILQEEEDLSEIVQLvgKASLAETDKVTLEVAKLLKD--DFLQQN 520
Cdd:PRK08927 347 PAINVLKSVSRTMPGC------NDPEENPLVRRARQLMATYADMEELIRL--GAYRAGSDPEVDEAIRLNPAleAFLRQG 418
|
330 340
....*....|....*....|....*...
gi 12643429 521 SyspyDRVCPFYKTVGMLRNIMAFYETA 548
Cdd:PRK08927 419 K----DEATSLAEGYARLAQILGGPETE 442
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
15-522 |
2.39e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 118.39 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 15 EYGRVYAVSGPVVTAEAMSGSAMYELVRVGYY---ELVGEIIRLEGDMATIQVYEETSGVTVGDPVLR-TGKPLSVELGP 90
Cdd:PRK04196 3 EYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPngeKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 91 GIMGSIFDGIQRPLRDIGVMTNSIYIPkgVNTTAL---SRSEMWEFnplnVRVG-SHITGgdlygvvhENTLVK-QRMIV 165
Cdd:PRK04196 83 DMLGRIFDGLGRPIDGGPEIIPEKRLD--INGAPInpvAREYPEEF----IQTGiSAIDG--------LNTLVRgQKLPI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 166 aprakgtvryiapagnynledivleteFDGEITKHTMLQVWPVRQPRPVTEklpanhplftgqrvlDSLFpcvqggttai 245
Cdd:PRK04196 149 ---------------------------FSGSGLPHNELAAQIARQAKVLGE---------------EENF---------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 246 pgafgcgktvisqalskysnsdVIIYVGCGERGNEMSEVLRDFPEltceiDGVtesiMKRTALVANTSNMPVAAREASIY 325
Cdd:PRK04196 177 ----------------------AVVFAAMGITFEEANFFMEDFEE-----TGA----LERSVVFLNLADDPAIERILTPR 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 326 TGITLSEYFR-DMGYNV-AMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKclgnpEREGSVSI 403
Cdd:PRK04196 226 MALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIK-----GKKGSITQ 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 404 VGAVSPPGGDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSINWLISYSKYM-RALDEYYDknypefvplRTKVKEIL 480
Cdd:PRK04196 300 IPILTMPDDDITHPIPDLTGYITegQIV--LSRELHRKGIYPPIDVLPSLSRLMkDGIGEGKT---------REDHKDVA 368
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 12643429 481 Q-------EEEDLSEIVQLVGKASLAETDKVTLEVAKLLKDDFLQQNSY 522
Cdd:PRK04196 369 NqlyaayaRGKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQGFD 417
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
212-543 |
1.02e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 116.34 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 212 RPVTEklpanhPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIyVG-CGERGNEMSEvlrdFPE 290
Cdd:PRK08972 140 RPITE------PLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIV-VGlVGERGREVKE----FIE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 291 ltcEIDGVTESimKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSG 370
Cdd:PRK08972 209 ---EILGEEGR--ARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKG 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 371 YPAYLGARLATFYERAGRvkclGNPeREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLIS 450
Cdd:PRK08972 284 YPPSVFAKLPALVERAGN----GGP-GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEAS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 451 YSKYMRALDEyydknyPEFVPLRTKVKEIL---QEEEDLSEIvqlvgKASLAETDKvTLEVAKLLK---DDFLQQNsysp 524
Cdd:PRK08972 359 ISRVMPMVIS------EEHLEAMRRVKQVYslyQQNRDLISI-----GAYKQGSDP-RIDNAIRLQpamNAFLQQT---- 422
|
330
....*....|....*....
gi 12643429 525 YDRVCPFYKTVGMLRNIMA 543
Cdd:PRK08972 423 MKEAVPYDMSVNMLKQLAA 441
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
15-519 |
2.02e-27 |
|
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: 115.63 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 15 EYGRVYAVSGPVVTAEAMSGSAMYELVRVgyyEL------VGEIIRLEGDMATIQVYEETSGVTVGDPVLR-TGKPLSVE 87
Cdd:COG1156 5 EYRTISEIAGPLLFVEGVEGVGYGELVEI---ELpdgerrRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 88 LGPGIMGSIFDGIQRPLRDIGvmtnSIYIPK--GVNTTAL---SRSEMWEFnplnVRVG-SHITGgdlygvvhENTLVK- 160
Cdd:COG1156 82 VSEDMLGRVFNGLGRPIDGGP----PIIPEKrlDINGSPInpvAREYPREF----IQTGiSAIDG--------LNTLVRg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 161 QRMIVaprakgtvryiapagnynledivleteFDGEITKHTMLQVWPVRQPRpvteklpanhplftgqrvldslfpcVQG 240
Cdd:COG1156 146 QKLPI---------------------------FSGSGLPHNELAAQIARQAK-------------------------VRG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 241 GTtaipGAFGcgktvisqalskysnsdvIIYVGCGERGNEMSEVLRDFPEltceiDGVtesiMKRTALVANTSNMPVAAR 320
Cdd:COG1156 174 EE----EKFA------------------VVFAAMGITHDEANFFREEFEE-----TGA----LDRVVMFLNLADDPAIER 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 321 EASIYTGITLSEYFR-DMGYNV-AMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKclgnpERE 398
Cdd:COG1156 223 IITPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIK-----GRK 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 399 GSVSIVGAVSPPGGDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSINWLISYSKYM-------------RAL-DEYY 462
Cdd:COG1156 297 GSITQIPILTMPNDDITHPIPDLTGYITegQIV--LSRDLHRKGIYPPIDVLPSLSRLMkdgigegktredhADVaNQLY 374
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 12643429 463 DKnYpefvplrTKVKeilqeeeDLSEIVQLVGKASLAETDKVTLEVAKLLKDDFLQQ 519
Cdd:COG1156 375 AA-Y-------ARGQ-------EVRELAAIVGEEALSETDKKYLKFADAFERRFVNQ 416
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
211-541 |
6.93e-27 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 113.71 E-value: 6.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 211 PRPVTEKLpANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEmsevLRDFPE 290
Cdd:PRK09099 135 PDPMSRRM-VEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGRE----VREFIE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 291 LTCEIDGvtesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSG 370
Cdd:PRK09099 210 LILGEDG-----MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRG 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 371 YPAYLGARLATFYERAGRvkclgnpEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLIS 450
Cdd:PRK09099 285 FPPSVFAELPRLLERAGM-------GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 451 YSKYMraldeyydknyPEFVP-----LRTKVKEILQEEEDLSEIVQlVGKASlAETDKVTLE-VAKLLK-DDFLQQnsys 523
Cdd:PRK09099 358 LSRVM-----------PQVVPrehvqAAGRLRQLLAKHREVETLLQ-VGEYR-AGSDPVADEaIAKIDAiRDFLSQ---- 420
|
330
....*....|....*...
gi 12643429 524 PYDRVCPFYKTVGMLRNI 541
Cdd:PRK09099 421 RTDEYSDPDATLAALAEL 438
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
219-519 |
2.85e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 109.05 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 219 PANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMSEVLRDfpeltceIDGv 298
Cdd:PRK05688 147 PISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKEFIEH-------ILG- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 299 tESIMKRTALVANTSN-MPVAAREASIYTgITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGA 377
Cdd:PRK05688 219 -EEGLKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFA 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 378 RLATFYERAgrvkclGNPER-EGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMR 456
Cdd:PRK05688 297 KLPKLVERA------GNAEPgGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMP 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643429 457 ALDEyydknyPEFVPLRTKVKEIL---QEEEDLSEIVQLVgKASLAETDKVTLEVAKLLKddFLQQ 519
Cdd:PRK05688 371 QVVD------PEHLRRAQRFKQLWsryQQSRDLISVGAYV-AGGDPETDLAIARFPHLVQ--FLRQ 427
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
222-540 |
6.46e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 108.16 E-value: 6.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 222 HPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEmsevLRDFpeltceIDGVTES 301
Cdd:PRK06002 147 TGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGRE----VREF------LEDTLAD 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 302 IMKRTALVANTSN-MPVAAREASIyTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLA 380
Cdd:PRK06002 217 NLKKAVAVVATSDeSPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 381 TFYERAGrvkclgnPEREGSVSIVG--AVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMral 458
Cdd:PRK06002 296 RLLERAG-------PGAEGGGSITGifSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLA--- 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 459 deyyDKNY-PEFVPLRTKVKEILQEEEDLSEIvQLVG---KASLAETDKVTLEVAKLLkdDFLQQnsySPYDRVC--PFY 532
Cdd:PRK06002 366 ----RHAWtPEQRKLVSRLKSMIARFEETRDL-RLIGgyrAGSDPDLDQAVDLVPRIY--EALRQ---SPGDPPSddAFA 435
|
....*...
gi 12643429 533 KTVGMLRN 540
Cdd:PRK06002 436 DLAAALKG 443
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
204-460 |
1.31e-24 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 103.84 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 204 QVWPV-RQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQAL----SKySNSDVIIYVGCGERG 278
Cdd:cd01133 30 ERWPIhREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinniAK-AHGGYSVFAGVGERT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 279 NEMSEVLRDFPEltceiDGVTESI-MKRTALVANTSNMPVAAREASIYTGITLSEYFRDM-GYNVAMMADSTSRWAEALR 356
Cdd:cd01133 109 REGNDLYHEMKE-----SGVINLDgLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 357 EISGRLAEMPADSGYPAYLGARLATFYERAGRVKclgnperEGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKL 436
Cdd:cd01133 184 EVSALLGRIPSAVGYQPTLATEMGSLQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGI 256
|
250 260
....*....|....*....|....
gi 12643429 437 AQRKHFPSINWLISYSkymRALDE 460
Cdd:cd01133 257 AELGIYPAVDPLDSTS---RILDP 277
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
210-543 |
7.93e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 104.59 E-value: 7.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 210 QPRPVT--EKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEmsevLRD 287
Cdd:PRK07196 123 QLPQIHplQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGRE----VKE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 288 FPELTCEIDGVTESIMkrtaLVANTSNMPVAAREASIYTGiTLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPA 367
Cdd:PRK07196 199 FIEHSLQAAGMAKSVV----VAAPADESPLMRIKATELCH-AIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 368 DSGYPAYLGARLATFYERAgrvkclGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINW 447
Cdd:PRK07196 274 TKGYPPSAFSIIPRLAESA------GNSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDI 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 448 LISYSKYMRALDEyydknyPEFVPLRTKVKEILQEEEDLSEIVQLVGKASLAE--TDKVTLEVAKLlkDDFLQQNSYSPy 525
Cdd:PRK07196 348 SQSISRCMSQVIG------SQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADpmADQAVHYYPAI--TQFLRQEVGHP- 418
|
330
....*....|....*...
gi 12643429 526 drvCPFYKTVGMLRNIMA 543
Cdd:PRK07196 419 ---ALFSASVEQLTGMFP 433
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
216-462 |
1.73e-22 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 100.63 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 216 EKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEmsevLRDFPELTCEI 295
Cdd:PRK07960 151 QRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGRE----VKDFIENILGA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 296 DGVTESIMkrTALVANTSNMpVAAREASIYTGItlSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYL 375
Cdd:PRK07960 227 EGRARSVV--IAAPADVSPL-LRMQGAAYATRI--AEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 376 GARLATFYERAGRVKCLGnpereGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYM 455
Cdd:PRK07960 302 FAKLPALVERAGNGISGG-----GSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM 376
|
....*....
gi 12643429 456 RAL--DEYY 462
Cdd:PRK07960 377 TALidEQHY 385
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
258-456 |
3.65e-21 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 93.83 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 258 QA-LSKYSNSDVIIYVGCGERGNEMSEVLRDFPELtceidGVtesiMKRTALVANTSNMPVAAReasIYT---GITLSEY 333
Cdd:cd01135 92 QAgVVGSEENFAIVFAAMGVTMEEARFFKDDFEET-----GA----LERVVLFLNLANDPTIER---IITprmALTTAEY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 334 FR-DMGYNV-AMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKclgnpEREGSVSIVGAVSPPG 411
Cdd:cd01135 160 LAyEKGKHVlVILTDMTN-YAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVE-----GRKGSITQIPILTMPN 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 12643429 412 GDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSINWLISYSKYMR 456
Cdd:cd01135 234 DDITHPIPDLTGYITegQIY--LDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
208-543 |
9.50e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 95.14 E-value: 9.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 208 VRQPRPVTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMSEVLRD 287
Cdd:PRK08472 125 MKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPEFIEK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 288 fpeltcEIDGVTESimkrTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPA 367
Cdd:PRK08472 205 ------NLGGDLEN----TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 368 DSGYPAYLGARLATFYERAgrvkclGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINW 447
Cdd:PRK08472 275 SKGYPPSVLSLLPQLMERA------GKEEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 448 LISYSKYMRalDEYYDKNYPEFVPLRtKVKEILQEEEDLSEIvqlvgKASLAETDKvTLEVA---KLLKDDFLQQNSysp 524
Cdd:PRK08472 349 LNSASRVMN--DIISPEHKLAARKFK-RLYSLLKENEVLIRI-----GAYQKGNDK-ELDEAiskKEFMEQFLKQNP--- 416
|
330
....*....|....*....
gi 12643429 525 yDRVCPFYKTVGMLRNIMA 543
Cdd:PRK08472 417 -NELFPFEQTFEQLEEILR 434
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
178-484 |
1.65e-20 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 94.66 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 178 PAGNYNLEDIVLET-EFDGEITKHTMLQVWPVRQPrPVT--EKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKT 254
Cdd:PRK06793 92 PRGNHLLGKVLSANgEVLNEEAENIPLQKIKLDAP-PIHafEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 255 VISQALSKYSNSDVIIYVGCGERGNEMSEVLRDfpELTceidgvtESIMKRTALVANTSNMP--VAAREASIYTGItlSE 332
Cdd:PRK06793 171 TLLGMIAKNAKADINVISLVGERGREVKDFIRK--ELG-------EEGMRKSVVVVATSDEShlMQLRAAKLATSI--AE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 333 YFRDMGYNVAMMADSTSRWAEALREISGRLAEMPAdSGYPAYLGARLATFYERAGRVKclgnperEGSVSIVGAVSPPGG 412
Cdd:PRK06793 240 YFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLLERSGKTQ-------KGSITGIYTVLVDGD 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12643429 413 DFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSINWLISYSKYMralDEYYDKNYPEFVPLRTKVKEILQEEE 484
Cdd:PRK06793 312 DLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIM---EEIVSPNHWQLANEMRKILSIYKENE 380
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
207-519 |
1.77e-20 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 95.11 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 207 PVRQPRPVTEKLPANHPLF-TGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQAL----SKySNSDVIIYVGCGER---G 278
Cdd:CHL00060 127 PIHRSAPAFIQLDTKLSIFeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELinniAK-AHGGVSVFGGVGERtreG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 279 N----EMSE--VLRDfpeltceiDGVTESimkRTALVANTSNMPVAAREASIYTGITLSEYFRDMGY-NVAMMADSTSRW 351
Cdd:CHL00060 206 NdlymEMKEsgVINE--------QNIAES---KVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRF 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 352 AEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVKclgnperEGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWG 431
Cdd:CHL00060 275 VQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTK-------EGSITSIQAVYVPADDLTDPAPATTFAHLDATTV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 432 LDKKLAQRKHFPSINWLISYSKYMRAL---DEYYDknypefvpLRTKVKEILQEEEDLSEIVQLVGKASLAETDKVTleV 508
Cdd:CHL00060 348 LSRGLAAKGIYPAVDPLDSTSTMLQPRivgEEHYE--------TAQRVKQTLQRYKELQDIIAILGLDELSEEDRLT--V 417
|
330
....*....|..
gi 12643429 509 AKLLK-DDFLQQ 519
Cdd:CHL00060 418 ARARKiERFLSQ 429
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
213-538 |
3.38e-18 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 87.27 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 213 PVTEKLPanhplfTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVISQALSKYSNSDVIIYVGCGERGNEMSEVLRDFPElt 292
Cdd:PRK05922 136 PIQEIFP------TGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKE-- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 293 ceidGVTEsimKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYP 372
Cdd:PRK05922 208 ----GLAA---QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 373 AYLGARLATFYERAgrvkclGNPEReGSVSIVGAV--SPPGGD-FSDPVTSATLGivQVFWGldkklAQRKHF--PSINW 447
Cdd:PRK05922 281 ASVFHHVSEFTERA------GNNDK-GSITALYAIlhYPNHPDiFTDYLKSLLDG--HFFLT-----PQGKALasPPIDI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 448 LISYSKYMRALdeyydkNYPEFVPLRTKVKEILQEEEDLSEIVQLvgKASLAETDKVTLEVAKLLKD--DFLQQnsysPY 525
Cdd:PRK05922 347 LTSLSRSARQL------ALPHHYAAAEELRSLLKAYHEALDIIQL--GAYVPGQDAHLDRAVKLLPSikQFLSQ----PL 414
|
330
....*....|...
gi 12643429 526 DRVCPFYKTVGML 538
Cdd:PRK05922 415 SSYCALHNTLKQL 427
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
303-522 |
2.48e-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: 85.16 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 303 MKRTALVANTSNMPVAAREASIYTGITLSEYFR-DMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLAT 381
Cdd:TIGR01040 210 MERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLAT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 382 FYERAGRVKclgnpEREGSVSIVGAVSPPGGDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSINWLISYSKYMR-AL 458
Cdd:TIGR01040 290 IYERAGRVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPINVLPSLSRLMKsAI 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12643429 459 DEYYDKNYPEFVPLRTKVKEILQeeEDLSEIVQLVGKASLAETDKVTLEVAKLLKDDFLQQNSY 522
Cdd:TIGR01040 363 GEGMTRKDHSDVSNQLYACYAIG--KDVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPY 424
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
4-399 |
1.60e-16 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 82.66 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 4 LRKFKDEERESEYGRVYAVSGPVVTAEAMSGSAMYELVRV--GYYELVGEiirLEGDMATIQVYEETSGVTVGDPVLRTG 81
Cdd:PRK13343 16 IARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFegGSRGFAFN---LEEELVGAVLLDDTADILAGTEVRRTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 82 KPLSVELGPGIMGSIFDGIQRPLRDIGvmtnsiyipkGVNTTALSrsemwefnPLNVrvgshitggdlygvvhentlvkq 161
Cdd:PRK13343 93 RVLEVPVGDGLLGRVIDPLGRPLDGGG----------PLQATARR--------PLER----------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 162 rmivaprakgtvryIAPAgnynlediVLEtefdgeitkhtmlqvwpvRQPrpVTEklpanhPLFTGQRVLDSLFPCVQGG 241
Cdd:PRK13343 132 --------------PAPA--------IIE------------------RDF--VTE------PLQTGIKVVDALIPIGRGQ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 242 TTAIPGAFGCGKT------VISQalskySNSDVI-IYVGCGERGNEMSEVLRdfpelTCEIDGVtesiMKRTALVANTSN 314
Cdd:PRK13343 164 RELIIGDRQTGKTaiaidaIINQ-----KDSDVIcVYVAIGQKASAVARVIE-----TLREHGA----LEYTTVVVAEAS 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 315 MPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPADSGYPA---YLGARLatfYERAGRVkc 391
Cdd:PRK13343 230 DPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRL---LERAAKL-- 304
|
....*...
gi 12643429 392 lgNPEREG 399
Cdd:PRK13343 305 --SPELGG 310
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
16-422 |
4.04e-14 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 74.69 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 16 YGRVYAVSGPVVTAEAmSGSAMYELVRVGYYE--LVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGKPLSVELGPGIM 93
Cdd:PRK02118 5 YTKITDITGNVITVEA-EGVGYGELATVERKDgsSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 94 GSIFDGIQRPlRDIGVMTNSIYIPKGVNTtalsrsemweFNPLN-------VRVGshITGGDLYgvvheNTLVKQRMIVA 166
Cdd:PRK02118 84 GRRFNGSGKP-IDGGPELEGEPIEIGGPS----------VNPVKrivpremIRTG--IPMIDVF-----NTLVESQKIPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 167 prakgtvrYIAPAGNYN--LEDIVLETEfdgeitkhtmlqvwpvrqprpvteklpanhplftgqrvldslfpcvqggtta 244
Cdd:PRK02118 146 --------FSVSGEPYNalLARIALQAE---------------------------------------------------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 245 ipgafgcgktvisqalskysnSDVIIYVGCGERGNEMSEVLRDFPELtceidGVtesiMKRTALVANTSNMPVAAREASI 324
Cdd:PRK02118 166 ---------------------ADIIILGGMGLTFDDYLFFKDTFENA-----GA----LDRTVMFIHTASDPPVECLLVP 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 325 YTGITLSEYFR-DMGYNV-AMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLATFYERAGRVkclgnpEREGSVS 402
Cdd:PRK02118 216 DMALAVAEKFAlEGKKKVlVLLTDMTN-FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDF------EDGGSIT 288
|
410 420
....*....|....*....|
gi 12643429 403 IVGAVSPPGGDFSDPVTSAT 422
Cdd:PRK02118 289 IIAVTTMPGDDVTHPVPDNT 308
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
207-453 |
5.49e-14 |
|
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: 72.59 E-value: 5.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 207 PVRQPRP-VTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKT------VISQalskySNSDVI-IYVGCGERG 278
Cdd:cd01132 35 RVESKAPgIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaiaidtIINQ-----KGKKVYcIYVAIGQKR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 279 NEMSEVLRDFPEltceidgvtESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREI 358
Cdd:cd01132 110 STVAQIVKTLEE---------HGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 359 SGRLAEMPADSGYPA---YLGARLatfYERAGRvkcLGNPEREGSVSIVGAVSPPGGDFSD--P--VTSATLGivQVFwg 431
Cdd:cd01132 181 SLLLRRPPGREAYPGdvfYLHSRL---LERAAK---LSDELGGGSLTALPIIETQAGDVSAyiPtnVISITDG--QIF-- 250
|
250 260
....*....|....*....|..
gi 12643429 432 LDKKLAQRKHFPSINWLISYSK 453
Cdd:cd01132 251 LESELFNKGIRPAINVGLSVSR 272
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
19-81 |
6.73e-14 |
|
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: 66.80 E-value: 6.73e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12643429 19 VYAVSGPVVTAEAMSGSA--MYELVRVGYYE----LVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTG 81
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLpgLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
214-453 |
6.67e-12 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 68.14 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 214 VTEKLPANHPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVIS------------QALSKysNSDVIIYVGCGERGNEM 281
Cdd:PTZ00185 163 IVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvstiinqvrinqQILSK--NAVISIYVSIGQRCSNV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 282 SEVLRDFPeltceidgvTESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGR 361
Cdd:PTZ00185 241 ARIHRLLR---------SYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 362 LAEMPADSGYPA---YLGARLatfYERAGRvkcLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQ 438
Cdd:PTZ00185 312 LRRPPGREAYPGdvfYLHSRL---LERAAM---LSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFT 385
|
250
....*....|....*
gi 12643429 439 RKHFPSINWLISYSK 453
Cdd:PTZ00185 386 GGQRPAVNIGLSVSR 400
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
212-453 |
1.30e-11 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 67.30 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 212 RPVTEklpanhPLFTGQRVLDSLFPCVQGGTTAIPGAFGCGKTVIsqALSKYSN---SDVI-IYVGCGERGNEMSEVLRD 287
Cdd:CHL00059 119 RSVYE------PLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAV--ATDTILNqkgQNVIcVYVAIGQKASSVAQVVTT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 288 FPEltceidgvtESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYNVAMMADSTSRWAEALREISGRLAEMPA 367
Cdd:CHL00059 191 LQE---------RGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 368 DSGYPA---YLGARLatfYERAGRvkcLGNPEREGSVSIVGAVSPPGGDFSD--P--VTSATLGivQVFwgLDKKLAQRK 440
Cdd:CHL00059 262 REAYPGdvfYLHSRL---LERAAK---LSSQLGEGSMTALPIVETQAGDVSAyiPtnVISITDG--QIF--LSADLFNAG 331
|
250
....*....|...
gi 12643429 441 HFPSINWLISYSK 453
Cdd:CHL00059 332 IRPAINVGISVSR 344
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
16-82 |
7.54e-11 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 58.09 E-value: 7.54e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12643429 16 YGRVYAVSGPVVTAEAMSGSAMYELVRVG------YYELVGEIIRLEGDMATIQVYEETSGVTVGDPVLRTGK 82
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIErgdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
475-541 |
4.03e-07 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 47.44 E-value: 4.03e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12643429 475 KVKEILQEEEDLSEIVQLVGKASLAETDKVTLEVAKLLKdDFLQQNSYSPYdrvcPFYKTVGMLRNI 541
Cdd:cd01429 7 GFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLE-EFLQQGQFEPE----TIEDTLEKLYPI 68
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
195-389 |
1.15e-06 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 51.60 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 195 GEI-TKHTMlqvwPVRQPRP-VTEKLPANHPLFTGQRVLDSLFPCVQG-----------GTTAIpgafgCGKTVISQals 261
Cdd:PRK09281 119 GPIeATETR----PVERKAPgVIDRKSVHEPLQTGIKAIDAMIPIGRGqreliigdrqtGKTAI-----AIDTIINQ--- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 262 kySNSDVI-IYVGCGERGNEMSEVLRdfpelTCEIDGVtesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYN 340
Cdd:PRK09281 187 --KGKDVIcIYVAIGQKASTVAQVVR-----KLEEHGA----MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKD 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 12643429 341 VAMMADSTSRWAEALREIS-------GRLAempadsgYPA---YLGARLatfYERAGRV 389
Cdd:PRK09281 256 ALIVYDDLSKQAVAYRQLSlllrrppGREA-------YPGdvfYLHSRL---LERAAKL 304
|
|
| 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 ... |
15-82 |
4.14e-06 |
|
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core, that is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex which forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349742 [Multi-domain] Cd Length: 72 Bit Score: 44.73 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643429 15 EYGRVYAVSGPVVTAEAMSGsamyelvrVGYYELV-----------GEIIRLEGDMATIQVYEETSGVTVGDPVLR-TGK 82
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKG--------VKYGEIVeitlpdgevrrGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRfTGE 72
|
|
| |
