|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
5-535 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 931.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 5 ASSVTTAVPSSLPQGRVVQVVGPVIDVGFLPPKknIPKVNETLLVCRVRPAtswnvligrqclpPGKVALACEVQCLLGN 84
Cdd:CHL00060 3 PTGPGVSTLEEKNLGRITQIIGPVLDVAFPPGK--MPNIYNALVVKGRDTA-------------GQEINVTCEVQQLLGN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 85 YKVRSVGMGDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPVwrflleksdvkegsnplqnlsqklELY 164
Cdd:CHL00060 68 NRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPV------------------------DTR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 165 ERRPIHSTAPTLADLVVEPSVLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAKFHGGVSVFAGVGERTR 244
Cdd:CHL00060 124 TTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 245 EGFDLYKEMREAGVIDAQYPPYSQVALVYGQMNEPPGARMRVALTALTISEFFRDERKQDVLLFVDNIFRFVQAGSEVSA 324
Cdd:CHL00060 204 EGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 325 LLGRMPSAVGYQPTLATEMGYLQERITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDP 404
Cdd:CHL00060 284 LLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 405 LESNSTVLQPEIVGEAHYDTAQSVRKILQQYKELQDLIAILGLDELSQEDRLVVSRARKIERFLSQPFYVAEVFTGSPGK 484
Cdd:CHL00060 364 LDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGK 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 301500988 485 YVSLKEAIEGFTEILQGQVDQLEEEAFYLVGGLAEAKEKDQTIKEEARKRQ 535
Cdd:CHL00060 444 YVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLEVESKLKK 494
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
18-531 |
0e+00 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 855.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 18 QGRVVQVVGPVIDVGFlpPKKNIPKVNETLLVCRvrpatswnvligrqclpPGKVALACEVQCLLGNYKVRSVGMGDSQG 97
Cdd:COG0055 5 TGKIVQVIGPVVDVEF--PEGELPAIYNALEVEN-----------------EGGGELVLEVAQHLGDNTVRCIAMDSTDG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 98 IRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPVwrflleKSDvkegsnplqnlsqklelyERRPIHSTAPTLA 177
Cdd:COG0055 66 LVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPI------EAK------------------ERRPIHRPAPPFE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 178 DLVVEPSVLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAKFHGGVSVFAGVGERTREGFDLYKEMREAG 257
Cdd:COG0055 122 EQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 258 VIDaqyppysQVALVYGQMNEPPGARMRVALTALTISEFFRDERKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQP 337
Cdd:COG0055 202 VLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 338 TLATEMGYLQERITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVLQPEIV 417
Cdd:COG0055 275 TLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 418 GEAHYDTAQSVRKILQQYKELQDLIAILGLDELSQEDRLVVSRARKIERFLSQPFYVAEVFTGSPGKYVSLKEAIEGFTE 497
Cdd:COG0055 355 GEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKE 434
|
490 500 510
....*....|....*....|....*....|....
gi 301500988 498 ILQGQVDQLEEEAFYLVGGLAEAKEKDQTIKEEA 531
Cdd:COG0055 435 ILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAEA 468
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
19-523 |
0e+00 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 750.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 19 GRVVQVVGPVIDVGFlpPKKNIPKVNETLlvcrvrpatswnvligrQCLPPGKVALACEVQCLLGNYKVRSVGMGDSQGI 98
Cdd:TIGR01039 3 GKVVQVIGPVVDVEF--EQGELPRIYNAL-----------------KVQNRAESELTLEVAQHLGDDTVRTIAMGSTDGL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 99 RRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPVwrflleksdvkegsnplqnlsqklELYERRPIHSTAPTLAD 178
Cdd:TIGR01039 64 VRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPI------------------------PAKERWPIHRKAPSFEE 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 179 LVVEPSVLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAKFHGGVSVFAGVGERTREGFDLYKEMREAGV 258
Cdd:TIGR01039 120 QSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 259 IDaqyppysQVALVYGQMNEPPGARMRVALTALTISEFFRDERKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPT 338
Cdd:TIGR01039 200 ID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 339 LATEMGYLQERITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVLQPEIVG 418
Cdd:TIGR01039 273 LATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 419 EAHYDTAQSVRKILQQYKELQDLIAILGLDELSQEDRLVVSRARKIERFLSQPFYVAEVFTGSPGKYVSLKEAIEGFTEI 498
Cdd:TIGR01039 353 EEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEI 432
|
490 500
....*....|....*....|....*
gi 301500988 499 LQGQVDQLEEEAFYLVGGLAEAKEK 523
Cdd:TIGR01039 433 LEGKYDHLPEQAFYMVGTIEEVVEK 457
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
19-520 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.
Pssm-ID: 132348 [Multi-domain] Cd Length: 449 Bit Score: 550.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 19 GRVVQVVGPVIDVGFlppKKNIPKVNETLLvcrvrpatswnvlIGRQclppGKVALacEVQCLLGNYKVRSVGMGDSQGI 98
Cdd:TIGR03305 1 GHVVAVRGSIVDVRF---DGELPAIHSVLR-------------AGRE----GEVVV--EVLSQLDAHHVRGIALTPTQGL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 99 RRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPVwrfllekSDVkegsnplqnlsqklelyERRPIHSTAPTLAD 178
Cdd:TIGR03305 59 ARGMPVRDSGGPLKAPVGKPTLSRMFDVFGNTIDRREPP-------KDV-----------------EWRSVHQAPPTLTR 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 179 LVVEPSVLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAKFHGGVSVFAGVGERTREGFDLYKEMREAGV 258
Cdd:TIGR03305 115 RSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 259 IDaqyppysQVALVYGQMNEPPGARMRVALTALTISEFFRDERKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPT 338
Cdd:TIGR03305 195 LD-------NTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 339 LATEMGYLQERITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVLQPEIVG 418
Cdd:TIGR03305 268 LGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVG 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 419 EAHYDTAQSVRKILQQYKELQDLIAILGLDELSQEDRLVVSRARKIERFLSQPFYVAEVFTGSPGKYVSLKEAIEGFTEI 498
Cdd:TIGR03305 348 ERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERI 427
|
490 500
....*....|....*....|..
gi 301500988 499 LQGQVDQLEEEAFYLVGGLAEA 520
Cdd:TIGR03305 428 LNDEFQDYPERDLYMIGKIDEA 449
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
114-414 |
0e+00 |
|
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: 549.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 114 PVGECTLGRIINVLGLPTDRLGPVwrflleksdvkegsnplqnlsqklELYERRPIHSTAPTLADLVVEPSVLETGIKVL 193
Cdd:cd01133 3 PVGEETLGRIFNVLGEPIDERGPI------------------------KAKERWPIHREAPEFVELSTEQEILETGIKVV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 194 DLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAKFHGGVSVFAGVGERTREGFDLYKEMREAGVIDaqYPPYSQVALVY 273
Cdd:cd01133 59 DLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVIN--LDGLSKVALVY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 274 GQMNEPPGARMRVALTALTISEFFRDERKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERITTT 353
Cdd:cd01133 137 GQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301500988 354 KTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVLQP 414
Cdd:cd01133 217 KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
114-411 |
1.90e-116 |
|
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: 345.21 E-value: 1.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 114 PVGECTLGRIINVLGLPTDRLGPVwrflleksdvkegsnplqnlsqklELYERRPIHSTAPTLADLVVEPSVLETGIKVL 193
Cdd:cd19476 3 PVGPELLGRILDGLGEPLDGLPPI------------------------KTKQRRPIHLKAPNPIERLPPEEPLQTGIKVI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 194 DLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAKFHGGVSVFAGVGERTREGFDLYKEMREAGVIdaqyppySQVALVY 273
Cdd:cd19476 59 DLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAM-------ERTVVVA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 274 GQMNEPPGARMRVALTALTISEFFRDeRKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERITTT 353
Cdd:cd19476 132 NTANDPPGARMRVPYTGLTIAEYFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 354 KT--GSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTV 411
Cdd:cd19476 211 KDggGSITAIPAVSTPGDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
189-409 |
4.13e-95 |
|
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: 288.49 E-value: 4.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 189 GIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAKfhgGVSVFAGVGERTREGFDLYKEMREAGVIDaqyppysQ 268
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK-------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 269 VALVYGQMNEPPGARMRVALTALTISEFFRDErKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQE 348
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 301500988 349 RITTT--KTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNS 409
Cdd:pfam00006 150 RAGRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-499 |
5.45e-67 |
|
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: 222.98 E-value: 5.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 3 DKASSVTTAVPSSLPQGRVVQVVGPVIDVGFLPPKknipkVNEtllVCRVRPATSWNVLigrqclppgkvalaCEVqcll 82
Cdd:COG1157 5 ARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDAS-----IGE---LCEIETADGRPVL--------------AEV---- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 83 gnykvrsVG----------MGDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPvwrflleksdvkegsn 152
Cdd:COG1157 59 -------VGfrgdrvllmpLGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGP---------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 153 plqnlsqkLELYERRPIHSTA--PTLADLVVEPsvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLI-MelinnIAKF 229
Cdd:COG1157 116 --------LPGEERRPLDAPPpnPLERARITEP--LDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLgM-----IARN 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 230 -HGGVSVFAGVGERTRE--GF---DLYKEMREAGVIdaqyppysqvalVYGQMNEPPGARMRVALTALTISEFFRDERKq 303
Cdd:COG1157 181 tEADVNVIALIGERGREvrEFiedDLGEEGLARSVV------------VVATSDEPPLMRLRAAYTATAIAEYFRDQGK- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 304 DVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERITTTKTGSITsiqAIY---VPADDLTDPATATTF 380
Cdd:COG1157 248 NVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlVEGDDMNDPIADAVR 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 381 SHLDATTVLSRQLAAKGIYPAIDPLESNSTVLqPEIVGEAHYDTAQSVRKILQQYKELQDLIAIlG---------LDEls 451
Cdd:COG1157 325 GILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRI-GayqpgsdpeLDE-- 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 301500988 452 qedrlVVSRARKIERFLSQpfyvaevftgSPGKYVSLKEAIEGFTEIL 499
Cdd:COG1157 401 -----AIALIPAIEAFLRQ----------GMDERVSFEESLAQLAELL 433
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
416-523 |
1.68e-65 |
|
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-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 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.
Pssm-ID: 349745 [Multi-domain] Cd Length: 108 Bit Score: 208.10 E-value: 1.68e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 416 IVGEAHYDTAQSVRKILQQYKELQDLIAILGLDELSQEDRLVVSRARKIERFLSQPFYVAEVFTGSPGKYVSLKEAIEGF 495
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 301500988 496 TEILQGQVDQLEEEAFYLVGGLAEAKEK 523
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
114-411 |
4.26e-51 |
|
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: 175.83 E-value: 4.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 114 PVGECTLGRIINVLGLPTDRLGPVwRFLLEKSDVKEGSNPLqnlsqklelyERRPIHStaptladlvvepsVLETGIKVL 193
Cdd:cd01136 3 PVGDGLLGRVIDALGEPLDGKGLP-DEPERRPLIAAPPNPL----------KRAPIEQ-------------PLPTGVRAI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 194 DLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAkfhGGVSVFAGVGERTREGFD-LYKEMREAGVidaqyppySQVALV 272
Cdd:cd01136 59 DGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTD---ADVNVIALIGERGREVREfIEKDLGEEGL--------KRSVLV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 273 YGQMNEPPGARMRVALTALTISEFFRDERKqDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERITT 352
Cdd:cd01136 128 VATSDESPLLRVRAAYTATAIAEYFRDQGK-KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 301500988 353 TKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTV 411
Cdd:cd01136 207 GEKGSITAFYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
92-472 |
1.57e-48 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 173.64 E-value: 1.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 92 MGDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPvwrflleksDVKEGSNPlqnlsqklelyERRPIHS 171
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDA---------PPTVGPIS-----------EERVIDV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 172 TAPTLADLVVEPSVLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAkfhGGVSVFAGVGERTREGFDLYK 251
Cdd:PRK08149 121 APPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSE---ADVFVIGLIGERGREVTEFVE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 252 EMReagvidaQYPPYSQVALVYGQMNEPPGARMRVALTALTISEFFRDERKqDVLLFVDNIFRFVQAGSEVSALLGRMPS 331
Cdd:PRK08149 198 SLR-------ASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGK-RVVLFIDSMTRYARALRDVALAAGELPA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 332 AVGYQPTLATEMGYLQERITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTV 411
Cdd:PRK08149 270 RRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301500988 412 LQpEIVGEAHYDTAQSVRKILQQYKELQDLIAiLG---LDELSQEDRlVVSRARKIERFLSQPF 472
Cdd:PRK08149 350 FG-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDV 410
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
11-470 |
2.52e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 170.77 E-value: 2.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 11 AVPSSLPQGrvVQVVGPVIDVGFLPPKKNIPKVNETLLvCRVRPAtswnvligrqclppgkvALACEVQCLLGNYKVRSv 90
Cdd:PRK06820 18 TRPSAPPEG--LRYRGPIVEIGPTLLRASLPGVAQGEL-CRIEPQ-----------------GMLAEVVSIEQEMALLS- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 91 GMGDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPV---WRFLleksdvkEGS--NPLQnlsqklelye 165
Cdd:PRK06820 77 PFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLtgqWREL-------DCPppSPLT---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 166 RRPIHStaptladlvvepsVLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAkfhGGVSVFAGVGERTRE 245
Cdd:PRK06820 140 RQPIEQ-------------MLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSA---ADVMVLALIGERGRE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 246 gfdlykeMREagVIDAQYPP--YSQVALVYGQMNEPPGARMRVALTALTISEFFRDERKqDVLLFVDNIFRFVQAGSEVS 323
Cdd:PRK06820 204 -------VRE--FLEQVLTPeaRARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGK-KVLLMADSLTRYARAAREIG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 324 ALLGRMPSAVGYQPTLATEMGYLQERITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAID 403
Cdd:PRK06820 274 LAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAID 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301500988 404 PLESNSTVLqPEIVGEAHYDTAQSVRKILQQYKELQDLIAI----LGLDELSQEdrlVVSRARKIERFLSQ 470
Cdd:PRK06820 354 IAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
18-470 |
1.34e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 168.78 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 18 QGRVVQVVGPVIdvgflppKKNIP--KVNEtllVCRVR-PATSWNVLigrqclppGKVALACEVQCLLgnykvrsVGMGD 94
Cdd:PRK06936 24 RGRVTQVTGTIL-------KAVVPgvRIGE---LCYLRnPDNSLSLQ--------AEVIGFAQHQALL-------TPLGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 95 SQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDrlgpvwrflleksdvkeGSNPLqnlsqklELYERRPIHSTAP 174
Cdd:PRK06936 79 MYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFD-----------------GGHPP-------EPAAWYPVYADAP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 175 T--LADLVVEPsvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAkfhGGVSVFAGVGERTRE--GF--- 247
Cdd:PRK06936 135 ApmSRRLIETP--LSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAE---VDVTVLALIGERGREvrEFies 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 248 DLYKEMREAGVidaqyppysqvaLVYGQMNEPPGARMRVALTALTISEFFRDERKQdVLLFVDNIFRFVQAGSEVSALLG 327
Cdd:PRK06936 210 DLGEEGLRKAV------------LVVATSDRPSMERAKAGFVATSIAEYFRDQGKR-VLLLMDSVTRFARAQREIGLAAG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 328 RMPSAVGYQPTLATEMGYLQERITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLES 407
Cdd:PRK06936 277 EPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRS 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301500988 408 NSTVLQpEIVGEAHYDTAQSVRKILQQYKELQDLIAI----LGLDELSQEdrlVVSRARKIERFLSQ 470
Cdd:PRK06936 357 ASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
76-444 |
2.32e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 159.87 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 76 CEVQCLLGNYKVRSVGMGDS----------QGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPvwrfLLEKS 145
Cdd:PRK08972 50 CSIETMAGELEAEVVGFDGDllylmpieelRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGP----IYTDQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 146 DVKEGSNPLQNLSqklelyeRRPIHstaptladlvvEPsvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLI-MELIN 224
Cdd:PRK08972 126 RASRHSPPINPLS-------RRPIT-----------EP--LDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLgMMTRG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 225 NIAKfhggVSVFAGVGERTREGFD-----LYKEMREAGVIdaqyppysqvalVYGQMNEPPGARMRVALTALTISEFFRD 299
Cdd:PRK08972 186 TTAD----VIVVGLVGERGREVKEfieeiLGEEGRARSVV------------VAAPADTSPLMRLKGCETATTIAEYFRD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 300 ErKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERITT--TKTGSITSIQAIYVPADDLTDPATA 377
Cdd:PRK08972 250 Q-GLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGDDLQDPIAD 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301500988 378 TTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVLqPEIVGEAHYDTAQSVRKILQQYKELQDLIAI 444
Cdd:PRK08972 329 ASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
94-444 |
1.94e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 157.19 E-value: 1.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 94 DSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRlGPVWRFLLEKSDVKEGSNPLqnlsqklelyERRPIhsta 173
Cdd:PRK07721 74 EVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDG-SALPKGLAPVSTDQDPPNPL----------KRPPI---- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 174 ptladlvVEPsvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAkfhGGVSVFAGVGERTREGFD-LYKE 252
Cdd:PRK07721 139 -------REP--MEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTS---ADLNVIALIGERGREVREfIERD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 253 MREAGVidaqyppySQVALVYGQMNEPPGARMRVALTALTISEFFRDeRKQDVLLFVDNIFRFVQAGSEVSALLGRMPSA 332
Cdd:PRK07721 207 LGPEGL--------KRSIVVVATSDQPALMRIKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 333 VGYQPTLATEMGYLQERITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVL 412
Cdd:PRK07721 278 KGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM 357
|
330 340 350
....*....|....*....|....*....|..
gi 301500988 413 qPEIVGEAHYDTAQSVRKILQQYKELQDLIAI 444
Cdd:PRK07721 358 -NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
121-457 |
4.59e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 156.70 E-value: 4.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 121 GRIINVLGLPTDRLGPVwrflleksdvKEGSnplqnlsqklelyERRPIHSTAP-TLADLVVEpSVLETGIKVLDLLTPY 199
Cdd:PRK06002 107 GRVINALGEPIDGLGPL----------APGT-------------RPMSIDATAPpAMTRARVE-TGLRTGVRVIDIFTPL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 200 RRGGKVGLFGGAGVGKTVLIMELINniAKFHGGVsVFAGVGERTREgfdlYKEMREAGVIDAQyppySQVALVYGQMNEP 279
Cdd:PRK06002 163 CAGQRIGIFAGSGVGKSTLLAMLAR--ADAFDTV-VIALVGERGRE----VREFLEDTLADNL----KKAVAVVATSDES 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 280 PGARMRVALTALTISEFFRDeRKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERI--TTTKTGS 357
Cdd:PRK06002 232 PMMRRLAPLTATAIAEYFRD-RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 358 ITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNS-------TVLQPEIVgeahydtaQSVRK 430
Cdd:PRK06002 311 ITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISrlarhawTPEQRKLV--------SRLKS 382
|
330 340 350
....*....|....*....|....*....|..
gi 301500988 431 ILQQYKELQDLIAI----LGLD-ELSQEDRLV 457
Cdd:PRK06002 383 MIARFEETRDLRLIggyrAGSDpDLDQAVDLV 414
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
73-444 |
1.10e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 152.44 E-value: 1.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 73 ALACEVQCLLGNykvRSVGM--GDSQGIRRGAR-VLSTTAPIYSPvGECTLGRIINVLGLPTDRLGPvwrflLEKSDVke 149
Cdd:PRK08927 53 PVPCEVVGFRGD---RALLMpfGPLEGVRRGCRaVIANAAAAVRP-SRAWLGRVVNALGEPIDGKGP-----LPQGPV-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 150 gSNPLQNLSQklelyerrPIHSTAPtladlVVEPsvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAkf 229
Cdd:PRK08927 122 -PYPLRAPPP--------PAHSRAR-----VGEP--LDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNAD-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 230 hGGVSVFAGVGERTRE--GF---DLYKEMREAGVIdaqyppysqvalVYGQMNEPPGARMRVALTALTISEFFRDERKqD 304
Cdd:PRK08927 184 -ADVSVIGLIGERGREvqEFlqdDLGPEGLARSVV------------VVATSDEPALMRRQAAYLTLAIAEYFRDQGK-D 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 305 VLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERI--TTTKTGSITSIQAIYVPADDLTDPATATTFSH 382
Cdd:PRK08927 250 VLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGI 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301500988 383 LDATTVLSRQLAAKGIYPAIDPLESNSTVLqPEIVGEAHYDTAQSVRKILQQYKELQDLIAI 444
Cdd:PRK08927 330 LDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
55-444 |
4.68e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 151.04 E-value: 4.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 55 ATSWNVLIGRQCL-------PPGKVAlaCEVQCLLGNyKVRSVGMGDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVL 127
Cdd:PRK05688 41 AEGLRAAVGSRCLvinddsyHPVQVE--AEVMGFSGD-KVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 128 GLPTDRLGPVW---RFLLEKSDVkegsNPLQnlsqklelyeRRPIHSTaptladlvvepsvLETGIKVLDLLTPYRRGGK 204
Cdd:PRK05688 118 GRALDGKGPMKaedWVPMDGPTI----NPLN----------RHPISEP-------------LDVGIRSINGLLTVGRGQR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 205 VGLFGGAGVGKTVLImeliNNIAKF-HGGVSVFAGVGERTREGFDLYKE-MREAGVidaqyppySQVALVYGQMNEPPGA 282
Cdd:PRK05688 171 LGLFAGTGVGKSVLL----GMMTRFtEADIIVVGLIGERGREVKEFIEHiLGEEGL--------KRSVVVASPADDAPLM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 283 RMRVALTALTISEFFRDERKqDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERITTTKTG--SITS 360
Cdd:PRK05688 239 RLRAAMYCTRIAEYFRDKGK-NVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 361 IQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVLqPEIVGEAHYDTAQSVRKILQQYKELQD 440
Cdd:PRK05688 318 FYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRD 396
|
....
gi 301500988 441 LIAI 444
Cdd:PRK05688 397 LISV 400
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
62-470 |
7.20e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 150.13 E-value: 7.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 62 IGRQCLPpGKVALACEV-------QCLLGNYKVRSVGMGDSqgirrgarVLSTTAPIYSPVGECTLGRIINVLGlptdrl 134
Cdd:PRK06793 42 IGDVCFV-GEHNVLCEViaiekenNMLLPFEQTEKVCYGDS--------VTLIAEDVVIPRGNHLLGKVLSANG------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 135 gpvwRFLLEKSdvkeGSNPLQnlsqKLELyERRPIHstAPTLADLVvepSVLETGIKVLDLLTPYRRGGKVGLFGGAGVG 214
Cdd:PRK06793 107 ----EVLNEEA----ENIPLQ----KIKL-DAPPIH--AFEREEIT---DVFETGIKSIDSMLTIGIGQKIGIFAGSGVG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 215 KTVLIMELINNiAKfhGGVSVFAGVGERTREGFD-LYKEMREAGVidaqyppySQVALVYGQMNEPPGARMRVALTALTI 293
Cdd:PRK06793 169 KSTLLGMIAKN-AK--ADINVISLVGERGREVKDfIRKELGEEGM--------RKSVVVVATSDESHLMQLRAAKLATSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 294 SEFFRDERKqDVLLFVDNIFRFVQAGSEVSALLGRMPSAvGYQPTLATEMGYLQERITTTKTGSITSIQAIYVPADDLTD 373
Cdd:PRK06793 238 AEYFRDQGN-NVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 374 PATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVLQpEIVGEAHYDTAQSVRKILQQYKElQDLIAILGLDELSQE 453
Cdd:PRK06793 316 PVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAE 393
|
410 420
....*....|....*....|
gi 301500988 454 DRLVVSRARKIE---RFLSQ 470
Cdd:PRK06793 394 NAYIFECKNKVEginTFLKQ 413
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
96-500 |
1.26e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 149.45 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 96 QGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPVwrflleksdvkegsnplqNLSQKLELYeRRPIhstAPT 175
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAI------------------DYERYAPIM-KAPI---AAM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 176 LADLVVEPsvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLiMELINNIAKfhGGVSVFAGVGERTRE---------G 246
Cdd:PRK08472 133 KRGLIDEV--FSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL-MGMIVKGCL--APIKVVALIGERGREipefieknlG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 247 FDLykemrEAGVIdaqyppysqvalVYGQMNEPPGARMRVALTALTISEFFRDERKqDVLLFVDNIFRFVQAGSEVSALL 326
Cdd:PRK08472 208 GDL-----ENTVI------------VVATSDDSPLMRKYGAFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLAL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 327 GRMPSAVGYQPTLATEMGYLQERITTTKT-GSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPL 405
Cdd:PRK08472 270 GEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINIL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 406 ESNSTVLQpEIVGEAHYDTAQSVRKILQQYKELQDLIAI----LGLD-ELSQedrlVVSRARKIERFLSQpfyvaevftg 480
Cdd:PRK08472 350 NSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGNDkELDE----AISKKEFMEQFLKQ---------- 414
|
410 420
....*....|....*....|
gi 301500988 481 SPGKYVSLKEAIEGFTEILQ 500
Cdd:PRK08472 415 NPNELFPFEQTFEQLEEILR 434
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
93-471 |
1.07e-38 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 147.22 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 93 GDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPvwrflleksdvkegsnplqnlsqkLELYERRPIHST 172
Cdd:PRK09099 78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGP------------------------LDCDELVPVIAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 173 APT-LADLVVEPSvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLImelinniAKFHGG----VSVFAGVGERTREGF 247
Cdd:PRK09099 134 PPDpMSRRMVEAP-LPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLM-------GMFARGtqcdVNVIALIGERGREVR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 248 DLYKE-MREAGVidaqyppySQVALVYGQMNEPPGARMRVALTALTISEFFRDeRKQDVLLFVDNIFRFVQAGSEVSALL 326
Cdd:PRK09099 206 EFIELiLGEDGM--------ARSVVVCATSDRSSIERAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 327 GRMPSAVGYQPTLATEMGYLQERITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLE 406
Cdd:PRK09099 277 GEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLG 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301500988 407 SNSTVLqPEIVGEAHYDTAQSVRKILQQYKELQDLIAI----LGLDELSQEdrlVVSRARKIERFLSQP 471
Cdd:PRK09099 357 SLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
60-444 |
1.67e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 146.25 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 60 VLIGRQC--LPPGKVAlacEVQCLLGNyKVRSVGMGDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRL--- 134
Cdd:PRK07594 40 VFMGELCciKPGEELA---EVVGINGS-KALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 135 -GPvWRFLleksdvkeGSNPLQNLSqklelyeRRPIhsTAPtladlvvepsvLETGIKVLDLLTPYRRGGKVGLFGGAGV 213
Cdd:PRK07594 116 dVC-WKDY--------DAMPPPAMV-------RQPI--TQP-----------LMTGIRAIDSVATCGEGQRVGIFSAPGV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 214 GKTVLIMELINNIAkfhGGVSVFAGVGERTRE-----GFDLYKEMREAGVIdaqyppysqvalVYGQMNEPPGARMRVAL 288
Cdd:PRK07594 167 GKSTLLAMLCNAPD---ADSNVLVLIGERGREvrefiDFTLSEETRKRCVI------------VVATSDRPALERVRALF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 289 TALTISEFFRDERKQdVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERITTTKTGSITSIQAIYVPA 368
Cdd:PRK07594 232 VATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEG 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 301500988 369 DDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVLqPEIVGEAHYDTAQSVRKILQQYKELQDLIAI 444
Cdd:PRK07594 311 DDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLIRI 385
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
97-470 |
1.51e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 138.10 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 97 GIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPVwrflleksdvkEGSNPLQNLSQKLELYERRPIHStaptl 176
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQL-----------GGSTPLQQQLPQIHPLQRRAVDT----- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 177 adlvvepsVLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIakfHGGVSVFAGVGERTREGFDLYKE-MRE 255
Cdd:PRK07196 138 --------PLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYT---QADVVVVGLIGERGREVKEFIEHsLQA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 256 AGVidaqyppySQVALVYGQMNEPPGARMRVALTALTISEFFRDeRKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGY 335
Cdd:PRK07196 207 AGM--------AKSVVVAAPADESPLMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 336 QPTLATEMGYLQERITTTK-TGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVLQp 414
Cdd:PRK07196 278 PPSAFSIIPRLAESAGNSSgNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS- 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 415 EIVGEAHYDTAQSVRKILQQYKELQDLIA----ILGLDELSQEdrlVVSRARKIERFLSQ 470
Cdd:PRK07196 357 QVIGSQQAKAASLLKQCYADYMAIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
94-444 |
1.19e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 130.29 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 94 DSQGIRRGARVLSTTAPIYS-------PVGECTLGRIINVLGLPTDRLGPV---WRFLLEKSDVkegsNPLQnlsqklel 163
Cdd:PRK07960 84 EVEGILPGARVYARNISGEGlqsgkqlPLGPALLGRVLDGSGKPLDGLPAPdtgETGALITPPF----NPLQ-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 164 yeRRPIHStaptladlvvepsVLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLImeliNNIAKF-HGGVSVFAGVGER 242
Cdd:PRK07960 152 --RTPIEH-------------VLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLL----GMMARYtQADVIVVGLIGER 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 243 TREGFD-----LYKEMREAGVIDAQYPPYSqvalvygqmnepPGARMRVALTALTISEFFRDeRKQDVLLFVDNIFRFVQ 317
Cdd:PRK07960 213 GREVKDfieniLGAEGRARSVVIAAPADVS------------PLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 318 AGSEVSALLGRMPSAVGYQPTLATEMGYLQERITT--TKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAA 395
Cdd:PRK07960 280 AQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAE 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 301500988 396 KGIYPAIDPLESNSTVLQpEIVGEAHYDTAQSVRKILQQYKELQDLIAI 444
Cdd:PRK07960 360 AGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
186-409 |
3.77e-25 |
|
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: 105.35 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 186 LETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVlimeLINNIAKF-HGGVSVFAGVGERTREGFDLYKEMREAGVIDAQYP 264
Cdd:cd01134 60 LLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTV----ISQSLSKWsNSDVVIYVGCGERGNEMAEVLEEFPELKDPITGES 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 265 PYSQVALVYGQMNEPPGARMRVALTALTISEFFRDERKqDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMG 344
Cdd:cd01134 136 LMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGY-NVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLA 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301500988 345 YLQERI-------TTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNS 409
Cdd:cd01134 215 EFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
93-473 |
2.52e-24 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 106.06 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 93 GDSQGI-RRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPVwrflleksdVKEgsnplqnlsqklelyERRPIHS 171
Cdd:PRK04196 57 EGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEI---------IPE---------------KRLDING 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 172 TA--PTLADlvvEPS-VLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNiAKFHGGVS----VFAGVGERTR 244
Cdd:PRK04196 113 APinPVARE---YPEeFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQ-AKVLGEEEnfavVFAAMGITFE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 245 EGFDLYKEMREAGVIDaqyppysQVALVYGQMNEPPGARMRVALTALTISEFFRDERKQDVLLFVDNIFRFVQAGSEVSA 324
Cdd:PRK04196 189 EANFFMEDFEETGALE-------RSVVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 325 LLGRMPSAVGYQPTLATEMGYLQER--ITTTKTGSITSIQAIYVPADDLTDPATattfshlDAT-------TVLSRQLAA 395
Cdd:PRK04196 262 AREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 396 KGIYPAIDPLESNSTVLQPEIvGEA-----HYDTAQSVRKILQQYKELQDLIAILGLDELSQEDRLVVSRARKIE-RFLS 469
Cdd:PRK04196 335 KGIYPPIDVLPSLSRLMKDGI-GEGktredHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVN 413
|
....
gi 301500988 470 QPFY 473
Cdd:PRK04196 414 QGFD 417
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
89-544 |
5.29e-23 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 102.30 E-value: 5.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 89 SVG---MGDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPVwrflleksdvkegsnplqnlsqklELYE 165
Cdd:PRK13343 70 LVGavlLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPL------------------------QATA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 166 RRPIHSTAPTLA--DLVVEPsvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELInnIAKFHGGV-SVFAGVGER 242
Cdd:PRK13343 126 RRPLERPAPAIIerDFVTEP--LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDViCVYVAIGQK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 243 TREGFDLYKEMREAGVidaqyPPYSQValVYGQMNEPPGARMRVALTALTISEFFRDeRKQDVLLFVDNIFRFVQAGSEV 322
Cdd:PRK13343 202 ASAVARVIETLREHGA-----LEYTTV--VVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYREL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 323 SALLGRMPSAVGYQPTLATEMGYLQERIT----TTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGI 398
Cdd:PRK13343 274 SLLLRRPPGREAYPGDIFYLHSRLLERAAklspELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQ 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 399 YPAIDPLESNSTV---LQPEIVGEAhydtAQSVRKILQQYKELQdLIAILG--LDELSQEdrlVVSRARKIERFLSQPFY 473
Cdd:PRK13343 354 RPAVDVGLSVSRVggkAQHPAIRKE----SGRLRLDYAQFLELE-AFTRFGglLDAGTQK---QITRGRRLRELLKQPRF 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 474 ----VAEvftgspgKYVSLKEAIEGF-----TEILQGQVDQLEEEAFYLVGGLAEAKEKDQTIKEEARKRQEELKKRAVK 544
Cdd:PRK13343 426 splsVEE-------QIALLYALNEGLldavpLANIQAFEERLLEKLDARFAALSLALESPRELDEAWLAALEEILREAGE 498
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
114-409 |
5.79e-23 |
|
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: 98.83 E-value: 5.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 114 PVGECTLGRIINVLGLPTDRLGPVwrflleksdVKEgsnplqnlsqklelyERRPIHSTAPTLADLVVEPSVLETGIKVL 193
Cdd:cd01135 5 PVSEDMLGRIFNGSGKPIDGGPPI---------LPE---------------DYLDINGPPINPVARIYPEEMIQTGISAI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 194 DLLTPYRRGGKVGLFGGAGVGKTVLIMELINNiAKFHGGVS----VFAGVGERTREGFDLYKEMREAGVIDaqyppysQV 269
Cdd:cd01135 61 DVMNTLVRGQKLPIFSGSGLPHNELAAQIARQ-AGVVGSEEnfaiVFAAMGVTMEEARFFKDDFEETGALE-------RV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 270 ALVYGQMNEPPGARMRVALTALTISEFFRDERKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQER 349
Cdd:cd01135 133 VLFLNLANDPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYER 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301500988 350 --ITTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNS 409
Cdd:cd01135 213 agRVEGRKGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLS 274
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
101-472 |
6.24e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 101.52 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 101 GARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPvwrflLEKSDVKegsnPLqnLSQKLELYERRPIHSTAPTladlv 180
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQ-----LPKTHLK----PL--FSSPPSPMSRQPIQEIFPT----- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 181 vepsvletGIKVLDLLTPYRRGGKVGLFGGAGVGKTvlimELINNIAK-FHGGVSVFAGVGERTREGFDLYKEMREAgvI 259
Cdd:PRK05922 144 --------GIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEG--L 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 260 DAQyppysQVALVYGQMNEPPGARMRVALTALTISEFFRDErKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYQPTL 339
Cdd:PRK05922 210 AAQ-----RTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQ-GHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 340 ATEMGYLQERITTTKTGSITSIQAI-YVP--ADDLTDPATattfSHLDATTVLSRQLAAKGiYPAIDPLESNSTVLQpEI 416
Cdd:PRK05922 284 FHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLK----SLLDGHFFLTPQGKALA-SPPIDILTSLSRSAR-QL 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 417 VGEAHYDTAQSVRKILQQYKELQDLIAiLGLDELSQEDRLvvSRARK----IERFLSQPF 472
Cdd:PRK05922 358 ALPHHYAAAEELRSLLKAYHEALDIIQ-LGAYVPGQDAHL--DRAVKllpsIKQFLSQPL 414
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
181-470 |
8.23e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 99.09 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 181 VEPsvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLImeliNNIAKF-HGGVSVFAGVGERTREGFDLYKEMREagVI 259
Cdd:PRK04192 208 VEP--LITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQ----HQLAKWaDADIVIYVGCGERGNEMTEVLEEFPE--LI 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 260 DaqypPYSQVALvygqM----------NEPPGARMRVALTALTISEFFRDerkQ--DVLLFVDNIFRFVQAGSEVSALLG 327
Cdd:PRK04192 280 D----PKTGRPL----MertvliantsNMPVAAREASIYTGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 328 RMPSAVGYQPTLATEMGYLQER---ITT--TKTGSITSIQAIYVPADDLTDPATATTfshLDATTV---LSRQLAAKGIY 399
Cdd:PRK04192 349 EMPGEEGYPAYLASRLAEFYERagrVKTlgGEEGSVTIIGAVSPPGGDFSEPVTQNT---LRIVKVfwaLDAELADRRHF 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301500988 400 PAIDPLESNS---TVLQP---EIVGEAHYDTAQSVRKILQQYKELQDLIAILGLDELSQEDRLVVSRARKI-ERFLSQ 470
Cdd:PRK04192 426 PAINWLTSYSlylDQVAPwweENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
233-497 |
1.28e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 93.16 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 233 VSVFAGVGERTREGFDLYKEMREAGVIDAQYPPYSQVALVYGQMNEPPGARMRVALTALTISEFFRDeRKQDVLLFVDNI 312
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYDVALMADST 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 313 FRFVQAGSEVSALLGRMPSAVGYQPTLATEMGYLQERI-------TTTKTGSITSIQAIYVPADDLTDPATATTFSHLDA 385
Cdd:PRK14698 763 SRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 386 TTVLSRQLAAKGIYPAIDPLESNSTV-----------LQPEivGEAHYDTAQsvrKILQQYKELQDLIAILGLDELSQED 454
Cdd:PRK14698 843 FWALDADLARRRHFPAINWLTSYSLYvdavkdwwhknVDPE--WKAMRDKAM---ELLQKEAELQEIVRIVGPDALPERE 917
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 301500988 455 RLVVSRARKI-ERFLSQPFYVAEVFTGSPGKYVSLKEAIEGFTE 497
Cdd:PRK14698 918 RAILLVARMLrEDYLQQDAFDEVDTYCPPEKQVTMMRVLLNFYD 961
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
113-473 |
5.29e-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: 86.70 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 113 SPVGECTLGRIINVLGLPTDRLGPVwrfLLEKSDVKEGSnplqnlsqklelyerrPIHSTAPTLADlvvepSVLETGIKV 192
Cdd:TIGR01040 76 TPVSEDMLGRVFNGSGKPIDKGPPV---LAEDYLDINGQ----------------PINPYARIYPE-----EMIQTGISA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 193 LDLLTPYRRGGKVGLFGGAGVGKTvlimELINNIAKFHGGVS----------------VFA--GVGERTREGFDlyKEMR 254
Cdd:TIGR01040 132 IDVMNSIARGQKIPIFSAAGLPHN----EIAAQICRQAGLVKlptkdvhdghednfaiVFAamGVNMETARFFK--QDFE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 255 EAGVIDaqyppysQVALVYGQMNEPPGARMRVALTALTISEFFRDERKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVG 334
Cdd:TIGR01040 206 ENGSME-------RVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 335 YQPTLATEMGYLQERI--TTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTVL 412
Cdd:TIGR01040 279 FPGYMYTDLATIYERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 301500988 413 QPEIvGEA-----HYDTAQSVRKILQQYKELQDLIAILGLDELSQEDRLVVSRARKIER-FLSQPFY 473
Cdd:TIGR01040 359 KSAI-GEGmtrkdHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQGPY 424
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
421-490 |
1.09e-17 |
|
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: 77.48 E-value: 1.09e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 421 HYDTAQSVRKILQQYKELQDLIAILGLDELSQEDRLVVSRARKIERFLSQPFYVAEVFTGSPGKYVSLKE 490
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
114-411 |
1.76e-14 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 73.75 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 114 PVGECTLGRIINVLGLPTDRLGPVwrflleksdvkegsnplqnlsqklELYERRPIHSTAPTLADL--VVEPsvLETGIK 191
Cdd:cd01132 5 PVGEALLGRVVDALGNPIDGKGPI------------------------QTKERRRVESKAPGIIPRqsVNEP--LQTGIK 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 192 VLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNiAKFHGGVSVFAGVGERTREGFDLYKEMREAGVIDaqyppYSQVal 271
Cdd:cd01132 59 AIDSLIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAME-----YTIV-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 272 VYGQMNEPPGARMRVALTALTISEFFRDeRKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAVGYqPtlaTEMGYLQERI- 350
Cdd:cd01132 131 VAATASDPAPLQYLAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY-P---GDVFYLHSRLl 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 301500988 351 -------TTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAIDPLESNSTV 411
Cdd:cd01132 206 eraaklsDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
18-111 |
8.72e-14 |
|
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-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 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.
Pssm-ID: 349739 [Multi-domain] Cd Length: 76 Bit Score: 66.39 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 18 QGRVVQVVGPVIDVGFlpPKKNIPKVNETLLVCRvrpatswnvligrqclpPGKVALACEVQCLLGNYKVRSVGMGDSQG 97
Cdd:cd18115 2 TGKIVQVIGPVVDVEF--PEGELPPIYNALEVKG-----------------DDGKKLVLEVQQHLGENTVRAIAMDSTDG 62
|
90
....*....|....
gi 301500988 98 IRRGARVLSTTAPI 111
Cdd:cd18115 63 LVRGMEVIDTGAPI 76
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
84-202 |
1.93e-10 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 63.16 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 84 NYKVRSVG---MGDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRLGPVwrflleKSDvkegsnplqnlsqk 160
Cdd:PRK09281 65 NLEEDNVGaviLGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPI------EAT-------------- 124
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 301500988 161 lelyERRPIHSTAPTLADL--VVEPsvLETGIKVLDLLTPYRRG 202
Cdd:PRK09281 125 ----ETRPVERKAPGVIDRksVHEP--LQTGIKAIDAMIPIGRG 162
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
82-403 |
4.23e-08 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 55.74 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 82 LGNYKVRSVGMGDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDrlgpvwrfllEKSDVKEGsnplqnlsqkl 161
Cdd:CHL00059 45 LESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPID----------GKGEISAS----------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 162 elyERRPIHSTAPTLADL--VVEPsvLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNiAKFHGGVSVFAGV 239
Cdd:CHL00059 104 ---ESRLIESPAPGIISRrsVYEP--LQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 240 GERTREGFDLYKEMREAGVIDaqyppYSQValVYGQMNEPPGARMRVALTALTISEFFRdERKQDVLLFVDNIFRFVQAG 319
Cdd:CHL00059 178 GQKASSVAQVVTTLQERGAME-----YTIV--VAETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 320 SEVSALLGRMPSAVGYqptlATEMGYLQERI--------TTTKTGSITSIQAIYVPADDLTDPATATTFSHLDATTVLSR 391
Cdd:CHL00059 250 RQMSLLLRRPPGREAY----PGDVFYLHSRLleraaklsSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSA 325
|
330
....*....|..
gi 301500988 392 QLAAKGIYPAID 403
Cdd:CHL00059 326 DLFNAGIRPAIN 337
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
93-374 |
1.11e-07 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 54.27 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 93 GDSQGIRRGARVLSTTAPIYSPVGECTLGRIINVLGLPTDRlGPVwrflLEKSDVKEGS---NPLqnlsqklelyeRRPI 169
Cdd:PRK02118 56 GGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPE----LEGEPIEIGGpsvNPV-----------KRIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 170 HStaptladlvvepSVLETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMelinNIA-KFHGGVSVFAGVGERtregFD 248
Cdd:PRK02118 120 PR------------EMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA----RIAlQAEADIIILGGMGLT----FD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 249 LY----KEMREAGVIDaqyppysQVALVYGQMNEPPGARMRVALTALTISEFFRDERKQDVLLFVDNIFRFVQAGSEVSA 324
Cdd:PRK02118 180 DYlffkDTFENAGALD-------RTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISI 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 301500988 325 LLGRMPSAVGYQPTLATEMGYLQER-ITTTKTGSITSIQAIYVPADDLTDP 374
Cdd:PRK02118 253 TMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDDVTHP 303
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
191-446 |
4.57e-06 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 48.36 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 191 KVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAKFHGGVSVFAG-VGERTREGFDlykeMREAgvIDAQyppysqv 269
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRS--VKGE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 270 aLVYGQMNEPPGARMRVAltALTISEFFRD-ERKQDVLLFVDNIFRFVQAGSEVSALLGRMPSAvGYQPTLAtemgYLQE 348
Cdd:cd01128 72 -VVASTFDEPPERHVQVA--EMVIEKAKRLvEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDANAL----HKPK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 349 RITTT-----KTGSITSIqaiyvpaddltdpATA--TTFSHLD------------ATTVLSRQLAAKGIYPAIDPLESnS 409
Cdd:cd01128 144 RFFGAarnieEGGSLTII-------------ATAlvDTGSRMDevifeefkgtgnMELVLDRKLAEKRIFPAIDILKS-G 209
|
250 260 270
....*....|....*....|....*....|....*..
gi 301500988 410 TVLQPEIVGEAHYDTAQSVRKILQQYKELQDLIAILG 446
Cdd:cd01128 210 TRKEELLLTPEELQKIWLLRRILSPMDPIEAMEFLLK 246
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
201-329 |
3.76e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 201 RGGKVGLFGGAGVGKTVLIMELINNIAKFHGGVSVFAGVGERTREGFDLYKEMreagvIDAQYPPYSQvalvygqmnepp 280
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII-----VGGKKASGSG------------ 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 301500988 281 GARMRVALTALtiseffrdERKQDVLLFVDNIFRFVQAGSEVSALLGRM 329
Cdd:smart00382 64 ELRLRLALALA--------RKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| ATP-synt_V_A-type_beta_C |
cd18112 |
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ... |
436-473 |
5.93e-05 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes 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. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 42.04 E-value: 5.93e-05
10 20 30
....*....|....*....|....*....|....*....
gi 301500988 436 KELQDLIAILGLDELSQEDRLVVSRARKIE-RFLSQPFY 473
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQGFY 60
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
21-107 |
1.71e-04 |
|
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: 39.84 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 21 VVQVVGPVIDVGFLPPKknIPKVNETLLVCRVRPATswnvligrqclppgkvaLACEVQCLLGNYKVRSVGMGDSQGIRR 100
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGR--LPGLLNALEVELVEFGS-----------------LVLGEVLNLGGDKVRVQVFGGTSGLSR 61
|
....*..
gi 301500988 101 GARVLST 107
Cdd:pfam02874 62 GDEVKRT 68
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
186-471 |
1.96e-04 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 44.19 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 186 LETGIKVLDLLTPYRRGGKVGLFGGAGVGKTVLIMELINNIAKfhGGVS-VFAGVGERTREGFDLYKEMREAG------V 258
Cdd:PRK07165 127 LYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKN--TNVKcIYVAIGQKRENLSRIYETLKEHDalkntiI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 259 IDA-QYPPYSQVALVYgqmneppgarmrVALT-ALTISEFfrderkQDVLLFVD------NIFRfvqagsEVSALLGR-- 328
Cdd:PRK07165 205 IDApSTSPYEQYLAPY------------VAMAhAENISYN------DDVLIVFDdltkhaNIYR------EIALLTNKpv 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500988 329 ----MPSAVGYQPTlatemgYLQERITTTKTG-SITSIQAIYVPADDLTDPATATTFSHLDATTVLSRQLAAKGIYPAID 403
Cdd:PRK07165 261 gkeaFPGDMFFAHS------KLLERAGKFKNRkTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAID 334
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301500988 404 PLESNS---TVLQPEIVGeahyDTAQSVRKILQQYKELQDLIAilgLD-ELSQEDRLVVSRARKIERFLSQP 471
Cdd:PRK07165 335 IDLSVSrtgSSVQSKTIT----KVAGEISKIYRAYKRQLKLSM---LDyDLNKETSDLLFKGKMIEKMFNQK 399
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
417-471 |
1.82e-03 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 37.03 E-value: 1.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301500988 417 VGEAHYDTAQSVRKILQQYKELQDLIAIlG---------LDElsqedrlVVSRARKIERFLSQP 471
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
|
|
| |
