|
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: 975.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 1 AFSPGEMPNIYNSLIVKGQNPAGQQVHVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNV 80
Cdd:CHL00060 30 AFPPGKMPNIYNALVVKGRDTAGQEINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 81 LGEPVDNLGPVRSSAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAH 160
Cdd:CHL00060 110 LGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 161 GGVSVFGGVGERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFID 240
Cdd:CHL00060 190 GGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFID 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 241 NIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLS 320
Cdd:CHL00060 270 NIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 321 RGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQ 400
Cdd:CHL00060 350 RGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQ 429
|
410 420
....*....|....*....|..
gi 42558426 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 42558426 2 FSPGEMPNIYNSLIVKgqNPAGQQVhvTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVL 81
Cdd:COG0055 20 FPEGELPAIYNALEVE--NEGGGEL--VLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 82 GEPVDNLGPVRSSAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAHG 161
Cdd:COG0055 96 GEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 162 GVSVFGGVGERTREGNDLYMEMKESKVINeqnisesKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDN 241
Cdd:COG0055 176 GVSVFAGVGERTREGNDLYREMKESGVLD-------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 242 IFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSR 321
Cdd:COG0055 249 IFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 322 GLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQP 401
Cdd:COG0055 329 KIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQP 408
|
410 420
....*....|....*....|.
gi 42558426 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: 742.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 2 FSPGEMPNIYNSLIVKGqnpaGQQVHVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVL 81
Cdd:TIGR01039 17 FEQGELPRIYNALKVQN----RAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 82 GEPVDNLGPVRSSAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAHG 161
Cdd:TIGR01039 93 GEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 162 GVSVFGGVGERTREGNDLYMEMKESKVINeqnisesKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDN 241
Cdd:TIGR01039 173 GYSVFAGVGERTREGNDLYHEMKESGVID-------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 242 IFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSR 321
Cdd:TIGR01039 246 IFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 322 GLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQP 401
Cdd:TIGR01039 326 KIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQP 405
|
410 420
....*....|....*....|.
gi 42558426 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: 557.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 66 SVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 145
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 146 TVPITESINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEqnISESKVALVYGQMNEPPGARMRVGSTALTMAE 225
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINL--DGLSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 226 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 305
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 42558426 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: 539.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 4 PGEMPNIYNSLIvkgqnpAGQQVHVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGE 83
Cdd:TIGR03305 16 DGELPAIHSVLR------AGREGEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 84 PVDNLGPVRSSAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAHGGV 163
Cdd:TIGR03305 90 TIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 164 SVFGGVGERTREGNDLYMEMKESKVINEqniseskVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDNIF 243
Cdd:TIGR03305 170 SIFCGIGERCREGEELYREMKEAGVLDN-------TVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 244 RFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGL 323
Cdd:TIGR03305 243 RFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLSRKR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 324 AAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFF 403
Cdd:TIGR03305 323 ASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQPFF 402
|
410
....*....|....*....
gi 42558426 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 |
1.36e-125 |
|
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: 364.08 E-value: 1.36e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 66 SVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 145
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 146 TVPITESINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVineqnisESKVALVYGQMNEPPGARMRVGSTALTMAE 225
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 226 YFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTK--EGSITSIQAVYVPADDLTD 303
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 42558426 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 |
2.12e-83 |
|
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: 254.20 E-value: 2.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 119 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVpiteSINNIAK-AHGGVSVFGGVGERTREGNDLYMEMKESKVIneqniseS 197
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTV----LAGMIARqASADVVVYALIGERGREVREFIEELLGSGAL-------K 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 198 KVALVYGQMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQ 277
Cdd:pfam00006 70 RTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558426 278 ERITSTKE--GSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS 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 |
1.20e-57 |
|
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: 184.22 E-value: 1.20e-57
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42558426 346 IVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLSETI 422
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTI 77
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-401 |
2.42e-56 |
|
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: 191.40 E-value: 2.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 28 VTCEVqqlLGNNEVRAVAM--SATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPA 105
Cdd:COG1157 54 VLAEV---VGFRGDRVLLMplGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 106 FTQ---LDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV---PITES----INNIAkahggvsvfgGVGERTRE 175
Cdd:COG1157 131 PLErarITEPL---DTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTllgMIARNteadVNVIA----------LIGERGRE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 176 GNDlYMEmkesKVINEQNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSAL 255
Cdd:COG1157 198 VRE-FIE----DDLGEEGLARSVV--VVATSDEPPLMRLRAAYTATAIAEYFRDQGK-NVLLLMDSLTRFAMAQREIGLA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 256 LGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPL 335
Cdd:COG1157 270 AGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVL 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42558426 336 DSTS-TMLQpwIVGEEHYETAQGVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 401
Cdd:COG1157 350 ASISrVMPD--IVSPEHRALARRLRRLLARYEENEDLIRI-GayqpgsdpeLDE-------AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
66-339 |
5.51e-49 |
|
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: 167.35 E-value: 5.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 66 SVPVGETTLGRISNVLGEPVDNLG--------PVRSSAISPIHRsaPAFTQldtklsIFETGIKVVDLLAPYRRGGKIGL 137
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGlpdeperrPLIAAPPNPLKR--APIEQ------PLPTGVRAIDGLLTCGEGQRIGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 138 FGGAGVGKTV---PITES----INNIAkahggvsvfgGVGERTREGNDlYMEmkesKVINEQNISESkvALVYGQMNEPP 210
Cdd:cd01136 73 FAGSGVGKSTllgMIARNtdadVNVIA----------LIGERGREVRE-FIE----KDLGEEGLKRS--VLVVATSDESP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 211 GARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITS 290
Cdd:cd01136 136 LLRVRAAYTATAIAEYFRDQGK-KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITA 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 42558426 291 IQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:cd01136 215 FYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
39-400 |
1.87e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 163.06 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 39 NEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNlGPVRSSAISPIHRSAPafTQLDTKL--SIF 116
Cdd:PRK06820 71 EMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPP--SPLTRQPieQML 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 117 ETGIKVVDLLAPYRRGGKIGLFGGAGVGKTvpiteSINNIAKAHGGVSVFGGVG--ERTREGNDLYmemkeskvinEQNI 194
Cdd:PRK06820 148 TTGIRAIDGILSCGEGQRIGIFAAAGVGKS-----TLLGMLCADSAADVMVLALigERGREVREFL----------EQVL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 195 SE---SKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGT 271
Cdd:PRK06820 213 TPearARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGK-KVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 272 EMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEH 351
Cdd:PRK06820 292 NLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQ 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 42558426 352 YETAQGVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 400
Cdd:PRK06820 371 LAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
30-402 |
3.61e-44 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 159.00 E-value: 3.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 30 CEVQQLLGNNEVRAVA--------------MSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLG-PVRSS 94
Cdd:PRK08149 31 CEIRAGWHSNEVIARAqvvgfqrertilslIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDaPPTVG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 95 AIS---PIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNiakAHGGVSVFGGVGE 171
Cdd:PRK08149 111 PISeerVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 172 RTREGNDLYMEMKESKvineqniSESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSE 251
Cdd:PRK08149 188 RGREVTEFVESLRASS-------RREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGK-RVVLFIDSMTRYARALRD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 252 VSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPA 331
Cdd:PRK08149 260 VALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPA 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558426 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 |
1.53e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 157.61 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 61 TGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPAFTQ---LDTKLSifeTGIKVVDLLAPYRRGGKIGL 137
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 138 FGGAGVGKTVPITESINNiakAHGGVSVFGGVGERTREgndlYMEMKESKVINEqniSESKVALVYGQMNEPPGARMRVG 217
Cdd:PRK06936 168 FAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESDLGEE---GLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 218 STALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVP 297
Cdd:PRK06936 238 FVATSIAEYFRDQGKR-VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 298 ADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGEEHYETAQGVKQTLQRYKELQDIIAI--- 374
Cdd:PRK06936 317 GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEEVELLLQIgey 395
|
330 340
....*....|....*....|....*..
gi 42558426 375 -LGLDELSEEdrlTVARARKIERFLSQ 400
Cdd:PRK06936 396 qKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
48-400 |
4.35e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 151.42 E-value: 4.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 48 ATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRS--------SAISPIHRsAPAFTQLDTklsifetG 119
Cdd:PRK05688 84 SVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAedwvpmdgPTINPLNR-HPISEPLDV-------G 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 120 IKVVDLLAPYRRGGKIGLFGGAGVGKTVPI------TESinniakahgGVSVFGGVGERTREgndlymeMKE--SKVINE 191
Cdd:PRK05688 156 IRSINGLLTVGRGQRLGLFAGTGVGKSVLLgmmtrfTEA---------DIIVVGLIGERGRE-------VKEfiEHILGE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 192 QNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGT 271
Cdd:PRK05688 220 EGLKRSVV--VASPADDAPLMRLRAAMYCTRIAEYFRDKGK-NVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 272 EMGSLQERITSTKEG--SITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGE 349
Cdd:PRK05688 297 KLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDP 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 42558426 350 EHYETAQGVKQTLQRYKELQDIIAI----LGLDelsEEDRLTVARARKIERFLSQ 400
Cdd:PRK05688 376 EHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
30-401 |
1.88e-40 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 149.53 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 30 CEVQQ----LLGNNEV----RAVAM----SATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSAIS 97
Cdd:PRK09099 49 CELRQrdgtLLQRAEVvgfsRDVALlspfGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 98 PIHRSAPAFTQ---LDTKLSifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPI------TE-SINNIAkahggvsvfg 167
Cdd:PRK09099 129 PVIAAPPDPMSrrmVEAPLP---TGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMgmfargTQcDVNVIA---------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 168 GVGERTREGNDlYMEMkeskVINEQNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQdVLLFIDNIFRFVQ 247
Cdd:PRK09099 196 LIGERGREVRE-FIEL----ILGEDGMARSVV--VCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFAR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 248 AGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKG 327
Cdd:PRK09099 268 AQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARN 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42558426 328 IYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQP 401
Cdd:PRK09099 348 QYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
27-400 |
2.19e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 148.97 E-value: 2.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 27 HVTCEVQQLLGNNEVrAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISN----VLGEPVDNLgPVRSSAIS--PIH 100
Cdd:PRK06793 52 NVLCEVIAIEKENNM-LLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENI-PLQKIKLDapPIH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 101 rsapAFTQLDTKlSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVpiteSINNIAK-AHGGVSVFGGVGERTREGNDL 179
Cdd:PRK06793 130 ----AFEREEIT-DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST----LLGMIAKnAKADINVISLVGERGREVKDF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 180 YmemkeSKVINEQNISESKValVYGQMNEPPGARMRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRM 259
Cdd:PRK06793 201 I-----RKELGEEGMRKSVV--VVATSDESHLMQLRAAKLATSIAEYFRDQGN-NVLLMMDSVTRFADARRSVDIAVKEL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 260 PSAvGYQPTLGTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:PRK06793 273 PIG-GKTLLMESYMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVS 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558426 340 TMLQPwIVGEEHYETAQGVKQTLQRYKElQDIIAILGLDELSEEDRLTVARARKIE---RFLSQ 400
Cdd:PRK06793 352 RIMEE-IVSPNHWQLANEMRKILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
65-400 |
2.78e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 148.68 E-value: 2.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 65 LSVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 144
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 145 KTVPITESINNiAKAhgGVSVFGGVGERTRE---------GNDLymemkESKVINEQNISESKVALVYGQMneppgarmr 215
Cdd:PRK08472 170 KSTLMGMIVKG-CLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYGAF--------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 216 vgsTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTK-EGSITSIQAV 294
Cdd:PRK08472 233 ---CAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 295 YVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGEEHYETAQGVKQTLQRYKELQDIIAI 374
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350
....*....|....*....|....*....|.
gi 42558426 375 ----LGLD-ELSEedrlTVARARKIERFLSQ 400
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
67-374 |
3.38e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 148.69 E-value: 3.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 67 VPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHrsAPAFTQLDTKlSIFE---TGIKVVDLLAPYRRGGKIGLFGGAGV 143
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAMLTVGKGQRMGLFAGSGV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 144 GKTVPI-------TESInniakahggvSVFGGVGERTREgndlymeMKE--SKVINEQNISESKValVYGQMNEPPGARM 214
Cdd:PRK08972 174 GKSVLLgmmtrgtTADV----------IVVGLVGERGRE-------VKEfiEEILGEEGRARSVV--VAAPADTSPLMRL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 215 RVGSTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERIT--STKEGSITSIQ 292
Cdd:PRK08972 235 KGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSITAFY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 293 AVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTLQRYKELQDII 372
Cdd:PRK08972 314 TVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLI 392
|
..
gi 42558426 373 AI 374
Cdd:PRK08972 393 SI 394
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
28-400 |
1.04e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 144.74 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 28 VTCEVqqlLGNNEVRAVAM--SATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPV-RSSAISPIHRSAP 104
Cdd:PRK08927 54 VPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 105 ---AFTQLDTKLsifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNIAKAhggVSVFGGVGERTRE-----G 176
Cdd:PRK08927 131 pahSRARVGEPL---DLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 177 NDLYME-MKESKVIneqniseskVAlvygQMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSAL 255
Cdd:PRK08927 205 DDLGPEgLARSVVV---------VA----TSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 256 LGRMPSAVGYQPTLGTEMGSLQERI--TSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVD 333
Cdd:PRK08927 271 AGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAIN 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42558426 334 PLDSTS-TMlqPWIVGEEHYETAQGVKQTLQRYKELQDIIAI----LGLDelSEEDRlTVARARKIERFLSQ 400
Cdd:PRK08927 351 VLKSVSrTM--PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSD--PEVDE-AIRLNPALEAFLRQ 417
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
75-376 |
1.83e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 143.98 E-value: 1.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 75 GRISNVLGEPVDNLGPVRSSAIS-PIHRSAPAF---TQLDTKlsiFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPIT 150
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPmSIDATAPPAmtrARVETG---LRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 151 EsinnIAKA-HGGVSVFGGVGERTREgndlYMEMKESKVINeqniSESKVALVYGQMNEPPGARMRVGSTALTMAEYFRD 229
Cdd:PRK06002 184 M----LARAdAFDTVVIALVGERGRE----VREFLEDTLAD----NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 230 VNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKE--GSITSIQAVYVPADDLTDPAPA 307
Cdd:PRK06002 252 RG-ENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVAD 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 308 TTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ-PWIVGEEhyETAQGVKQTLQRYKELQDIIAILG 376
Cdd:PRK06002 331 SIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARhAWTPEQR--KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
61-374 |
3.77e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 142.94 E-value: 3.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 61 TGAPLSVPVGETTLGRISNVLGEPVDN------LGPVrssaisPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGK 134
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGsalpkgLAPV------STDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 135 IGLFGGAGVGKTVPI------TES-INNIAkahggvsvfgGVGERTREGNDlYMEmkesKVINEQNISESKValVYGQMN 207
Cdd:PRK07721 161 VGIFAGSGVGKSTLMgmiarnTSAdLNVIA----------LIGERGREVRE-FIE----RDLGPEGLKRSIV--VVATSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 208 EPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKEGS 287
Cdd:PRK07721 224 QPALMRIKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 288 ITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTLQRYKE 367
Cdd:PRK07721 303 ITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQN 381
|
....*..
gi 42558426 368 LQDIIAI 374
Cdd:PRK07721 382 SEDLINI 388
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
69-400 |
4.54e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 131.94 E-value: 4.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 69 VGETTLGRISNVLGEPVDNLGPVRSSAisPIHRSAPAFTQLDTKL--SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 146
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 147 VpITESINNIAKAHGGVSVFGGvgERTREgndlymeMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTALTMAEY 226
Cdd:PRK07196 170 V-LLGMITRYTQADVVVVGLIG--ERGRE-------VKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 227 FRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERI-TSTKEGSITSIQAVYVPADDLTDPA 305
Cdd:PRK07196 240 YRDKGH-DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVLAEGDDQQDPI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 306 PATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMLQpwIVGEEHYETAQGVKQTLQRYKELQDIIA----ILGLDEL 380
Cdd:PRK07196 319 VDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISrCMSQ--VIGSQQAKAASLLKQCYADYMAIKPLIPlggyVAGADPM 396
|
330 340
....*....|....*....|
gi 42558426 381 SEEdrlTVARARKIERFLSQ 400
Cdd:PRK07196 397 ADQ---AVHYYPAITQFLRQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
47-374 |
1.18e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 130.46 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 47 SATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNL----GPVRSSAISPihrsAPAFTQLDTKLSIFeTGIKV 122
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 123 VDLLAPYRRGGKIGLFGGAGVGKTVpITESINNIAKAHGGVSVFGGvgERTREgndlYMEMKESKVINEqniSESKVALV 202
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKST-LLAMLCNAPDADSNVLVLIG--ERGRE----VREFIDFTLSEE---TRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 203 YGQMNEPPGARMRVGSTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITS 282
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 283 TKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGEEHYETAQGVKQTL 362
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330
....*....|..
gi 42558426 363 QRYKELQDIIAI 374
Cdd:PRK07594 374 ALYQEVELLIRI 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
54-403 |
3.19e-30 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 121.43 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 54 RGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNL--------GPVRSSAISPIHRSAPAftqldtklSIFETGIKVVDL 125
Cdd:PRK07960 97 RNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLpapdtgetGALITPPFNPLQRTPIE--------HVLDTGVRAINA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 126 LAPYRRGGKIGLFGGAGVGKTVpiteSINNIAK-AHGGVSVFGGVGERTREGNDlYMEmkesKVINEQNISESKValVYG 204
Cdd:PRK07960 169 LLTVGRGQRMGLFAGSGVGKSV----LLGMMARyTQADVIVVGLIGERGREVKD-FIE----NILGAEGRARSVV--IAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 205 QMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITS-- 282
Cdd:PRK07960 238 PADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgi 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 283 TKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGEEHYETAQGVKQTL 362
Cdd:PRK07960 317 SGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTA-LIDEQHYARVRQFKQLL 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 42558426 363 QRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQPFF 403
Cdd:PRK07960 396 SSFQRNRDLVSVgayaKGSDPMLDK---AIALWPQLEAFLQQGIF 437
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
49-402 |
2.40e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 113.00 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 49 TDGL-TRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRS--------SAISPIHRSAPA-FTQldtklsifeT 118
Cdd:PRK04196 59 TTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPekrldingAPINPVAREYPEeFIQ---------T 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 119 GIKVVDLLAPYRRGGKIGLFGGAGVgktvpitesinniakAHggvsvfggvgertregNDLYMEM-KESKVINEqnisES 197
Cdd:PRK04196 130 GISAIDGLNTLVRGQKLPIFSGSGL---------------PH----------------NELAAQIaRQAKVLGE----EE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 198 KVALVYGQM------------------------------NEPPGARMRVGSTALTMAEYF---RDVNkqdVLLFIDNIFR 244
Cdd:PRK04196 175 NFAVVFAAMgitfeeanffmedfeetgalersvvflnlaDDPAIERILTPRMALTAAEYLafeKGMH---VLVILTDMTN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 245 FVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQER--ITSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRG 322
Cdd:PRK04196 252 YCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 323 LAAKGIYPAVDPLDSTSTMLQPWIvGEEHY-ETAQGVKQTL----QRYKELQDIIAILGLDELSEEDRLTVARARKIE-R 396
Cdd:PRK04196 332 LHRKGIYPPIDVLPSLSRLMKDGI-GEGKTrEDHKDVANQLyaayARGKDLRELAAIVGEEALSERDRKYLKFADAFErE 410
|
....*.
gi 42558426 397 FLSQPF 402
Cdd:PRK04196 411 FVNQGF 416
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
38-402 |
4.92e-26 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 109.22 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 38 NNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPAFTQLDTKLSIFE 117
Cdd:PRK05922 63 NRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 118 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPIT-------ESINNIAkahggvsvfgGVGERTREGNDlYMEMKESkvin 190
Cdd:PRK05922 143 TGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLStiakgskSTINVIA----------LIGERGREVRE-YIEQHKE---- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 191 eqNISESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLG 270
Cdd:PRK05922 208 --GLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 271 TEMGSLQERITSTKEGSITSIQAV-YVP--ADDLTDPAPATTSAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQPWIV 347
Cdd:PRK05922 285 HHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSARQLAL 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 42558426 348 gEEHYETAQGVKQTLQRYKELQDIIAiLGLDELSEEDRL--TVARARKIERFLSQPF 402
Cdd:PRK05922 360 -PHHYAAAEELRSLLKAYHEALDIIQ-LGAYVPGQDAHLdrAVKLLPSIKQFLSQPL 414
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
64-343 |
5.26e-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: 106.15 E-value: 5.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 64 PLSVPVGETTLGRISNVLGEPVDNLGPVRS--------SAISPIHRSAPAftqldtklSIFETGIKVVDLLAPYRRGGKI 135
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPedyldingPPINPVARIYPE--------EMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 136 GLFGGAGVgktvPITESINNIAKahggvsvfgGVGERTREGNDL---------YMEMKESKVINEQNISESKVALVYGQM 206
Cdd:cd01135 73 PIFSGSGL----PHNELAAQIAR---------QAGVVGSEENFAivfaamgvtMEEARFFKDDFEETGALERVVLFLNLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 207 NEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQER--ITSTK 284
Cdd:cd01135 140 NDPTIERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGR 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 42558426 285 EGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 343
Cdd:cd01135 220 KGSITQIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 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 |
1.87e-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: 92.96 E-value: 1.87e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42558426 1 AFSPGEMPNIYNSLIVKGQNPAgqqvHVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTGAPL 65
Cdd:cd18115 16 EFPEGELPPIYNALEVKGDDGK----KLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
219-400 |
4.51e-23 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 101.40 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 219 TALTMAEYFRDvnkQ--DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQER----IT-STKEGSITSI 291
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 292 QAVYVPADDLTDPapaTTSAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQPWI---VGEEHYETAQGVKQTL 362
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPWWeenVDPDWRELRDEAMDLL 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 42558426 363 QRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 400
Cdd:PRK04192 465 QREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
36-339 |
4.77e-23 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 101.15 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 36 LGNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPAFTQLDTKLSI 115
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 116 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNiakahggvsvfggvgertREGNDLY-----MEMKESKVIN 190
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 191 ------EQNISESKVaLVYGQMNEPPGARMRVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG 264
Cdd:PRK13343 208 vietlrEHGALEYTT-VVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREA 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42558426 265 YQPTLGTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:PRK13343 286 YPGDIFYLHSRLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVS 364
|
|
| 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 42558426 61 TGAPLSVPVGETTLGRISNVLGEPVDNLGPV--------RSSAISPIHRSAPAftqldtklSIFETGIKVVDLLAPYRRG 132
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVlaedyldiNGQPINPYARIYPE--------EMIQTGISAIDVMNSIARG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 133 GKIGLFGGAGVgktvPITESINNIAKAHGGVSVFGGVGERTREGN------DLYMEMKESKVIN---EQNISESKVALVY 203
Cdd:TIGR01040 142 QKIPIFSAAGL----PHNEIAAQICRQAGLVKLPTKDVHDGHEDNfaivfaAMGVNMETARFFKqdfEENGSMERVCLFL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 204 GQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERI--T 281
Cdd:TIGR01040 218 NLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 282 STKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIvGE-----EHYETAQ 356
Cdd:TIGR01040 298 EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSN 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 42558426 357 GVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 400
Cdd:TIGR01040 377 QLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
64-339 |
1.21e-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: 94.18 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 64 PLSVPVGETTLGRISNVLGEPVDNLGPVRSSAIS--------PIHRSAPAFTQLDTKLsIFETGIKVVDLLAPYRRGGKI 135
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGSIFIPrgvnvqrwPVRQPRPVKEKLPPNV-PLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 136 GLFGGAGVGKTVpITESinnIAK-AHGGVSVFGGVGERTREGNDLYMEMKESKV-INEQNISEsKVALVYGQMNEPPGAR 213
Cdd:cd01134 80 AIPGPFGCGKTV-ISQS---LSKwSNSDVVIYVGCGERGNEMAEVLEEFPELKDpITGESLME-RTVLIANTSNMPVAAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 214 MRVGSTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERI-------TSTKEG 286
Cdd:cd01134 155 EASIYTGITIAEYFRDMGY-NVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 42558426 287 SITSIQAVYVPADDLTDPapaTTSAHLDATTV---LSRGLAAKGIYPAVDPLDSTS 339
Cdd:cd01134 234 SVTIVGAVSPPGGDFSEP---VTQATLRIVQVfwgLDKKLAQRRHFPSINWLISYS 286
|
|
| 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 |
1.54e-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: 82.11 E-value: 1.54e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42558426 351 HYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGK 414
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
171-412 |
1.03e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 88.93 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 171 ERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGSTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGS 250
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 251 EVSALLGRMPSAVGYQPTLGTEMGSLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGL 323
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 324 AAKGIYPAVDPLDSTS---TMLQPWI---VGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ER 396
Cdd:PRK14698 851 ARRRHFPAINWLTSYSlyvDAVKDWWhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250
....*....|....*.
gi 42558426 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 |
1.73e-15 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 76.06 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 65 LSVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 144
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 145 KTVPITESINNiakahggvsvfggvgertREGNDLY-----MEMKESKVINEQNISESKVALVY-----GQMNEPPGARM 214
Cdd:cd01132 82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 215 RVGSTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGYQPTlgtemgSLQERITSTKE--- 285
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYLHS------RLLERAAKLSDelg 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 42558426 286 -GSITSIQAVYVPADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVDPLDSTS 339
Cdd:cd01132 217 gGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
39-132 |
3.03e-13 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 71.25 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 39 NEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPAFTQldtKLSIFE- 117
Cdd:PRK09281 69 DNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEp 145
|
90
....*....|....*..
gi 42558426 118 --TGIKVVDLLAPYRRG 132
Cdd:PRK09281 146 lqTGIKAIDAMIPIGRG 162
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
53-309 |
2.24e-12 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 68.14 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 53 TRGMGAVDT----GAPLSVPVGETTLGRISNVLGEPVDNlGP--------VRSSAISPIHRSAPAftqldtklSIFETGI 120
Cdd:PRK02118 58 TRGISTGDEvvflGRPMQVTYSESLLGRRFNGSGKPIDG-GPelegepieIGGPSVNPVKRIVPR--------EMIRTGI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 121 KVVDLLAPYRRGGKIGLFGGAGVgktvPITESINNIAKAHGGVSVFGGVGERTregNDLYMEMKESKvinEQNISESKVA 200
Cdd:PRK02118 129 PMIDVFNTLVESQKIPIFSVSGE----PYNALLARIALQAEADIIILGGMGLT---FDDYLFFKDTF---ENAGALDRTV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 201 LVYGQMNEPPGARMRVGSTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERI 280
Cdd:PRK02118 199 MFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA 278
|
250 260 270
....*....|....*....|....*....|
gi 42558426 281 TSTKE-GSITSIQAVYVPADDLTDPAPATT 309
Cdd:PRK02118 279 VDFEDgGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
36-333 |
3.83e-10 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 61.52 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 36 LGNNEVRAVAMSatDGLT--RGMGAVDTGAPLSVPVGETTLGRISNVLGEPVDNLGPVRSSAISPIHRSAPAFTqldTKL 113
Cdd:CHL00059 45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 114 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVPITESINNiakahggvsvfggvgertREGND---LYMEM--KE 185
Cdd:CHL00059 120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 186 SKVINEQNISESKVALVY-----GQMNEPPGARMRVGSTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMP 260
Cdd:CHL00059 182 SSVAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42558426 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 |
1.01e-08 |
|
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: 51.39 E-value: 1.01e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42558426 2 FSPGEMPNIYNSLIVKGQNpagqQVHVTCEVQQLLGNNEVRAVAMSATDGLTRGMGAVDTG 62
Cdd:pfam02874 13 FGIGRLPGLLNALEVELVE----FGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
3-333 |
3.40e-06 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 49.27 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 3 SPGEMPNIYNSLIVKGQNPAGQQVHVTCEVQQllgNNEVRAVAMSATDGLTRGMGAVDTGAPLSVPVGETTLGRISNVLG 82
Cdd:PTZ00185 56 APGNPGVAYNTIIMIQVSPTTFAAGLVFNLEK---DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 83 EPV---------------DNLGPVRSSAISPIHRSAPAFTQLdtklsifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 147
Cdd:PTZ00185 133 HEVpvglltrsralleseQTLGKVDAGAPNIVSRSPVNYNLL--------TGFKAVDTMIPIGRGQRELIVGDRQTGKTS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 148 PITESINNIAKAHGGVSVFGGVGErtregndLYMEMKE--SKVINEQNISESKVALVY-----GQMNEPPGARMRVGSTA 220
Cdd:PTZ00185 205 IAVSTIINQVRINQQILSKNAVIS-------IYVSIGQrcSNVARIHRLLRSYGALRYttvmaATAAEPAGLQYLAPYSG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42558426 221 LTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLGTEMGSLQERITSTKE----GSITSIQAVYV 296
Cdd:PTZ00185 278 VTMGEYFMNRGRH-CLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVET 356
|
330 340 350
....*....|....*....|....*....|....*..
gi 42558426 297 PADDLTDPAPATTSAHLDATTVLSRGLAAKGIYPAVD 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 42558426 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 |
5.44e-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: 39.29 E-value: 5.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 42558426 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 42558426 347 VGEEHYETAQGVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 401
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
|
|
| |
