|
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 ... |
17-609 |
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: 1258.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 17 TFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMG 96
Cdd:TIGR01042 1 EYGYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 97 AIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWDFTPcKNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTV 176
Cdd:TIGR01042 81 NIFDGIQRPLKAIAEQSQSIYIPRGVNVPALDRDKKWEFTP-KKLRVGDHITGGDIYGTVFENSLIKHKIMLPPRARGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 177 TYIAPPGNYDTSDVVLELEFEGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGK 256
Cdd:TIGR01042 160 TYIAPAGNYTVDDTVLEVEFQGVKKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 257 TVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEY 336
Cdd:TIGR01042 240 TVISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEVDGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 337 FRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGD 416
Cdd:TIGR01042 320 FRDMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 417 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLV 496
Cdd:TIGR01042 400 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 497 GKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDNKITWSIIREHMGD 576
Cdd:TIGR01042 480 GKDALAETDKITLEVAKLIKEDFLQQNGYTPYDRFCPFYKTVGMMRNMIAFYDLARQAVERTAQDDNKITWSIIKESLGD 559
|
570 580 590
....*....|....*....|....*....|...
6WM2_A 577 ILYKLSSMKFKDPLkDGEAKIKSDYAQLLEDMQ 609
Cdd:TIGR01042 560 LLYRLSSMKFEDPS-DGEAKIKADYEKLNEDMQ 591
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
15-615 |
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: 926.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 15 ESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGI 94
Cdd:COG1155 1 MMTKGKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 95 MGAIFDGIQRPLSDISSQTqSIYIPRGVNVSALSRDIKWDFTPCKnlRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRG 174
Cdd:COG1155 81 LGNIFDGIQRPLDKIAEKS-GDFIPRGVDVPALDREKKWDFTPTV--KVGDKVSAGDILGTVQETPLIEHKIMVPPGVSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 175 TVTYIAPPGNYDTSDVVLELE-FEGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFG 253
Cdd:COG1155 158 TVKEIAPEGEYTVEDTIAVLEdEDGEEHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 254 CGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTmevDGKV-ESIMKRTALVANTSNMPVAAREASIYTGIT 332
Cdd:COG1155 238 TGKTVTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPELI---DPKTgRPLMERTVLIANTSNMPVAAREASIYTGIT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 333 LSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPerEGSVSIVGAVSP 412
Cdd:COG1155 315 IAEYYRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 413 PGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTE-FVPLRTKAKEILQEEEDLAE 491
Cdd:COG1155 393 PGGDFSEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYDENVDPdWSELRNEAMDLLQEEAELQE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 492 IVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVEttaqsdNKITWSIIR 571
Cdd:COG1155 473 IVRLVGEDALPDEDRLTLEVARLIREGFLQQNAFDDVDTYCPLEKQYKMLKLILTFYDKAFEALE------KGVPLSEIK 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....
6WM2_A 572 EHmgDILYKLSSMKFkDPLKDGEAKIKsdyaQLLEDMQNAFRSL 615
Cdd:COG1155 547 EL--PLREKIARMKY-SPENELLEKFD----ELEKEIDEEIEEL 583
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
19-606 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 893.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 19 GYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAI 98
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 99 FDGIQRPLSDISSQTqSIYIPRGVNVSALSRDIKWDFTPckNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTY 178
Cdd:PRK04192 85 FDGIQRPLDELAEKS-GDFLERGVYVPALDREKKWEFTP--TVKVGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 179 IAPPGNYDTSDVVLELE-FEGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 257
Cdd:PRK04192 162 IVSEGDYTVDDTIAVLEdEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 258 VISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKveSIMKRTALVANTSNMPVAAREASIYTGITLSEYF 337
Cdd:PRK04192 242 VTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELIDPKTGR--PLMERTVLIANTSNMPVAAREASIYTGITIAEYY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 338 RDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPerEGSVSIVGAVSPPGGDF 417
Cdd:PRK04192 320 RDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGDF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 418 SDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHF-TEFVPLRTKAKEILQEEEDLAEIVQLV 496
Cdd:PRK04192 398 SEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWEENVdPDWRELRDEAMDLLQREAELQEIVRLV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 497 GKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAqSDNKITWSIIREHMGD 576
Cdd:PRK04192 478 GPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQYEMLKLILTFYDEAFKALEKGV-PVSEILELEVRDRIAR 556
|
570 580 590
....*....|....*....|....*....|
6WM2_A 577 ILYKLSSMkFKDPLKDGEAKIKSDYAQLLE 606
Cdd:PRK04192 557 LKYIPENE-YLEKIDEIFEKLEEELEELIA 585
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
19-613 |
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: 810.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 19 GYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAI 98
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 99 FDGIQRPLSDISSQTQSiYIPRGVNVSALSRDIKWDFTPckNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTY 178
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGD-FIARGVDAPGLDRDKKWHFKP--TVKEGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 179 IAPPGNYDTSDVVLELEFEGvKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTV 258
Cdd:TIGR01043 159 IAEEGDYTVEDTIAVVDTDG-DEEIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 259 ISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKveSIMKRTALVANTSNMPVAAREASIYTGITLSEYFR 338
Cdd:TIGR01043 238 TQHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPELKDPKTGK--PLMERTVLIANTSNMPVAAREASIYTGITIAEYFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 339 DMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFS 418
Cdd:TIGR01043 316 DMGYDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDFS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 419 DPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFT-EFVPLRTKAKEILQEEEDLAEIVQLVG 497
Cdd:TIGR01043 396 EPVTQNTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVQDWWHENVDpDWREMRDEAMDLLQKESELQEIVQLVG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 498 KASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDnKITWSIIREhmgdi 577
Cdd:TIGR01043 476 PDALPERQKLILEVARMIREAFLQQNAFDPVDTYCPPQKQYRILRAIMNFYDEAMEALERGVPVE-EILKLEVKE----- 549
|
570 580 590
....*....|....*....|....*....|....*.
6WM2_A 578 lyKLSSMKFkDPLKDGEAKIKsdyaQLLEDMQNAFR 613
Cdd:TIGR01043 550 --EIGRMKY-EPDNDILAKID----EILEKIEKEFK 578
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
85-457 |
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: 624.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 85 PLSVELGPGIMGAIFDGIQRPLSDISsQTQSIYIPRGVnvsalsrdikwdftpcknlrvgshitggdiygivsenslikh 164
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIA-ETGSIFIPRGV------------------------------------------ 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 165 kimlpprnrgtvtyiappgnydtsdvvlelefegvkekftMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGG 244
Cdd:cd01134 38 ----------------------------------------NVQRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGG 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 245 TTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGkvESIMKRTALVANTSNMPVAARE 324
Cdd:cd01134 78 TAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITG--ESLMERTVLIANTSNMPVAARE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 325 ASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSV 404
Cdd:cd01134 156 ASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSV 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
6WM2_A 405 SIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKY 457
Cdd:cd01134 236 TIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
257-606 |
6.32e-118 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 374.74 E-value: 6.32e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 257 TVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKveSIMKRTALVANTSNMPVAAREASIYTGITLSEY 336
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGK--PLMERTVLIANTSNMPVAAREASIYTGITIAEY 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 337 FRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGD 416
Cdd:PRK14698 748 FRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGD 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 417 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFT-EFVPLRTKAKEILQEEEDLAEIVQL 495
Cdd:PRK14698 828 FSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNVDpEWKAMRDKAMELLQKEAELQEIVRI 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 496 VGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMARRAVETTAQSDnKITWSIIREHMG 575
Cdd:PRK14698 908 VGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYDKTMDAISRGVPLE-EIAKLPVREEIG 986
|
330 340 350
....*....|....*....|....*....|.
6WM2_A 576 dilyklsSMKFKDPLKDGEAKIKSDYAQLLE 606
Cdd:PRK14698 987 -------RMKFEPDIEKIKALIDKTNEQFDE 1010
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
230-455 |
4.32e-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: 311.21 E-value: 4.32e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 230 GQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPEltmevdgkvESIMKRT 309
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLG---------SGALKRT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 310 ALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERA 389
Cdd:pfam00006 72 VVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6WM2_A 390 GRVKclgnpEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYS 455
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 ... |
205-457 |
6.54e-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: 282.04 E-value: 6.54e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 205 MVQVWPVRQVRP-VTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNS---DVIIYVGCGER 280
Cdd:cd19476 28 TKQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKahaGVVVFAGIGER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 281 GNEMSEVLRDFPELtmevdgkveSIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALRE 360
Cdd:cd19476 108 GREVNDLYEEFTKS---------GAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALRE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 361 ISGRLAEMPADSGYPAYLGARLASFYERAGRVKclgnpEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLA 440
Cdd:cd19476 179 MSALLGEPPGREGYPPYLFTKLATLYERAGKVK-----DGGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELA 253
|
250
....*....|....*..
6WM2_A 441 QRKHFPSVNWLISYSKY 457
Cdd:cd19476 254 RKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
19-263 |
2.68e-73 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 254.18 E-value: 2.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 19 GYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAI 98
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 99 FDGIQRPLSDISSQTQSiYIPRGVNVSALSRDIKWDFTPckNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTY 178
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFIP--KVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 179 IAPPGNYDTSDVVLELEF-EGVKEKFTMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 257
Cdd:PRK14698 162 IADEGEYTIEEVIAKVKTpSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKC 241
|
....*.
6WM2_A 258 VISQSL 263
Cdd:PRK14698 242 VDGDTL 247
|
|
| ATP-synt_ab_Xtn |
pfam16886 |
ATPsynthase alpha/beta subunit N-term extension; ATP-synt_ab_Xtn is an extension of the ... |
99-221 |
4.76e-66 |
|
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: 211.49 E-value: 4.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 99 FDGIQRPLSDISSQTQSiYIPRGVNVSALSRDIKWDFTPckNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTY 178
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTP--TVKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
6WM2_A 179 IAPPGNYDTSDVVLELEFEGVKEKFTMVQVWPVRQVRPVTEKL 221
Cdd:pfam16886 78 IAPEGEYTVEDTIAEVEDEGKEKELTMMQKWPVRRPRPYKEKL 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 ... |
472-577 |
1.89e-51 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 172.19 E-value: 1.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 472 FVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMIAFYDMA 551
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDTYCPLEKQYKMLKLILTFYDKA 80
|
90 100
....*....|....*....|....*.
6WM2_A 552 RRAVEtTAQSDNKITWSIIREHMGDI 577
Cdd:cd18111 81 LEALE-KGVPLSKILELPVREKIARM 105
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
44-522 |
3.21e-46 |
|
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: 169.09 E-value: 3.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 44 RVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSdissqtqsiyiprgvn 123
Cdd:TIGR01026 53 RGSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSIKVGDGLLGRVLDGLGKPID---------------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 124 vsalsrdikwdftpcknlrvgshiTGGDIYGIVSENSLIKHKImlPPRNRGtvtyiappgnydtsdvvlelefegvkekf 203
Cdd:TIGR01026 117 ------------------------GKGKFLDNVETEGLITAPI--NPLKRA----------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 204 tmvqvwPVRQVrpvteklpanhpLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNE 283
Cdd:TIGR01026 142 ------PIREI------------LSTGVRSIDGLLTVGKGQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGRE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 284 msevLRDFPELTMEVDGkvesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISG 363
Cdd:TIGR01026 204 ----VREFIEHDLGEEG-----LKRSVVVVATSDQSPLLRLKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 364 RLAEMPADSGYPAYLGARLASFYERAGrvkclgnPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRK 443
Cdd:TIGR01026 275 AAGEPPATKGYTPSVFSTLPRLLERAG-------ASGKGSITAFYTVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 444 HFPSVNWLISYSKYMRAL--DEYYDKhftefvplRTKAKEIL---QEEEDLAEIvQLVGKASLAETDKITLEVAKLIKdd 518
Cdd:TIGR01026 348 HYPAIDVLASISRLMTAIvsEEHRRA--------ARKFRELLskyKDNEDLIRI-GAYQRGSDRELDFAIAKYPKLER-- 416
|
....
6WM2_A 519 FLQQ 522
Cdd:TIGR01026 417 FLKQ 420
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
18-541 |
2.22e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 155.74 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 18 FGYVHGVsGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGA 97
Cdd:PRK06820 30 RGPIVEI-GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 98 IFDGIQRPLSDissqtqsiYIPRGvnvsalsrdikwdfTPCKNLrvgshitggdiygivsenslikhkimlpprnrgtvt 177
Cdd:PRK06820 109 ILDGLGAPIDG--------GPPLT--------------GQWREL------------------------------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 178 YIAPPGnydtsdvvlelefegvkekftmvqvwpvrqvrPVTEKlPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 257
Cdd:PRK06820 131 DCPPPS--------------------------------PLTRQ-PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKS 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 258 VISQSLSKYSNSDVIIYVGCGERGNEmsevLRDFPELTMEVDGKvesimKRTALVANTSNMPVAAREASIYTGITLSEYF 337
Cdd:PRK06820 178 TLLGMLCADSAADVMVLALIGERGRE----VREFLEQVLTPEAR-----ARTVVVVATSDRPALERLKGLSTATTIAEYF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 338 RDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGrvkclgnPEREGSVSIVGAVSPPGGDF 417
Cdd:PRK06820 249 RDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG-------NSDRGSITAFYTVLVEGDDM 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 418 SDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEyydkhfTEFVPLRTKAKEILQEEEDLAEIVQlVG 497
Cdd:PRK06820 322 NEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVS------AGQLAMAQKLRRMLACYQEIELLVR-VG 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
6WM2_A 498 ---KASLAETDKiTLEVAKLIKdDFLQQNGytpyDRFCPFYKTVGML 541
Cdd:PRK06820 395 eyqAGEDLQADE-ALQRYPAIC-AFLQQDH----SETAHLETTLEHL 435
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
18-545 |
4.16e-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: 4.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 18 FGYVHGVSGPVVTAcdmAG--AAMYELVRV---GHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGP 92
Cdd:COG1157 20 SGRVTRVVGLLIEA---VGpdASIGELCEIetaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 93 GIMGAIFDGIQRPLSDissqtqsiyipRGvnvsalsrdikwdftpcknlrvgshitggdiygivsenslikhkimlPPRN 172
Cdd:COG1157 97 GLLGRVLDGLGRPLDG-----------KG-----------------------------------------------PLPG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 173 RGTVTYIAPPGNYdtsdvvleLEfegvkekftmvqvwpvRQvrPVTEklpanhPLLTGQRVLDALFPCVQG---GTTAip 249
Cdd:COG1157 119 EERRPLDAPPPNP--------LE----------------RA--RITE------PLDTGVRAIDGLLTVGRGqriGIFA-- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 250 GAfGCGKTVISQSLSKYSNSDVIIyVG-CGERGNEmsevLRDFPELTMEVDGkvesiMKRTALVANTSNMPVAAREASIY 328
Cdd:COG1157 165 GS-GVGKSTLLGMIARNTEADVNV-IAlIGERGRE----VREFIEDDLGEEG-----LARSVVVVATSDEPPLMRLRAAY 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 329 TGITLSEYFRDMGYHVSMMADSTSRWAEALREISgrLA--EMPADSGYPAYLGARLASFYERAGrvkclgnPEREGSVSI 406
Cdd:COG1157 234 TATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIG--LAagEPPATRGYPPSVFALLPRLLERAG-------NGGKGSITA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 407 VGAVSPPGGDFSDPVTSATLG-----IVqvfwgLDKKLAQRKHFPSVNWLISYSKYMRAL--DEYYDkhftefvpLRTKA 479
Cdd:COG1157 305 FYTVLVEGDDMNDPIADAVRGildghIV-----LSRKLAERGHYPAIDVLASISRVMPDIvsPEHRA--------LARRL 371
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6WM2_A 480 KEIL---QEEEDLaeIvqLVG---KASLAETDK-ITLeVAKLikDDFLQQngytPYDRFCPFYKTVGMLSNMI 545
Cdd:COG1157 372 RRLLaryEENEDL--I--RIGayqPGSDPELDEaIAL-IPAI--EAFLRQ----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 ... |
18-84 |
2.79e-39 |
|
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349743 [Multi-domain] Cd Length: 67 Bit Score: 138.04 E-value: 2.79e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6WM2_A 18 FGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGK 84
Cdd:cd18119 1 KGKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTGK 67
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
222-456 |
8.00e-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: 143.85 E-value: 8.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 222 PANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEmsevLRDFPELTMEVDGk 301
Cdd:cd01136 46 PIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE----VREFIEKDLGEEG- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 302 vesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGAR 381
Cdd:cd01136 121 ----LKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFAL 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6WM2_A 382 LASFYERAGrvkclgnPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSK 456
Cdd:cd01136 197 LPRLLERAG-------NGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
19-523 |
8.29e-35 |
|
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: 136.45 E-value: 8.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 19 GYVHGVSGPVVTA--CDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMG 96
Cdd:TIGR03496 1 GRVTRVVGLVLEAvgLRAPVGSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 97 AIFDGIQRPLSDISsqtqsiyiprgvnvsalsrdikwdftpcknlrvgshitggdiygivsenslikhkimlPPRNRGTV 176
Cdd:TIGR03496 81 RVIDGLGRPLDGKG----------------------------------------------------------PLDAGERV 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 177 TYIAPPGNydtsdvvlelefegvkekftmvqvwPVRQvRPVTEklpanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGK 256
Cdd:TIGR03496 103 PLYAPPIN-------------------------PLKR-APIDE------PLDVGVRAINGLLTVGRGQRMGIFAGSGVGK 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 257 TVISQSLSKYSNSDVIIyVG-CGERGNEmsevLRDFPELTMEVDGkvesiMKRTALVANTSNMPVAAREASIYTGITLSE 335
Cdd:TIGR03496 151 STLLGMMARYTEADVVV-VGlIGERGRE----VKEFIEDILGEEG-----LARSVVVAATADESPLMRLRAAFYATAIAE 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 336 YFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGrvkclgnPEREGSVSIVG--AVSPP 413
Cdd:TIGR03496 221 YFRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAG-------NGEEGKGSITAfyTVLVE 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 414 GGDFSDPVTSATLGIVQvfwG---LDKKLAQRKHFPSVNWLISYSKYMRAL--DEYYDkhftefvpLRTKAKEIL---QE 485
Cdd:TIGR03496 294 GDDQQDPIADAARAILD---GhivLSRELAEQGHYPAIDILASISRVMPDVvsPEHRQ--------AARRFKQLLsryQE 362
|
490 500 510 520
....*....|....*....|....*....|....*....|
6WM2_A 486 EEDLAEIvqlvGkASLAETDKITLEVAKLIK--DDFLQQN 523
Cdd:TIGR03496 363 NRDLISI----G-AYQAGSDPELDQAIALYPriEAFLQQG 397
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
216-461 |
3.00e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 132.57 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 216 PVTEKLpANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEmsevLRDFPELT 295
Cdd:PRK06936 136 PMSRRL-IETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGRE----VREFIESD 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 296 MEVDGkvesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYP 375
Cdd:PRK06936 211 LGEEG-----LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYP 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 376 AYLGARLASFYERAGrvkclgnPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYS 455
Cdd:PRK06936 286 PSVFAALPRLMERAG-------QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSAS 358
|
....*.
6WM2_A 456 KYMRAL 461
Cdd:PRK06936 359 RVMNQI 364
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
219-492 |
1.69e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 130.23 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 219 EKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEmsevLRDFPELTMEV 298
Cdd:PRK07721 134 KRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIALIGERGRE----VREFIERDLGP 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 299 DGkvesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYL 378
Cdd:PRK07721 210 EG-----LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSV 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 379 GARLASFYERAGrvkclgnPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYM 458
Cdd:PRK07721 285 FAILPKLLERTG-------TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM 357
|
250 260 270
....*....|....*....|....*....|....*..
6WM2_A 459 RALDEYYDKHFTEfvplrtKAKEIL---QEEEDLAEI 492
Cdd:PRK07721 358 NHIVSPEHKEAAN------RFRELLstyQNSEDLINI 388
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
34-461 |
3.21e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 129.30 E-value: 3.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 34 MAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISsqt 113
Cdd:PRK07594 37 LPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRE--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 114 qsiyIPRGvnvsalsrdikwdftPCKNLRVgshitggdiygivsenslikhkimLPPrnrgtvtyiaPPgnydtsdvvle 193
Cdd:PRK07594 114 ----LPDV---------------CWKDYDA------------------------MPP----------PA----------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 194 lefegvkekftMVQvwpvrqvRPVTEklpanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVII 273
Cdd:PRK07594 130 -----------MVR-------QPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDADSNV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 274 YVGCGERGNEmsevLRDFPELTMEVDGKvesimKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSR 353
Cdd:PRK07594 186 LVLIGERGRE----VREFIDFTLSEETR-----KRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 354 WAEALREISGRLAEMPADSGYPAYLGARLASFYERAGrvkcLGNperEGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFW 433
Cdd:PRK07594 257 YARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG----MGE---KGSITAFYTVLVEGDDMNEPLADEVRSLLDGHI 329
|
410 420
....*....|....*....|....*...
6WM2_A 434 GLDKKLAQRKHFPSVNWLISYSKYMRAL 461
Cdd:PRK07594 330 VLSRRLAERGHYPAIDVLATLSRVFPVV 357
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
215-546 |
8.76e-32 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 128.19 E-value: 8.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 215 RPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEvlrdFPEl 294
Cdd:PRK08149 123 PSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTE----FVE- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 295 TMEVDGKVEsimkRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGY 374
Cdd:PRK08149 198 SLRASSRRE----KCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 375 PAYLGARLASFYERAGRVKclgnperEGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISY 454
Cdd:PRK08149 274 PASVFDSLPRLLERPGATL-------AGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 455 SkymRALDEYYDKHFTEfvpLRTKAKEILQEEEDLAEIVQLvGKASL---AETDKITLEVAKLikDDFLQQngytPYDRF 531
Cdd:PRK08149 347 S---RVFGQVTDPKHRQ---LAAAFRKLLTRLEELQLFIDL-GEYRRgenADNDRAMDKRPAL--EAFLKQ----DVAEK 413
|
330
....*....|....*
6WM2_A 532 CPFYKTVGMLSNMIA 546
Cdd:PRK08149 414 SSFSDTLERLNEFAA 428
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
226-523 |
2.07e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 127.02 E-value: 2.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 226 PLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDfpelTMEVDGkvesi 305
Cdd:PRK08927 141 PLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQD----DLGPEG----- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 306 MKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASF 385
Cdd:PRK08927 212 LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 386 YERAGRvkclgNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYM-RALDEy 464
Cdd:PRK08927 292 LERAGP-----GPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMpGCNDP- 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
6WM2_A 465 ydkhftEFVPLRTKAKEILQEEEDLAEIVQLvgKASLAETDKITLEVAKLIKD--DFLQQN 523
Cdd:PRK08927 366 ------EENPLVRRARQLMATYADMEELIRL--GAYRAGSDPEVDEAIRLNPAleAFLRQG 418
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
21-526 |
4.08e-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: 114.86 E-value: 4.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 21 VHGVSGPVVTACDMAGAAMYELVRV---GHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLR-TGKPLSVELGPGIMG 96
Cdd:COG1156 9 ISEIAGPLLFVEGVEGVGYGELVEIelpDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSEDMLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 97 AIFDGIQRP---LSDISSQTQsiyipRGVNVSAL---SRDIKWDFtpcknlrvgshI-TGgdIYGIVSENSLIK-HKimL 168
Cdd:COG1156 89 RVFNGLGRPidgGPPIIPEKR-----LDINGSPInpvAREYPREF-----------IqTG--ISAIDGLNTLVRgQK--L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 169 P-------PRNRgtvtyIAppgnydtsdvvlelefegvkekftmVQVwpVRQVRpvteklpanhplltgqrvldalfpcV 241
Cdd:COG1156 149 PifsgsglPHNE-----LA-------------------------AQI--ARQAK-------------------------V 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 242 QGGTtaipGAFGcgktvisqslskysnsdvIIYVGCGERGNEMSEVLRDFPEltmevdgkvESIMKRTALVANTSNMPVA 321
Cdd:COG1156 172 RGEE----EKFA------------------VVFAAMGITHDEANFFREEFEE---------TGALDRVVMFLNLADDPAI 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 322 AREASIYTGITLSEYFR-DMGYHV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKclgnpE 399
Cdd:COG1156 221 ERIITPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIK-----G 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 400 REGSVSIVGAVSPPGGDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSVNWLISYSKYM-------------RAL-DE 463
Cdd:COG1156 295 RKGSITQIPILTMPNDDITHPIPDLTGYITegQIV--LSRDLHRKGIYPPIDVLPSLSRLMkdgigegktredhADVaNQ 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
6WM2_A 464 YYDKHftefvplrTKAKeilqeeeDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYT 526
Cdd:COG1156 373 LYAAY--------ARGQ-------EVRELAAIVGEEALSETDKKYLKFADAFERRFVNQGFDE 420
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
21-526 |
6.24e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 114.15 E-value: 6.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 21 VHGVSGPVVTACDMAGAAMYELVRV---GHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLR-TGKPLSVELGPGIMG 96
Cdd:PRK04196 7 VSEIKGPLLFVEGVEGVAYGEIVEIelpNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSEDMLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 97 AIFDGIQRPLSD----ISSQTQSIyiprgvNVSAL---SRDIKWDFtpcknlrvgshI-TGgdIYGIVSENSLIK-HKim 167
Cdd:PRK04196 87 RIFDGLGRPIDGgpeiIPEKRLDI------NGAPInpvAREYPEEF-----------IqTG--ISAIDGLNTLVRgQK-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 168 LP-------PRNRgtvtyIAppgnydtsdvvlelefegvkekftmVQVwpVRQVRpvteklpanhplltgqrvldalfpc 240
Cdd:PRK04196 146 LPifsgsglPHNE-----LA-------------------------AQI--ARQAK------------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 241 VQGGTTAipgaFgcgktvisqslskysnsdVIIYVGCGERGNEMSEVLRDFPEltmevdgkvESIMKRTALVANTSNMPV 320
Cdd:PRK04196 169 VLGEEEN----F------------------AVVFAAMGITFEEANFFMEDFEE---------TGALERSVVFLNLADDPA 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 321 AAREASIYTGITLSEYFR-DMGYHV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKclgnp 398
Cdd:PRK04196 218 IERILTPRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIK----- 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 399 EREGSVSIVGAVSPPGGDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSVNWLISYSKYMralDEYYDKHFTefvplR 476
Cdd:PRK04196 292 GKKGSITQIPILTMPDDDITHPIPDLTGYITegQIV--LSRELHRKGIYPPIDVLPSLSRLM---KDGIGEGKT-----R 361
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
6WM2_A 477 TKAKEILQ-------EEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYT 526
Cdd:PRK04196 362 EDHKDVANqlyaayaRGKDLRELAAIVGEEALSERDRKYLKFADAFEREFVNQGFDE 418
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
16-546 |
1.07e-26 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 113.32 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 16 STFGYVHGVSGPV--VTACDMAGAAMYELvRVGHSELV--GEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELG 91
Cdd:PRK09099 23 RRTGKVVEVIGTLlrVSGLDVTLGELCEL-RQRDGTLLqrAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 92 PGIMGAIFDGIQRPlsdissqtqsiyiprgvnvsalsrdikwdftpcknlrvgshITGGdiygivsenslikhkimlppr 171
Cdd:PRK09099 102 PALLGRVIDGLGEP-----------------------------------------IDGG--------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 172 nrgtvtyiaPPGNYDTSDVVLELEfegvkekftmvqvwPVRQVRPVTEklpanHPLLTGQRVLDALFPCVQGGTTAIPGA 251
Cdd:PRK09099 120 ---------GPLDCDELVPVIAAP--------------PDPMSRRMVE-----APLPTGVRIVDGLMTLGEGQRMGIFAP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 252 FGCGKTVISQSLSKYSNSDVIIYVGCGERGNEmsevLRDFPELTMEVDGkvesiMKRTALVANTSNMPVAAREASIYTGI 331
Cdd:PRK09099 172 AGVGKSTLMGMFARGTQCDVNVIALIGERGRE----VREFIELILGEDG-----MARSVVVCATSDRSSIERAKAAYVAT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 332 TLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRvkclgnpEREGSVSIVGAVS 411
Cdd:PRK09099 243 AIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM-------GETGSITALYTVL 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 412 PPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEyyDKHFTEFVPLRtkakEILQEEEDLAE 491
Cdd:PRK09099 316 AEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVP--REHVQAAGRLR----QLLAKHREVET 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
6WM2_A 492 IVQL---------VGKASLAETDKItlevaklikDDFLQQngytPYDRFCPFYKTVGMLSNMIA 546
Cdd:PRK09099 390 LLQVgeyragsdpVADEAIAKIDAI---------RDFLSQ----RTDEYSDPDATLAALAELSG 440
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
215-458 |
6.93e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 110.95 E-value: 6.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 215 RPVTEklpanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIyVG-CGERGNEMSEvlrdFPE 293
Cdd:PRK08972 140 RPITE------PLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIV-VGlVGERGREVKE----FIE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 294 LTMEVDGKVESIMkrTALVANTSN-MPVAAREasiyTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADS 372
Cdd:PRK08972 209 EILGEEGRARSVV--VAAPADTSPlMRLKGCE----TATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 373 GYPAYLGARLASFYERAGRvkclGNPeREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLI 452
Cdd:PRK08972 283 GYPPSVFAKLPALVERAGN----GGP-GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEA 357
|
....*.
6WM2_A 453 SYSKYM 458
Cdd:PRK08972 358 SISRVM 363
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
219-465 |
3.01e-24 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 106.02 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 219 EKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEmsevLRDFPELTMEV 298
Cdd:PRK07960 151 QRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGRE----VKDFIENILGA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 299 DGKVESIMkrTALVANTSNMpVAAREASIYTGItlSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYL 378
Cdd:PRK07960 227 EGRARSVV--IAAPADVSPL-LRMQGAAYATRI--AEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 379 GARLASFYERAGRVKCLGnpereGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYM 458
Cdd:PRK07960 302 FAKLPALVERAGNGISGG-----GSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM 376
|
....*....
6WM2_A 459 RAL--DEYY 465
Cdd:PRK07960 377 TALidEQHY 385
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
225-456 |
5.61e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 105.08 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 225 HPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEmsevLRDFPELTMevdgkVES 304
Cdd:PRK06002 147 TGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGRE----VREFLEDTL-----ADN 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 305 IMKRTALVANTSNMPVAAREASIyTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLAS 384
Cdd:PRK06002 218 LKKAVAVVATSDESPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPR 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
6WM2_A 385 FYERAGrvkclgnPEREGSVSIVG--AVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSK 456
Cdd:PRK06002 297 LLERAG-------PGAEGGGSITGifSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
206-463 |
1.07e-23 |
|
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: 101.14 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 206 VQVWPVRQVRP-VTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSL----SKySNSDVIIYVGCGER 280
Cdd:cd01133 29 KERWPIHREAPeFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinniAK-AHGGYSVFAGVGER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 281 GNEMSEVLRDFpeltmeVDGKVESI--MKRTALVANTSNMPVAAREASIYTGITLSEYFRDM-GYHVSMMADSTSRWAEA 357
Cdd:cd01133 108 TREGNDLYHEM------KESGVINLdgLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 358 LREISGRLAEMPADSGYPAYLGARLASFYERAGRVKclgnperEGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDK 437
Cdd:cd01133 182 GSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTK-------KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSR 254
|
250 260
....*....|....*....|....*.
6WM2_A 438 KLAQRKHFPSVNWLISYSkymRALDE 463
Cdd:cd01133 255 GIAELGIYPAVDPLDSTS---RILDP 277
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
213-546 |
2.03e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 103.43 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 213 QVRPVtEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEmsevLRDFP 292
Cdd:PRK07196 126 QIHPL-QRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGRE----VKEFI 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 293 ELTMEVDGkvesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADS 372
Cdd:PRK07196 201 EHSLQAAG-----MAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATK 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 373 GYPAYLGARLASFYERAgrvkclGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLI 452
Cdd:PRK07196 276 GYPPSAFSIIPRLAESA------GNSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQ 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 453 SYSKYMRALDEyydkhfTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAE--TDKITLEVAKLikDDFLQQNGYTPydr 530
Cdd:PRK07196 350 SISRCMSQVIG------SQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADpmADQAVHYYPAI--TQFLRQEVGHP--- 418
|
330
....*....|....*.
6WM2_A 531 fCPFYKTVGMLSNMIA 546
Cdd:PRK07196 419 -ALFSASVEQLTGMFP 433
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
222-458 |
2.97e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 102.89 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 222 PANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEvlrdFPELTMEVDGk 301
Cdd:PRK05688 147 PISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKE----FIEHILGEEG- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 302 vesiMKRTALVANTSN-MPVAAREASIYTgITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGA 380
Cdd:PRK05688 222 ----LKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFA 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6WM2_A 381 RLASFYERAgrvkclGNPER-EGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYM 458
Cdd:PRK05688 297 KLPKLVERA------GNAEPgGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM 369
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
262-459 |
2.18e-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: 94.60 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 262 SLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMevdgkvesiMKRTALVANTSNMPVAAReasIYT---GITLSEYFR 338
Cdd:cd01135 94 GVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGA---------LERVVLFLNLANDPTIER---IITprmALTTAEYLA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 339 -DMGYHV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKclgnpEREGSVSIVGAVSPPGGD 416
Cdd:cd01135 162 yEKGKHVlVILTDMTN-YAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVE-----GRKGSITQIPILTMPNDD 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
6WM2_A 417 FSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSVNWLISYSKYMR 459
Cdd:cd01135 236 ITHPIPDLTGYITegQIY--LDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
229-522 |
3.10e-20 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 94.34 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 229 TGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSL----SKySNSDVIIYVGCGER---GN----EMSE----VLRDFPE 293
Cdd:CHL00060 147 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELinniAK-AHGGVSVFGGVGERtreGNdlymEMKEsgviNEQNIAE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 294 ltmevdGKVesimkrtALVANTSNMPVAAREASIYTGITLSEYFRDMGYH-VSMMADSTSRWAEALREISGRLAEMPADS 372
Cdd:CHL00060 226 ------SKV-------ALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 373 GYPAYLGARLASFYERAGRVKclgnperEGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLI 452
Cdd:CHL00060 293 GYQPTLSTEMGSLQERITSTK-------EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLD 365
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6WM2_A 453 SYSKYMRAL---DEYYDkhftefvpLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIkDDFLQQ 522
Cdd:CHL00060 366 STSTMLQPRivgEEHYE--------TAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 429
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
229-458 |
8.65e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 89.27 E-value: 8.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 229 TGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDfpELTmevdgkvESIMKR 308
Cdd:PRK06793 142 TGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRK--ELG-------EEGMRK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 309 TALVANTSNMP--VAAREASIYTGItlSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPAdSGYPAYLGARLASFY 386
Cdd:PRK06793 213 SVVVVATSDEShlMQLRAAKLATSI--AEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLL 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6WM2_A 387 ERAGRVKclgnperEGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYM 458
Cdd:PRK06793 290 ERSGKTQ-------KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIM 354
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
224-546 |
1.33e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 88.59 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 224 NHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEvlrdFPELTMevDGKVE 303
Cdd:PRK08472 138 DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPE----FIEKNL--GGDLE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 304 SimkrTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLA 383
Cdd:PRK08472 212 N----TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLP 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 384 SFYERAgrvkclGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRalDE 463
Cdd:PRK08472 288 QLMERA------GKEEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN--DI 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 464 YYDKHFTEFVPLRtKAKEILQEEEDLAEIvqlvgKASLAETDKiTLEVA---KLIKDDFLQQNGYTPYdrfcPFYKTVGM 540
Cdd:PRK08472 360 ISPEHKLAARKFK-RLYSLLKENEVLIRI-----GAYQKGNDK-ELDEAiskKEFMEQFLKQNPNELF----PFEQTFEQ 428
|
....*.
6WM2_A 541 LSNMIA 546
Cdd:PRK08472 429 LEEILR 434
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
306-525 |
1.98e-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: 88.24 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 306 MKRTALVANTSNMPVAAREASIYTGITLSEYFR-DMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLAS 384
Cdd:TIGR01040 210 MERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLAT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 385 FYERAGRVKclgnpEREGSVSIVGAVSPPGGDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSVNWLISYSKYMR-AL 461
Cdd:TIGR01040 290 IYERAGRVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPINVLPSLSRLMKsAI 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
6WM2_A 462 DEYYDKHFTEFVPLRTKAKEILQeeEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGY 525
Cdd:TIGR01040 363 GEGMTRKDHSDVSNQLYACYAIG--KDVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPY 424
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
216-545 |
1.13e-17 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 85.73 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 216 PVTEKLPanhpllTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELT 295
Cdd:PRK05922 136 PIQEIFP------TGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 296 MEvdgkvesimKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYP 375
Cdd:PRK05922 210 AA---------QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 376 AYLGARLASFYERAgrvkclGNPEReGSVSIVGAV--SPPGGD-FSDPVTSATLGivQVFWGldkklAQRKHF--PSVNW 450
Cdd:PRK05922 281 ASVFHHVSEFTERA------GNNDK-GSITALYAIlhYPNHPDiFTDYLKSLLDG--HFFLT-----PQGKALasPPIDI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 451 LISYSKYMRALDeyYDKHFTEFVPLRTkakeILQEEEDLAEIVQLvgKASLAETDKITLEVAKLIKD--DFLQQngytPY 528
Cdd:PRK05922 347 LTSLSRSARQLA--LPHHYAAAEELRS----LLKAYHEALDIIQL--GAYVPGQDAHLDRAVKLLPSikQFLSQ----PL 414
|
330
....*....|....*..
6WM2_A 529 DRFCPFYKTVGMLSNMI 545
Cdd:PRK05922 415 SSYCALHNTLKQLEALL 431
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
222-456 |
1.80e-15 |
|
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: 76.83 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 222 PANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT------VISQSlskysNSDVI-IYVGCGERGNEMSEVLRdfpel 294
Cdd:cd01132 48 SVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaiaidtIINQK-----GKKVYcIYVAIGQKRSTVAQIVK----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 295 TMEVDGKvesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGY 374
Cdd:cd01132 118 TLEEHGA----MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 375 PA---YLGARLasfYERAGRvkcLGNPEREGSVSIVGAVSPPGGDFSD--P--VTSATLGivQVFwgLDKKLAQRKHFPS 447
Cdd:cd01132 194 PGdvfYLHSRL---LERAAK---LSDELGGGSLTALPIIETQAGDVSAyiPtnVISITDG--QIF--LESELFNKGIRPA 263
|
....*....
6WM2_A 448 VNWLISYSK 456
Cdd:cd01132 264 INVGLSVSR 272
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
34-402 |
1.95e-15 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 79.19 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 34 MAGAAMYELVRV--GHSELVGEiirLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDiss 111
Cdd:PRK13343 44 LPDAALDELLRFegGSRGFAFN---LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDG--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 112 qtqsiyiprgvnvsalsrdikwdftpcknlrvgshitGGDiygivsenslikhkimLPPRNRGTVTYIAPPgnydtsdvV 191
Cdd:PRK13343 118 -------------------------------------GGP----------------LQATARRPLERPAPA--------I 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 192 LElefegvkekftmvqvwpvRQvrPVTEklpanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT------VISQSlsk 265
Cdd:PRK13343 137 IE------------------RD--FVTE------PLQTGIKVVDALIPIGRGQRELIIGDRQTGKTaiaidaIINQK--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 266 ysNSDVI-IYVGCGERGNEMSEVLRdfpelTMEVDGKvesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHV 344
Cdd:PRK13343 188 --DSDVIcVYVAIGQKASAVARVIE-----TLREHGA----LEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDA 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
6WM2_A 345 SMMADSTSRWAEALREISGRLAEMPADSGYPA---YLGARLasfYERAGRVkclgNPEREG 402
Cdd:PRK13343 257 LIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRL---LERAAKL----SPELGG 310
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
21-83 |
2.00e-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: 68.34 E-value: 2.00e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6WM2_A 21 VHGVSGPVVTACDMAGAA--MYELVRVGHSE----LVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTG 83
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLpgLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
217-456 |
3.31e-13 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 72.38 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 217 VTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVIS------------QSLSKysNSDVIIYVGCGERGNEM 284
Cdd:PTZ00185 163 IVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvstiinqvrinqQILSK--NAVISIYVSIGQRCSNV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 285 SEVLRDFpeltmevdgKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGR 364
Cdd:PTZ00185 241 ARIHRLL---------RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 365 LAEMPADSGYPA---YLGARLasfYERAGRvkcLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQ 441
Cdd:PTZ00185 312 LRRPPGREAYPGdvfYLHSRL---LERAAM---LSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFT 385
|
250
....*....|....*
6WM2_A 442 RKHFPSVNWLISYSK 456
Cdd:PTZ00185 386 GGQRPAVNIGLSVSR 400
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
215-432 |
1.34e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 70.38 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 215 RPVTEklpanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVIS-QSLSKYSNSDVI-IYVGCGERGNEMSEVLRDFP 292
Cdd:CHL00059 119 RSVYE------PLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVAtDTILNQKGQNVIcVYVAIGQKASSVAQVVTTLQ 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 293 EltmevdgkvESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADS 372
Cdd:CHL00059 193 E---------RGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGRE 263
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6WM2_A 373 GYPA---YLGARLasfYERAGRvkcLGNPEREGSVSIVGAVSPPGGDFSD--P--VTSATLGivQVF 432
Cdd:CHL00059 264 AYPGdvfYLHSRL---LERAAK---LSSQLGEGSMTALPIVETQAGDVSAyiPtnVISITDG--QIF 322
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|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
19-84 |
3.63e-12 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 61.94 E-value: 3.63e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6WM2_A 19 GYVHGVSGPVVTACDMAGAAMYELVRVGHS------ELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGK 84
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIERGdgnnetVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
36-425 |
3.55e-11 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 65.44 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 36 GAAMYELVRV--GHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPlsdissqt 113
Cdd:PRK02118 22 GVGYGELATVerKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKP-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 114 qsiyiprgvnvsalsrdikwdftpcknlrvgshITGGdiygivsenslikhkimlpPRNRGTVTYIAPPgnydtsdvvle 193
Cdd:PRK02118 94 ---------------------------------IDGG-------------------PELEGEPIEIGGP----------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 194 lefegvkekftmvqvwpvrQVRPVTEKLPANHpLLTGQRVLDaLFPCVqggttaipgafgcgktVISQSLSKYSNS---- 269
Cdd:PRK02118 111 -------------------SVNPVKRIVPREM-IRTGIPMID-VFNTL----------------VESQKIPIFSVSgepy 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 270 -------------DVIIYVGCGERGNEMSEVLRDFPELtmevdgkveSIMKRTALVANTSNMPVAAREASIYTGITLSEY 336
Cdd:PRK02118 154 nallarialqaeaDIIILGGMGLTFDDYLFFKDTFENA---------GALDRTVMFIHTASDPPVECLLVPDMALAVAEK 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 337 FRDMGYH--VSMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVkclgnpEREGSVSIVGAVSPPG 414
Cdd:PRK02118 225 FALEGKKkvLVLLTDMTN-FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDF------EDGGSITIIAVTTMPG 297
|
410
....*....|.
6WM2_A 415 GDFSDPVTSAT 425
Cdd:PRK02118 298 DDVTHPVPDNT 308
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
212-392 |
1.30e-08 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 57.77 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 212 RQvrPVTEklpanhPLLTGQRVLDALFPCVQG-----------GTTAIpgafgCGKTVISQSlskysNSDVI-IYVGCGE 279
Cdd:PRK09281 139 RK--SVHE------PLQTGIKAIDAMIPIGRGqreliigdrqtGKTAI-----AIDTIINQK-----GKDVIcIYVAIGQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6WM2_A 280 RGNEMSEVLRdfpelTMEVDGKvesiMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALR 359
Cdd:PRK09281 201 KASTVAQVVR-----KLEEHGA----MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYR 271
|
170 180 190 200
....*....|....*....|....*....|....*....|...
6WM2_A 360 EIS-------GRLAempadsgYPA---YLGARLasfYERAGRV 392
Cdd:PRK09281 272 QLSlllrrppGREA-------YPGdvfYLHSRL---LERAAKL 304
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
480-541 |
5.13e-06 |
|
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: 44.36 E-value: 5.13e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
6WM2_A 480 KEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKdDFLQQNGYTPYdrfcPFYKTVGML 541
Cdd:cd01429 9 KAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLE-EFLQQGQFEPE----TIEDTLEKL 65
|
|
| 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 ... |
21-84 |
1.39e-05 |
|
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: 43.19 E-value: 1.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6WM2_A 21 VHGVSGPVVTACDMAGAAMYELVRV----GHSELvGEIIRLEGDMATIQVYEETSGVSVGDPVLR-TGK 84
Cdd:cd18118 5 VSEINGPLVIVEGVKGVKYGEIVEItlpdGEVRR-GQVLEVSGDKAVVQVFEGTSGLDLKGTKVRfTGE 72
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