|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-422 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 973.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 1 AFSPGEMPNIYNSLVVKGQNPAGQQINVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNV 80
Cdd:CHL00060 30 AFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 81 LGEPVDNLGPVRSNAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAH 160
Cdd:CHL00060 110 LGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 161 GGVSVSGGVGERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVYKQDVLLFID 240
Cdd:CHL00060 190 GGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFID 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 241 NIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLS 320
Cdd:CHL00060 270 NIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 321 RGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQ 400
Cdd:CHL00060 350 RGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQ 429
|
410 420
....*....|....*....|..
gi 42558334 401 PFFVAEVFTGSPGKYVSLLETI 422
Cdd:CHL00060 430 PFFVAEVFTGSPGKYVGLAETI 451
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
2-422 |
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: 834.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 2 FSPGEMPNIYNSLVVKGQNPagqqINVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVL 81
Cdd:COG0055 20 FPEGELPAIYNALEVENEGG----GELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 82 GEPVDNLGPVRSNAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAHG 161
Cdd:COG0055 96 GEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 162 GVSVSGGVGERTREGNDLYMEMKESKVINeqnisesKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVYKQDVLLFIDN 241
Cdd:COG0055 176 GVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 242 IFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSR 321
Cdd:COG0055 249 IFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 322 GLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQP 401
Cdd:COG0055 329 KIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQP 408
|
410 420
....*....|....*....|.
gi 42558334 402 FFVAEVFTGSPGKYVSLLETI 422
Cdd:COG0055 409 FFVAEQFTGIPGKYVPLEDTI 429
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-422 |
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: 744.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 2 FSPGEMPNIYNSLVVKGqnpaGQQINVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVL 81
Cdd:TIGR01039 17 FEQGELPRIYNALKVQN----RAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 82 GEPVDNLGPVRSNAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAHG 161
Cdd:TIGR01039 93 GEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 162 GVSVSGGVGERTREGNDLYMEMKESKVINeqnisesKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVYKQDVLLFIDN 241
Cdd:TIGR01039 173 GYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 242 IFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSR 321
Cdd:TIGR01039 246 IFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 322 GLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQP 401
Cdd:TIGR01039 326 KIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQP 405
|
410 420
....*....|....*....|.
gi 42558334 402 FFVAEVFTGSPGKYVSLLETI 422
Cdd:TIGR01039 406 FFVAEVFTGQPGKYVPLKDTI 426
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
66-344 |
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: 558.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 66 SVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 145
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 146 TVPITESINNIAKAHGGVSVSGGVGERTREGNDLYMEMKESKVINEqnISESKVALVYGQMNEPPGARMRVGSTALTMAE 225
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL--DGLSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 226 YFRDVYKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPA 305
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 42558334 306 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 344
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-422 |
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: 540.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 4 PGEMPNIYNSLVvkgqnpAGQQINVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGE 83
Cdd:TIGR03305 16 DGELPAIHSVLR------AGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 84 PVDNLGPVRSNAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAHGGV 163
Cdd:TIGR03305 90 TIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 164 SVSGGVGERTREGNDLYMEMKESKVINEqniseskVALVYGQMNEPPGARMRVGSTALTMAEYFRDVYKQDVLLFIDNIF 243
Cdd:TIGR03305 170 SIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 244 RFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 323
Cdd:TIGR03305 243 RFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLSRKR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 324 AAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFF 403
Cdd:TIGR03305 323 ASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQPFF 402
|
410
....*....|....*....
gi 42558334 404 VAEVFTGSPGKYVSLLETI 422
Cdd:TIGR03305 403 TTEQFTGMKGKTVSLEDAL 421
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
66-341 |
5.93e-126 |
|
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: 365.24 E-value: 5.93e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 66 SVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 145
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 146 TVPITESINNIAKAHGGVSVSGGVGERTREGNDLYMEMKESKVineqnisESKVALVYGQMNEPPGARMRVGSTALTMAE 225
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 226 YFRDVyKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTK--EGSITFIQAVYVPADDLTD 303
Cdd:cd19476 154 YFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 42558334 304 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 341
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
119-339 |
8.69e-82 |
|
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: 250.35 E-value: 8.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 119 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVpiteSINNIAK-AHGGVSVSGGVGERTREGNDLYMEMKESKVIneqniseS 197
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTV----LAGMIARqASADVVVYALIGERGREVREFIEELLGSGAL-------K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 198 KVALVYGQMNEPPGARMRVGSTALTMAEYFRDvYKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQ 277
Cdd:pfam00006 70 RTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558334 278 ERITSTKE--GSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:pfam00006 149 ERAGRVKGkgGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
346-422 |
1.32e-56 |
|
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: 181.52 E-value: 1.32e-56
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42558334 346 IVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLLETI 422
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTI 77
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-401 |
1.51e-54 |
|
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: 186.78 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 28 VTCEVqqlLGNNEVRAVAM--SATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPA 105
Cdd:COG1157 54 VLAEV---VGFRGDRVLLMplGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 106 FTQ---LDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV---PITES----INNIAkahggvsvsgGVGERTRE 175
Cdd:COG1157 131 PLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTllgMIARNteadVNVIA----------LIGERGRE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 176 GNDlYMEmkesKVINEQNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDvykQ--DVLLFIDNIFRFVQAGSEVS 253
Cdd:COG1157 198 VRE-FIE----DDLGEEGLARSVV--VVATSDEPPLMRLRAAYTATAIAEYFRD---QgkNVLLLMDSLTRFAMAQREIG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 254 ALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 333
Cdd:COG1157 268 LAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAID 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42558334 334 PLDSTS-TMlqPWIVGEEHYETAQGVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 401
Cdd:COG1157 348 VLASISrVM--PDIVSPEHRALARRLRRLLARYEENEDLIRI-GayqpgsdpeLDE-------AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
66-339 |
3.47e-48 |
|
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: 165.43 E-value: 3.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 66 SVPVGETTLGRIFNVLGEPVDNLG--------PVRSNAISPIHRsaPAFTQldtklsIFETGIKVVDLLAPYRRGGKIGL 137
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGlpdeperrPLIAAPPNPLKR--APIEQ------PLPTGVRAIDGLLTCGEGQRIGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 138 FGGAGVGKTV---PITES----INNIAkahggvsvsgGVGERTREGNDlYMEmkesKVINEQNISESkvALVYGQMNEPP 210
Cdd:cd01136 73 FAGSGVGKSTllgMIARNtdadVNVIA----------LIGERGREVRE-FIE----KDLGEEGLKRS--VLVVATSDESP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 211 GARMRVGSTALTMAEYFRDVYKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITF 290
Cdd:cd01136 136 LLRVRAAYTATAIAEYFRDQGK-KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITA 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 42558334 291 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:cd01136 215 FYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
39-400 |
2.56e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 159.98 E-value: 2.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 39 NEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPV----RSN---AISPIHRSApaftqLDT 111
Cdd:PRK06820 71 EMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLtgqwRELdcpPPSPLTRQP-----IEQ 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 112 KLSifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTvpiteSINNIAKAHGGVSVSGGVG--ERTREGNDLYmemkeskvi 189
Cdd:PRK06820 146 MLT---TGIRAIDGILSCGEGQRIGIFAAAGVGKS-----TLLGMLCADSAADVMVLALigERGREVREFL--------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 190 nEQNISE---SKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVYKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQ 266
Cdd:PRK06820 209 -EQVLTPearARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGK-KVLLMADSLTRYARAAREIGLAAGEPPAAGSFP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 267 PTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWI 346
Cdd:PRK06820 287 PSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQI 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 42558334 347 VGEEHYETAQGVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 400
Cdd:PRK06820 366 VSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
30-402 |
1.06e-43 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 157.85 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 30 CEVQQLLGNNEVRAVA--------------MSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLG-PVRSN 94
Cdd:PRK08149 31 CEIRAGWHSNEVIARAqvvgfqrertilslIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDaPPTVG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 95 AIS---PIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNiakAHGGVSVSGGVGE 171
Cdd:PRK08149 111 PISeerVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 172 RTREGNDLYMEMKESKvineqniSESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVYKqDVLLFIDNIFRFVQAGSE 251
Cdd:PRK08149 188 RGREVTEFVESLRASS-------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGK-RVVLFIDSMTRYARALRD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 252 VSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPA 331
Cdd:PRK08149 260 VALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPA 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558334 332 VDPLDSTSTMLQPwIVGEEHYETAQGVKQTLQRYKELQDIIAiLG---LDELSEEDRlTVARARKIERFLSQPF 402
Cdd:PRK08149 340 IDVLKSVSRVFGQ-VTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDV 410
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
61-400 |
1.91e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 154.91 E-value: 1.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 61 TGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPAFTQ---LDTKLSifeTGIKVVDLLAPYRRGGKIGL 137
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 138 FGGAGVGKTVPITESINNiakAHGGVSVSGGVGERTREgndlYMEMKESKVINEqniSESKVALVYGQMNEPPGARMRVG 217
Cdd:PRK06936 168 FAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESDLGEE---GLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 218 STALTMAEYFRDVYKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVP 297
Cdd:PRK06936 238 FVATSIAEYFRDQGKR-VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 298 ADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGEEHYETAQGVKQTLQRYKELQDIIAI--- 374
Cdd:PRK06936 317 GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEEVELLLQIgey 395
|
330 340
....*....|....*....|....*..
gi 42558334 375 -LGLDELSEEdrlTVARARKIERFLSQ 400
Cdd:PRK06936 396 qKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
30-401 |
1.53e-39 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 146.84 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 30 CEVQQ----LLGNNEV----RAVAM----SATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAIS 97
Cdd:PRK09099 49 CELRQrdgtLLQRAEVvgfsRDVALlspfGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 98 PIHRSAPAFTQ---LDTKLSifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPI------TE-SINNIAkahggvsvsg 167
Cdd:PRK09099 129 PVIAAPPDPMSrrmVEAPLP---TGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMgmfargTQcDVNVIA---------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 168 GVGERTREGNDlYMEMkeskVINEQNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDVYKQdVLLFIDNIFRFVQ 247
Cdd:PRK09099 196 LIGERGREVRE-FIEL----ILGEDGMARSVV--VCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFAR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 248 AGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKG 327
Cdd:PRK09099 268 AQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARN 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42558334 328 IYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQP 401
Cdd:PRK09099 348 QYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
48-400 |
1.66e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 147.18 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 48 ATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNA--------ISPIHRsAPAFTQLDTklsifetG 119
Cdd:PRK05688 84 SVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDwvpmdgptINPLNR-HPISEPLDV-------G 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 120 IKVVDLLAPYRRGGKIGLFGGAGVGKTVPI------TESinniakahgGVSVSGGVGERTREgndlymeMKE--SKVINE 191
Cdd:PRK05688 156 IRSINGLLTVGRGQRLGLFAGTGVGKSVLLgmmtrfTEA---------DIIVVGLIGERGRE-------VKEfiEHILGE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 192 QNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDVYKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGT 271
Cdd:PRK05688 220 EGLKRSVV--VASPADDAPLMRLRAAMYCTRIAEYFRDKGK-NVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 272 EMGLLQERITSTKEG--SITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGE 349
Cdd:PRK05688 297 KLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDP 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 42558334 350 EHYETAQGVKQTLQRYKELQDIIAI----LGLDelsEEDRLTVARARKIERFLSQ 400
Cdd:PRK05688 376 EHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
67-374 |
1.91e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 146.77 E-value: 1.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 67 VPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHrsAPAFTQLDTKlSIFE---TGIKVVDLLAPYRRGGKIGLFGGAGV 143
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAMLTVGKGQRMGLFAGSGV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 144 GKTVPI-------TESInniakahggvSVSGGVGERTREgndlymeMKE--SKVINEQNISESKValVYGQMNEPPGARM 214
Cdd:PRK08972 174 GKSVLLgmmtrgtTADV----------IVVGLVGERGRE-------VKEfiEEILGEEGRARSVV--VAAPADTSPLMRL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 215 RVGSTALTMAEYFRDVyKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERIT--STKEGSITFIQ 292
Cdd:PRK08972 235 KGCETATTIAEYFRDQ-GLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSITAFY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 293 AVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTLQRYKELQDII 372
Cdd:PRK08972 314 TVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLI 392
|
..
gi 42558334 373 AI 374
Cdd:PRK08972 393 SI 394
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
27-400 |
3.74e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 145.89 E-value: 3.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 27 NVTCEVQQLLGNNEVrAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFN----VLGEPVDN--LGPVRSNAiSPIH 100
Cdd:PRK06793 52 NVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENipLQKIKLDA-PPIH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 101 rsapAFTQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVpiteSINNIAK-AHGGVSVSGGVGERTREGNDL 179
Cdd:PRK06793 130 ----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST----LLGMIAKnAKADINVISLVGERGREVKDF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 180 YmemkeSKVINEQNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDvYKQDVLLFIDNIFRFVQAGSEVSALLGRM 259
Cdd:PRK06793 201 I-----RKELGEEGMRKSVV--VVATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKEL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 260 PSAvGYQPTLGTEMGLLQERITSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:PRK06793 273 PIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVS 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558334 340 TMLQPwIVGEEHYETAQGVKQTLQRYKElQDIIAILGLDELSEEDRLTVARARKIE---RFLSQ 400
Cdd:PRK06793 352 RIMEE-IVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
65-400 |
5.59e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 142.52 E-value: 5.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 65 LSVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 144
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 145 KTVPITESINNiAKAhgGVSVSGGVGERTRE---------GNDLymemkESKVINEQNISESKVALVYGQMneppgarmr 215
Cdd:PRK08472 170 KSTLMGMIVKG-CLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYGAF--------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 216 vgsTALTMAEYFRDVYKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTK-EGSITFIQAV 294
Cdd:PRK08472 233 ---CAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 295 YVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGEEHYETAQGVKQTLQRYKELQDIIAI 374
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350
....*....|....*....|....*....|.
gi 42558334 375 ----LGLD-ELSEedrlTVARARKIERFLSQ 400
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
75-376 |
7.34e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 142.44 E-value: 7.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 75 GRIFNVLGEPVDNLGPVRSNAIS-PIHRSAPAF---TQLDTKlsiFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPIT 150
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAmtrARVETG---LRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 151 EsinnIAKA-HGGVSVSGGVGERTREgndlYMEMKESKVINeqniSESKVALVYGQMNEPPGARMRVGSTALTMAEYFRD 229
Cdd:PRK06002 184 M----LARAdAFDTVVIALVGERGRE----VREFLEDTLAD----NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 230 VyKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKE--GSITFIQAVYVPADDLTDPAPA 307
Cdd:PRK06002 252 R-GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVAD 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 308 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ-PWIVGEEhyETAQGVKQTLQRYKELQDIIAILG 376
Cdd:PRK06002 331 SIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARhAWTPEQR--KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
61-374 |
2.38e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 141.01 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 61 TGAPLSVPVGETTLGRIFNVLGEPVDN------LGPVRSNAISPIHRSAPAFTQldtklsIFETGIKVVDLLAPYRRGGK 134
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGsalpkgLAPVSTDQDPPNPLKRPPIRE------PMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 135 IGLFGGAGVGKTVPI------TES-INNIAkahggvsvsgGVGERTREGNDlYMEmkesKVINEQNISESKValVYGQMN 207
Cdd:PRK07721 161 VGIFAGSGVGKSTLMgmiarnTSAdLNVIA----------LIGERGREVRE-FIE----RDLGPEGLKRSIV--VVATSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 208 EPPGARMRVGSTALTMAEYFRDvYKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKEGS 287
Cdd:PRK07721 224 QPALMRIKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 288 ITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTLQRYKE 367
Cdd:PRK07721 303 ITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQN 381
|
....*..
gi 42558334 368 LQDIIAI 374
Cdd:PRK07721 382 SEDLINI 388
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
28-400 |
2.81e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 140.88 E-value: 2.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 28 VTCEVqqlLGNNEVRAVAM--SATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAIS-PIHRSAP 104
Cdd:PRK08927 54 VPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPyPLRAPPP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 105 ---AFTQLDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAhggVSVSGGVGERTRE-----G 176
Cdd:PRK08927 131 pahSRARVGEPL---DLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 177 NDLYME-MKESKVIneqniseskVAlvygQMNEPPGARMRVGSTALTMAEYFRDvYKQDVLLFIDNIFRFVQAGSEVSAL 255
Cdd:PRK08927 205 DDLGPEgLARSVVV---------VA----TSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 256 LGRMPSAVGYQPTLGTEMGLLQERI--TSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 333
Cdd:PRK08927 271 AGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAIN 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42558334 334 PLDSTS-TMlqPWIVGEEHYETAQGVKQTLQRYKELQDIIAI----LGLDelSEEDRlTVARARKIERFLSQ 400
Cdd:PRK08927 351 VLKSVSrTM--PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSD--PEVDE-AIRLNPALEAFLRQ 417
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
47-374 |
9.11e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 128.15 E-value: 9.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 47 SATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNL----GPVRS-NAISPihrsaPAFTQLDTKLSIFeTGIK 121
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDyDAMPP-----PAMVRQPITQPLM-TGIR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 122 VVDLLAPYRRGGKIGLFGGAGVGKTVpITESINNIAKAHGGVSVSGGvgERTREgndlYMEMKESKVINEqniSESKVAL 201
Cdd:PRK07594 145 AIDSVATCGEGQRVGIFSAPGVGKST-LLAMLCNAPDADSNVLVLIG--ERGRE----VREFIDFTLSEE---TRKRCVI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 202 VYGQMNEPPGARMRVGSTALTMAEYFRDVYKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERIT 281
Cdd:PRK07594 215 VVATSDRPALERVRALFVATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 282 STKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQT 361
Cdd:PRK07594 294 MGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRC 372
|
330
....*....|...
gi 42558334 362 LQRYKELQDIIAI 374
Cdd:PRK07594 373 LALYQEVELLIRI 385
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
69-400 |
1.07e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 128.08 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 69 VGETTLGRIFNVLGEPVDNLGPVRSNAI-----SPIH--RSAPAFTQLDTklsifetGIKVVDLLAPYRRGGKIGLFGGA 141
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPlqqqlPQIHplQRRAVDTPLDV-------GVNAINGLLTIGKGQRVGLMAGS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 142 GVGKTVpITESINNIAKAHGGVSVSGGvgERTREgndlymeMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTAL 221
Cdd:PRK07196 165 GVGKSV-LLGMITRYTQADVVVVGLIG--ERGRE-------VKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCH 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 222 TMAEYFRDVyKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERI-TSTKEGSITFIQAVYVPADD 300
Cdd:PRK07196 235 AIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 301 LTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMLQpwIVGEEHYETAQGVKQTLQRYKELQDIIA----IL 375
Cdd:PRK07196 314 QQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISrCMSQ--VIGSQQAKAASLLKQCYADYMAIKPLIPlggyVA 391
|
330 340
....*....|....*....|....*
gi 42558334 376 GLDELSEEdrlTVARARKIERFLSQ 400
Cdd:PRK07196 392 GADPMADQ---AVHYYPAITQFLRQ 413
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
54-403 |
2.38e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 118.73 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 54 RGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNL--------GPVRSNAISPIHRSAPAftqldtklSIFETGIKVVDL 125
Cdd:PRK07960 97 RNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLpapdtgetGALITPPFNPLQRTPIE--------HVLDTGVRAINA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 126 LAPYRRGGKIGLFGGAGVGKTVpiteSINNIAK-AHGGVSVSGGVGERTREGNDlYMEmkesKVINEQNISESKValVYG 204
Cdd:PRK07960 169 LLTVGRGQRMGLFAGSGVGKSV----LLGMMARyTQADVIVVGLIGERGREVKD-FIE----NILGAEGRARSVV--IAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 205 QMNEPPGARMRVGSTALTMAEYFRDvYKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITS-- 282
Cdd:PRK07960 238 PADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgi 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 283 TKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGEEHYETAQGVKQTL 362
Cdd:PRK07960 317 SGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTA-LIDEQHYARVRQFKQLL 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 42558334 363 QRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQPFF 403
Cdd:PRK07960 396 SSFQRNRDLVSVgayaKGSDPMLDK---AIALWPQLEAFLQQGIF 437
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
49-402 |
1.00e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 114.15 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 49 TDGL-TRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRS--------NAISPIHRSAPA-FTQldtklsifeT 118
Cdd:PRK04196 59 TTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPekrldingAPINPVAREYPEeFIQ---------T 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 119 GIKVVDLLAPYRRGGKIGLFGGAGVgktvpitesinniakAHggvsvsggvgertregNDLYMEM-KESKVINEqnisES 197
Cdd:PRK04196 130 GISAIDGLNTLVRGQKLPIFSGSGL---------------PH----------------NELAAQIaRQAKVLGE----EE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 198 KVALVYGQM------------------------------NEPPGARMRVGSTALTMAEYFrdVYKQD--VLLFIDNIFRF 245
Cdd:PRK04196 175 NFAVVFAAMgitfeeanffmedfeetgalersvvflnlaDDPAIERILTPRMALTAAEYL--AFEKGmhVLVILTDMTNY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 246 VQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQER--ITSTKEGSITFIQAVYVPADDLTDPAPattfahlDAT------- 316
Cdd:PRK04196 253 CEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegq 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 317 TVLSRGLAAKGIYPAVDPLDSTSTMLQPWIvGEEHY-ETAQGVKQTL----QRYKELQDIIAILGLDELSEEDRLTVARA 391
Cdd:PRK04196 326 IVLSRELHRKGIYPPIDVLPSLSRLMKDGI-GEGKTrEDHKDVANQLyaayARGKDLRELAAIVGEEALSERDRKYLKFA 404
|
410
....*....|..
gi 42558334 392 RKIE-RFLSQPF 402
Cdd:PRK04196 405 DAFErEFVNQGF 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
64-343 |
3.22e-26 |
|
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: 106.92 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 64 PLSVPVGETTLGRIFNVLGEPVDNLGPVRS--------NAISPIHRSAPAftqldtklSIFETGIKVVDLLAPYRRGGKI 135
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPedyldingPPINPVARIYPE--------EMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 136 GLFGGAGvgktVPITESINNIAKahggvsvsgGVGERTREGNDL---------YMEMKESKVINEQNISESKVALVYGQM 206
Cdd:cd01135 73 PIFSGSG----LPHNELAAQIAR---------QAGVVGSEENFAivfaamgvtMEEARFFKDDFEETGALERVVLFLNLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 207 NEPPGARMRVGSTALTMAEYFRDVYKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQER--ITSTK 284
Cdd:cd01135 140 NDPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGR 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 42558334 285 EGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 343
Cdd:cd01135 220 KGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
38-402 |
1.51e-24 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 104.99 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 38 NNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPAFTQLDTKLSIFE 117
Cdd:PRK05922 63 NRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 118 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPIT-------ESINNIAkahggvsvsgGVGERTREGNDlYMEMKESkvin 190
Cdd:PRK05922 143 TGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLStiakgskSTINVIA----------LIGERGREVRE-YIEQHKE---- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 191 eqNISESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDvYKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLG 270
Cdd:PRK05922 208 --GLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 271 TEMGLLQERITSTKEGSITFIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQPWIV 347
Cdd:PRK05922 285 HHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSARQLAL 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 42558334 348 gEEHYETAQGVKQTLQRYKELQDIIAiLGLDELSEEDRLTvaRARK----IERFLSQPF 402
Cdd:PRK05922 360 -PHHYAAAEELRSLLKAYHEALDIIQ-LGAYVPGQDAHLD--RAVKllpsIKQFLSQPL 414
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
1-65 |
4.01e-24 |
|
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: 94.89 E-value: 4.01e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42558334 1 AFSPGEMPNIYNSLVVKGQNPagqqINVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPL 65
Cdd:cd18115 16 EFPEGELPPIYNALEVKGDDG----KKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
61-400 |
1.86e-22 |
|
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: 99.03 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 61 TGAPLSVPVGETTLGRIFNVLGEPVDNLGPV--------RSNAISPIHRSAPAftqldtklSIFETGIKVVDLLAPYRRG 132
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedyldiNGQPINPYARIYPE--------EMIQTGISAIDVMNSIARG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 133 GKIGLFGGAGvgktVPITESINNIAKAHGGVSVSGGVGERTREGN------DLYMEMKESKVIN---EQNISESKVALVY 203
Cdd:TIGR01040 142 QKIPIFSAAG----LPHNEIAAQICRQAGLVKLPTKDVHDGHEDNfaivfaAMGVNMETARFFKqdfEENGSMERVCLFL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 204 GQMNEPPGARMRVGSTALTMAEYFRDVYKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERI--T 281
Cdd:TIGR01040 218 NLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 282 STKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIvGE-----EHYETAQ 356
Cdd:TIGR01040 298 EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSN 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 42558334 357 GVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 400
Cdd:TIGR01040 377 QLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
219-400 |
2.54e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 99.09 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 219 TALTMAEYFRDV-YkqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQER----IT-STKEGSITFIQ 292
Cdd:PRK04192 311 TGITIAEYYRDMgY--DVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTIIG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 293 AVYVPADDLTDPapaTTFAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQPWI---VGEEHYETAQGVKQTLQ 363
Cdd:PRK04192 389 AVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPWWeenVDPDWRELRDEAMDLLQ 465
|
170 180 190
....*....|....*....|....*....|....*...
gi 42558334 364 RYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 400
Cdd:PRK04192 466 REAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
64-339 |
1.44e-21 |
|
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: 93.79 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 64 PLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAIS--------PIHRSAPAFTQLDTKLsIFETGIKVVDLLAPYRRGGKI 135
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGSIFIPrgvnvqrwPVRQPRPVKEKLPPNV-PLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 136 GLFGGAGVGKTVpITESinnIAK-AHGGVSVSGGVGERTREGNDLYMEMKESKV-INEQNISEsKVALVYGQMNEPPGAR 213
Cdd:cd01134 80 AIPGPFGCGKTV-ISQS---LSKwSNSDVVIYVGCGERGNEMAEVLEEFPELKDpITGESLME-RTVLIANTSNMPVAAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 214 MRVGSTALTMAEYFRDVYKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERI-------TSTKEG 286
Cdd:cd01134 155 EASIYTGITIAEYFRDMGY-NVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 42558334 287 SITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:cd01134 234 SVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
36-339 |
2.12e-21 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 96.14 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 36 LGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPAFTQLDTKLSI 115
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 116 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNiakahggvsvsggvgertREGNDLY-----MEMKESKVIN 190
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 191 ------EQNISESKVaLVYGQMNEPPGARMRVGSTALTMAEYFRDvYKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG 264
Cdd:PRK13343 208 vietlrEHGALEYTT-VVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 265 YqPtlGTEMGL---LQERITSTKE----GSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDS 337
Cdd:PRK13343 286 Y-P--GDIFYLhsrLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLS 362
|
..
gi 42558334 338 TS 339
Cdd:PRK13343 363 VS 364
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
351-420 |
9.53e-20 |
|
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: 82.88 E-value: 9.53e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 351 HYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLLE 420
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
171-422 |
6.94e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 89.31 E-value: 6.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 171 ERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVyKQDVLLFIDNIFRFVQAGS 250
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 251 EVSALLGRMPSAVGYQPTLGTEMGLLQERI-------TSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 323
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 324 AAKGIYPAVDPLDSTS---TMLQPWI---VGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ER 396
Cdd:PRK14698 851 ARRRHFPAINWLTSYSlyvDAVKDWWhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250 260
....*....|....*....|....*.
gi 42558334 397 FLSQPFFVAEVFTGSPGKYVSLLETI 422
Cdd:PRK14698 931 YLQQDAFDEVDTYCPPEKQVTMMRVL 956
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
65-339 |
7.51e-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: 71.44 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 65 LSVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 144
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 145 KTVPITESINNiakahggvsvsggvgertREGNDLY-----MEMKESKVINEQNISESKVALVY-----GQMNEPPGARM 214
Cdd:cd01132 82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 215 RVGSTALTMAEYFRDvYKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGYqptlgtemgL---LQERITSTKE 285
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFY---------LhsrLLERAAKLSD 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 42558334 286 ----GSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:cd01132 214 elggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
53-309 |
2.04e-13 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 71.60 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 53 TRGMGAVDT----GAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAIsPIhrSAPAFTQLDTKL--SIFETGIKVVDLL 126
Cdd:PRK02118 58 TRGISTGDEvvflGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEPI-EI--GGPSVNPVKRIVprEMIRTGIPMIDVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 127 APYRRGGKIGLFGGAGvgktVPITESINNIAKAHGGVSVSGGVGERTregNDLYMEMKESKvinEQNISESKVALVYGQM 206
Cdd:PRK02118 135 NTLVESQKIPIFSVSG----EPYNALLARIALQAEADIIILGGMGLT---FDDYLFFKDTF---ENAGALDRTVMFIHTA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 207 NEPPGARMRVGSTALTMAEYFRDVYKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKE- 285
Cdd:PRK02118 205 SDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDg 284
|
250 260
....*....|....*....|....
gi 42558334 286 GSITFIQAVYVPADDLTDPAPATT 309
Cdd:PRK02118 285 GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
39-132 |
5.27e-13 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 70.48 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 39 NEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPAFTQldtKLSIFE- 117
Cdd:PRK09281 69 DNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEp 145
|
90
....*....|....*..
gi 42558334 118 --TGIKVVDLLAPYRRG 132
Cdd:PRK09281 146 lqTGIKAIDAMIPIGRG 162
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
36-333 |
1.58e-09 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 59.59 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 36 LGNNEVRAVAMSatDGLT--RGMGAVDTGAPLSVPVGETTLGRIFNVLGEPVDNLGPVRSNAISPIHRSAPAFTqldTKL 113
Cdd:CHL00059 45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 114 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNiakahggvsvsggvgertREGND---LYMEM--KE 185
Cdd:CHL00059 120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 186 SKVINEQNISESKVALVY-----GQMNEPPGARMRVGSTALTMAEYFrdVYK-QDVLLFIDNIFRFVQAGSEVSALLGRM 259
Cdd:CHL00059 182 SSVAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYF--MYRgRHTLIIYDDLSKQAQAYRQMSLLLRRP 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42558334 260 PSAVGYQPTLGTEMGLLQERI----TSTKEGSITFIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 333
Cdd:CHL00059 260 PGREAYPGDVFYLHSRLLERAaklsSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAIN 337
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
2-62 |
2.09e-09 |
|
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: 53.32 E-value: 2.09e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42558334 2 FSPGEMPNIYNSLVVKGQNpagqQINVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTG 62
Cdd:pfam02874 13 FGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
3-333 |
1.71e-05 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 46.96 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 3 SPGEMPNIYNSLVVKGQNPAGQQINVTCEVQQllgNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRIFNVLG 82
Cdd:PTZ00185 56 APGNPGVAYNTIIMIQVSPTTFAAGLVFNLEK---DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 83 EPV---------------DNLGPVRSNAISPIHRSAPAFTQLdtklsifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 147
Cdd:PTZ00185 133 HEVpvglltrsralleseQTLGKVDAGAPNIVSRSPVNYNLL--------TGFKAVDTMIPIGRGQRELIVGDRQTGKTS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 148 PITESINNIAKAHGGVSVSGGVGErtregndLYMEMKE--SKVINEQNISESKVALVY-----GQMNEPPGARMRVGSTA 220
Cdd:PTZ00185 205 IAVSTIINQVRINQQILSKNAVIS-------IYVSIGQrcSNVARIHRLLRSYGALRYttvmaATAAEPAGLQYLAPYSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558334 221 LTMAEYFRDVYKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGLLQERITSTKE----GSITFIQAVYV 296
Cdd:PTZ00185 278 VTMGEYFMNRGRH-CLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVET 356
|
330 340 350
....*....|....*....|....*....|....*..
gi 42558334 297 PADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 333
Cdd:PTZ00185 357 LSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
|
| 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 ... |
366-400 |
2.29e-04 |
|
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: 40.11 E-value: 2.29e-04
10 20 30
....*....|....*....|....*....|....*.
gi 42558334 366 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 400
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
|
|
| 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 ... |
362-400 |
6.42e-04 |
|
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: 38.91 E-value: 6.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 42558334 362 LQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 400
Cdd:cd18111 12 LQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
347-401 |
8.08e-04 |
|
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: 37.80 E-value: 8.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558334 347 VGEEHYETAQGVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 401
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
|
|
| |
