|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-465 |
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: 1002.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 1 MANTGKIAQVIGAVVDVEFADGNLPNILSALEIKNPNNIDapvLICEVAQHLGNNVVRTIAMDATEGLVRGMSALDLGQP 80
Cdd:COG0055 2 AMNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGGGE---LVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 81 ISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVG 160
Cdd:COG0055 79 ISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 161 KTVILMEMINNIAKQHGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDEE 240
Cdd:COG0055 159 KTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 241 GQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPATTFS 320
Cdd:COG0055 239 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 321 HLDGTLVLSRQIAELGIYPAVDPLDSTSRILSPDVLGVEHYATAREVQAVLQKYKELQDIIAILGMDELGDDDKTTVARA 400
Cdd:COG0055 319 HLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1782519476 401 RRIQRFLSQPFHVAEVFTGVAGKYVKTEDTVKAFRDILDGKYDDLPEQAFYMCGGIEEAIEKAKQ 465
Cdd:COG0055 399 RKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKK 463
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
3-465 |
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: 873.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 3 NTGKIAQVIGAVVDVEFADGNLPNILSALEIKNPNNIDapvLICEVAQHLGNNVVRTIAMDATEGLVRGMSALDLGQPIS 82
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAESE---LTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 83 VPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKT 162
Cdd:TIGR01039 78 VPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 163 VILMEMINNIAKQHGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDEEGQ 242
Cdd:TIGR01039 158 VLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 243 DVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPATTFSHL 322
Cdd:TIGR01039 238 DVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 323 DGTLVLSRQIAELGIYPAVDPLDSTSRILSPDVLGVEHYATAREVQAVLQKYKELQDIIAILGMDELGDDDKTTVARARR 402
Cdd:TIGR01039 318 DATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARR 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1782519476 403 IQRFLSQPFHVAEVFTGVAGKYVKTEDTVKAFRDILDGKYDDLPEQAFYMCGGIEEAIEKAKQ 465
Cdd:TIGR01039 398 IQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKK 460
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
3-464 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 837.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 3 NTGKIAQVIGAVVDVEFADGNLPNILSALEIKNPNNIDAPVLI-CEVAQHLGNNVVRTIAMDATEGLVRGMSALDLGQPI 81
Cdd:CHL00060 15 NLGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQEINVtCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 82 SVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGK 161
Cdd:CHL00060 95 SVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 162 TVILMEMINNIAKQHGGISVFAGVGERTREGNDLYHEMKDAGVLE-------KAALVYGQMNEPPGARARVALTALTCAE 234
Cdd:CHL00060 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 235 YFRDEEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPA 314
Cdd:CHL00060 255 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 315 PATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSPDVLGVEHYATAREVQAVLQKYKELQDIIAILGMDELGDDDK 394
Cdd:CHL00060 335 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 395 TTVARARRIQRFLSQPFHVAEVFTGVAGKYVKTEDTVKAFRDILDGKYDDLPEQAFYMCGGIEEAIEKAK 464
Cdd:CHL00060 415 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAA 484
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
5-459 |
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: 586.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 5 GKIAQVIGAVVDVEFaDGNLPNILSALEIKNPNNIdapvlICEVAQHLGNNVVRTIAMDATEGLVRGMSALDLGQPISVP 84
Cdd:TIGR03305 1 GHVVAVRGSIVDVRF-DGELPAIHSVLRAGREGEV-----VVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 85 VGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVI 164
Cdd:TIGR03305 75 VGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 165 LMEMINNIAKQHGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDEEGQDV 244
Cdd:TIGR03305 155 LTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 245 LLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPATTFSHLDG 324
Cdd:TIGR03305 235 LLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 325 TLVLSRQIAELGIYPAVDPLDSTSRILSPDVLGVEHYATAREVQAVLQKYKELQDIIAILGMDELGDDDKTTVARARRIQ 404
Cdd:TIGR03305 315 SLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLE 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1782519476 405 RFLSQPFHVAEVFTGVAGKYVKTEDTVKAFRDILDGKYDDLPEQAFYMCGGIEEA 459
Cdd:TIGR03305 395 RFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
82-353 |
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: 583.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 82 SVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGK 161
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 162 TVILMEMINNIAKQHGGISVFAGVGERTREGNDLYHEMKDAGV-----LEKAALVYGQMNEPPGARARVALTALTCAEYF 236
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVinldgLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 237 RDEEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPA 316
Cdd:cd01133 161 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1782519476 317 TTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSP 353
Cdd:cd01133 241 TTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
82-350 |
4.76e-133 |
|
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: 384.89 E-value: 4.76e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 82 SVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGK 161
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 162 TVILMEMINNIAKQHGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDeEG 241
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-NG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 242 QDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTN--KGSITSVQAVYVPADDLTDPAPATTF 319
Cdd:cd19476 160 QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 1782519476 320 SHLDGTLVLSRQIAELGIYPAVDPLDSTSRI 350
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
135-348 |
1.80e-101 |
|
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: 301.97 E-value: 1.80e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 135 GIKVVDLLIPFPKGGKMGLFGGAGVGKTVILMEMINNIAKQhggISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQ 214
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD---VVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 215 MNEPPGARARVALTALTCAEYFRDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTN- 293
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1782519476 294 -KGSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTS 348
Cdd:pfam00006 157 kGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
4-438 |
3.45e-73 |
|
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: 236.85 E-value: 3.45e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 4 TGKIAQVIGAVVDVEfadGNLPNILSALEIKNPNNidaPVLICEVaqhLGNNVVRTIAM--DATEGLVRGMSALDLGQPI 81
Cdd:COG1157 20 SGRVTRVVGLLIEAV---GPDASIGELCEIETADG---RPVLAEV---VGFRGDRVLLMplGDLEGISPGARVVPTGRPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 82 SVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGK 161
Cdd:COG1157 91 SVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 162 TViLMEMinnIAKQ-HGGISVFAGVGERTREGND-LYHEMKDAGvLEKAALVYGQMNEPPGARARVALTALTCAEYFRDe 239
Cdd:COG1157 171 ST-LLGM---IARNtEADVNVIALIGERGREVREfIEDDLGEEG-LARSVVVVATSDEPPLMRLRAAYTATAIAEYFRD- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 240 EGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPATTF 319
Cdd:COG1157 245 QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 320 SHLDGTLVLSRQIAELGIYPAVDPLDSTSRILsPDVLGVEHYATAREVQAVLQKYKELQDIIAI----LGMDELGDddkT 395
Cdd:COG1157 325 GILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDPELD---E 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1782519476 396 TVARARRIQRFLSQPFHVAEVFtgvagkyvktEDTVKAFRDIL 438
Cdd:COG1157 401 AIALIPAIEAFLRQGMDERVSF----------EESLAQLAELL 433
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
355-462 |
3.07e-70 |
|
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: 218.12 E-value: 3.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 355 VLGVEHYATAREVQAVLQKYKELQDIIAILGMDELGDDDKTTVARARRIQRFLSQPFHVAEVFTGVAGKYVKTEDTVKAF 434
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 1782519476 435 RDILDGKYDDLPEQAFYMCGGIEEAIEK 462
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
82-350 |
9.37e-66 |
|
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: 212.03 E-value: 9.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 82 SVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGK 161
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 162 TViLMEMINNIAKqhGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDEeG 241
Cdd:cd01136 81 ST-LLGMIARNTD--ADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQ-G 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 242 QDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPATTFSH 321
Cdd:cd01136 157 KKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSI 236
|
250 260
....*....|....*....|....*....
gi 1782519476 322 LDGTLVLSRQIAELGIYPAVDPLDSTSRI 350
Cdd:cd01136 237 LDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
66-409 |
4.62e-57 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 194.90 E-value: 4.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 66 EGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPF 145
Cdd:PRK08472 75 EGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTC 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 146 PKGGKMGLFGGAGVGKTViLMEMINNIAKqhGGISVFAGVGERTREGNDLYHEMKDaGVLEKAALVYGQMNEPPGARARV 225
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKST-LMGMIVKGCL--APIKVVALIGERGREIPEFIEKNLG-GDLENTVIVVATSDDSPLMRKYG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 226 ALTALTCAEYFRDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITST-NKGSITSVQAVY 304
Cdd:PRK08472 231 AFCAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEeGKGSITAFFTVL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 305 VPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSpDVLGVEHYATAREVQAVLQKYKELQDIIAI- 383
Cdd:PRK08472 310 VEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIg 388
|
330 340
....*....|....*....|....*....
gi 1782519476 384 ---LGMDELGDDdktTVARARRIQRFLSQ 409
Cdd:PRK08472 389 ayqKGNDKELDE---AISKKEFMEQFLKQ 414
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
78-412 |
1.26e-56 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 193.82 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 78 GQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGA 157
Cdd:PRK06936 92 GTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 158 GVGKTVILMEMINNIAKQhggISVFAGVGERTREGND-LYHEMKDAGvLEKAALVYGQMNEPPGARARVALTALTCAEYF 236
Cdd:PRK06936 172 GGGKSTLLASLIRSAEVD---VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYF 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 237 RDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPA 316
Cdd:PRK06936 248 RDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVAD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 317 TTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSpDVLGVEHYATAREVQAVLQKYKELQDIIAI----LGMDELGDD 392
Cdd:PRK06936 327 ETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ 405
|
330 340
....*....|....*....|
gi 1782519476 393 dktTVARARRIQRFLSQPFH 412
Cdd:PRK06936 406 ---AIERIGAIRGFLRQGTH 422
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
35-411 |
3.41e-55 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 189.82 E-value: 3.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 35 NPNNIDAPVL-----------ICEV------------AQHLGNNVVRTI--AMDATEGLVRGMSALDLGQPISVPVGKGS 89
Cdd:PRK08149 9 HPLRIQGPIIeaelpdvaigeICEIragwhsneviarAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 90 LGRIMNVVGEPADEMGPVPCD----KRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTViL 165
Cdd:PRK08149 89 LGAVLDPTGKIVERFDAPPTVgpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTS-L 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 166 MEMInnIAKQHGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDeEGQDVL 245
Cdd:PRK08149 168 MNML--IEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 246 LFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPATTFSHLDGT 325
Cdd:PRK08149 245 LFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 326 LVLSRQIAELGIYPAVDPLDSTSRILSpDVLGVEHYATAREVQAVLQKYKELQDIIAiLGMDELGDDDKTTVARARR--I 403
Cdd:PRK08149 325 IYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGEYRRGENADNDRAMDKRpaL 402
|
....*...
gi 1782519476 404 QRFLSQPF 411
Cdd:PRK08149 403 EAFLKQDV 410
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
24-409 |
8.87e-55 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 188.87 E-value: 8.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 24 LPNI-LSALEIKNPNNIDAPVLICEvaqhlGNNVVRTiAMDATEGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPAD 102
Cdd:PRK06820 45 LPGVaQGELCRIEPQGMLAEVVSIE-----QEMALLS-PFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 103 EMGPVPCDKRlPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTViLMEMInnIAKQHGGISVF 182
Cdd:PRK06820 119 GGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKST-LLGML--CADSAADVMVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 183 AGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDEeGQDVLLFVDNIFRFTQAGAEVS 262
Cdd:PRK06820 195 ALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 263 ALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVD 342
Cdd:PRK06820 274 LAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAID 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1782519476 343 PLDSTSRILsPDVLGVEHYATAREVQAVLQKYKELQDIIAIlGMDELGDDDKT--TVARARRIQRFLSQ 409
Cdd:PRK06820 354 IAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRV-GEYQAGEDLQAdeALQRYPAICAFLQQ 420
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
67-383 |
1.07e-54 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 188.76 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 67 GLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFP 146
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 147 KGGKMGLFGGAGVGKTVILMEMINNIAKQhggISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVA 226
Cdd:PRK08972 161 KGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 227 LTALTCAEYFRDeEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERI--TSTNKGSITSVQAVY 304
Cdd:PRK08972 238 ETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTVL 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1782519476 305 VPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILsPDVLGVEHYATAREVQAVLQKYKELQDIIAI 383
Cdd:PRK08972 317 TEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
2-439 |
6.45e-53 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 183.82 E-value: 6.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 2 ANTGKIAQVIGAVVDVEFADGNLPNILsalEIKNPnniDAPVLICEVAQHLGNNVVRTIAMDATEGLVRGMSALDLGQPI 81
Cdd:PRK09099 23 RRTGKVVEVIGTLLRVSGLDVTLGELC---ELRQR---DGTLLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 82 SVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGK 161
Cdd:PRK09099 97 SVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 162 TViLMEMINNIAKqhGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDeEG 241
Cdd:PRK09099 177 ST-LMGMFARGTQ--CDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRD-RG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 242 QDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPATTFSH 321
Cdd:PRK09099 253 LRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVRGI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 322 LDGTLVLSRQIAELGIYPAVDPLDSTSRILsPDVLGVEHYATAREVQAVLQKYKELQDIIAI----LGMDELGDDdktTV 397
Cdd:PRK09099 333 LDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE---AI 408
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1782519476 398 ARARRIQRFLSQPfhvaevftgvAGKYVKTEDTVKAFRDILD 439
Cdd:PRK09099 409 AKIDAIRDFLSQR----------TDEYSDPDATLAALAELSG 440
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
78-383 |
1.04e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 177.99 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 78 GQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGA 157
Cdd:PRK07721 88 GKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 158 GVGKTViLMEMInniAKQ-HGGISVFAGVGERTREGNDLYHemKDAGV--LEKAALVYGQMNEPPGARARVALTALTCAE 234
Cdd:PRK07721 168 GVGKST-LMGMI---ARNtSADLNVIALIGERGREVREFIE--RDLGPegLKRSIVVVATSDQPALMRIKGAYTATAIAE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 235 YFRDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQAVYVPADDLTDPA 314
Cdd:PRK07721 242 YFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPI 320
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1782519476 315 PATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSpDVLGVEHYATAREVQAVLQKYKELQDIIAI 383
Cdd:PRK07721 321 ADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMN-HIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
40-409 |
1.10e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 177.86 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 40 DAPVLICEVaqhLGNNVVRTIAM--DATEGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVP-CDKRLPIH 116
Cdd:PRK08927 50 GGRPVPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPqGPVPYPLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 117 RPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVILMEMINNIAKQhggISVFAGVGERTREGNDLY 196
Cdd:PRK08927 127 APPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 197 HEmkDAGV--LEKAALVYGQMNEPPGARARVALTALTCAEYFRDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGY 274
Cdd:PRK08927 204 QD--DLGPegLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 275 QPTLGTDLGGLQERIT--STNKGSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILs 352
Cdd:PRK08927 281 TPTVFAELPRLLERAGpgPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM- 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1782519476 353 PDVLGVEHYATAREVQAVLQKYKELQDIIAiLGMDELGDDDKT--TVARARRIQRFLSQ 409
Cdd:PRK08927 360 PGCNDPEENPLVRRARQLMATYADMEELIR-LGAYRAGSDPEVdeAIRLNPALEAFLRQ 417
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
64-409 |
1.21e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 175.30 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 64 ATEGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLI 143
Cdd:PRK05688 84 SVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 144 PFPKGGKMGLFGGAGVGKTViLMEMINNIAKqhGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARA 223
Cdd:PRK05688 164 TVGRGQRLGLFAGTGVGKSV-LLGMMTRFTE--ADIIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 224 RVALTALTCAEYFRDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKG--SITSVQ 301
Cdd:PRK05688 241 RAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGggSITAFY 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 302 AVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILsPDVLGVEHYATAREVQAVLQKYKELQDII 381
Cdd:PRK05688 320 TVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSRYQQSRDLI 398
|
330 340 350
....*....|....*....|....*....|
gi 1782519476 382 AIlGMDELGDDDKTTVARAR--RIQRFLSQ 409
Cdd:PRK05688 399 SV-GAYVAGGDPETDLAIARfpHLVQFLRQ 427
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
91-385 |
1.39e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 175.19 E-value: 1.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 91 GRIMNVVGEPADEMGPV-PCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVILMEMi 169
Cdd:PRK06002 107 GRVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 170 nniAKQHGGISV-FAGVGERTREgndlYHEMKD---AGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDEeGQDVL 245
Cdd:PRK06002 186 ---ARADAFDTVvIALVGERGRE----VREFLEdtlADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR-GENVL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 246 LFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERI--TSTNKGSITSVQAVYVPADDLTDPAPATTFSHLD 323
Cdd:PRK06002 258 LIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLD 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1782519476 324 GTLVLSRQIAELGIYPAVDPLDSTSRiLSPDVLGVEHYATAREVQAVLQKYKELQDIIAILG 385
Cdd:PRK06002 338 GHIVLDRAIAEQGRYPAVDPLASISR-LARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
44-376 |
8.54e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 170.16 E-value: 8.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 44 LICEV-AQHLGNNVVrtIAMDATEGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADE-MGPVPCDKrLPIHRPAPS 121
Cdd:PRK06793 53 VLCEViAIEKENNML--LPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEeAENIPLQK-IKLDAPPIH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 122 FTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTViLMEMINNIAKqhGGISVFAGVGERTREGND-LYHEMK 200
Cdd:PRK06793 130 AFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST-LLGMIAKNAK--ADINVISLVGERGREVKDfIRKELG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 201 DAGvLEKAALVYGQMNEPPGARARVALTALTCAEYFRDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAvGYQPTLGT 280
Cdd:PRK06793 207 EEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMES 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 281 DLGGLQERITSTNKGSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSpDVLGVEH 360
Cdd:PRK06793 284 YMKKLLERSGKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNH 362
|
330
....*....|....*.
gi 1782519476 361 YATAREVQAVLQKYKE 376
Cdd:PRK06793 363 WQLANEMRKILSIYKE 378
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
67-409 |
1.55e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 163.91 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 67 GLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFP 146
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 147 KGGKMGLFGGAGVGKTViLMEMINNIAKqhGGISVFAGVGERTREGNDLY-HEMKDAGvLEKAALVYGQMNEPPGARARV 225
Cdd:PRK07196 154 KGQRVGLMAGSGVGKSV-LLGMITRYTQ--ADVVVVGLIGERGREVKEFIeHSLQAAG-MAKSVVVAAPADESPLMRIKA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 226 ALTALTCAEYFRDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERI-TSTNKGSITSVQAVY 304
Cdd:PRK07196 230 TELCHAIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTVL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 305 VPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSpDVLGVEHYATAREVQAVLQKYKELQDIIAiL 384
Cdd:PRK07196 309 AEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIP-L 386
|
330 340
....*....|....*....|....*..
gi 1782519476 385 GMDELGDDDKT--TVARARRIQRFLSQ 409
Cdd:PRK07196 387 GGYVAGADPMAdqAVHYYPAITQFLRQ 413
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
64-392 |
6.78e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 162.43 E-value: 6.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 64 ATEGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMgPVP--CDKRLPIhRPAPSFTEQSTKVELLeTGIKVVDL 141
Cdd:PRK07594 72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPdvCWKDYDA-MPPPAMVRQPITQPLM-TGIRAIDS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 142 LIPFPKGGKMGLFGGAGVGKTViLMEMINNIAKqhGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGA 221
Cdd:PRK07594 149 VATCGEGQRVGIFSAPGVGKST-LLAMLCNAPD--ADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 222 RARVALTALTCAEYFRDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTNKGSITSVQ 301
Cdd:PRK07594 226 RVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 302 AVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILsPDVLGVEHYATAREVQAVLQKYKELQDII 381
Cdd:PRK07594 305 TVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLI 383
|
330
....*....|.
gi 1782519476 382 AIlGMDELGDD 392
Cdd:PRK07594 384 RI-GEYQRGVD 393
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
80-349 |
4.74e-39 |
|
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: 142.75 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 80 PISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGV 159
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 160 GKTVILMEminnIAKQHGGIS-------VFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTC 232
Cdd:cd01135 81 PHNELAAQ----IARQAGVVGseenfaiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 233 AEYFRDEEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQER--ITSTNKGSITSVQAVYVPADDL 310
Cdd:cd01135 157 AEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDDI 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 1782519476 311 TDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSR 349
Cdd:cd01135 237 THPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
48-350 |
9.07e-39 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 146.98 E-value: 9.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 48 VAQHLGNNVVRTIAMDATEGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQST 127
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 128 KVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVILMEMINNiakQHGG--ISVFAGVGERTREGNDLYHEMKDAGVL 205
Cdd:PRK13343 142 VTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN---QKDSdvICVYVAIGQKASAVARVIETLREHGAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 206 EKAALVYGQMNEPPGARARVALTALTCAEYFRDeEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYqPtlgtdlgG- 284
Cdd:PRK13343 219 EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY-P-------Gd 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1782519476 285 -------LQERITSTNK----GSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRI 350
Cdd:PRK13343 290 ifylhsrLLERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
42-439 |
1.23e-38 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 145.43 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 42 PVLICEVAQhLGNNVVRTIAMDATEGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPS 121
Cdd:PRK05922 52 PPILAEVIG-FHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 122 FTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVILmemiNNIAK-QHGGISVFAGVGERTREGNDLYHEMK 200
Cdd:PRK05922 131 PMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLL----STIAKgSKSTINVIALIGERGREVREYIEQHK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 201 DAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDeEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGT 280
Cdd:PRK05922 207 EGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFH 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 281 DLGGLQERITSTNKGSITSVQAV-YVP--ADDLTDPAPattfSHLDGTLVLSRQIAELGiYPAVDPLDSTSRilSPDVLG 357
Cdd:PRK05922 286 HVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLK----SLLDGHFFLTPQGKALA-SPPIDILTSLSR--SARQLA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 358 V-EHYATAREVQAVLQKYKELQDIIAiLGMDELGDDDKttVARARR----IQRFLSQPFhvaevftgvaGKYVKTEDTVK 432
Cdd:PRK05922 359 LpHHYAAAEELRSLLKAYHEALDIIQ-LGAYVPGQDAH--LDRAVKllpsIKQFLSQPL----------SSYCALHNTLK 425
|
....*..
gi 1782519476 433 AFRDILD 439
Cdd:PRK05922 426 QLEALLK 432
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
62-383 |
1.96e-38 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 145.31 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 62 MDATEGLV-------RGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLET 134
Cdd:PRK07960 82 LEEVEGILpgarvyaRNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 135 GIKVVDLLIPFPKGGKMGLFGGAGVGKTVILMEMINniaKQHGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQ 214
Cdd:PRK07960 162 GVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR---YTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 215 MNEPPGARARVALTALTCAEYFRDeEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITS--T 292
Cdd:PRK07960 239 ADVSPLLRMQGAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 293 NKGSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSpDVLGVEHYATAREVQAVLQ 372
Cdd:PRK07960 318 GGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMT-ALIDEQHYARVRQFKQLLS 396
|
330
....*....|.
gi 1782519476 373 KYKELQDIIAI 383
Cdd:PRK07960 397 SFQRNRDLVSV 407
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
65-412 |
2.36e-38 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 144.97 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 65 TEGL-VRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIH--------RPAPSfteqstkvELLETG 135
Cdd:PRK04196 59 TTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINgapinpvaREYPE--------EFIQTG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 136 IKVVDLLIPFPKGGKMGLFGGAGVGKTvilmEMINNIAKQ---HGGIS----VFAGVGERTREGNDLYHEMKDAGVLEKA 208
Cdd:PRK04196 131 ISAIDGLNTLVRGQKLPIFSGSGLPHN----ELAAQIARQakvLGEEEnfavVFAAMGITFEEANFFMEDFEETGALERS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 209 ALVYGQMNEPPGARARVALTALTCAEYFRDEEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQER 288
Cdd:PRK04196 207 VVFLNLADDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 289 --ITSTNKGSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRiLSPDVLGV-----EHY 361
Cdd:PRK04196 287 agRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR-LMKDGIGEgktreDHK 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1782519476 362 ATAREVQAVLQKYKELQDIIAILGMDELGDDDKTTVARARRI-QRFLSQPFH 412
Cdd:PRK04196 366 DVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGFD 417
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
3-81 |
2.01e-37 |
|
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: 131.48 E-value: 2.01e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1782519476 3 NTGKIAQVIGAVVDVEFADGNLPNILSALEIKNPNNIDapvLICEVAQHLGNNVVRTIAMDATEGLVRGMSALDLGQPI 81
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDDGKK---LVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
80-349 |
1.70e-28 |
|
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: 113.82 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 80 PISVPVGKGSLGRIMNVVGEP----ADEMGP-----VPCdKRLPIHRPAPsFTEQSTKVELLETGIKVVDLLIPFPKGGK 150
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPleviAETGSIfiprgVNV-QRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 151 MGLFGGAGVGKTVILmemiNNIAKQ-HGGISVFAGVGERtreGND----------LYHEMKDAGVLEKAALVYGQMNEPP 219
Cdd:cd01134 79 AAIPGPFGCGKTVIS----QSLSKWsNSDVVIYVGCGER---GNEmaevleefpeLKDPITGESLMERTVLIANTSNMPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 220 GARARVALTALTCAEYFRDeEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQER------ITSTN 293
Cdd:cd01134 152 AAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERagrvrcLGSPG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1782519476 294 K-GSITSVQAVYVPADDLTDPAPATT------FSHLDGTLVLSRQiaelgiYPAVDPLDSTSR 349
Cdd:cd01134 231 ReGSVTIVGAVSPPGGDFSEPVTQATlrivqvFWGLDKKLAQRRH------FPSINWLISYSK 287
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
81-350 |
3.95e-27 |
|
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: 109.96 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 81 ISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVG 160
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 161 KTVILMEMINNiAKQHGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDeE 240
Cdd:cd01132 82 KTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD-N 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 241 GQDVLLFVDNIFRFTQAGAEVSALLGR------MPSAVGYQPTlgtdlgGLQERITSTNK----GSITSVQAVYVPADDL 310
Cdd:cd01132 160 GKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYLHS------RLLERAAKLSDelggGSLTALPIIETQAGDV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1782519476 311 TDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRI 350
Cdd:cd01132 234 SAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
114-439 |
2.76e-24 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 105.63 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 114 PIHRPAPsFTEQSTKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVilmeMINNIAKQ-HGGISVFAGVGERtreG 192
Cdd:PRK04192 194 PVRRPRP-YKEKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV----TQHQLAKWaDADIVIYVGCGER---G 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 193 NdlyhEMKDagVL----------------EKAALVYGQMNEPPGAR-ARVaLTALTCAEYFRDEeGQDVLLFVDNIFRFT 255
Cdd:PRK04192 266 N----EMTE--VLeefpelidpktgrplmERTVLIANTSNMPVAAReASI-YTGITIAEYYRDM-GYDVLLMADSTSRWA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 256 QAGAEVSALLGRMPSAVGYQPTLGTDLGGLQER----IT-STNKGSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSR 330
Cdd:PRK04192 338 EALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDA 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 331 QIAELGIYPAVDPLDSTSRILspDVLG-------VEHYATAR-EVQAVLQKYKELQDIIAILGMDELGDDDKTTVARARR 402
Cdd:PRK04192 418 ELADRRHFPAINWLTSYSLYL--DQVApwweenvDPDWRELRdEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARL 495
|
330 340 350
....*....|....*....|....*....|....*....
gi 1782519476 403 I-QRFLSQ-PFHVAEVFTGVAgkyvKTEDTVKAFRDILD 439
Cdd:PRK04192 496 IrEDFLQQnAFDPVDTYCPPE----KQYEMLKLILTFYD 530
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
6-350 |
1.30e-23 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 102.80 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 6 KIAQVIGAVVDVEfADGNLPNILSALEIKNPNNIdAPVLicevaqHLGNNVVRTIAMDATEGLVRGMSALDLGQPISVPV 85
Cdd:PRK02118 7 KITDITGNVITVE-AEGVGYGELATVERKDGSSL-AQVI------RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 86 GKGSLGRIMNVVGEPADEmGPVPCDKRLPIHrpAPSFTEQSTKV--ELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTV 163
Cdd:PRK02118 79 SESLLGRRFNGSGKPIDG-GPELEGEPIEIG--GPSVNPVKRIVprEMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 164 ILMeminNIAKQ-HGGISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDEEGQ 242
Cdd:PRK02118 156 LLA----RIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 243 DVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQER-ITSTNKGSITSVQAVYVPADDLTDPAPATTFSH 321
Cdd:PRK02118 232 KVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYI 311
|
330 340
....*....|....*....|....*....
gi 1782519476 322 LDGTLVLSRQiaelgiypAVDPLDSTSRI 350
Cdd:PRK02118 312 TEGQFYLRRG--------RIDPFGSLSRL 332
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
78-394 |
6.66e-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: 97.87 E-value: 6.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 78 GQPISVPVGKGSLGRIMNVVGEPADEMGPVPCDKRL-----PIHRPAPSFTEqstkvELLETGIKVVDLLIPFPKGGKMG 152
Cdd:TIGR01040 71 GDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLdingqPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 153 LFGGAGVGKTvilmEMINNIAKQHGGIS----------------VFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMN 216
Cdd:TIGR01040 146 IFSAAGLPHN----EIAAQICRQAGLVKlptkdvhdghednfaiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLAN 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 217 EPPGARARVALTALTCAEYFRDEEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERITSTN--K 294
Cdd:TIGR01040 222 DPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 295 GSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSPDV----LGVEHYATAREVQAV 370
Cdd:TIGR01040 302 GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmTRKDHSDVSNQLYAC 381
|
330 340
....*....|....*....|....
gi 1782519476 371 LQKYKELQDIIAILGMDELGDDDK 394
Cdd:TIGR01040 382 YAIGKDVQAMKAVVGEEALSSEDL 405
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
48-438 |
4.50e-19 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 89.64 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 48 VAQHLGNNVVRTIAMDATEGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPADEMGPVPC-DKRLpIHRPAPSFTEQS 126
Cdd:CHL00059 41 IALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISAsESRL-IESPAPGIISRR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 127 TKVELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVILMEMINNiAKQHGGISVFAGVGERTREGNDLYHEMKDAGVLE 206
Cdd:CHL00059 120 SVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERGAME 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 207 KAALVYGQMNEPPGARARVALTALTCAEYFRdEEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYqP---------- 276
Cdd:CHL00059 199 YTIVVAETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY-Pgdvfylhsrl 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 277 -----TLGTDLGGlqeritstnkGSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRIL 351
Cdd:CHL00059 277 leraaKLSSQLGE----------GSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 352 SpdvlgvehyatAREVQAVLQ---KYK-ELQDIIAILGMDELGDD-DKTT---VARARRIQRFLSQ----PFHVAE---- 415
Cdd:CHL00059 347 S-----------AAQIKAMKQvagKLKlELAQFAELEAFAQFASDlDKATqnqLARGQRLRELLKQsqsaPLTVEEqvat 415
|
410 420
....*....|....*....|....
gi 1782519476 416 VFTGVAGKYVKTE-DTVKAFRDIL 438
Cdd:CHL00059 416 IYTGTNGYLDSLEiGQVRKFLVEL 439
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
168-409 |
8.26e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 89.70 E-value: 8.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 168 MINNIAKQH-------GGISVFAGVGERTREGNDLYHE---MKDAG----VLEKAALVYGQMNEPPGARARVALTALTCA 233
Cdd:PRK14698 666 LLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEfpkLKDPKtgkpLMERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 234 EYFRDEeGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGGLQERI-------TSTNKGSITSVQAVYVP 306
Cdd:PRK14698 746 EYFRDM-GYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPP 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 307 ADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSP------DVLGVEHYATAREVQAVLQKYKELQDI 380
Cdd:PRK14698 825 GGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEI 904
|
250 260 270
....*....|....*....|....*....|
gi 1782519476 381 IAILGMDELGDDDKTTVARARRIQR-FLSQ 409
Cdd:PRK14698 905 VRIVGPDALPERERAILLVARMLREdYLQQ 934
|
|
| 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 |
4.29e-18 |
|
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: 78.25 E-value: 4.29e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 360 HYATAREVQAVLQKYKELQDIIAILGMDELGDDDKTTVARARRIQRFLSQPFHVAEVFTG 419
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIED 60
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
60-377 |
6.84e-17 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 83.17 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 60 IAMDATEGLVRGMSALDLGQPISVPVGKGSLGRIMNVVGEPAdEMGPVPCDKRL--------PIHRPAPSFTEQSTKVEL 131
Cdd:PTZ00185 94 ILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV-PVGLLTRSRALleseqtlgKVDAGAPNIVSRSPVNYN 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 132 LETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVILMEMINN-------IAKQHGGISVFAGVGERTREGNDLYHEMKDAGV 204
Cdd:PTZ00185 173 LLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRSYGA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 205 LEKAALVYGQMNEPPGARARVALTALTCAEYFRDeEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAVGYQPTLGTDLGG 284
Cdd:PTZ00185 253 LRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSR 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 285 LQER--ITSTNK--GSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTSRILSpDVLGVEH 360
Cdd:PTZ00185 332 LLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGS-SAQNVAM 410
|
330
....*....|....*..
gi 1782519476 361 YATAREVQAVLQKYKEL 377
Cdd:PTZ00185 411 KAVAGKLKGILAEYRKL 427
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
7-78 |
8.34e-17 |
|
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: 74.50 E-value: 8.34e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1782519476 7 IAQVIGAVVDVEFADGNLPNILSALEIKNPNNIDapvLICEVAQHLGNNVVRTIAMDATEGLVRGMSALDLG 78
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEFGS---LVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
11-269 |
1.21e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 82.04 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 11 IGAVVDVefADG-----NLPNILSALEIKNPNNIDApvliceVAQHLGNNVVRTIAMDATEGLVRGMSALDLGQPISVPV 85
Cdd:PRK09281 28 VGTVISV--GDGiarvyGLDNVMAGELLEFPGGVYG------IALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 86 GKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTE-QSTKvELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVI 164
Cdd:PRK09281 100 GEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDrKSVH-EPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 165 LMEMINNiakQHGG--ISVFAGVGERTREGNDLYHEMKDAGVLEKAALVYGQMNEPPGARARVALTALTCAEYFRDeEGQ 242
Cdd:PRK09281 179 AIDTIIN---QKGKdvICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMD-NGK 254
|
250 260
....*....|....*....|....*....
gi 1782519476 243 DVLLFVDNIFRftQAGA--EVSALLGRMP 269
Cdd:PRK09281 255 DALIVYDDLSK--QAVAyrQLSLLLRRPP 281
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
86-349 |
2.37e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 62.03 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 86 GKGSLGRIMNVVGEPADEM-GPVPCDKRLPIHrPAPSFteqstkveLLETG-----IKVVDLLIPFPKGGKMGLFGGAGV 159
Cdd:PRK12608 74 RYRVLVRVDSVNGTDPEKLaRRPHFDDLTPLH-PRERL--------RLETGsddlsMRVVDLVAPIGKGQRGLIVAPPRA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 160 GKTVILMEMINNIAKQHGGISVFAG-VGERTREGNDLYHEMKdagvlekaALVYGQMN-EPPGARARVALTALTCAEYFR 237
Cdd:PRK12608 145 GKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTFdRPPDEHIRVAELVLERAKRLV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 238 dEEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAvgyqptlGTDLGGLQ--ERITST-----NKGSITSVQAVYVP---- 306
Cdd:PRK12608 217 -EQGKDVVILLDSLTRLARAYNNEVESSGRTLSG-------GVDARALQrpKRLFGAarnieEGGSLTIIATALVDtgsr 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1782519476 307 ADDLTdpapattFSHLDGT----LVLSRQIAELGIYPAVDPLDSTSR 349
Cdd:PRK12608 289 MDEVI-------FEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
137-356 |
1.11e-09 |
|
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: 58.76 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 137 KVVDLLIPFPKGGKMGLFGGAGVGKTVILMEMINNIAKQHGGISVFAG-VGERTREGNDlyheMKDAGvleKAALVYGQM 215
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSV---KGEVVASTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 216 NEPPGARARVALTALTCAEYfRDEEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAvgyqptlGTDLGGLQ--ERITST- 292
Cdd:cd01128 78 DEPPERHVQVAEMVIEKAKR-LVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-------GVDANALHkpKRFFGAa 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 293 ----NKGSITSVqavyvpADDLTDpapatTFSHLD--------GT----LVLSRQIAELGIYPAVDPLDSTSR----ILS 352
Cdd:cd01128 150 rnieEGGSLTII------ATALVD-----TGSRMDevifeefkGTgnmeLVLDRKLAEKRIFPAIDILKSGTRkeelLLT 218
|
....
gi 1782519476 353 PDVL 356
Cdd:cd01128 219 PEEL 222
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
130-352 |
9.86e-09 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 57.29 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 130 ELLETGIKVVDLLIPFPKGGKMGLFGGAGVGKTVI-LMEMINNiaKQHGGISVFAGVGERTREGNDLYHEMKDAGVLEKA 208
Cdd:PRK07165 125 EQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIaLNTIINQ--KNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNT 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 209 ALV-------YGQMNEPpgararvaLTALTCAEYFRDEEgqDVLLFVD------NIFRftqagaEVSALLGR------MP 269
Cdd:PRK07165 203 IIIdapstspYEQYLAP--------YVAMAHAENISYND--DVLIVFDdltkhaNIYR------EIALLTNKpvgkeaFP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 270 SAVGYQPTlgtdlgGLQERITS-TNKGSITSVQAVYVPADDLTDPAPATTFSHLDGTLVLSRQIAELGIYPAVDPLDSTS 348
Cdd:PRK07165 267 GDMFFAHS------KLLERAGKfKNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVS 340
|
....
gi 1782519476 349 RILS 352
Cdd:PRK07165 341 RTGS 344
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
98-356 |
2.11e-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: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 98 GEPADEMGPVPCDKRLPIHRPAPSFTEQSTkvELLETgiKVVDLLIPFPKGGKMGLFGGAGVGKTVILMEMINNIAKQHG 177
Cdd:TIGR00767 122 DDPEKAKNRVLFENLTPLYPNERLRLETST--EDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 178 GISVFAG-VGERTREGNDLYHEMKdagvlekAALVYGQMNEPPGARARVALTALTCAEYfRDEEGQDVLLFVDNIFRFTQ 256
Cdd:TIGR00767 198 EVELIVLlIDERPEEVTDMQRSVK-------GEVVASTFDEPASRHVQVAEMVIEKAKR-LVEHKKDVVILLDSITRLAR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 257 AGAEVSALLGRMPSAvgyqptlGTDLGGLQ--ERITST-----NKGSITSVQAVYVPADDLTDpapATTFSHLDGT---- 325
Cdd:TIGR00767 270 AYNTVTPASGKVLSG-------GVDANALHrpKRFFGAarnieEGGSLTIIATALIDTGSRMD---EVIFEEFKGTgnme 339
|
250 260 270
....*....|....*....|....*....|....*
gi 1782519476 326 LVLSRQIAELGIYPAVDPLDSTSR----ILSPDVL 356
Cdd:TIGR00767 340 LHLDRKLADRRIFPAIDIKKSGTRkeelLLTPEEL 374
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
138-356 |
4.47e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 48.60 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 138 VVDLLIPFPKGGKmGLFggagV-----GKTVILMEMINNIAKQHGGISVFAG-VGERTREGNDlyheMKDaGVleKAALV 211
Cdd:PRK09376 159 IIDLIAPIGKGQR-GLI----VappkaGKTVLLQNIANSITTNHPEVHLIVLlIDERPEEVTD----MQR-SV--KGEVV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 212 YGQMNEPPGARARVALTALTCAEyfRD-EEGQDVLLFVDNIFRFTQAGAEVSALLGRMPSAvgyqptlGTDLGGLQeRIT 290
Cdd:PRK09376 227 ASTFDEPAERHVQVAEMVIEKAK--RLvEHGKDVVILLDSITRLARAYNTVVPSSGKVLSG-------GVDANALH-RPK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 291 S--------TNKGSITSVqavyvpADDLTDpapatTFSHLD--------GT----LVLSRQIAELGIYPAVDPLDSTSR- 349
Cdd:PRK09376 297 RffgaarniEEGGSLTII------ATALID-----TGSRMDevifeefkGTgnmeLHLDRKLAEKRIFPAIDINRSGTRk 365
|
250
....*....|
gi 1782519476 350 ---ILSPDVL 356
Cdd:PRK09376 366 eelLLSPEEL 375
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
147-268 |
2.34e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 147 KGGKMGLFGGAGVGKTVILMEMINNIAKQHGGISVFAGvgertregndlyhEMKDAGVLEKAALVYGQMNEPPGARARVA 226
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------EDILEEVLDQLLLIIVGGKKASGSGELRL 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1782519476 227 LTALTCAEYFRDEegqdvLLFVDNIFRFTQAGAEVSALLGRM 268
Cdd:smart00382 68 RLALALARKLKPD-----VLILDEITSLLDAEQEALLLLLEE 104
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
86-386 |
1.30e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.55 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 86 GKGSLGRIMNVVGEPADEMGPVPCDKRLPIHRPAPSFTEQSTKVELLeTGIKVVDLLIPFPKGGKMGLFGGAGVGKTVIL 165
Cdd:PRK14698 166 GEYTIEEVIAKVKTPSGEIKELKMYQRWPVRVKRPYKEKLPPEVPLI-TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVDG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 166 MEMInnIAKQHGGISV------FAGVGERTREGNDLYHEmkdagvLEKAALVYGQMNeppGARARVALT-----ALTCAE 234
Cdd:PRK14698 245 DTLI--LTKEFGLIKIkdlyeiLDGKGKKTVEGNEEWTE------LEEPITLYGYKD---GKIVEIKAThvykgASAGMI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782519476 235 YFRDEEGQDVLLF-VDNIF--RFTQAGAEVSALLGrMPSAVGYQPTLGTDLGGlQERITSTNKGSITSVQAVYVPadDLT 311
Cdd:PRK14698 314 EIKTRTGRKIKVTpIHKLFtgRVTKDGLEIEEVMA-KDIKKGDRIAVAKKIDG-GERVKLNIRVDQKRGKKIKIP--DVL 389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1782519476 312 DPAPATTFSHL--DGTLVlSRQIAelgIYPAVDPLDSTSRILSPDVLGVE-HYATAREVQAVLQKYKELQDIIAILGM 386
Cdd:PRK14698 390 DEELAEFLGYLiaDGTLK-PRTVA---IYNNDESLLKRANELAMELFGIEgKIVKERTVKALLIHSKALVDFFKKLGI 463
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-79 |
9.36e-03 |
|
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: 34.98 E-value: 9.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1782519476 4 TGKIAQVIGAVVDVEFADGnlPNILSALEIKNPNNIDAPVLICEVAQHLGNNVVrTIAMDATEGLVRGMSALDLGQ 79
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGE--VAIGEVCEIERGDGNNETVLKAEVIGFRGDRAI-LQLFESTRGLSRGALVEPTGR 73
|
|
| |
