|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-466 |
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: 984.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 1 MSSGKIAQVVGPVVDVAFDAGDkLPEINNALIVYKDGDKskKIVLEVALELGDGIIRTIAMESTDGLTRGLEVFDTGRAI 80
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGE-LPAIYNALEVENEGGG--ELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 81 SVPVGTETLGRVFNVLGDTIDLEEPFaEDAPREPIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 160
Cdd:COG0055 80 SVPVGEATLGRIFNVLGEPIDGKGPI-EAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 161 KTVLIQELIHNIAQEHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVE 240
Cdd:COG0055 159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFA 320
Cdd:COG0055 239 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 321 HLDSTTNLERKLTQMGIYPAVDPLASSSRALAPEIVGQEHYDVATEVQRVLQRYRELQDIIAILGMDELSDEEKTLVGRA 400
Cdd:COG0055 319 HLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777826716 401 RRIQFFLSQNFNVAEQFTGMPGSYVPVAETVRGFKEILEGKYDDLPEDAFRNVGPIEDVVEKAKKM 466
Cdd:COG0055 399 RKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKL 464
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-466 |
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: 867.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 2 SSGKIAQVVGPVVDVAFDaGDKLPEINNALIVYkdGDKSKKIVLEVALELGDGIIRTIAMESTDGLTRGLEVFDTGRAIS 81
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFE-QGELPRIYNALKVQ--NRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 82 VPVGTETLGRVFNVLGDTIDLEEPFAEDaPREPIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGK 161
Cdd:TIGR01039 78 VPVGKETLGRIFNVLGEPIDEKGPIPAK-ERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 162 TVLIQELIHNIAQEHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEG 241
Cdd:TIGR01039 157 TVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 242 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFAH 321
Cdd:TIGR01039 237 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 322 LDSTTNLERKLTQMGIYPAVDPLASSSRALAPEIVGQEHYDVATEVQRVLQRYRELQDIIAILGMDELSDEEKTLVGRAR 401
Cdd:TIGR01039 317 LDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERAR 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777826716 402 RIQFFLSQNFNVAEQFTGMPGSYVPVAETVRGFKEILEGKYDDLPEDAFRNVGPIEDVVEKAKKM 466
Cdd:TIGR01039 397 RIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
2-467 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 785.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 2 SSGKIAQVVGPVVDVAFDAGdKLPEINNALIVYKDGDKSKKIVL--EVALELGDGIIRTIAMESTDGLTRGLEVFDTGRA 79
Cdd:CHL00060 15 NLGRITQIIGPVLDVAFPPG-KMPNIYNALVVKGRDTAGQEINVtcEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 80 ISVPVGTETLGRVFNVLGDTIDLEEPFAEDAPRePIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGV 159
Cdd:CHL00060 94 LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTS-PIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 160 GKTVLIQELIHNIAQEHGGISVFTGVGERTREGNDLYWEMKESGVIE-------KTAMVFGQMNEPPGARMRVALTGLTI 232
Cdd:CHL00060 173 GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 233 AEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTD 312
Cdd:CHL00060 253 AEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 313 PAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALAPEIVGQEHYDVATEVQRVLQRYRELQDIIAILGMDELSDE 392
Cdd:CHL00060 333 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777826716 393 EKTLVGRARRIQFFLSQNFNVAEQFTGMPGSYVPVAETVRGFKEILEGKYDDLPEDAFRNVGPIEDVVEKAKKMN 467
Cdd:CHL00060 413 DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLE 487
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-458 |
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: 571.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 4 GKIAQVVGPVVDVAFDagDKLPEINNALIVYKDGDkskkIVLEVALELGDGIIRTIAMESTDGLTRGLEVFDTGRAISVP 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFD--GELPAIHSVLRAGREGE----VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 84 VGTETLGRVFNVLGDTIDLEEPfAEDAPREPIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTV 163
Cdd:TIGR03305 75 VGKPTLSRMFDVFGNTIDRREP-PKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 164 LIQELIHNIAQEHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVEGQD 243
Cdd:TIGR03305 154 LLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 244 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLD 323
Cdd:TIGR03305 234 VLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 324 STTNLERKLTQMGIYPAVDPLASSSRALAPEIVGQEHYDVATEVQRVLQRYRELQDIIAILGMDELSDEEKTLVGRARRI 403
Cdd:TIGR03305 314 ASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1777826716 404 QFFLSQNFNVAEQFTGMPGSYVPVAETVRGFKEILEGKYDDLPEDAFRNVGPIED 458
Cdd:TIGR03305 394 ERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
81-353 |
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: 566.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 81 SVPVGTETLGRVFNVLGDTID-LEEPFAEDapREPIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGV 159
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDeRGPIKAKE--RWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 160 GKTVLIQELIHNIAQEHGGISVFTGVGERTREGNDLYWEMKESGVI-----EKTAMVFGQMNEPPGARMRVALTGLTIAE 234
Cdd:cd01133 79 GKTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 235 YFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPA 314
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 1777826716 315 PATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALAP 353
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
81-350 |
2.90e-123 |
|
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: 359.85 E-value: 2.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 81 SVPVGTETLGRVFNVLGDTIDLEEPFAEDApREPIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 160
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQ-RRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 161 KTVLIQELIHNIAQEHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvE 240
Cdd:cd19476 80 KTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-N 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTK--KGSVTSIQAIYVPADDYTDPAPATA 318
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 1777826716 319 FAHLDSTTNLERKLTQMGIYPAVDPLASSSRA 350
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
135-348 |
1.01e-96 |
|
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: 290.03 E-value: 1.01e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 135 GIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQehgGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQ 214
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 215 MNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITST-- 292
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVkg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1777826716 293 KKGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSS 348
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
355-462 |
1.01e-66 |
|
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: 209.26 E-value: 1.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 355 IVGQEHYDVATEVQRVLQRYRELQDIIAILGMDELSDEEKTLVGRARRIQFFLSQNFNVAEQFTGMPGSYVPVAETVRGF 434
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 1777826716 435 KEILEGKYDDLPEDAFRNVGPIEDVVEK 462
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-438 |
1.12e-63 |
|
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: 212.20 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 3 SGKIAQVVGPVVDVA-FDA--GDklpeinnalIVYKDGDKSKKIVLEVaLELGDGIIRTIAMESTDGLTRGLEVFDTGRA 79
Cdd:COG1157 20 SGRVTRVVGLLIEAVgPDAsiGE---------LCEIETADGRPVLAEV-VGFRGDRVLLMPLGDLEGISPGARVVPTGRP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 80 ISVPVGTETLGRVFNVLGDTIDLEEPFAEDAPRePIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGV 159
Cdd:COG1157 90 LSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERR-PLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 160 GKTVLIQELIHNIAQEhggISVFTGVGERTRE-----GNDLYWE-MKESGVIEKTAmvfgqmNEPPGARMRVALTGLTIA 233
Cdd:COG1157 169 GKSTLLGMIARNTEAD---VNVIALIGERGREvrefiEDDLGEEgLARSVVVVATS------DEPPLMRLRAAYTATAIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 234 EYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTsiqAIY---VPADDY 310
Cdd:COG1157 240 EYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlVEGDDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 311 TDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRaLAPEIVGQEHYDVATEVQRVLQRYRELQDIIAI----LGM 386
Cdd:COG1157 316 NDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISR-VMPDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGS 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1777826716 387 DELSDEEKTLVGrarRIQFFLSQNfnvaeqftgmPGSYVPVAETVRGFKEIL 438
Cdd:COG1157 395 DPELDEAIALIP---AIEAFLRQG----------MDERVSFEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
81-349 |
8.07e-57 |
|
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: 188.92 E-value: 8.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 81 SVPVGTETLGRVFNVLGDTIDLEEPFAEDAPRePIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVG 160
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERR-PLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 161 KTVLIQELIHNIAQEhggISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvE 240
Cdd:cd01136 80 KSTLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-Q 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 241 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDPAPATAFA 320
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRS 235
|
250 260
....*....|....*....|....*....
gi 1777826716 321 HLDSTTNLERKLTQMGIYPAVDPLASSSR 349
Cdd:cd01136 236 ILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-412 |
1.30e-50 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 178.08 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 62 ESTDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFAEDAprEPIHKKAPafDELSTS--SEILETGIKVI 139
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQW--RELDCPPP--SPLTRQpiEQMLTTGIRAI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 140 DLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPP 219
Cdd:PRK06820 155 DGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAAD---VMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 220 GARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTS 299
Cdd:PRK06820 232 LERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 300 IQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALaPEIVGQEHYDVATEVQRVLQRYRELQD 379
Cdd:PRK06820 311 FYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIEL 389
|
330 340 350
....*....|....*....|....*....|....*..
gi 1777826716 380 IIAI----LGMDELSDEEktlVGRARRIQFFLSQNFN 412
Cdd:PRK06820 390 LVRVgeyqAGEDLQADEA---LQRYPAICAFLQQDHS 423
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
66-409 |
2.87e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 171.47 E-value: 2.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 66 GLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPfAEDAPREPIHKKAPAFDELSTSSEILETGIKVIDLLAPY 145
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHP-PEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 146 LKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGND-LYWEMKESGvIEKTAMVFGQMNEPPGARMR 224
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRSAEVD---VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 225 VALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIY 304
Cdd:PRK06936 236 AGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 305 VPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALApEIVGQEHYDVATEVQRVLQRYRELQDIIAI- 383
Cdd:PRK06936 315 VEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIg 393
|
330 340
....*....|....*....|....*....
gi 1777826716 384 ---LGMDELSDEEktlVGRARRIQFFLSQ 409
Cdd:PRK06936 394 eyqKGQDKEADQA---IERIGAIRGFLRQ 419
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
59-376 |
1.36e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 167.08 E-value: 1.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 59 IAMESTDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEepfAEDAPREPIHKKAP---AFdELSTSSEILETG 135
Cdd:PRK06793 68 LPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEE---AENIPLQKIKLDAPpihAF-EREEITDVFETG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 136 IKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGND-LYWEMKESGvIEKTAMVFGQ 214
Cdd:PRK06793 144 IKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD---INVISLVGERGREVKDfIRKELGEEG-MRKSVVVVAT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 215 MNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLATEMGQLQERITSTKK 294
Cdd:PRK06793 220 SDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 295 GSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALApEIVGQEHYDVATEVQRVLQRY 374
Cdd:PRK06793 298 GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIY 376
|
..
gi 1777826716 375 RE 376
Cdd:PRK06793 377 KE 378
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
65-439 |
3.98e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 165.63 E-value: 3.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 65 DGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFaEDAPREPIHKKAPAFDELSTSSEILETGIKVIDLLAP 144
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAI-DYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 145 YLKGGKVGLFGGAGVGKTVLIQELIHN-IAQehggISVFTGVGERTRE---------GNDLywemkesgviEKTAMVFGQ 214
Cdd:PRK08472 154 CGKGQKLGIFAGSGVGKSTLMGMIVKGcLAP----IKVVALIGERGREipefieknlGGDL----------ENTVIVVAT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 215 MNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTK- 293
Cdd:PRK08472 220 SDDSPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEg 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 294 KGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRaLAPEIVGQEHYDVATEVQRVLQR 373
Cdd:PRK08472 299 KGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASR-VMNDIISPEHKLAARKFKRLYSL 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 374 YRELQDIIAI----LGMDELSDEEktlVGRARRIQFFLSQNFNvaEQFtgmpgsyvPVAETVRGFKEILE 439
Cdd:PRK08472 378 LKENEVLIRIgayqKGNDKELDEA---ISKKEFMEQFLKQNPN--ELF--------PFEQTFEQLEEILR 434
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-383 |
1.24e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 164.51 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 4 GKIAQVVGPVVDvafdagDKLPE--INNALIVYKDGDKSKKIVLEVaLELGDGIIRTIAMESTDGLTRGLEVFDTGRAIS 81
Cdd:PRK07721 20 GKVSRVIGLMIE------SKGPEssIGDVCYIHTKGGGDKAIKAEV-VGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 82 VPVGTETLGRVFNVLGDTIDLEE------PFA-EDAPREPIhKKAPAfdelstsSEILETGIKVIDLLAPYLKGGKVGLF 154
Cdd:PRK07721 93 VKVGSGLIGQVLDALGEPLDGSAlpkglaPVStDQDPPNPL-KRPPI-------REPMEVGVRAIDSLLTVGKGQRVGIF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 155 GGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGND-LYWEMKESGvIEKTAMVFGQMNEPPGARMRVALTGLTIA 233
Cdd:PRK07721 165 AGSGVGKSTLMGMIARNTSAD---LNVIALIGERGREVREfIERDLGPEG-LKRSIVVVATSDQPALMRIKGAYTATAIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 234 EYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAIYVPADDYTDP 313
Cdd:PRK07721 241 EYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEP 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 314 APATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALaPEIVGQEHYDVATEVQRVLQRYRELQDIIAI 383
Cdd:PRK07721 320 IADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
63-381 |
2.09e-45 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 163.63 E-value: 2.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 63 STDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLG---DTIDLEEPFAEDAPREPIHKKAPAFDELSTSSEILETGIKVI 139
Cdd:PRK08149 63 NAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGkivERFDAPPTVGPISEERVIDVAPPSYAERRPIREPLITGVRAI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 140 DLLAPYLKGGKVGLFGGAGVGKTVLIQELIhniaqEHGGISVFT-G-VGERTREGNDLYWEMKESGVIEKTAMVFGQMNE 217
Cdd:PRK08149 143 DGLLTCGVGQRMGIFASAGCGKTSLMNMLI-----EHSEADVFViGlIGERGREVTEFVESLRASSRREKCVLVYATSDF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 218 PPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSV 297
Cdd:PRK08149 218 SSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 298 TSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRaLAPEIVGQEHYDVATEVQRVLQRYREL 377
Cdd:PRK08149 297 TAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR-VFGQVTDPKHRQLAAAFRKLLTRLEEL 375
|
....
gi 1777826716 378 QDII 381
Cdd:PRK08149 376 QLFI 379
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
90-385 |
1.08e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 162.09 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 90 GRVFNVLGDTIDLEEPFAEDAPREPIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELi 169
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 170 hniAQEHGGISVFTG-VGERTREGNdlywEMKE---SGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVL 245
Cdd:PRK06002 186 ---ARADAFDTVVIAlVGERGREVR----EFLEdtlADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD-RGENVL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 246 LFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLD 323
Cdd:PRK06002 258 LIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLD 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777826716 324 STTNLERKLTQMGIYPAVDPLASSSRaLAPEIVGQEHYDVATEVQRVLQRYRELQDIIAILG 385
Cdd:PRK06002 338 GHIVLDRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
1-441 |
2.09e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 161.41 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 1 MSSGKIAQVVGpvvdVAFDA-GDKLPEINNALIVYKDGDkskkIVLEVaLELGDGIIRTIAMESTDGLTRGLEVFDTGRA 79
Cdd:PRK08972 24 VASGKLVRVVG----LTLEAtGCRAPVGSLCSIETMAGE----LEAEV-VGFDGDLLYLMPIEELRGVLPGARVTPLGEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 80 ISVPVGTETLGRVFNVLGDTID-LEEPFAEDapREPIHkkAPAFDELSTS--SEILETGIKVIDLLAPYLKGGKVGLFGG 156
Cdd:PRK08972 95 SGLPVGMSLLGRVIDGVGNPLDgLGPIYTDQ--RASRH--SPPINPLSRRpiTEPLDVGVRAINAMLTVGKGQRMGLFAG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 157 AGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGNDLYWE-MKESGViEKTAMVFGQMNEPPGARMRVALTGLTIAEY 235
Cdd:PRK08972 171 SGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEiLGEEGR-ARSVVVAAPADTSPLMRLKGCETATTIAEY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 236 FRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTKKGSVTSIQAIYVPADDYTDP 313
Cdd:PRK08972 247 FRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTVLTEGDDLQDP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 314 APATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRaLAPEIVGQEHYDVATEVQRVLQRYRELQDIIAILGMDELSDEE 393
Cdd:PRK08972 326 IADASRAILDGHIVLSRELADSGHYPAIDIEASISR-VMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQGSDPR 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1777826716 394 KTLVGRAR-RIQFFLSQNFNVAeqftgmpgsyVPVAETVRGFKEILEGK 441
Cdd:PRK08972 405 IDNAIRLQpAMNAFLQQTMKEA----------VPYDMSVNMLKQLAAQC 443
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
63-392 |
4.41e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 157.42 E-value: 4.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 63 STDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEE----PFAE-DAPREPIHKKAPAfdelstsSEILETGIK 137
Cdd:PRK07594 72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRElpdvCWKDyDAMPPPAMVRQPI-------TQPLMTGIR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 138 VIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhniAQEHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNE 217
Cdd:PRK07594 145 AIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC---NAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 218 PPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSV 297
Cdd:PRK07594 222 PALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 298 TSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALaPEIVGQEHYDVATEVQRVLQRYREL 377
Cdd:PRK07594 301 TAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEV 379
|
330
....*....|....*....
gi 1777826716 378 QDIIAI----LGMDELSDE 392
Cdd:PRK07594 380 ELLIRIgeyqRGVDTDTDK 398
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
57-433 |
2.70e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 155.52 E-value: 2.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 57 RTIAM--ESTDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFAEDAPREPIHKKAPAFDELSTSSEILET 134
Cdd:PRK08927 65 RALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 135 GIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTRE-----GNDLYWE-MKESGVIEKT 208
Cdd:PRK08927 145 GVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEgLARSVVVVAT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 209 AmvfgqmNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER 288
Cdd:PRK08927 222 S------DEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLER 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 289 I--TSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALaPEIVGQEHYDVATE 366
Cdd:PRK08927 295 AgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRR 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1777826716 367 VQRVLQRYRELQDIIAILGMDELSDEEktlVGRARR----IQFFLSQNFNVAeqfTGMPGSYVPVAETVRG 433
Cdd:PRK08927 374 ARQLMATYADMEELIRLGAYRAGSDPE---VDEAIRlnpaLEAFLRQGKDEA---TSLAEGYARLAQILGG 438
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
54-409 |
2.09e-41 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 153.00 E-value: 2.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 54 GIIRTIAMES----TDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFAEDAPRePIHKKAPAFDELSTSS 129
Cdd:PRK09099 66 GFSRDVALLSpfgeLGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELV-PVIAAPPDPMSRRMVE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 130 EILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGNDLYWEMKESGVIEKTA 209
Cdd:PRK09099 145 APLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 210 MVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI 289
Cdd:PRK09099 222 VVCATSDRSSIERAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 290 TSTKKGSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALaPEIVGQEHYDVATEVQR 369
Cdd:PRK09099 301 GMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQ 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1777826716 370 VLQRYRELQDIIAI----LGMDELSDEEktlVGRARRIQFFLSQ 409
Cdd:PRK09099 380 LLAKHREVETLLQVgeyrAGSDPVADEA---IAKIDAIRDFLSQ 420
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
63-383 |
5.38e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 152.19 E-value: 5.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 63 STDGLTRGLEVF---DTGRaisVPVGTETLGRVFNVLGDTIDLEEPF-AED-APREPihkkaPAFDELSTS--SEILETG 135
Cdd:PRK05688 84 SVAGIAPGARVVplaDTGR---LPMGMSMLGRVLDGAGRALDGKGPMkAEDwVPMDG-----PTINPLNRHpiSEPLDVG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 136 IKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQM 215
Cdd:PRK05688 156 IRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 216 NEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKG 295
Cdd:PRK05688 233 DDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 296 --SVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALaPEIVGQEHYDVATEVQRVLQR 373
Cdd:PRK05688 312 ggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSR 390
|
330
....*....|
gi 1777826716 374 YRELQDIIAI 383
Cdd:PRK05688 391 YQQSRDLISV 400
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
66-410 |
1.24e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 150.81 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 66 GLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFAEDAPRE----PIH--KKAPAFDelstsseILETGIKVI 139
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQqqlpQIHplQRRAVDT-------PLDVGVNAI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 140 DLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPP 219
Cdd:PRK07196 147 NGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 220 GARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-TSTKKGSVT 298
Cdd:PRK07196 224 LMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 299 SIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALApEIVGQEHYDVATEVQRVLQRYRELQ 378
Cdd:PRK07196 303 AIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIK 381
|
330 340 350
....*....|....*....|....*....|....*.
gi 1777826716 379 DIIA----ILGMDELSDEEktlVGRARRIQFFLSQN 410
Cdd:PRK07196 382 PLIPlggyVAGADPMADQA---VHYYPAITQFLRQE 414
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-412 |
1.02e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 137.65 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 5 KIAQVVGPVVDVAFDAGDKLPEINNalIVYKDGDKSKKIVLEValelGDGIIRTIAMESTDGL-TRGLEVFDTGRAISVP 83
Cdd:PRK04196 6 TVSEIKGPLLFVEGVEGVAYGEIVE--IELPNGEKRRGQVLEV----SEDKAVVQVFEGTTGLdLKDTKVRFTGEPLKLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 84 VGTETLGRVFNVLGDTID-LEEPFAED------APREPIHKKAPafdelstsSEILETGIKVIDLLAPYLKGGKVGLFGG 156
Cdd:PRK04196 80 VSEDMLGRIFDGLGRPIDgGPEIIPEKrldingAPINPVAREYP--------EEFIQTGISAIDGLNTLVRGQKLPIFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 157 AGvgktvliqeLIHN-----IAQ-------EHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARM- 223
Cdd:PRK04196 152 SG---------LPHNelaaqIARqakvlgeEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERIl 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 224 --RVAltgLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER--ITSTKKGSVTS 299
Cdd:PRK04196 223 tpRMA---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 300 IQAIYVPADDYTDPAPatafahlDST---TN----LERKLTQMGIYPAVDPLASSSRaLAPEIVG-----QEHYDVATEV 367
Cdd:PRK04196 300 IPILTMPDDDITHPIP-------DLTgyiTEgqivLSRELHRKGIYPPIDVLPSLSR-LMKDGIGegktrEDHKDVANQL 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1777826716 368 QRVLQRYRELQDIIAILGMDELSDEEKTLVGRARRI-QFFLSQNFN 412
Cdd:PRK04196 372 YAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGFD 417
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
4-383 |
9.40e-34 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 132.21 E-value: 9.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 4 GKIAQVVGPVVDVAfdaGDKLPEINNALIVYKDGDKSKKIVLEVALELGDGIIrTIAMESTDGLTRGLEVF-------DT 76
Cdd:PRK07960 29 GRLTRATGLVLEAT---GLQLPLGATCVIERQNGSETHEVESEVVGFNGQRLF-LMPLEEVEGILPGARVYarnisgeGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 77 GRAISVPVGTETLGRVFNVLGDTIDlEEPFAEDAPREPIHkkAPAFDELSTS--SEILETGIKVIDLLAPYLKGGKVGLF 154
Cdd:PRK07960 105 QSGKQLPLGPALLGRVLDGSGKPLD-GLPAPDTGETGALI--TPPFNPLQRTpiEHVLDTGVRAINALLTVGRGQRMGLF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 155 GGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAE 234
Cdd:PRK07960 182 AGSGVGKSVLLGMMARYTQAD---VIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 235 YFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITS--TKKGSVTSIQAIYVPADDYTD 312
Cdd:PRK07960 259 DFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQD 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1777826716 313 PAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRALApEIVGQEHYDVATEVQRVLQRYRELQDIIAI 383
Cdd:PRK07960 338 PIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
67-409 |
1.04e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 126.17 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 67 LTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFAEdAPREPIHKKAPAFDELSTSSEILETGIKVIDLLAPYL 146
Cdd:PRK05922 77 VALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPK-THLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 147 KGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFTGVGERTREGNDlYWEMKESGVIE-KTAMVFGQMNEPPGARMRV 225
Cdd:PRK05922 156 KGQRIGVFSEPGSGKSSLLSTIAKGSKST---INVIALIGERGREVRE-YIEQHKEGLAAqRTIIIASPAHETAPTKVIA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 226 ALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSVTSIQAI-Y 304
Cdd:PRK05922 232 GRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlH 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 305 VP--ADDYTDPAPATAFAHLdSTTNLERKLTQmgiyPAVDPLASSSRAlAPEIVGQEHYDVATEVQRVLQRYRELQDIIA 382
Cdd:PRK05922 311 YPnhPDIFTDYLKSLLDGHF-FLTPQGKALAS----PPIDILTSLSRS-ARQLALPHHYAAAEELRSLLKAYHEALDIIQ 384
|
330 340 350
....*....|....*....|....*....|.
gi 1777826716 383 ILGMDELSDEEktlVGRARR----IQFFLSQ 409
Cdd:PRK05922 385 LGAYVPGQDAH---LDRAVKllpsIKQFLSQ 412
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
48-349 |
7.06e-31 |
|
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: 120.37 E-value: 7.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 48 ALELGDGIIRTIamesTDGLTRGLEVFDTGRAISVPVGTetlgrvfnvlgdtidleepfaeDAPREPIHKKAPAFDELsT 127
Cdd:cd01134 3 SVELGPGLLGSI----FDGIQRPLEVIAETGSIFIPRGV----------------------NVQRWPVRQPRPVKEKL-P 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 128 SSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEhggISVFTGVGERtreGND----------LYW 197
Cdd:cd01134 56 PNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSD---VVIYVGCGER---GNEmaevleefpeLKD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 198 EMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPT 277
Cdd:cd01134 130 PITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 278 LATEMGQLQERI-------TSTKKGSVTSIQAIYVPADDYTDP-APAT-----AFAHLDsttnleRKLTQMGIYPAVDPL 344
Cdd:cd01134 209 LGARLAEFYERAgrvrclgSPGREGSVTIVGAVSPPGGDFSEPvTQATlrivqVFWGLD------KKLAQRRHFPSINWL 282
|
....*
gi 1777826716 345 ASSSR 349
Cdd:cd01134 283 ISYSK 287
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
47-466 |
2.53e-30 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 123.10 E-value: 2.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 47 VALELGDGIIRTIAMESTDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFAEDApREPIHKKAPAFDELS 126
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATA-RRPLERPAPAIIERD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 127 TSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhnIAQEHGG-ISVFTGVGERTREGNDLYWEMKESGVI 205
Cdd:PRK13343 141 FVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 206 EKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQL 285
Cdd:PRK13343 219 EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 286 QERIT--STKK--GSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSR----ALAPEIvg 357
Cdd:PRK13343 298 LERAAklSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRvggkAQHPAI-- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 358 qehYDVATEVQRVLQRYRELQdIIAILGMDeLSDEEKTLVGRARRIQFFLSQN----FNVAEQ-----------FTGMPg 422
Cdd:PRK13343 376 ---RKESGRLRLDYAQFLELE-AFTRFGGL-LDAGTQKQITRGRRLRELLKQPrfspLSVEEQiallyalneglLDAVP- 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1777826716 423 syvpvAETVRGFKEILEGKYDDLPEDAFRNVGPIEDVVEKAKKM 466
Cdd:PRK13343 450 -----LANIQAFEERLLEKLDARFAALSLALESPRELDEAWLAA 488
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
1-468 |
3.31e-30 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 123.35 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 1 MSSGKIAQVVGPVVDVAFDAGDKLPEI-----------------NNALI-VYKD--GDKSKKIV------LEValELGDG 54
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGGARMYEVvrvgeegligeiiriegDKATIqVYEEtsGIKPGEPVeftgepLSV--ELGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 55 IIRTIamesTDGLTRGLEVFDT------GRAISVP--------------------VGTETLGRV-------------FNV 95
Cdd:PRK04192 80 LLGSI----FDGIQRPLDELAEksgdflERGVYVPaldrekkweftptvkvgdkvEAGDILGTVqetpsiehkimvpPGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 96 LGdTI---------DLEEPFA--EDAPRE----------PIHKKAPAFDELsTSSEILETGIKVIDLLAPYLKGGKVGLF 154
Cdd:PRK04192 156 SG-TVkeivsegdyTVDDTIAvlEDEDGEgveltmmqkwPVRRPRPYKEKL-PPVEPLITGQRVIDTFFPVAKGGTAAIP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 155 GGAGVGKTVLIQELIHNIAQEhggISVFTGVGERtreGNdlywEMKE------------SG--VIEKTAMVFGQMNEPPG 220
Cdd:PRK04192 234 GPFGSGKTVTQHQLAKWADAD---IVIYVGCGER---GN----EMTEvleefpelidpkTGrpLMERTVLIANTSNMPVA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 221 ARMRVALTGLTIAEYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER----IT-STKKG 295
Cdd:PRK04192 304 AREASIYTGITIAEYYRDM-GYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 296 SVTSIQAIYVPADDYTDP-APAT-----AFAHLDsttnleRKLTQMGIYPAVDPLASSSR---ALAP---EIVGQEHYDV 363
Cdd:PRK04192 383 SVTIIGAVSPPGGDFSEPvTQNTlrivkVFWALD------AELADRRHFPAINWLTSYSLyldQVAPwweENVDPDWREL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 364 ATEVQRVLQRYRELQDIIAILGMDELSDEEKTLVGRARRIQF-FLSQN-FNVAEqftgmpgSYVPVAETVRGFKEILegK 441
Cdd:PRK04192 457 RDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIREdFLQQNaFDPVD-------TYCPPEKQYEMLKLIL--T 527
|
570 580 590
....*....|....*....|....*....|..
gi 1777826716 442 YDDLPEDAFRNVGPIE-----DVVEKAKKMNY 468
Cdd:PRK04192 528 FYDEAFKALEKGVPVSeilelEVRDRIARLKY 559
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
82-349 |
8.58e-30 |
|
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: 117.32 E-value: 8.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 82 VPVGTETLGRVFNVLGDTID-LEEPFAED------APREPIHKKAPafdelstsSEILETGIKVIDLLAPYLKGGKVGLF 154
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDgGPPILPEDyldingPPINPVARIYP--------EEMIQTGISAIDVMNTLVRGQKLPIF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 155 GGAGvgktvliqeLIHN-----IA-------QEHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGAR 222
Cdd:cd01135 76 SGSG---------LPHNelaaqIArqagvvgSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIER 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 223 MRVALTGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQER--ITSTKKGSVTSI 300
Cdd:cd01135 147 IITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQI 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1777826716 301 QAIYVPADDYTDPAPatafahlDST---TN----LERKLTQMGIYPAVDPLASSSR 349
Cdd:cd01135 227 PILTMPNDDITHPIP-------DLTgyiTEgqiyLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
2-80 |
2.22e-29 |
|
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: 109.91 E-value: 2.22e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1777826716 2 SSGKIAQVVGPVVDVAFDAGdKLPEINNALIVykDGDKSKKIVLEVALELGDGIIRTIAMESTDGLTRGLEVFDTGRAI 80
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEG-ELPPIYNALEV--KGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
6-394 |
8.48e-23 |
|
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: 100.57 E-value: 8.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 6 IAQVVGPVVDVAFDAGDKLPEINNalIVYKDGDKSKKIVLEVAlelGDGIIRTIaMESTDGL-TRGLEVFDTGRAISVPV 84
Cdd:TIGR01040 5 VSGVNGPLVILDNVKFPRFAEIVN--LTLPDGTVRSGQVLEVS---GNKAVVQV-FEGTSGIdAKKTTCEFTGDILRTPV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 85 GTETLGRVFNVLGDTIDLEEP-FAE---DAPREPIHKKAPAFDElstssEILETGIKVIDLLAPYLKGGKVGLFGGAGV- 159
Cdd:TIGR01040 79 SEDMLGRVFNGSGKPIDKGPPvLAEdylDINGQPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKIPIFSAAGLp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 160 ------------GKTVLIQELIHNIAQEHGGIsVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVAL 227
Cdd:TIGR01040 154 hneiaaqicrqaGLVKLPTKDVHDGHEDNFAI-VFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 228 TGLTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI--TSTKKGSVTSIQAIYV 305
Cdd:TIGR01040 233 LALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQIPILTM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 306 PADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSR----ALAPEIVGQEHYDVATEVQRVLQRYRELQDII 381
Cdd:TIGR01040 313 PNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRlmksAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMK 392
|
410
....*....|...
gi 1777826716 382 AILGMDELSDEEK 394
Cdd:TIGR01040 393 AVVGEEALSSEDL 405
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
168-461 |
1.29e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 101.64 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 168 LIHNIAQEH-------GGISVFTGVGERTREGNDLYWEMKE-------SGVIEKTAMVFGQMNEPPGARMRVALTGLTIA 233
Cdd:PRK14698 666 LLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 234 EYFRDVeGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERI-------TSTKKGSVTSIQAIYVP 306
Cdd:PRK14698 746 EYFRDM-GYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPP 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 307 ADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSrALAPEIVGQEHYDVATEVQR-------VLQRYRELQD 379
Cdd:PRK14698 825 GGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS-LYVDAVKDWWHKNVDPEWKAmrdkameLLQKEAELQE 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 380 IIAILGMDELSDEEKT--LVGRARRIQFFLSQNFNVAEqftgmpgSYVPVAETVRGFKeILEGKYDDLPEDAFRNVgPIE 457
Cdd:PRK14698 904 IVRIVGPDALPERERAilLVARMLREDYLQQDAFDEVD-------TYCPPEKQVTMMR-VLLNFYDKTMDAISRGV-PLE 974
|
....
gi 1777826716 458 DVVE 461
Cdd:PRK14698 975 EIAK 978
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
80-349 |
1.15e-21 |
|
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: 94.55 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 80 ISVPVGTETLGRVFNVLGDTIDLEEPFAEDAPRePIHKKAPAFDELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGV 159
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERR-RVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 160 GKTVLIQELIHNiAQEHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDv 239
Cdd:cd01132 81 GKTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 240 EGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKK----GSVTSIQAIYVPADDYTDPAP 315
Cdd:cd01132 159 NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPIIETQAGDVSAYIP 238
|
250 260 270
....*....|....*....|....*....|....
gi 1777826716 316 ATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSR 349
Cdd:cd01132 239 TNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-315 |
1.54e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 84.70 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 5 KIAQVVGPVVDVAFDaGDKLPEInnALIVYKDGDKSKKIVL----EVALELGDGiirtiamesTDGLTRGLEVFDTGRAI 80
Cdd:PRK02118 7 KITDITGNVITVEAE-GVGYGEL--ATVERKDGSSLAQVIRldgdKVTLQVFGG---------TRGISTGDEVVFLGRPM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 81 SVPVGTETLGRVFNVLGDTIDLE-EPFAEDAP-----REPIHKKAPafdelstsSEILETGIKVIDLLAPYLKGGKVGLF 154
Cdd:PRK02118 75 QVTYSESLLGRRFNGSGKPIDGGpELEGEPIEiggpsVNPVKRIVP--------REMIRTGIPMIDVFNTLVESQKIPIF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 155 GGAGVGktvlIQELIHNIA-QEHGGISVFTGVGERtregNDLYW----EMKESGVIEKTAMVFGQMNEPPGARMRVALTG 229
Cdd:PRK02118 147 SVSGEP----YNALLARIAlQAEADIIILGGMGLT----FDDYLffkdTFENAGALDRTVMFIHTASDPPVECLLVPDMA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 230 LTIAEYFRDVEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKK-GSVTSIQAIYVPAD 308
Cdd:PRK02118 219 LAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDgGSITIIAVTTMPGD 298
|
....*..
gi 1777826716 309 DYTDPAP 315
Cdd:PRK02118 299 DVTHPVP 305
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
53-377 |
6.70e-16 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 80.08 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 53 DGIIRTIAMESTDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDL------EEPFAEDAPREPIHKKAPAFDELS 126
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVglltrsRALLESEQTLGKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 127 TSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHN-------IAQEHGGISVFTGVGERTREGNDLYWEM 199
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 200 KESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLA 279
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 280 TEMGQLQER--ITSTKK--GSVTSIQAIYVPADDYTDPAPATAFAHLDSTTNLERKLTQMGIYPAVDPLASSSRaLAPEI 355
Cdd:PTZ00185 327 YLHSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR-VGSSA 405
|
330 340
....*....|....*....|..
gi 1777826716 356 VGQEHYDVATEVQRVLQRYREL 377
Cdd:PTZ00185 406 QNVAMKAVAGKLKGILAEYRKL 427
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
360-419 |
8.37e-16 |
|
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: 71.71 E-value: 8.37e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 360 HYDVATEVQRVLQRYRELQDIIAILGMDELSDEEKTLVGRARRIQFFLSQNFNVAEQFTG 419
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIED 60
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
63-269 |
4.67e-15 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 77.39 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 63 STDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFAEDApREPIHKKAPAFDELSTSSEILETGIKVIDLL 142
Cdd:COG0056 78 DYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEE-RRPVERPAPGVIDRQPVHEPLQTGIKAIDAM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 143 APylkggkVG------LFGGAGVGKTVLIQELIhnIAQEHGG-ISVFTGVGERT----REGNDLywemKESGVIEKTAMV 211
Cdd:COG0056 157 IP------IGrgqrelIIGDRQTGKTAIAIDTI--INQKGKDvICIYVAIGQKAstvaQVVETL----EEHGAMEYTIVV 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1777826716 212 FGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 269
Cdd:COG0056 225 AATASDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRPP 281
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-77 |
6.12e-15 |
|
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: 69.50 E-value: 6.12e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1777826716 6 IAQVVGPVVDVAFDAGdKLPEINNALIVykDGDKSKKIVLEVALELGDGIIRTIAMESTDGLTRGLEVFDTG 77
Cdd:pfam02874 1 IVQVIGPVVDVEFGIG-RLPGLLNALEV--ELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
44-269 |
1.60e-12 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 69.32 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 44 VLEVALELGDGIIRTIAMESTDGLTRGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFAEDApREPIHKKAPAFD 123
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATE-TRPVERKAPGVI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 124 ELSTSSEILETGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhnIAQEHGG-ISVFTGVGER------TREgndly 196
Cdd:PRK09281 138 DRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTI--INQKGKDvICIYVAIGQKastvaqVVR----- 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1777826716 197 wEMKESGVIEKTAMVFGQMNEPPGARMRVALTGLTIAEYFRDvEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 269
Cdd:PRK09281 211 -KLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
65-269 |
4.05e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 68.07 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 65 DGLT--RGLEVFDTGRAISVPVGTETLGRVFNVLGDTIDLEEPFAEDAPRePIHKKAPAFDELSTSSEILETGIKVIDLL 142
Cdd:CHL00059 57 DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESR-LIESPAPGIISRRSVYEPLQTGLIAIDSM 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 143 APYLKGGKVGLFGGAGVGKTVLIQELIHNiAQEHGGISVFTGVGERTREGNDLYWEMKESGVIEKTAMVFGQMNEPPGAR 222
Cdd:CHL00059 136 IPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQ 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1777826716 223 MRVALTGLTIAEYFRdVEGQDVLLFIDNIFRFTQAGSEVSALLGRMP 269
Cdd:CHL00059 215 YLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
111-349 |
1.13e-11 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 66.26 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 111 PREPIHKKAPAfDELSTsseiletgiKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFTG-VGERT 189
Cdd:PRK12608 106 PRERLRLETGS-DDLSM---------RVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 190 REGNDlyweMKESgvieKTAMVFGQMNEPPGARmRVALTGLTIAEYFRDVE-GQDVLLFIDNIFRFTQAGSEVSALLGRM 268
Cdd:PRK12608 176 EEVTD----MRRS----VKGEVYASTFDRPPDE-HIRVAELVLERAKRLVEqGKDVVILLDSLTRLARAYNNEVESSGRT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 269 PSAvgyqpTLATEMGQLQERITSTKK-----GSVTSIQAIYVP----ADDYTdpapataFAHLDSTTNLE----RKLTQM 335
Cdd:PRK12608 247 LSG-----GVDARALQRPKRLFGAARnieegGSLTIIATALVDtgsrMDEVI-------FEEFKGTGNMEivldRELADK 314
|
250
....*....|....
gi 1777826716 336 GIYPAVDPLASSSR 349
Cdd:PRK12608 315 RVFPAIDIAKSGTR 328
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
137-349 |
4.08e-08 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 54.13 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 137 KVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFTG-VGERTREGNDlyweMKESGVIEKTAMVFgqm 215
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSVKGEVVASTF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 216 NEPPGARMRVALTGLTIAEyfRDVE-GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTlATEMGQlqeRITSTKK 294
Cdd:cd01128 78 DEPPERHVQVAEMVIEKAK--RLVEhGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDAN-ALHKPK---RFFGAAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777826716 295 -----GSVTSIQAIYVPADDYTDPApatAFAHLDSTTNLE----RKLTQMGIYPAVDPLASSSR 349
Cdd:cd01128 151 nieegGSLTIIATALVDTGSRMDEV---IFEEFKGTGNMElvldRKLAEKRIFPAIDILKSGTR 211
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
125-349 |
2.55e-06 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 49.69 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 125 LSTSSEILETgiKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFTG-VGERTREGNDlyweMKESG 203
Cdd:TIGR00767 147 LETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLlIDERPEEVTD----MQRSV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 204 VIEKTAMVFgqmNEPPGARMRVAltGLTIAEYFRDVE-GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLAtem 282
Cdd:TIGR00767 221 KGEVVASTF---DEPASRHVQVA--EMVIEKAKRLVEhKKDVVILLDSITRLARAYNTVTPASGKVLSG-GVDANAL--- 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1777826716 283 gQLQERITSTKK-----GSVTSIQAIYVPADDYTDpapATAFAHLDSTTNLE----RKLTQMGIYPAVDPLASSSR 349
Cdd:TIGR00767 292 -HRPKRFFGAARnieegGSLTIIATALIDTGSRMD---EVIFEEFKGTGNMElhldRKLADRRIFPAIDIKKSGTR 363
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
147-268 |
6.99e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.83 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 147 KGGKVGLFGGAGVGKTVLIQELIHNIAQEHGGISVFTGvgertregndlywEMKESGVIEKTAMVFGQMNEPPGARMRVA 226
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1777826716 227 LTGLTIAEYFRdvegqDVLLFIDNIFRFTQAGSEVSALLGRM 268
Cdd:smart00382 68 RLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-78 |
2.31e-05 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 42.30 E-value: 2.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1777826716 4 GKIAQVVGPVVDVAFDagdKLPEINNALIVYKDGDKSKKIVLEVALELGDGIIRTIAMESTDGLTRGLEVFDTGR 78
Cdd:cd01426 2 GRVIRVNGPLVEAELE---GEVAIGEVCEIERGDGNNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
98-349 |
1.40e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 43.98 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 98 DTIDLEEPfaEDAprepihKKAPAFDELS----TSSEILETGI------KVIDLLAPYLKGGKvGLFggagV-----GKT 162
Cdd:PRK09376 117 ETVNGEDP--EKA------RNRPLFENLTplypNERLRLETGNpedlstRIIDLIAPIGKGQR-GLI----VappkaGKT 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 163 VLIQELIHNIAQEHGGISVFTG-VGERTREGNDlyweMKES---GVIEKTamvfgqMNEPPGARMRVAltGLTIAEYFRD 238
Cdd:PRK09376 184 VLLQNIANSITTNHPEVHLIVLlIDERPEEVTD----MQRSvkgEVVAST------FDEPAERHVQVA--EMVIEKAKRL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 239 VE-GQDVLLFIDNIFRFTQAGSEVSALLGRM------PSAVgYQPT------LATEMGqlqeritstkkGSVTSIqaiyv 305
Cdd:PRK09376 252 VEhGKDVVILLDSITRLARAYNTVVPSSGKVlsggvdANAL-HRPKrffgaaRNIEEG-----------GSLTII----- 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 306 paddytdpapATA------------FAHLDSTTN----LERKLTQMGIYPAVDPLASSSR 349
Cdd:PRK09376 315 ----------ATAlidtgsrmdeviFEEFKGTGNmelhLDRKLAEKRIFPAIDINRSGTR 364
|
|
| 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 ... |
365-410 |
2.36e-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: 37.37 E-value: 2.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1777826716 365 TEVQRVLQRYRELQDIIAILGMDELSDEEK-TL-VGRARRiQFFLSQN 410
Cdd:cd18111 6 TEAMEILQEEAELQEIVQLVGPDALPEEDRlTLeVARMIR-EDFLQQN 52
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
112-201 |
7.72e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 38.85 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777826716 112 REPIHKKAPAFDELSTSSEILeTGIKVIDLLAPYLKGGKVGLFGGAGVGKTVLIQELIhnIAQEHGGISV------FTGV 185
Cdd:PRK14698 192 RWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDGDTLI--LTKEFGLIKIkdlyeiLDGK 268
|
90
....*....|....*.
gi 1777826716 186 GERTREGNDLYWEMKE 201
Cdd:PRK14698 269 GKKTVEGNEEWTELEE 284
|
|
| |
