|
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 ... |
19-530 |
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: 1066.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 19 GAVHGVSGPVVTAIRMAGAAMYELVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSI 98
Cdd:TIGR01042 3 GYIYKVSGPVVVAENMAGAAMYELVRVGHDELVGEIIRLEGDKATIQVYEETSGLTVGDPVLRTGKPLSVELGPGILGNI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 99 FDGIQRPLRDIAQLTGGIYIPRGVNVPALPRHLTWDFVPSKsIQVGSHVTGGDIYGTVTENSLIQHKIMVPPRSRGTVTH 178
Cdd:TIGR01042 83 FDGIQRPLKAIAEQSQSIYIPRGVNVPALDRDKKWEFTPKK-LRVGDHITGGDIYGTVFENSLIKHKIMLPPRARGTITY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 179 IAPPGHYSVSDVVLELDFEGVAEQLTMMQVWPVRQTRPVVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTV 258
Cdd:TIGR01042 162 IAPAGNYTVDDTVLEVEFQGVKKKFSMLQTWPVRSPRPVTEKLPANTPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 259 ISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDFPELTMEVDGRTESIMKRTTLVANTSNMPVAAREASIYTGITLSEYFR 338
Cdd:TIGR01042 242 ISQSLSKYSNSDAIVYVGCGERGNEMAEVLMDFPELTMEVDGREESIMKRTTLVANTSNMPVAAREASIYTGITLAEYFR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 339 DMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRARCLGSPLREGSVSIVGAVSPPGGDFS 418
Cdd:TIGR01042 322 DMGYNVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGSPEREGSVSIVGAVSPPGGDFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 419 DPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRALEPHYEQLHPEFPALRTRAREILQEEEDLAEIVQLVGK 498
Cdd:TIGR01042 402 DPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALEEFYEKFYPEFVPLRTKAKEILQEEEDLNEIVQLVGK 481
|
490 500 510
....*....|....*....|....*....|..
gi 2024383982 499 ASLAEADKVTLEVARLLKDDFLQQNGYSSYDR 530
Cdd:TIGR01042 482 DALAETDKITLEVAKLIKEDFLQQNGYTPYDR 513
|
|
| NtpA |
COG1155 |
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ... |
19-529 |
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: 897.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 19 GAVHGVSGPVVTAIRMAGAAMYELVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSI 98
Cdd:COG1155 5 GKIVKINGPLVTAEGMGGAKMYEVVYVGEERLIGEVIRIEGDKATIQVYEETSGLKPGEPVESTGEPLSVELGPGLLGNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 99 FDGIQRPLRDIAQLTGgIYIPRGVNVPALPRHLTWDFVPSKsiQVGSHVTGGDIYGTVTENSLIQHKIMVPPRSRGTVTH 178
Cdd:COG1155 85 FDGIQRPLDKIAEKSG-DFIPRGVDVPALDREKKWDFTPTV--KVGDKVSAGDILGTVQETPLIEHKIMVPPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 179 IAPPGHYSVSDVVLEL-DFEGVAEQLTMMQVWPVRQTRPVVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 257
Cdd:COG1155 162 IAPEGEYTVEDTIAVLeDEDGEEHELTMYQKWPVRRPRPYKEKLPPSEPLITGQRVIDTFFPIAKGGTAAIPGPFGTGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 258 VISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDFPELtmeVDGRT-ESIMKRTTLVANTSNMPVAAREASIYTGITLSEY 336
Cdd:COG1155 242 VTQHQLAKWSDADIVVYVGCGERGNEMTEVLEEFPEL---IDPKTgRPLMERTVLIANTSNMPVAAREASIYTGITIAEY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 337 FRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRARCLGSPlrEGSVSIVGAVSPPGGD 416
Cdd:COG1155 319 YRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 417 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRALEPHY-EQLHPEFPALRTRAREILQEEEDLAEIVQL 495
Cdd:COG1155 397 FSEPVTQNTLRIVKVFWALDASLAYARHYPAINWLTSYSLYLDDLAEWYdENVDPDWSELRNEAMDLLQEEAELQEIVRL 476
|
490 500 510
....*....|....*....|....*....|....
gi 2024383982 496 VGKASLAEADKVTLEVARLLKDDFLQQNGYSSYD 529
Cdd:COG1155 477 VGEDALPDEDRLTLEVARLIREGFLQQNAFDDVD 510
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
19-529 |
0e+00 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 866.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 19 GAVHGVSGPVVTAIRMAGAAMYELVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSI 98
Cdd:PRK04192 5 GKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLLGSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 99 FDGIQRPLRDIAQLTGgIYIPRGVNVPALPRHLTWDFVPSKSiqVGSHVTGGDIYGTVTENSLIQHKIMVPPRSRGTVTH 178
Cdd:PRK04192 85 FDGIQRPLDELAEKSG-DFLERGVYVPALDREKKWEFTPTVK--VGDKVEAGDILGTVQETPSIEHKIMVPPGVSGTVKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 179 IAPPGHYSVSDVVLEL-DFEGVAEQLTMMQVWPVRQTRPVVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 257
Cdd:PRK04192 162 IVSEGDYTVDDTIAVLeDEDGEGVELTMMQKWPVRRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 258 VISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDFPELTmevDGRT-ESIMKRTTLVANTSNMPVAAREASIYTGITLSEY 336
Cdd:PRK04192 242 VTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPELI---DPKTgRPLMERTVLIANTSNMPVAAREASIYTGITIAEY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 337 FRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRARCLGSPlrEGSVSIVGAVSPPGGD 416
Cdd:PRK04192 319 YRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGE--EGSVTIIGAVSPPGGD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 417 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRALEPHY-EQLHPEFPALRTRAREILQEEEDLAEIVQL 495
Cdd:PRK04192 397 FSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDQVAPWWeENVDPDWRELRDEAMDLLQREAELQEIVRL 476
|
490 500 510
....*....|....*....|....*....|....
gi 2024383982 496 VGKASLAEADKVTLEVARLLKDDFLQQNGYSSYD 529
Cdd:PRK04192 477 VGPDALPEEDRLILEVARLIREDFLQQNAFDPVD 510
|
|
| ATP_syn_A_arch |
TIGR01043 |
ATP synthase archaeal, A subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
19-530 |
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: 784.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 19 GAVHGVSGPVVTAIRMAGAAMYELVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSI 98
Cdd:TIGR01043 2 GRIIRVSGPLVVADGMKGAQMYEVVKVGEEGLIGEIIRIEGDKAFIQVYEETSGIKPGEPVVGTGAPLSVELGPGLLGSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 99 FDGIQRPLRDIAQLTGGiYIPRGVNVPALPRHLTWDFVPSksIQVGSHVTGGDIYGTVTENSLIQHKIMVPPRSRGTVTH 178
Cdd:TIGR01043 82 YDGVQRPLDVLKEKTGD-FIARGVDAPGLDRDKKWHFKPT--VKEGDKVEGGDIIGVVPETSLIEHKILVPPNVEGEIVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 179 IAPPGHYSVSDVVLELDFEGvAEQLTMMQVWPVRQTRPVVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTV 258
Cdd:TIGR01043 159 IAEEGDYTVEDTIAVVDTDG-DEEIKMYQKWPVRIPRPYKEKLPPEVPLITGQRILDTFFPIAKGGTAAIPGPFGSGKTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 259 ISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDFPELTmevDGRT-ESIMKRTTLVANTSNMPVAAREASIYTGITLSEYF 337
Cdd:TIGR01043 238 TQHQLAKWSDADIVVYIGCGERGNEMTDVLEEFPELK---DPKTgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 338 RDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRARCLGSPLREGSVSIVGAVSPPGGDF 417
Cdd:TIGR01043 315 RDMGYDVALMADSTSRWAEAMREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKTLGGEERVGSVTVIGAVSPPGGDF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 418 SDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRALEPHY-EQLHPEFPALRTRAREILQEEEDLAEIVQLV 496
Cdd:TIGR01043 395 SEPVTQNTLRIVKVFWALDADLAQRRHFPAINWLQSYSLYVDLVQDWWhENVDPDWREMRDEAMDLLQKESELQEIVQLV 474
|
490 500 510
....*....|....*....|....*....|....
gi 2024383982 497 GKASLAEADKVTLEVARLLKDDFLQQNGYSSYDR 530
Cdd:TIGR01043 475 GPDALPERQKLILEVARMIREAFLQQNAFDPVDT 508
|
|
| 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: 613.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 85 PLSVELGPGILGSIFDGIQRPLRDIAQlTGGIYIPRGVNVpalprhltwdfvpsksiqvgshvtggdiygtvtensliqh 164
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAE-TGSIFIPRGVNV---------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 165 kimvpprsrgtvthiappghysvsdvvleldfegvaeqltmmQVWPVRQTRPVVEKLTANHPLLTGQRVLDALFPCVQGG 244
Cdd:cd01134 40 ------------------------------------------QRWPVRQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGG 77
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 245 TTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDFPELTMEVDGrtESIMKRTTLVANTSNMPVAARE 324
Cdd:cd01134 78 TAAIPGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEFPELKDPITG--ESLMERTVLIANTSNMPVAARE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 325 ASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRARCLGSPLREGSV 404
Cdd:cd01134 156 ASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRCLGSPGREGSV 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2024383982 405 SIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKY 457
Cdd:cd01134 236 TIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSKY 288
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
257-529 |
3.92e-111 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 353.94 E-value: 3.92e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 257 TVISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDFPELTMEVDGRteSIMKRTTLVANTSNMPVAAREASIYTGITLSEY 336
Cdd:PRK14698 670 TVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEEFPKLKDPKTGK--PLMERTVLIANTSNMPVAAREASIYTGITIAEY 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 337 FRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRARCLGSPLREGSVSIVGAVSPPGGD 416
Cdd:PRK14698 748 FRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVVTLGSDYRVGSVSVIGAVSPPGGD 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 417 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRALEPHYEQ-LHPEFPALRTRAREILQEEEDLAEIVQL 495
Cdd:PRK14698 828 FSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKnVDPEWKAMRDKAMELLQKEAELQEIVRI 907
|
250 260 270
....*....|....*....|....*....|....
gi 2024383982 496 VGKASLAEADKVTLEVARLLKDDFLQQNGYSSYD 529
Cdd:PRK14698 908 VGPDALPERERAILLVARMLREDYLQQDAFDEVD 941
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
230-455 |
5.33e-100 |
|
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: 300.43 E-value: 5.33e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 230 GQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDFPEltmevdgrtESIMKRT 309
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLG---------SGALKRT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 310 TLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERA 389
Cdd:pfam00006 72 VVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024383982 390 GRARClgsplREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYS 455
Cdd:pfam00006 152 GRVKG-----KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
203-457 |
2.82e-84 |
|
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: 262.39 E-value: 2.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 203 LTMMQVWPVRQTRP-VVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNS---DIIVYVGCG 278
Cdd:cd19476 26 IKTKQRRPIHLKAPnPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKahaGVVVFAGIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 279 ERGNEMSEVLRDFPELtmevdgrteSIMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEAL 358
Cdd:cd19476 106 ERGREVNDLYEEFTKS---------GAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 359 REISGRLAEMPADSGYPAYLGARLASFYERAGRARClgsplREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKK 438
Cdd:cd19476 177 REMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD-----GGGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRE 251
|
250
....*....|....*....
gi 2024383982 439 LAQRKHFPSVNWLISYSKY 457
Cdd:cd19476 252 LARKGIYPAINVLDSTSRV 270
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
19-263 |
8.31e-78 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 263.81 E-value: 8.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 19 GAVHGVSGPVVTAIRMAGAAMYELVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSI 98
Cdd:PRK14698 5 GRIIRVTGPLVIADGMKGAKMYEVVRVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 99 FDGIQRPLRDIAQLTGGiYIPRGVNVPALPRHLTWDFVPskSIQVGSHVTGGDIYGTVTENSLIQHKIMVPPRSRGTVTH 178
Cdd:PRK14698 85 YDGIQRPLEVIREKSGD-FIARGISAPALPRDKKWHFIP--KVKVGDKVVGGDIIGEVPETSIITHKIMVPPGIEGEIVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 179 IAPPGHYSVSDVVLELDF-EGVAEQLTMMQVWPVRQTRPVVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT 257
Cdd:PRK14698 162 IADEGEYTIEEVIAKVKTpSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLITGQRVIDTFFPQAKGGTAAIPGPFGSGKC 241
|
....*.
gi 2024383982 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 |
6.64e-67 |
|
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: 211.87 E-value: 6.64e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 99 FDGIQRPLRDIAQLTGGiYIPRGVNVPALPRHLTWDFVPSksIQVGSHVTGGDIYGTVTENSLIQHKIMVPPRSRGTVTH 178
Cdd:pfam16886 1 FDGIQRPLEKIAEKSGS-FIPRGVDVPALDREKKWEFTPT--VKVGDKVSGGDILGTVQETSLIEHKIMVPPGVSGTVTE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2024383982 179 IAPPGHYSVSDVVLELDFEGVAEQLTMMQVWPVRQTRPVVEKL 221
Cdd:pfam16886 78 IAPEGEYTVEDTIAEVEDEGKEKELTMMQKWPVRRPRPYKEKL 120
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
7-522 |
1.28e-47 |
|
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: 171.40 E-value: 1.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 7 TRMADVEEESLLGAVHGVSGPVVTAIRMAgAAMYELVRV----GHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRT 82
Cdd:TIGR01026 13 CQEMDLRLVKRVGRVTKVKGLLIEAVGPQ-ASVGDLCLIerrgSEGRLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 83 GQPLSVELGPGILGSIFDGIQRPLRdiaqltggiyiprgvnvpalprhltwdfvpsksiqvgshvTGGDIYGTVTENSLI 162
Cdd:TIGR01026 92 GEGLSIKVGDGLLGRVLDGLGKPID----------------------------------------GKGKFLDNVETEGLI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 163 QHKImvPPRSRGTVTHIappghysvsdvvleldfegvaeqltmmqvwpvrqtrpvvekltanhpLLTGQRVLDALFPCVQ 242
Cdd:TIGR01026 132 TAPI--NPLKRAPIREI-----------------------------------------------LSTGVRSIDGLLTVGK 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 243 GGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEmsevLRDFPELTMEVDGrtesiMKRTTLVANTSNMPVAA 322
Cdd:TIGR01026 163 GQRIGIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGRE----VREFIEHDLGEEG-----LKRSVVVVATSDQSPLL 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 323 REASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRArclgsplREG 402
Cdd:TIGR01026 234 RLKGAYVATAIAEYFRDQGKDVLLLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGAS-------GKG 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 403 SVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRAL--EPHYEQLHpefpalrtRAR 480
Cdd:TIGR01026 307 SITAFYTVLVEGDDMNEPIADSVRGILDGHIVLSRALAQRGHYPAIDVLASISRLMTAIvsEEHRRAAR--------KFR 378
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2024383982 481 EIL---QEEEDLAEIvQLVGKASLAEADKVTLEVARLlkDDFLQQ 522
Cdd:TIGR01026 379 ELLskyKDNEDLIRI-GAYQRGSDRELDFAIAKYPKL--ERFLKQ 420
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
8-489 |
9.68e-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: 149.41 E-value: 9.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 8 RMADVEEESLLGAVHGVSGPVVTAiRMAGAAMYELVRV---GHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQ 84
Cdd:COG1157 10 RLEELPPVRVSGRVTRVVGLLIEA-VGPDASIGELCEIetaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 85 PLSVELGPGILGSIFDGIQRPLRDIAQLTGGIYIPrgvnvpalprhltwdfvpsksiqvgshvtggdIYGTVtensliqh 164
Cdd:COG1157 89 PLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRP--------------------------------LDAPP-------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 165 kimVPPRSRGTVTHiappghysvsdvvleldfegvaeqltmmqvwpvrqtrpvvekltanhPLLTGQRVLDALFPCVQG- 243
Cdd:COG1157 129 ---PNPLERARITE-----------------------------------------------PLDTGVRAIDGLLTVGRGq 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 244 --GTTAipGAfGCGKTVISQSLSKYSNSDIIVyVG-CGERGNEmsevLRDFPELTMEVDGrtesiMKRTTLVANTSNMPV 320
Cdd:COG1157 159 riGIFA--GS-GVGKSTLLGMIARNTEADVNV-IAlIGERGRE----VREFIEDDLGEEG-----LARSVVVVATSDEPP 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 321 AAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISgrLA--EMPADSGYPAYLGARLASFYERAGRArclgsp 398
Cdd:COG1157 226 LMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIG--LAagEPPATRGYPPSVFALLPRLLERAGNG------ 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 399 lREGSVSIVGAVSPPGGDFSDPVTSATLGI-----VqvfwgLDKKLAQRKHFPSVNWLISYSKYLRAL--EPHYEqlhpe 471
Cdd:COG1157 298 -GKGSITAFYTVLVEGDDMNDPIADAVRGIldghiV-----LSRKLAERGHYPAIDVLASISRVMPDIvsPEHRA----- 366
|
490 500
....*....|....*....|.
gi 2024383982 472 fpaLRTRAREIL---QEEEDL 489
Cdd:COG1157 367 ---LARRLRRLLaryEENEDL 384
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
26-531 |
3.17e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 145.34 E-value: 3.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 26 GPVVTAIRMAGAAMYELVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSIFDGIQRP 105
Cdd:PRK06820 37 GPTLLRASLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 106 LRDIAQLTGGIyipRGVNVPAlprhltwdfvPSksiqvgshvtggdiygtvtensliqhkimvpPRSRGTVTHiappghy 185
Cdd:PRK06820 117 IDGGPPLTGQW---RELDCPP----------PS-------------------------------PLTRQPIEQ------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 186 svsdvvleldfegvaeqltmmqvwpvrqtrpvvekltanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSK 265
Cdd:PRK06820 146 ----------------------------------------MLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 266 YSNSDIIVYVGCGERGNEmsevLRDFPELTMEVDGRTesimkRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVS 345
Cdd:PRK06820 186 DSAADVMVLALIGERGRE----VREFLEQVLTPEARA-----RTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 346 MMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGrarclgsPLREGSVSIVGAVSPPGGDFSDPVTSAT 425
Cdd:PRK06820 257 LMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG-------NSDRGSITAFYTVLVEGDDMNEPVADEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 426 LGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRALephyeqLHPEFPALRTRAREILQEEEDLAEIVQlVG---KASLA 502
Cdd:PRK06820 330 RSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQI------VSAGQLAMAQKLRRMLACYQEIELLVR-VGeyqAGEDL 402
|
490 500 510
....*....|....*....|....*....|.
gi 2024383982 503 EADKVTLEVARLlkDDFLQQNG--YSSYDRT 531
Cdd:PRK06820 403 QADEALQRYPAI--CAFLQQDHseTAHLETT 431
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
213-456 |
3.60e-38 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 140.77 E-value: 3.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 213 QTRPVVEKltanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEmsevLRDFP 292
Cdd:cd01136 42 LKRAPIEQ-----PLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVNVIALIGERGRE----VREFI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 293 ELTMEVDGrtesiMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADS 372
Cdd:cd01136 113 EKDLGEEG-----LKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 373 GYPAYLGARLASFYERAGrarclgsPLREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLI 452
Cdd:cd01136 188 GYPPSVFALLPRLLERAG-------NGEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLA 260
|
....
gi 2024383982 453 SYSK 456
Cdd:cd01136 261 SISR 264
|
|
| 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 ... |
19-83 |
4.35e-36 |
|
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: 128.41 E-value: 4.35e-36
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024383982 19 GAVHGVSGPVVTAIRMAGAAMYELVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTG 83
Cdd:cd18119 2 GKIYRVSGPVVVAEGMSGAAMYELVRVGEEGLIGEIIRLEGDKATIQVYEETSGLKVGEPVERTG 66
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
19-523 |
9.06e-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: 135.30 E-value: 9.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 19 GAVHGVSGPVVTAI--RMAGAAMYELVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILG 96
Cdd:TIGR03496 1 GRVTRVVGLVLEAVglRAPVGSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 97 SIFDGIQRPLRDIAQLTGGIYIPrgvnvpalprhltwdfvpsksiqvgshvtggdIYGTVtensliqhkimVPPRSRGTV 176
Cdd:TIGR03496 81 RVIDGLGRPLDGKGPLDAGERVP--------------------------------LYAPP-----------INPLKRAPI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 177 THiappghysvsdvvleldfegvaeqltmmqvwpvrqtrpvvekltanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGK 256
Cdd:TIGR03496 118 DE-----------------------------------------------PLDVGVRAINGLLTVGRGQRMGIFAGSGVGK 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 257 TVISQSLSKYSNSDIIVyVG-CGERGNEmsevLRDFPELTMEVDGrtesiMKRTTLVANTSNMPVAAREASIYTGITLSE 335
Cdd:TIGR03496 151 STLLGMMARYTEADVVV-VGlIGERGRE----VKEFIEDILGEEG-----LARSVVVAATADESPLMRLRAAFYATAIAE 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 336 YFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGrarclgsPLREGSVSIVG--AVSPP 413
Cdd:TIGR03496 221 YFRDQGKDVLLLMDSLTRFAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAG-------NGEEGKGSITAfyTVLVE 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 414 GGDFSDPVTSATLGIVQvfwG---LDKKLAQRKHFPSVNWLISYSKYLRAL--EPHYEQLHpefpalrtRAREIL---QE 485
Cdd:TIGR03496 294 GDDQQDPIADAARAILD---GhivLSRELAEQGHYPAIDILASISRVMPDVvsPEHRQAAR--------RFKQLLsryQE 362
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2024383982 486 EEDLAEIvqlvG---KASLAEADKVTLEVARLlkDDFLQQN 523
Cdd:TIGR03496 363 NRDLISI----GayqAGSDPELDQAIALYPRI--EAFLQQG 397
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
17-492 |
4.47e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 130.84 E-value: 4.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 17 LLGAVHGVSGPVVTAiRMAGAAMYELVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILG 96
Cdd:PRK07594 21 RWGRIQDVSATLLNA-WLPGVFMGELCCIKPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 97 SIFDGIQRPLRDIAqltggiyiprgvnvpaLPRhltwdfVPSKSIQvgshvtggdiygtvtensliqhkimvpprsrgtv 176
Cdd:PRK07594 100 RVIDGFGRPLDGRE----------------LPD------VCWKDYD---------------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 177 thiAPPGhysvsdvvleldfegvaeqltmmqvwPVRQTRPVVEkltanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGK 256
Cdd:PRK07594 124 ---AMPP--------------------------PAMVRQPITQ------PLMTGIRAIDSVATCGEGQRVGIFSAPGVGK 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 257 TVISQSLSKYSNSDIIVYVGCGERGNEmsevLRDFPELTMEVDGRtesimKRTTLVANTSNMPVAAREASIYTGITLSEY 336
Cdd:PRK07594 169 STLLAMLCNAPDADSNVLVLIGERGRE----VREFIDFTLSEETR-----KRCVIVVATSDRPALERVRALFVATTIAEF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 337 FRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGrarcLGSplrEGSVSIVGAVSPPGGD 416
Cdd:PRK07594 240 FRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG----MGE---KGSITAFYTVLVEGDD 312
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024383982 417 FSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRALEPHYeqlHPEFPALRTRAREILQEEEDLAEI 492
Cdd:PRK07594 313 MNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHE---HRQLAAILRRCLALYQEVELLIRI 385
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
210-522 |
4.07e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 128.33 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 210 PVRQTRPVVEKltanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEmsevLR 289
Cdd:PRK06936 134 PAPMSRRLIET-----PLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGRE----VR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 290 DFPELTMEVDGrtesiMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMP 369
Cdd:PRK06936 205 EFIESDLGEEG-----LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 370 ADSGYPAYLGARLASFYERAGRArclgsplREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVN 449
Cdd:PRK06936 280 TRRGYPPSVFAALPRLMERAGQS-------DKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAID 352
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024383982 450 WLISYSKYLRALephyeqLHPEFPALRTRAREILQEEEDLAEIVQL--VGKASLAEADKVTLEVARLlkDDFLQQ 522
Cdd:PRK06936 353 VLRSASRVMNQI------VSKEHKTWAGRLRELLAKYEEVELLLQIgeYQKGQDKEADQAIERIGAI--RGFLRQ 419
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
48-492 |
1.25e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 126.76 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 48 AELVGeiirLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSIFDGIQRPLRDiaqltggiyiprgvnvPAL 127
Cdd:PRK07721 57 AEVVG----FKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDG----------------SAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 128 PRHLTwdFVPsksiqvgshvtggdiygtvTENSliqhkimvpprsrgtvthiaPPGhysvsdvvleldfegvaeqltmmq 207
Cdd:PRK07721 117 PKGLA--PVS-------------------TDQD--------------------PPN------------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 208 vwPVrqTRPVVekltaNHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEmsev 287
Cdd:PRK07721 132 --PL--KRPPI-----REPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIALIGERGRE---- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 288 LRDFPELTMEVDGrtesiMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAE 367
Cdd:PRK07721 199 VREFIERDLGPEG-----LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 368 MPADSGYPAYLGARLASFYERAGRArclgsplREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPS 447
Cdd:PRK07721 274 PPTTKGYTPSVFAILPKLLERTGTN-------ASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPA 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2024383982 448 VNWLISYSKYLRAL--EPHYEQLHpefpalrtRAREIL---QEEEDLAEI 492
Cdd:PRK07721 347 INVLKSVSRVMNHIvsPEHKEAAN--------RFRELLstyQNSEDLINI 388
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
215-495 |
1.37e-31 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 126.65 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 215 RPVVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEMSEvlrdFPEl 294
Cdd:PRK08149 123 PSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTE----FVE- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 295 TMEVDGRTEsimkRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGY 374
Cdd:PRK08149 198 SLRASSRRE----KCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 375 PAYLGARLASFYERAGRarclgspLREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISY 454
Cdd:PRK08149 274 PASVFDSLPRLLERPGA-------TLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSV 346
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2024383982 455 SK-YLRALEPHYEQLHPEFpalrtraREILQEEEDLAEIVQL 495
Cdd:PRK08149 347 SRvFGQVTDPKHRQLAAAF-------RKLLTRLEELQLFIDL 381
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
226-523 |
3.51e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 125.48 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 226 PLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDfpelTMEVDGrtesi 305
Cdd:PRK08927 141 PLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADADVSVIGLIGERGREVQEFLQD----DLGPEG----- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 306 MKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASF 385
Cdd:PRK08927 212 LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 386 YERAGRArclgsPLREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLralePHY 465
Cdd:PRK08927 292 LERAGPG-----PIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM----PGC 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 466 EQlhPEFPALRTRAREILQEEEDLAEIVQLvgKASLAEADKVTLEVARLLKD--DFLQQN 523
Cdd:PRK08927 363 ND--PEENPLVRRARQLMATYADMEELIRL--GAYRAGSDPEVDEAIRLNPAleAFLRQG 418
|
|
| 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 ... |
472-530 |
1.22e-29 |
|
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: 112.10 E-value: 1.22e-29
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024383982 472 FPALRTRAREILQEEEDLAEIVQLVGKASLAEADKVTLEVARLLKDDFLQQNGYSSYDR 530
Cdd:cd18111 1 WVELRTEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIREDFLQQNAFDEVDT 59
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
8-532 |
1.91e-29 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 120.64 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 8 RMADVEEESLLGAVHGV-SGPVV----TAIRMAG--AAMYEL--VRVGHAELV--GEIIRLEGDMATLQVYEETSGLRVG 76
Cdd:PRK09099 7 RLADALERELAALPAVRrTGKVVevigTLLRVSGldVTLGELceLRQRDGTLLqrAEVVGFSRDVALLSPFGELGGLSRG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 77 DPVLRTGQPLSVELGPGILGSIFDGIQRPLRDIAQLTGGIYIPrgvnVPALPrhltwdfvpsksiqvgshvtggdiygtv 156
Cdd:PRK09099 87 TRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVP----VIAAP---------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 157 tensliqhkimvpprsrgtvthiappghysvsdvvleldfegvaeqltmmqvwPVRQTRPVVEkltanHPLLTGQRVLDA 236
Cdd:PRK09099 135 -----------------------------------------------------PDPMSRRMVE-----APLPTGVRIVDG 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 237 LFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEmsevLRDFPELTMEVDGrtesiMKRTTLVANTS 316
Cdd:PRK09099 157 LMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCDVNVIALIGERGRE----VREFIELILGEDG-----MARSVVVCATS 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 317 NMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRArclg 396
Cdd:PRK09099 228 DRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMG---- 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 397 splREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRALEPHyeqlhpEFPALR 476
Cdd:PRK09099 304 ---ETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPR------EHVQAA 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024383982 477 TRAREILQEEEDLAEIVQL----VGKASLAEADKVTLEVARllkdDFLQQ--NGYSSYDRTR 532
Cdd:PRK09099 375 GRLRQLLAKHREVETLLQVgeyrAGSDPVADEAIAKIDAIR----DFLSQrtDEYSDPDATL 432
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
21-531 |
1.54e-25 |
|
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: 109.46 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 21 VHGVSGPVVTAIRMAGAAMYELVRV---GHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLR-TGQPLSVELGPGILG 96
Cdd:COG1156 9 ISEIAGPLLFVEGVEGVGYGELVEIelpDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRfLGEPLELPVSEDMLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 97 SIFDGIQRPlRDiaqltGG--IYIPRGVNVPALPRHLTWDFVPSKSIQVG-SHVTGgdiygtvtENSLIqhkimvpprsR 173
Cdd:COG1156 89 RVFNGLGRP-ID-----GGppIIPEKRLDINGSPINPVAREYPREFIQTGiSAIDG--------LNTLV----------R 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 174 GTVTHIappghYSVSDvvleLDFEGVAEQLtmmqvwpVRQTRpvvekltanhplltgqrvldalfpcVQGGTtaipGAFG 253
Cdd:COG1156 145 GQKLPI-----FSGSG----LPHNELAAQI-------ARQAK-------------------------VRGEE----EKFA 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 254 cgktvisqslskysnsdiIVYVGCGERGNEMSEVLRDFpeltmevdgrTES-IMKRTTLVANTSNMPVAAREASIYTGIT 332
Cdd:COG1156 180 ------------------VVFAAMGITHDEANFFREEF----------EETgALDRVVMFLNLADDPAIERIITPRMALT 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 333 LSEYFR-DMGLHV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRARclGsplREGSVSIVGAV 410
Cdd:COG1156 232 AAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIK--G---RKGSITQIPIL 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 411 SPPGGDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSVNWLISYSK---------YLRalEPHYE---QLHpefpALR 476
Cdd:COG1156 306 TMPNDDITHPIPDLTGYITegQIV--LSRDLHRKGIYPPIDVLPSLSRlmkdgigegKTR--EDHADvanQLY----AAY 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2024383982 477 TRAReilqeeeDLAEIVQLVGKASLAEADKVTLEVARLLKDDFLQQNGYSsyDRT 531
Cdd:COG1156 378 ARGQ-------EVRELAAIVGEEALSETDKKYLKFADAFERRFVNQGFDE--NRS 423
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
42-449 |
2.01e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 105.94 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 42 LVRVGHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSIFDGIQRPLRDIaqltggiyiprg 121
Cdd:PRK08972 51 SIETMAGELEAEVVGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGL------------ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 122 vnvpalprhltwdfvpsksiqvgshvtgGDIYgtvTENSLIQHKIMVPPRSRgtvthiappghysvsdvvleldfegvae 201
Cdd:PRK08972 119 ----------------------------GPIY---TDQRASRHSPPINPLSR---------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 202 qltmmqvwpvrqtRPVVEkltanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVyVG-CGER 280
Cdd:PRK08972 140 -------------RPITE------PLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIV-VGlVGER 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 281 GNEMSEvlrdFPELTMEVDGRtesimKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALRE 360
Cdd:PRK08972 200 GREVKE----FIEEILGEEGR-----ARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQRE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 361 ISGRLAEMPADSGYPAYLGARLASFYERAGRarclGSPlREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLA 440
Cdd:PRK08972 271 IALAVGEPPATKGYPPSVFAKLPALVERAGN----GGP-GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELA 345
|
....*....
gi 2024383982 441 QRKHFPSVN 449
Cdd:PRK08972 346 DSGHYPAID 354
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
207-458 |
2.48e-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: 99.60 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 207 QVWPVRQTRP-VVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSL----SKySNSDIIVYVGCGERG 281
Cdd:cd01133 30 ERWPIHREAPeFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELinniAK-AHGGYSVFAGVGERT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 282 NEMSEVLRDFpeltMEVDGRTESIMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDM-GLHVSMMADSTSRWAEALRE 360
Cdd:cd01133 109 REGNDLYHEM----KESGVINLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYFRDEeGQDVLLFIDNIFRFTQAGSE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 361 ISGRLAEMPADSGYPAYLGARLASFYERAgrarclgSPLREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLA 440
Cdd:cd01133 185 VSALLGRIPSAVGYQPTLATEMGSLQERI-------TSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIA 257
|
250
....*....|....*...
gi 2024383982 441 QRKHFPSVNWLISYSKYL 458
Cdd:cd01133 258 ELGIYPAVDPLDSTSRIL 275
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
225-468 |
2.94e-23 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 102.55 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 225 HPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEmsevLRDFPELTMEVDGRTES 304
Cdd:PRK07960 157 HVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGRE----VKDFIENILGAEGRARS 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 305 IMkrttLVANTSNMPVAAREASIYtGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLAS 384
Cdd:PRK07960 233 VV----IAAPADVSPLLRMQGAAY-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 385 FYERAGRARCLGsplreGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRAL--E 462
Cdd:PRK07960 308 LVERAGNGISGG-----GSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALidE 382
|
....*.
gi 2024383982 463 PHYEQL 468
Cdd:PRK07960 383 QHYARV 388
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
226-492 |
3.33e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 102.50 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 226 PLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEMSEvlrdFPELTMEVDGrtesi 305
Cdd:PRK05688 151 PLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIVVGLIGERGREVKE----FIEHILGEEG----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 306 MKRTTLVANTSN-MPVAAREASIYTgITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLAS 384
Cdd:PRK05688 222 LKRSVVVASPADdAPLMRLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPK 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 385 FYERAGRARCLGsplreGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRAL-EP 463
Cdd:PRK05688 301 LVERAGNAEPGG-----GSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVvDP 375
|
250 260
....*....|....*....|....*....
gi 2024383982 464 HYEQLHPEFPALRTRareiLQEEEDLAEI 492
Cdd:PRK05688 376 EHLRRAQRFKQLWSR----YQQSRDLISV 400
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
21-531 |
7.12e-23 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 101.44 E-value: 7.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 21 VHGVSGPVVTAIRMAGAAMYELVRVGHA---ELVGEIIRLEGDMATLQVYEETSGLRVGDPVLR-TGQPLSVELGPGILG 96
Cdd:PRK04196 7 VSEIKGPLLFVEGVEGVAYGEIVEIELPngeKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSEDMLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 97 SIFDGIQRPLRDiaqltGGIYIP---RGVNVPAL-------PRhltwDFvpsksIQVGshVTGgdIYGTvteNSLIqhki 166
Cdd:PRK04196 87 RIFDGLGRPIDG-----GPEIIPekrLDINGAPInpvareyPE----EF-----IQTG--ISA--IDGL---NTLV---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 167 mvpprsRGTVTHIappghYSVSdvvleldfeGVAEQLTMMQVwpVRQTRpvvekltanhplltgqrvldalfpcvqggtt 246
Cdd:PRK04196 142 ------RGQKLPI-----FSGS---------GLPHNELAAQI--ARQAK------------------------------- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 247 aIPGafgcgktvisqSLSKYSnsdiIVYVGCGERGNEMSEVLRDFpeltmevdgRTESIMKRTTLVANTSNMPVAAREAS 326
Cdd:PRK04196 169 -VLG-----------EEENFA----VVFAAMGITFEEANFFMEDF---------EETGALERSVVFLNLADDPAIERILT 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 327 IYTGITLSEYFR-DMGLHV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRARclGsplREGSV 404
Cdd:PRK04196 224 PRMALTAAEYLAfEKGMHVlVILTDMTN-YCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIK--G---KKGSI 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 405 SIVGAVSPPGGDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSVNWLISYSK---------YLRalEPHYE---QLHp 470
Cdd:PRK04196 298 TQIPILTMPDDDITHPIPDLTGYITegQIV--LSRELHRKGIYPPIDVLPSLSRlmkdgigegKTR--EDHKDvanQLY- 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024383982 471 efpALRTRAReilqeeeDLAEIVQLVGKASLAEADKVTLEVARLLKDDFLQQNGYSsyDRT 531
Cdd:PRK04196 373 ---AAYARGK-------DLRELAAIVGEEALSERDRKYLKFADAFEREFVNQGFDE--NRS 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
210-456 |
1.44e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 100.46 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 210 PVRQTRPVVEKltanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEmsevLR 289
Cdd:PRK06002 137 PPAMTRARVET-----GLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVVIALVGERGRE----VR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 290 DFPELTMeVDGRTESImkrtTLVANTSNMPVAAREASIyTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMP 369
Cdd:PRK06002 208 EFLEDTL-ADNLKKAV----AVVATSDESPMMRRLAPL-TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPP 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 370 ADSGYPAYLGARLASFYERAGrarclgsPLREGSVSIVG--AVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPS 447
Cdd:PRK06002 282 VARGYPPSVFSELPRLLERAG-------PGAEGGGSITGifSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPA 354
|
....*....
gi 2024383982 448 VNWLISYSK 456
Cdd:PRK06002 355 VDPLASISR 363
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
262-456 |
1.68e-19 |
|
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: 88.82 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 262 SLSKYSNSDIIVYVGCGERGNEMSEVLRDFPELTMevdgrtesiMKRTTLVANTSNMPVAAReasIYT---GITLSEYFR 338
Cdd:cd01135 94 GVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGA---------LERVVLFLNLANDPTIER---IITprmALTTAEYLA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 339 -DMGLHV-SMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRARClgsplREGSVSIVGAVSPPGGD 416
Cdd:cd01135 162 yEKGKHVlVILTDMTN-YAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEG-----RKGSITQIPILTMPNDD 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2024383982 417 FSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSVNWLISYSK 456
Cdd:cd01135 236 ITHPIPDLTGYITegQIY--LDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
229-494 |
3.23e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 90.04 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 229 TGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDfpELTmevdgrtESIMKR 308
Cdd:PRK06793 142 TGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGERGREVKDFIRK--ELG-------EEGMRK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 309 TTLVANTSNMP--VAAREASIYTGItlSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPAdSGYPAYLGARLASFY 386
Cdd:PRK06793 213 SVVVVATSDEShlMQLRAAKLATSI--AEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPI-GGKTLLMESYMKKLL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 387 ERAGRArclgsplREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYLRAL-EPHY 465
Cdd:PRK06793 290 ERSGKT-------QKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIvSPNH 362
|
250 260 270
....*....|....*....|....*....|....*..
gi 2024383982 466 EQLHPEFPALRTRARE--------ILQEEEDLAEIVQ 494
Cdd:PRK06793 363 WQLANEMRKILSIYKEnelyfklgTIQENAENAYIFE 399
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
229-522 |
3.59e-19 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 90.49 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 229 TGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSL----SKySNSDIIVYVGCGER---GN----EMSE----VLRDFPE 293
Cdd:CHL00060 147 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELinniAK-AHGGVSVFGGVGERtreGNdlymEMKEsgviNEQNIAE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 294 ltmevdgrtesimKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLH-VSMMADSTSRWAEALREISGRLAEMPADS 372
Cdd:CHL00060 226 -------------SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 373 GYPAYLGARLASFYERAgrarclgSPLREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLI 452
Cdd:CHL00060 293 GYQPTLSTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLD 365
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024383982 453 SYSKYLRAL---EPHYEQLHpefpalrtRAREILQEEEDLAEIVQLVGKASLAEADKVTleVARLLK-DDFLQQ 522
Cdd:CHL00060 366 STSTMLQPRivgEEHYETAQ--------RVKQTLQRYKELQDIIAILGLDELSEEDRLT--VARARKiERFLSQ 429
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
207-456 |
1.41e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 88.02 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 207 QVWPVRQtRPVvekltaNHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEmse 286
Cdd:PRK07196 126 QIHPLQR-RAV------DTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGRE--- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 287 vLRDFPELTMEVDGrtesiMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLA 366
Cdd:PRK07196 196 -VKEFIEHSLQAAG-----MAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 367 EMPADSGYPAYLGARLASFYERAGRARclgsplREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFP 446
Cdd:PRK07196 270 EPPATKGYPPSAFSIIPRLAESAGNSS------GNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYP 343
|
250
....*....|
gi 2024383982 447 SVNWLISYSK 456
Cdd:PRK07196 344 AIDISQSISR 353
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
224-456 |
1.12e-17 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 85.51 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 224 NHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEMSEvlrdFPELTMevDGRTE 303
Cdd:PRK08472 138 DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAPIKVVALIGERGREIPE----FIEKNL--GGDLE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 304 SimkrTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLA 383
Cdd:PRK08472 212 N----TVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLP 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024383982 384 SFYERAGRARclgsplREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSK 456
Cdd:PRK08472 288 QLMERAGKEE------GKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASR 354
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
229-528 |
2.03e-17 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 84.57 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 229 TGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDIIVYVGCGERGNEMSEVLRDFPELTMEvdgrtesimKR 308
Cdd:PRK05922 143 TGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLAA---------QR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 309 TTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYER 388
Cdd:PRK05922 214 TIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTER 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 389 AGRArclgsplREGSVSIVGAV--SPPGGD-FSDPVTSATLGivQVFWGldkklAQRKHF--PSVNWLISYSKYLRALE- 462
Cdd:PRK05922 294 AGNN-------DKGSITALYAIlhYPNHPDiFTDYLKSLLDG--HFFLT-----PQGKALasPPIDILTSLSRSARQLAl 359
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024383982 463 PHYEqlhpefpALRTRAREILQEEEDLAEIVQLvgKASLAEADKVTLEVARLLKD--DFLQQNgYSSY 528
Cdd:PRK05922 360 PHHY-------AAAEELRSLLKAYHEALDIIQL--GAYVPGQDAHLDRAVKLLPSikQFLSQP-LSSY 417
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
306-529 |
3.05e-16 |
|
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: 81.31 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 306 MKRTTLVANTSNMPVAAREASIYTGITLSEYFR-DMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLAS 384
Cdd:TIGR01040 210 MERVCLFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLAT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 385 FYERAGRARClgsplREGSVSIVGAVSPPGGDFSDPVTSATLGIV--QVFwgLDKKLAQRKHFPSVNWLISYSKYLRAL- 461
Cdd:TIGR01040 290 IYERAGRVEG-----RNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPINVLPSLSRLMKSAi 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024383982 462 -EPHYEQLHPEFPALRTRAREILQeeeDLAEIVQLVGKASLAEADKVTLEVARLLKDDFLQQNGYSSYD 529
Cdd:TIGR01040 363 gEGMTRKDHSDVSNQLYACYAIGK---DVQAMKAVVGEEALSSEDLLYLEFLDKFEKNFIAQGPYENRT 428
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
217-456 |
2.36e-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: 76.44 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 217 VVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT------VISQSLSKYsnsdIIVYVGCGERGNEMSEVLRd 290
Cdd:cd01132 43 IIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTaiaidtIINQKGKKV----YCIYVAIGQKRSTVAQIVK- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 291 fpelTMEVDGRtesiMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPA 370
Cdd:cd01132 118 ----TLEEHGA----MEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 371 DSGYPA---YLGARLasfYERAGRarcLGSPLREGSVSIVGAVSPPGGDFSD--P--VTSATLGivQVFwgLDKKLAQRK 443
Cdd:cd01132 190 REAYPGdvfYLHSRL---LERAAK---LSDELGGGSLTALPIIETQAGDVSAyiPtnVISITDG--QIF--LESELFNKG 259
|
250
....*....|...
gi 2024383982 444 HFPSVNWLISYSK 456
Cdd:cd01132 260 IRPAINVGLSVSR 272
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
34-389 |
3.50e-15 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 78.03 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 34 MAGAAMYELVRV--GHaelVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSIFDGIQRPLrdiaq 111
Cdd:PRK13343 44 LPDAALDELLRFegGS---RGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPL----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 112 ltggiyiprgvnvpalprhltwdfvpsksiqvgshvtggdiYGtvtensliqhKIMVPPRSRGTVTHIAPPghysvsdvV 191
Cdd:PRK13343 116 -----------------------------------------DG----------GGPLQATARRPLERPAPA--------I 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 192 LELDFegvaeqltmmqvwpVRQtrpvvekltanhPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKT------VISQSlsk 265
Cdd:PRK13343 137 IERDF--------------VTE------------PLQTGIKVVDALIPIGRGQRELIIGDRQTGKTaiaidaIINQK--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 266 ysNSDII-VYVGCGERGNEMSEVLRDFpeltmevdgRTESIMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHV 344
Cdd:PRK13343 188 --DSDVIcVYVAIGQKASAVARVIETL---------REHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDA 256
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2024383982 345 SMMADSTSRWAEALREISGRLAEMPADSGYPA---YLGARLasfYERA 389
Cdd:PRK13343 257 LIVYDDLSKHAAAYRELSLLLRRPPGREAYPGdifYLHSRL---LERA 301
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
226-432 |
6.75e-14 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 73.84 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 226 PLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQS--LSKYSNSDIIVYVGCGERGNEMSEVLRDFPEltmevdgrtE 303
Cdd:CHL00059 124 PLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDtiLNQKGQNVICVYVAIGQKASSVAQVVTTLQE---------R 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 304 SIMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGRLAEMPADSGYPA---YLGA 380
Cdd:CHL00059 195 GAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHS 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024383982 381 RLasfYERAGRarcLGSPLREGSVSIVGAVSPPGGDFSD--P--VTSATLGivQVF 432
Cdd:CHL00059 275 RL---LERAAK---LSSQLGEGSMTALPIVETQAGDVSAyiPtnVISITDG--QIF 322
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
217-456 |
9.56e-14 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 73.92 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 217 VVEKLTANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVIS------------QSLSKysNSDIIVYVGCGERGNEM 284
Cdd:PTZ00185 163 IVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvstiinqvrinqQILSK--NAVISIYVSIGQRCSNV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 285 SEVLRDFpeltmevdgRTESIMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREISGR 364
Cdd:PTZ00185 241 ARIHRLL---------RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 365 LAEMPADSGYPA---YLGARLASfyeragRARCLGSPLREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQ 441
Cdd:PTZ00185 312 LRRPPGREAYPGdvfYLHSRLLE------RAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFT 385
|
250
....*....|....*
gi 2024383982 442 RKHFPSVNWLISYSK 456
Cdd:PTZ00185 386 GGQRPAVNIGLSVSR 400
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
21-83 |
4.69e-13 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 64.10 E-value: 4.69e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024383982 21 VHGVSGPVVTAIRMAGAA--MYELVRVGHAE----LVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTG 83
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLpgLLNALEVELVEfgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
21-425 |
3.43e-11 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 65.44 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 21 VHGVSGPVVTaIRMAGAAMYELVRV--GHAELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQPLSVELGPGILGSI 98
Cdd:PRK02118 8 ITDITGNVIT-VEAEGVGYGELATVerKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 99 FDGIQRPLRDIAQLTGGIYIPRGVNVPALPRhltwdFVPSKSIQVGshVTGGDIYGTVTENsliqHKIMVpprsrgtvth 178
Cdd:PRK02118 87 FNGSGKPIDGGPELEGEPIEIGGPSVNPVKR-----IVPREMIRTG--IPMIDVFNTLVES----QKIPI---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 179 iappghYSVSDvvleldfEGVAEQLTMMQVwpvrQTrpvvekltanhplltgqrvldalfpcvqggttaipgafgcgktv 258
Cdd:PRK02118 146 ------FSVSG-------EPYNALLARIAL----QA-------------------------------------------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 259 isqslskysNSDIIVYVGCGERGNEMSEVLRDFPELtmevdgrteSIMKRTTLVANTSNMPVAAREASIYTGITLSEYFR 338
Cdd:PRK02118 165 ---------EADIIILGGMGLTFDDYLFFKDTFENA---------GALDRTVMFIHTASDPPVECLLVPDMALAVAEKFA 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 339 DMGLH--VSMMADSTSrWAEALREISGRLAEMPADSGYPAYLGARLASFYERAgrARCLGSplreGSVSIVGAVSPPGGD 416
Cdd:PRK02118 227 LEGKKkvLVLLTDMTN-FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA--VDFEDG----GSITIIAVTTMPGDD 299
|
....*....
gi 2024383982 417 FSDPVTSAT 425
Cdd:PRK02118 300 VTHPVPDNT 308
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
18-84 |
1.50e-10 |
|
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: 57.32 E-value: 1.50e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024383982 18 LGAVHGVSGPVVTAIRMAGAAMYELVRVGHA------ELVGEIIRLEGDMATLQVYEETSGLRVGDPVLRTGQ 84
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGdgnnetVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
226-391 |
9.44e-08 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 54.69 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 226 PLLTGQRVLDALFPCVQG-----------GTTAIpgafgCGKTVISQSlskysNSDII-VYVGCGERGNEMSEVLRdfpe 293
Cdd:PRK09281 145 PLQTGIKAIDAMIPIGRGqreliigdrqtGKTAI-----AIDTIINQK-----GKDVIcIYVAIGQKASTVAQVVR---- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024383982 294 lTMEVDGrtesIMKRTTLVANTSNMPVAAREASIYTGITLSEYFRDMGLHVSMMADSTSRWAEALREIS-------GRLA 366
Cdd:PRK09281 211 -KLEEHG----AMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSlllrrppGREA 285
|
170 180
....*....|....*....|....*...
gi 2024383982 367 empadsgYPA---YLGARLasfYERAGR 391
Cdd:PRK09281 286 -------YPGdvfYLHSRL---LERAAK 303
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
482-526 |
3.21e-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: 44.74 E-value: 3.21e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2024383982 482 ILQEEEDLAEIVQLVGKASLAEADKVTLEVARLLKdDFLQQNGYS 526
Cdd:cd01429 11 ILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLE-EFLQQGQFE 54
|
|
| 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 ... |
21-73 |
2.72e-04 |
|
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: 39.33 E-value: 2.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024383982 21 VHGVSGPVVTAIRMAGAAMYELVRVGHA---ELVGEIIRLEGDMATLQVYEETSGL 73
Cdd:cd18118 5 VSEINGPLVIVEGVKGVKYGEIVEITLPdgeVRRGQVLEVSGDKAVVQVFEGTSGL 60
|
|
| |
