|
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: 977.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 1 AFSPGEMPNIYNSIVIKGQNPAGQQIDVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNV 80
Cdd:CHL00060 30 AFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 81 LGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITELINNIAKAH 160
Cdd:CHL00060 110 LGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 161 GGVSVSGGVGERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFID 240
Cdd:CHL00060 190 GGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFID 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 241 NIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLS 320
Cdd:CHL00060 270 NIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 321 RGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLTVARARKIERFLSQ 400
Cdd:CHL00060 350 RGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQ 429
|
410 420
....*....|....*....|..
gi 42558436 401 PFFVAEVFTGSPGKYVSLSETI 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: 833.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 2 FSPGEMPNIYNSIVIKGQNPagqqIDVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVL 81
Cdd:COG0055 20 FPEGELPAIYNALEVENEGG----GELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 82 GEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITELINNIAKAHG 161
Cdd:COG0055 96 GEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 162 GVSVSGGVGERTREGNDLYMEMKESKVINeqnisesKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDN 241
Cdd:COG0055 176 GVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 242 IFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSR 321
Cdd:COG0055 249 IFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 322 GLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLTVARARKIERFLSQP 401
Cdd:COG0055 329 KIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQP 408
|
410 420
....*....|....*....|.
gi 42558436 402 FFVAEVFTGSPGKYVSLSETI 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: 741.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 2 FSPGEMPNIYNSIVIKGqnpaGQQIDVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVL 81
Cdd:TIGR01039 17 FEQGELPRIYNALKVQN----RAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 82 GEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITELINNIAKAHG 161
Cdd:TIGR01039 93 GEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 162 GVSVSGGVGERTREGNDLYMEMKESKVINeqnisesKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDN 241
Cdd:TIGR01039 173 GYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 242 IFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSR 321
Cdd:TIGR01039 246 IFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 322 GLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLTVARARKIERFLSQP 401
Cdd:TIGR01039 326 KIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQP 405
|
410 420
....*....|....*....|.
gi 42558436 402 FFVAEVFTGSPGKYVSLSETI 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: 561.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 66 SVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 145
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 146 TVPITELINNIAKAHGGVSVSGGVGERTREGNDLYMEMKESKVINEqnISESKVALVYGQMNEPPGARMRVGSTALTMAE 225
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL--DGLSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 226 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 305
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 42558436 306 PATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 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: 535.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 4 PGEMPNIYNSIVikgqnpAGQQIDVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGE 83
Cdd:TIGR03305 16 DGELPAIHSVLR------AGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 84 PVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITELINNIAKAHGGV 163
Cdd:TIGR03305 90 TIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 164 SVSGGVGERTREGNDLYMEMKESKVINEqniseskVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDNIF 243
Cdd:TIGR03305 170 SIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 244 RFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGL 323
Cdd:TIGR03305 243 RFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLSRKR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 324 AAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLTVARARKIERFLSQPFF 403
Cdd:TIGR03305 323 ASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQPFF 402
|
410
....*....|....*....
gi 42558436 404 VAEVFTGSPGKYVSLSETI 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 |
8.88e-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: 364.47 E-value: 8.88e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 66 SVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 145
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 146 TVPITELINNIAKAHGGVSVSGGVGERTREGNDLYMEMKESKVineqnisESKVALVYGQMNEPPGARMRVGSTALTMAE 225
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 226 YFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTK--EGSITSIQAVYVPADDLTD 303
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 42558436 304 PAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 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 |
7.20e-85 |
|
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: 258.06 E-value: 7.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 119 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVpiteLINNIAK-AHGGVSVSGGVGERTREGNDLYMEMKESKVIneqniseS 197
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTV----LAGMIARqASADVVVYALIGERGREVREFIEELLGSGAL-------K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 198 KVALVYGQMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQ 277
Cdd:pfam00006 70 RTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558436 278 ERITSTKE--GSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:pfam00006 149 ERAGRVKGkgGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-401 |
2.98e-59 |
|
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: 199.10 E-value: 2.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 28 VTCEVqqlLGNNEVRAVAM--SATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPA 105
Cdd:COG1157 54 VLAEV---VGFRGDRVLLMplGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 106 FTQ---LDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVpiteLINNIAKAhggvsvsggVG----------ER 172
Cdd:COG1157 131 PLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGSGVGKST----LLGMIARN---------TEadvnvialigER 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 173 TREGNDlYMEmkesKVINEQNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEV 252
Cdd:COG1157 195 GREVRE-FIE----DDLGEEGLARSVV--VVATSDEPPLMRLRAAYTATAIAEYFRDQGK-NVLLLMDSLTRFAMAQREI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 253 SALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAV 332
Cdd:COG1157 267 GLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAI 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558436 333 DPLDSTS-TMLQpwIVGEEHYETAQGVKQTLQRYKELQDIIAI----PGLDElsEEDRlTVARARKIERFLSQP 401
Cdd:COG1157 347 DVLASISrVMPD--IVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDP--ELDE-AIALIPAIEAFLRQG 415
|
|
| 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 |
4.06e-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: 180.37 E-value: 4.06e-56
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42558436 346 IVGEEHYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLSETI 422
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTI 77
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
66-339 |
6.72e-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: 172.36 E-value: 6.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 66 SVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 145
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 146 TVPITELINNiAKAhgGVSVSGGVGERTREGNDlYMEmkesKVINEQNISESkvALVYGQMNEPPGARMRVGSTALTMAE 225
Cdd:cd01136 81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGLKRS--VLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 226 YFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 305
Cdd:cd01136 151 YFRDQGK-KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....
gi 42558436 306 PATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
39-400 |
3.84e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 164.60 E-value: 3.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 39 NEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNlGPVRSSVTFPIHRSAPafTQLDTKL--SIF 116
Cdd:PRK06820 71 EMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPP--SPLTRQPieQML 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 117 ETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVpiteLINNIAkAHGGVSVSGGVG--ERTREGNDLYmemkeskvinEQNI 194
Cdd:PRK06820 148 TTGIRAIDGILSCGEGQRIGIFAAAGVGKST----LLGMLC-ADSAADVMVLALigERGREVREFL----------EQVL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 195 SE---SKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGT 271
Cdd:PRK06820 213 TPearARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGK-KVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 272 EMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEH 351
Cdd:PRK06820 292 NLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQ 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 42558436 352 YETAQGVKQTLQRYKELQDIIAI----PGLDELSEEdrlTVARARKIERFLSQ 400
Cdd:PRK06820 371 LAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
30-402 |
5.85e-46 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 164.01 E-value: 5.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 30 CEVQQLLGNNEVRAVA--------------MSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSV 95
Cdd:PRK08149 31 CEIRAGWHSNEVIARAqvvgfqrertilslIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 96 TFPIHR----SAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITELINNiakAHGGVSVSGGVGE 171
Cdd:PRK08149 111 PISEERvidvAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 172 RTREGNDLYMEMKESKvineqniSESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSE 251
Cdd:PRK08149 188 RGREVTEFVESLRASS-------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGK-RVVLFIDSMTRYARALRD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 252 VSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPA 331
Cdd:PRK08149 260 VALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPA 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42558436 332 VDPLDSTSTMLQPwIVGEEHYETAQGVKQTLQRYKELQDIIAI----PGldELSEEDRlTVARARKIERFLSQPF 402
Cdd:PRK08149 340 IDVLKSVSRVFGQ-VTDPKHRQLAAAFRKLLTRLEELQLFIDLgeyrRG--ENADNDR-AMDKRPALEAFLKQDV 410
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
61-400 |
6.26e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 164.16 E-value: 6.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 61 TGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQ---LDTKLSifeTGIKVVDLLAPYRRGGKIGL 137
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 138 FGGAGVGKTVPITELINNiakAHGGVSVSGGVGERTREgndlYMEMKESKVINEqniSESKVALVYGQMNEPPGARMRVG 217
Cdd:PRK06936 168 FAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESDLGEE---GLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 218 STALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVP 297
Cdd:PRK06936 238 FVATSIAEYFRDQGKR-VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 298 ADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGEEHYETAQGVKQTLQRYKELQDIIAI--- 374
Cdd:PRK06936 317 GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEEVELLLQIgey 395
|
330 340
....*....|....*....|....*..
gi 42558436 375 -PGLDELSEEdrlTVARARKIERFLSQ 400
Cdd:PRK06936 396 qKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
26-401 |
4.73e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 153.77 E-value: 4.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 26 IDVT----CEVQQ----LLGNNEV----RAVAM----SATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLG 89
Cdd:PRK09099 41 LDVTlgelCELRQrdgtLLQRAEVvgfsRDVALlspfGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 90 PVRSSVTFPIHRSAPAFTQ---LDTKLSifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVpiteLINNIAK-AHGGVSV 165
Cdd:PRK09099 121 PLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGLMTLGEGQRMGIFAPAGVGKST----LMGMFARgTQCDVNV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 166 SGGVGERTREGNDlYMEMkeskVINEQNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQdVLLFIDNIFRF 245
Cdd:PRK09099 194 IALIGERGREVRE-FIEL----ILGEDGMARSVV--VCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 246 VQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAA 325
Cdd:PRK09099 266 ARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 326 KGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTLQRYKELQDIIAI----PGLDELSEEdrlTVARARKIERFLSQP 401
Cdd:PRK09099 346 RNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
28-400 |
2.35e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 151.67 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 28 VTCEVqqlLGNNEVRAVAM--SATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPV-RSSVTFPIHRSAP 104
Cdd:PRK08927 54 VPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 105 ---AFTQLDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITELINNIAKAhggVSVSGGVGERTRE-----G 176
Cdd:PRK08927 131 pahSRARVGEPL---DLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 177 NDLYME-MKESKVIneqniseskVAlvygQMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSAL 255
Cdd:PRK08927 205 DDLGPEgLARSVVV---------VA----TSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 256 LGRMPSAVGYQPTLGTEMGSLQERI--TSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVD 333
Cdd:PRK08927 271 AGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAIN 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42558436 334 PLDSTS-TMlqPWIVGEEHYETAQGVKQTLQRYKELQDIIAI----PGLDelSEEDRlTVARARKIERFLSQ 400
Cdd:PRK08927 351 VLKSVSrTM--PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSD--PEVDE-AIRLNPALEAFLRQ 417
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
48-400 |
4.81e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 151.04 E-value: 4.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 48 ATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRS--------SVTFPIHRsAPAFTQLDTklsifetG 119
Cdd:PRK05688 84 SVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAedwvpmdgPTINPLNR-HPISEPLDV-------G 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 120 IKVVDLLAPYRRGGKIGLFGGAGVGKTVpITELINNIAKAHGGVSVSGGvgERTREgndlymeMKE--SKVINEQNISES 197
Cdd:PRK05688 156 IRSINGLLTVGRGQRLGLFAGTGVGKSV-LLGMMTRFTEADIIVVGLIG--ERGRE-------VKEfiEHILGEEGLKRS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 198 KValVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQ 277
Cdd:PRK05688 226 VV--VASPADDAPLMRLRAAMYCTRIAEYFRDKGK-NVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 278 ERITSTKEG--SITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETA 355
Cdd:PRK05688 303 ERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRA 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 42558436 356 QGVKQTLQRYKELQDIIAI----PGLDelsEEDRLTVARARKIERFLSQ 400
Cdd:PRK05688 382 QRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
65-400 |
1.54e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 149.45 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 65 LSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 144
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 145 KTVpiteLINNIAK-AHGGVSVSGGVGERTRE---------GNDLymemkESKVINEQNISESKVALVYGQMneppgarm 214
Cdd:PRK08472 170 KST----LMGMIVKgCLAPIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYGAF-------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 215 rvgsTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTK-EGSITSIQA 293
Cdd:PRK08472 233 ----CAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFT 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 294 VYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGEEHYETAQGVKQTLQRYKELQDIIA 373
Cdd:PRK08472 308 VLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIR 386
|
330 340 350
....*....|....*....|....*....|..
gi 42558436 374 I----PGLD-ELSEedrlTVARARKIERFLSQ 400
Cdd:PRK08472 387 IgayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
75-400 |
2.37e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 149.38 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 75 GRISNVLGEPVDNLGPVRS-SVTFPIHRSAPAF---TQLDTKlsiFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVpit 150
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAmtrARVETG---LRTGVRVIDIFTPLCAGQRIGIFAGSGVGKST--- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 151 eLINNIAKA-HGGVSVSGGVGERTREgndlYMEMKESKVINeqniSESKVALVYGQMNEPPGARMRVGSTALTMAEYFRD 229
Cdd:PRK06002 181 -LLAMLARAdAFDTVVIALVGERGRE----VREFLEDTLAD----NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 230 VNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKE--GSITSIQAVYVPADDLTDPAPA 307
Cdd:PRK06002 252 RG-ENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVAD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 308 TTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ-PWIVGEEhyETAQGVKQTLQRYKELQDIIAI----PGLDelSE 382
Cdd:PRK06002 331 SIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARhAWTPEQR--KLVSRLKSMIARFEETRDLRLIggyrAGSD--PD 406
|
330
....*....|....*...
gi 42558436 383 EDrLTVARARKIERFLSQ 400
Cdd:PRK06002 407 LD-QAVDLVPRIYEALRQ 423
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
67-374 |
2.42e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 149.08 E-value: 2.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 67 VPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHrsAPAFTQLDTKlSIFE---TGIKVVDLLAPYRRGGKIGLFGGAGV 143
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAMLTVGKGQRMGLFAGSGV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 144 GKTVpiteLINNIAKAHGGVSVSGGVG-ERTREgndlymeMKE--SKVINEQNISESKValVYGQMNEPPGARMRVGSTA 220
Cdd:PRK08972 174 GKSV----LLGMMTRGTTADVIVVGLVgERGRE-------VKEfiEEILGEEGRARSVV--VAAPADTSPLMRLKGCETA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 221 LTMAEYFRDVNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERIT--STKEGSITSIQAVYVPA 298
Cdd:PRK08972 241 TTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSITAFYTVLTEG 319
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42558436 299 DDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTLQRYKELQDIIAI 374
Cdd:PRK08972 320 DDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
61-374 |
1.60e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 146.79 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 61 TGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGG 140
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 141 AGVGKTVpiteLINNIAK-AHGGVSVSGGVGERTREGNDlYMEmkesKVINEQNISESKValVYGQMNEPPGARMRVGST 219
Cdd:PRK07721 167 SGVGKST----LMGMIARnTSADLNVIALIGERGREVRE-FIE----RDLGPEGLKRSIV--VVATSDQPALMRIKGAYT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 220 ALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPAD 299
Cdd:PRK07721 236 ATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGD 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42558436 300 DLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTLQRYKELQDIIAI 374
Cdd:PRK07721 315 DMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
28-400 |
2.59e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 146.28 E-value: 2.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 28 VTCEVQQLLGNNEVrAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISN----VLGEPVDNLGPVRSSVTFP-IHrs 102
Cdd:PRK06793 53 VLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPLQKIKLDAPpIH-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 103 apAFTQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVpiteLINNIAK-AHGGVSVSGGVGERTREGNDLYm 181
Cdd:PRK06793 130 --AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST----LLGMIAKnAKADINVISLVGERGREVKDFI- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 182 emkeSKVINEQNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPS 261
Cdd:PRK06793 202 ----RKELGEEGMRKSVV--VVATSDESHLMQLRAAKLATSIAEYFRDQGN-NVLLMMDSVTRFADARRSVDIAVKELPI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 262 AvGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 341
Cdd:PRK06793 275 G-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42558436 342 LQPwIVGEEHYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLTVARARK--IERFLSQ 400
Cdd:PRK06793 354 MEE-IVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAENAYIFECKNKVegINTFLKQ 413
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
69-400 |
2.06e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 135.40 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 69 VGETTLGRISNVLGEPVDNLGPVRSSVtfPIHRSAPAFTQLDTKL--SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 146
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 147 VpiteLINNIAKA-HGGVSVSGGVGERTREgndlymeMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTALTMAE 225
Cdd:PRK07196 170 V----LLGMITRYtQADVVVVGLIGERGRE-------VKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIAT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 226 YFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERI-TSTKEGSITSIQAVYVPADDLTDP 304
Cdd:PRK07196 239 YYRDKGH-DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDDQQDP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 305 APATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMLQpwIVGEEHYETAQGVKQTLQRYKELQDIIA----IPGLDE 379
Cdd:PRK07196 318 IVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISrCMSQ--VIGSQQAKAASLLKQCYADYMAIKPLIPlggyVAGADP 395
|
330 340
....*....|....*....|.
gi 42558436 380 LSEEdrlTVARARKIERFLSQ 400
Cdd:PRK07196 396 MADQ---AVHYYPAITQFLRQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
47-374 |
1.22e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 133.15 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 47 SATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNL----GPVRSSVTFPihrsAPAFTQLDTKLSIFeTGIKV 122
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 123 VDLLAPYRRGGKIGLFGGAGVGKTVPITELINniaKAHGGVSVSGGVGERTREgndlYMEMKESKVINEqniSESKVALV 202
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFIDFTLSEE---TRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 203 YGQMNEPPGARMRVGSTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITS 282
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 283 TKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTL 362
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330
....*....|..
gi 42558436 363 QRYKELQDIIAI 374
Cdd:PRK07594 374 ALYQEVELLIRI 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
54-403 |
2.38e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 124.51 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 54 RGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIhrSAPAFTQLD-TKLS-IFETGIKVVDLLAPYRR 131
Cdd:PRK07960 97 RNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFNPLQrTPIEhVLDTGVRAINALLTVGR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 132 GGKIGLFGGAGVGKTVpiteLINNIAK-AHGGVSVSGGVGERTREGNDlYMEmkesKVINEQNISESKValVYGQMNEPP 210
Cdd:PRK07960 175 GQRMGLFAGSGVGKSV----LLGMMARyTQADVIVVGLIGERGREVKD-FIE----NILGAEGRARSVV--IAAPADVSP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 211 GARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITS--TKEGSI 288
Cdd:PRK07960 244 LLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 289 TSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGEEHYETAQGVKQTLQRYKEL 368
Cdd:PRK07960 323 TAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTA-LIDEQHYARVRQFKQLLSSFQRN 401
|
330 340 350
....*....|....*....|....*....|....*....
gi 42558436 369 QDIIAI----PGLDELSEEdrlTVARARKIERFLSQPFF 403
Cdd:PRK07960 402 RDLVSVgayaKGSDPMLDK---AIALWPQLEAFLQQGIF 437
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
38-402 |
9.34e-27 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 111.15 E-value: 9.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 38 NNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFE 117
Cdd:PRK05922 63 NRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 118 TGIKVVDLLAPYRRGGKIGLFGGAGVGKtvpiTELINNIAK-AHGGVSVSGGVGERTREGNDlYMEMKESkvineqNISE 196
Cdd:PRK05922 143 TGIKAIDAFLTLGKGQRIGVFSEPGSGK----SSLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKE------GLAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 197 SKVALVYGQMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSL 276
Cdd:PRK05922 212 QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 277 QERITSTKEGSITSIQAV-YVP--ADDLTDPAPATTSAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQPWIVgEEHYE 353
Cdd:PRK05922 291 TERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSARQLAL-PHHYA 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 42558436 354 TAQGVKQTLQRYKELQDIIAI----PGLDElsEEDRlTVARARKIERFLSQPF 402
Cdd:PRK05922 365 AAEELRSLLKAYHEALDIIQLgayvPGQDA--HLDR-AVKLLPSIKQFLSQPL 414
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
11-402 |
9.34e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 111.46 E-value: 9.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 11 YNSIV-IKGQNPA---GQQIDVTCE--VQQLLGNnevravamsaTDGL-TRGMGAVDTGAPLSVPVGETTLGRISNVLGE 83
Cdd:PRK04196 25 YGEIVeIELPNGEkrrGQVLEVSEDkaVVQVFEG----------TTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 84 PVDNLGPVRSSVTFPIHRSA--PA-------FTQldtklsifeTGIKVVDLLAPYRRGGKIGLFGGAGvgktVPITELIN 154
Cdd:PRK04196 95 PIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------TGISAIDGLNTLVRGQKLPIFSGSG----LPHNELAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 155 NIAkahggvsvsggvgertregndlymemKESKVINEqnisESKVALVYGQM---------------------------- 206
Cdd:PRK04196 162 QIA--------------------------RQAKVLGE----EENFAVVFAAMgitfeeanffmedfeetgalersvvfln 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 207 --NEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQER--ITS 282
Cdd:PRK04196 212 laDDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 283 TKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIvGEEHY-ETAQGVKQT 361
Cdd:PRK04196 292 GKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGI-GEGKTrEDHKDVANQ 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 42558436 362 L----QRYKELQDIIAIPGLDELSEEDRLTVARARKIE-RFLSQPF 402
Cdd:PRK04196 371 LyaayARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGF 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 |
6.82e-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: 105.77 E-value: 6.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 64 PLSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV 143
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 144 gktvPITELINNIAKahggvsvsgGVGERTREGNDL---------YMEMKESKVINEQNISESKVALVYGQMNEPPGARM 214
Cdd:cd01135 81 ----PHNELAAQIAR---------QAGVVGSEENFAivfaamgvtMEEARFFKDDFEETGALERVVLFLNLANDPTIERI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 215 RVGSTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQER--ITSTKEGSITSIQ 292
Cdd:cd01135 148 ITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 42558436 293 AVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 343
Cdd:cd01135 228 ILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| 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 |
1.31e-23 |
|
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: 93.35 E-value: 1.31e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42558436 1 AFSPGEMPNIYNSIVIKGQNPagqqIDVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPL 65
Cdd:cd18115 16 EFPEGELPPIYNALEVKGDDG----KKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
36-339 |
1.98e-23 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 102.30 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 36 LGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSI 115
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 116 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKT-VPITELINniakahggvsvsggvgertREGNDLY-----MEMKESKVI 189
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTaIAIDAIIN-------------------QKDSDVIcvyvaIGQKASAVA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 190 N------EQNISESKVaLVYGQMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV 263
Cdd:PRK13343 207 RvietlrEHGALEYTT-VVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGRE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 264 GYQPTLGTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:PRK13343 285 AYPGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVS 364
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
219-400 |
3.95e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 98.70 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 219 TALTMAEYFRDvnkQ--DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQER----IT-STKEGSITSI 291
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 292 QAVYVPADDLTDPapaTTSAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQPWI---VGEEHYETAQGVKQTL 362
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPWWeenVDPDWRELRDEAMDLL 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 42558436 363 QRYKELQDIIAIPGLDELSEEDRLTVARARKI-ERFLSQ 400
Cdd:PRK04192 465 QREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 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 |
5.88e-22 |
|
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: 94.95 E-value: 5.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 64 PLSVPVGETTLGRISNVLGEPVDNLG----------------PVRssVTFPIHRSAPAFTQLdtklsifETGIKVVDLLA 127
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAetgsifiprgvnvqrwPVR--QPRPVKEKLPPNVPL-------LTGQRVLDTLF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 128 PYRRGGKIGLFGGAGVGKTVpiteLINNIAK-AHGGVSVSGGVGERTREGNDLYMEMKESKV-INEQNISEsKVALVYGQ 205
Cdd:cd01134 72 PVAKGGTAAIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGERGNEMAEVLEEFPELKDpITGESLME-RTVLIANT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 206 MNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERI----- 280
Cdd:cd01134 147 SNMPVAAREASIYTGITIAEYFRDMGY-NVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrc 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558436 281 --TSTKEGSITSIQAVYVPADDLTDPapaTTSAHLDATTV---LSRGLAAKGIYPAVDPLDSTS 339
Cdd:cd01134 226 lgSPGREGSVTIVGAVSPPGGDFSEP---VTQATLRIVQVfwgLDKKLAQRRHFPSINWLISYS 286
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
61-400 |
2.99e-21 |
|
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: 95.56 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 61 TGAPLSVPVGETTLGRISNVLGEPVDNlGPVRSSVTF------PIHRSAPAFTQldtklSIFETGIKVVDLLAPYRRGGK 134
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDK-GPPVLAEDYldingqPINPYARIYPE-----EMIQTGISAIDVMNSIARGQK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 135 IGLFGGAGVgktvPITELINNIAKAHGGVSVSGGVGERTREGN------DLYMEMKESKVIN---EQNISESKVALVYGQ 205
Cdd:TIGR01040 144 IPIFSAAGL----PHNEIAAQICRQAGLVKLPTKDVHDGHEDNfaivfaAMGVNMETARFFKqdfEENGSMERVCLFLNL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 206 MNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERI--TST 283
Cdd:TIGR01040 220 ANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 284 KEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIvGE-----EHYETAQGV 358
Cdd:TIGR01040 300 RNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSNQL 378
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 42558436 359 KQTLQRYKELQDIIAIPGLDELSEEDRLTVARARKIER-FLSQ 400
Cdd:TIGR01040 379 YACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
351-414 |
7.34e-19 |
|
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: 80.18 E-value: 7.34e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558436 351 HYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGK 414
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
171-412 |
3.18e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 87.38 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 171 ERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGS 250
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 251 EVSALLGRMPSAVGYQPTLGTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGL 323
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 324 AAKGIYPAVDPLDSTS---TMLQPWI---VGEEHYETAQGVKQTLQRYKELQDIIAIPGLDELSEEDRLTVARARKI-ER 396
Cdd:PRK14698 851 ARRRHFPAINWLTSYSlyvDAVKDWWhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250
....*....|....*.
gi 42558436 397 FLSQPFFvAEVFTGSP 412
Cdd:PRK14698 931 YLQQDAF-DEVDTYCP 945
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
65-339 |
9.45e-16 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 76.83 E-value: 9.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 65 LSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 144
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 145 KT-VPITELINniakahggvsvsggvgertREGNDLY-----MEMKESKVINEQNISESKVALVY-----GQMNEPPGAR 213
Cdd:cd01132 82 KTaIAIDTIIN-------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 214 MRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGYQPTlgtemgSLQERITSTKE-- 285
Cdd:cd01132 143 YLAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYLHS------RLLERAAKLSDel 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 42558436 286 --GSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:cd01132 216 ggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
39-260 |
8.98e-14 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 72.79 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 39 NEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTQldtKLSIFE- 117
Cdd:PRK09281 69 DNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEp 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 118 --TGIKVVDLLAPYRRGGKIGLFGGAGVGKT-VPITELINniakahggvsvsggvgertREGNDLY-----MEMKESKVI 189
Cdd:PRK09281 146 lqTGIKAIDAMIPIGRGQRELIIGDRQTGKTaIAIDTIIN-------------------QKGKDVIciyvaIGQKASTVA 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42558436 190 NEQNISESKVALVY-----GQMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMP 260
Cdd:PRK09281 207 QVVRKLEEHGAMEYtivvaATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
53-309 |
6.46e-13 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 70.06 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 53 TRGMGAVDT----GAPLSVPVGETTLGRISNVLGEPVDNlGPVRSSVTFPIhrSAPAFTQLDTKL--SIFETGIKVVDLL 126
Cdd:PRK02118 58 TRGISTGDEvvflGRPMQVTYSESLLGRRFNGSGKPIDG-GPELEGEPIEI--GGPSVNPVKRIVprEMIRTGIPMIDVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 127 APYRRGGKIGLFGGAGVgktvPITELINNIAKAHGGVSVSGGVGERTregNDLYMEMKESKvinEQNISESKVALVYGQM 206
Cdd:PRK02118 135 NTLVESQKIPIFSVSGE----PYNALLARIALQAEADIIILGGMGLT---FDDYLFFKDTF---ENAGALDRTVMFIHTA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 207 NEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKE- 285
Cdd:PRK02118 205 SDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDg 284
|
250 260
....*....|....*....|....
gi 42558436 286 GSITSIQAVYVPADDLTDPAPATT 309
Cdd:PRK02118 285 GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
36-333 |
7.63e-10 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 60.75 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 36 LGNNEVRAVAMSatDGLT--RGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSVTFPIHRSAPAFTqldTKL 113
Cdd:CHL00059 45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 114 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITELINNiakahggvsvsggvgertREGND---LYMEM--KE 185
Cdd:CHL00059 120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 186 SKVINEQNISESKVALVY-----GQMNEPPGARMRVGSTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMP 260
Cdd:CHL00059 182 SSVAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42558436 261 SAVGYQPTLGTEMGSLQERI----TSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVD 333
Cdd:CHL00059 261 GREAYPGDVFYLHSRLLERAaklsSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAIN 337
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
2-62 |
3.69e-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: 52.93 E-value: 3.69e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42558436 2 FSPGEMPNIYNSIVIKGQNpagqQIDVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTG 62
Cdd:pfam02874 13 FGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
3-333 |
1.28e-05 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 47.34 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 3 SPGEMPNIYNSIVIKGQNPAGQQIDVTCEVQQllgNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLG 82
Cdd:PTZ00185 56 APGNPGVAYNTIIMIQVSPTTFAAGLVFNLEK---DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 83 EPV---------------DNLGPVRSSVTFPIHRSAPAFTQLdtklsifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKT- 146
Cdd:PTZ00185 133 HEVpvglltrsralleseQTLGKVDAGAPNIVSRSPVNYNLL--------TGFKAVDTMIPIGRGQRELIVGDRQTGKTs 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 147 VPITELINNIAKAHGGVSVSGGVgertregnDLYMEMKE--SKVINEQNISESKVALVY-----GQMNEPPGARMRVGST 219
Cdd:PTZ00185 205 IAVSTIINQVRINQQILSKNAVI--------SIYVSIGQrcSNVARIHRLLRSYGALRYttvmaATAAEPAGLQYLAPYS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558436 220 ALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKE----GSITSIQAVY 295
Cdd:PTZ00185 277 GVTMGEYFMNRGRH-CLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVE 355
|
330 340 350
....*....|....*....|....*....|....*...
gi 42558436 296 VPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVD 333
Cdd:PTZ00185 356 TLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
347-401 |
3.20e-05 |
|
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: 41.65 E-value: 3.20e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 42558436 347 VGEEHYETAQGVKQTLQRYKELQDIIAI----PGLDelSEEDRlTVARARKIERFLSQP 401
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSD--PEIDE-AIAKRPAINAFLRQG 56
|
|
| 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 |
2.07e-03 |
|
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: 37.41 E-value: 2.07e-03
10 20 30
....*....|....*....|....*....|....*.
gi 42558436 366 KELQDIIAIPGLDELSEEDRLTVARARKIE-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 |
3.87e-03 |
|
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: 36.60 E-value: 3.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 42558436 362 LQRYKELQDIIAIPGLDELSEEDRLTVARARKI-ERFLSQ 400
Cdd:cd18111 12 LQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
351-403 |
4.39e-03 |
|
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the 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 flagellum-specific ATPase FliI is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of FoF1-ATP synthase. Although they both are proton driven rotary molecular devices, 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: 349749 [Multi-domain] Cd Length: 71 Bit Score: 35.66 E-value: 4.39e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 42558436 351 HYETAQGVKQTLQRYKELQDIIAI----PGLDELSEEdrlTVARARKIERFLSQPFF 403
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIgaykKGSDPEVDE---AIRLKPQIEAFLKQGLN 54
|
|
| |
