|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-462 |
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: 1016.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 1 MQEGKISQIIGPVVDVDFPEGRLPSILDALTITRPDGTKLVLETQQHLGEERVRTVSMESTDGLVRGTSVANTGMPIQVP 80
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 81 VGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVL 160
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 161 IMELINNIAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEEGRDV 240
Cdd:COG0055 163 IMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 241 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPATAFAHLDA 320
Cdd:COG0055 243 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 321 TTVLSRQIAELGIYPAVDPLDSTSRILDPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLVVSRARKVQ 400
Cdd:COG0055 323 TTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQ 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493410791 401 RFLSQPFFVAEAFTGLAGKYVKLEETIKGFKEIIAGKHDNLPESAFYLVGTIEEAIEKAKTL 462
Cdd:COG0055 403 RFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKL 464
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
3-462 |
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: 874.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 3 EGKISQIIGPVVDVDFPEGRLPSILDALTITRPDGTKLVLETQQHLGEERVRTVSMESTDGLVRGTSVANTGMPIQVPVG 82
Cdd:TIGR01039 2 KGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 83 PEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLIM 162
Cdd:TIGR01039 82 KETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 163 ELINNIAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEEGRDVLL 242
Cdd:TIGR01039 162 ELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 243 FIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPATAFAHLDATT 322
Cdd:TIGR01039 242 FIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 323 VLSRQIAELGIYPAVDPLDSTSRILDPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLVVSRARKVQRF 402
Cdd:TIGR01039 322 VLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRF 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 403 LSQPFFVAEAFTGLAGKYVKLEETIKGFKEIIAGKHDNLPESAFYLVGTIEEAIEKAKTL 462
Cdd:TIGR01039 402 LSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
4-462 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 844.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 4 GKISQIIGPVVDVDFPEGRLPSILDALTITRPDGT----KLVLETQQHLGEERVRTVSMESTDGLVRGTSVANTGMPIQV 79
Cdd:CHL00060 17 GRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAgqeiNVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 80 PVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTV 159
Cdd:CHL00060 97 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 160 LIMELINNIAKQQSGFSVFAGVGERTREGNDLWHEMMESGVID-------KTALVFGQMNEPPGARQRVALTGLSIAEYF 232
Cdd:CHL00060 177 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINeqniaesKVALVYGQMNEPPGARMRVGLTALTMAEYF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 233 RDEEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPA 312
Cdd:CHL00060 257 RDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 313 TAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLV 392
Cdd:CHL00060 337 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLT 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 393 VSRARKVQRFLSQPFFVAEAFTGLAGKYVKLEETIKGFKEIIAGKHDNLPESAFYLVGTIEEAIEKAKTL 462
Cdd:CHL00060 417 VARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANL 486
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-455 |
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: 597.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 4 GKISQIIGPVVDVDFpEGRLPSILDALTITRPDgtKLVLETQQHLGEERVRTVSMESTDGLVRGTSVANTGMPIQVPVGP 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRF-DGELPAIHSVLRAGREG--EVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 84 EVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLIME 163
Cdd:TIGR03305 78 PTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 164 LINNIAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEEGRDVLLF 243
Cdd:TIGR03305 158 MIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 244 IDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPATAFAHLDATTV 323
Cdd:TIGR03305 238 IDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 324 LSRQIAELGIYPAVDPLDSTSRILDPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLVVSRARKVQRFL 403
Cdd:TIGR03305 318 LSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 493410791 404 SQPFFVAEAFTGLAGKYVKLEETIKGFKEIIAGKHDNLPESAFYLVGTIEEA 455
Cdd:TIGR03305 398 TQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDEA 449
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
78-349 |
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: 589.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 78 QVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGK 157
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 158 TVLIMELINNIAKQQSGFSVFAGVGERTREGNDLWHEMMESGVI-----DKTALVFGQMNEPPGARQRVALTGLSIAEYF 232
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVInldglSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 233 RDEEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPA 312
Cdd:cd01133 161 RDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAPA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 493410791 313 TAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDP 349
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 ... |
78-346 |
4.18e-128 |
|
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: 372.17 E-value: 4.18e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 78 QVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGK 157
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 158 TVLIMELINNIAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDeEG 237
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-NG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 238 RDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTK--KGSVTSVQAIYVPADDLTDPAPATAF 315
Cdd:cd19476 160 QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 493410791 316 AHLDATTVLSRQIAELGIYPAVDPLDSTSRI 346
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
131-344 |
3.56e-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: 288.49 E-value: 3.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 131 GIKVIDLLEPYSRGGKTGLFGGAGVGKTVLImeliNNIAKQQS-GFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFG 209
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA----GMIARQASaDVVVYALIGERGREVREFIEELLGSGALKRTVVVVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 210 QMNEPPGARQRVALTGLSIAEYFRDeEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRI--VS 287
Cdd:pfam00006 77 TSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAgrVK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493410791 288 TKKGSVTSVQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTS 344
Cdd:pfam00006 156 GKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
351-458 |
2.46e-73 |
|
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: 225.82 E-value: 2.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 351 IVGDDHYDTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLVVSRARKVQRFLSQPFFVAEAFTGLAGKYVKLEETIKGF 430
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 493410791 431 KEIIAGKHDNLPESAFYLVGTIEEAIEK 458
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-434 |
2.18e-72 |
|
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: 234.93 E-value: 2.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 3 EGKISQIIGPVVDVdfpEGRLPSILDALTITRPDGTKLVLETqqhLG--EERVRTVSMESTDGLVRGTSVANTGMPIQVP 80
Cdd:COG1157 20 SGRVTRVVGLLIEA---VGPDASIGELCEIETADGRPVLAEV---VGfrGDRVLLMPLGDLEGISPGARVVPTGRPLSVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 81 VGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKF---DEISTKaemFETGIKVIDLLEPYSRGGKTGLFGGAGVGK 157
Cdd:COG1157 94 VGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPlerARITEP---LDTGVRAIDGLLTVGRGQRIGIFAGSGVGK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 158 TVLI-MelinnIAKQ-QSGFSVFAGVGERTRE-----GNDLWHEMME-SGVIDKTAlvfgqmNEPPGARQRVALTGLSIA 229
Cdd:COG1157 171 STLLgM-----IARNtEADVNVIALIGERGREvrefiEDDLGEEGLArSVVVVATS------DEPPLMRLRAAYTATAIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 230 EYFRDeEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTsvqAIY---VPADDL 306
Cdd:COG1157 240 EYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlVEGDDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 307 TDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILdPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAI----LGM 382
Cdd:COG1157 316 NDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGS 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 493410791 383 DELSDEdklVVSRARKVQRFLSQPffVAEAFTglagkyvkLEETIKGFKEII 434
Cdd:COG1157 395 DPELDE---AIALIPAIEAFLRQG--MDERVS--------FEESLAQLAELL 433
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
78-346 |
2.90e-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: 190.08 E-value: 2.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 78 QVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGK 157
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 158 TVLIMELINNIAkqqSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEeG 237
Cdd:cd01136 81 STLLGMIARNTD---ADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQ-G 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 238 RDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPATAFAH 317
Cdd:cd01136 157 KKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRSI 236
|
250 260
....*....|....*....|....*....
gi 493410791 318 LDATTVLSRQIAELGIYPAVDPLDSTSRI 346
Cdd:cd01136 237 LDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
72-435 |
6.89e-56 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 191.44 E-value: 6.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 72 NTGMpiQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHR---SAPKFDEIStkaEMFETGIKVIDLLEPYSRGGKTG 148
Cdd:PRK08472 87 KEGL--NIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKapiAAMKRGLID---EVFSVGVKSIDGLLTCGKGQKLG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 149 LFGGAGVGKTVLiMELINNIAKQQsgFSVFAGVGERTREGNDLWHEMMeSGVIDKTALVFGQMNEPPGARQRVALTGLSI 228
Cdd:PRK08472 162 IFAGSGVGKSTL-MGMIVKGCLAP--IKVVALIGERGREIPEFIEKNL-GGDLENTVIVVATSDDSPLMRKYGAFCAMSV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 229 AEYFRDEeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTK-KGSVTSVQAIYVPADDLT 307
Cdd:PRK08472 238 AEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVEGDDMS 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 308 DPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDpNIVGDDHYDTAQAVKQLLQRYKDLQDIIAI----LGMD 383
Cdd:PRK08472 317 DPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGND 395
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 493410791 384 ELSDEdklVVSRARKVQRFLSQPFfvAEAFtglagkyvKLEETIKGFKEIIA 435
Cdd:PRK08472 396 KELDE---AISKKEFMEQFLKQNP--NELF--------PFEQTFEQLEEILR 434
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
4-379 |
2.67e-55 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 190.32 E-value: 2.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 4 GKISQIIGPVVDVDFPEGrlpSILDALTI-TRPDGTKLVLETQQHLGEERVRTVSMESTDGLVRGTSVANTGMPIQVPVG 82
Cdd:PRK07721 20 GKVSRVIGLMIESKGPES---SIGDVCYIhTKGGGDKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 83 PEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGK-TVLI 161
Cdd:PRK07721 97 SGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKsTLMG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 162 MelinnIAKQQSG-FSVFAGVGERTREGND-LWHEMMESGvIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEeGRD 239
Cdd:PRK07721 177 M-----IARNTSAdLNVIALIGERGREVREfIERDLGPEG-LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQ-GLN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 240 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPATAFAHLD 319
Cdd:PRK07721 250 VMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGDDMNEPIADTVRGILD 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 320 ATTVLSRQIAELGIYPAVDPLDSTSRILdPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAI 379
Cdd:PRK07721 330 GHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
59-405 |
1.74e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 182.71 E-value: 1.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 59 ESTDGLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGrGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLL 138
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 139 EPYSRGGKTGLFGGAGVGKTVLIMELInniAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGAR 218
Cdd:PRK06820 158 LSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALER 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 219 QRVALTGLSIAEYFRDEeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQA 298
Cdd:PRK06820 235 LKGLSTATTIAEYFRDR-GKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 299 IYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILdPNIVGDDHYDTAQAVKQLLQRYKDLQDIIA 378
Cdd:PRK06820 314 VLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVR 392
|
330 340 350
....*....|....*....|....*....|.
gi 493410791 379 I----LGMDELSDEdklVVSRARKVQRFLSQ 405
Cdd:PRK06820 393 VgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
63-405 |
3.75e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 181.87 E-value: 3.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 63 GLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPkfDEISTK--AEMFETGIKVIDLLEP 140
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAP--APMSRRliETPLSLGVRVIDGLLT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 141 YSRGGKTGLFGGAGVGKTVLIMELINNIAkqqSGFSVFAGVGERTREGND-LWHEMMESGvIDKTALVFGQMNEPPGARQ 219
Cdd:PRK06936 159 CGEGQRMGIFAAAGGGKSTLLASLIRSAE---VDVTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 220 RVALTGLSIAEYFRDEeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAI 299
Cdd:PRK06936 235 KAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 300 YVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDpNIVGDDHYDTAQAVKQLLQRYKDLQDIIAI 379
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQI 392
|
330 340 350
....*....|....*....|....*....|
gi 493410791 380 ----LGMDELSDEdklVVSRARKVQRFLSQ 405
Cdd:PRK06936 393 geyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
59-379 |
2.90e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 176.81 E-value: 2.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 59 ESTDGLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHrsAPKFDEISTKA--EMFETGIKVID 136
Cdd:PRK08972 77 EELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRRPitEPLDVGVRAIN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 137 LLEPYSRGGKTGLFGGAGVGKTVLIMELINNIAKQqsgFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPG 216
Cdd:PRK08972 155 AMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 217 ARQRVALTGLSIAEYFRDEeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIV--STKKGSVT 294
Cdd:PRK08972 232 MRLKGCETATTIAEYFRDQ-GLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngGPGQGSIT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 295 SVQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILdPNIVGDDHYDTAQAVKQLLQRYKDLQ 374
Cdd:PRK08972 311 AFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNR 389
|
....*
gi 493410791 375 DIIAI 379
Cdd:PRK08972 390 DLISI 394
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
50-405 |
2.28e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 171.84 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 50 EERVRTVSMESTDGLVRGTSV---ANTGmpiQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSA--P-KFDEISt 123
Cdd:PRK05688 74 GDKVFLMPVGSVAGIAPGARVvplADTG---RLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTinPlNRHPIS- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 124 kaEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLI--MELINniakqQSGFSVFAGVGERTREGNDLWHEMMESGVI 201
Cdd:PRK05688 150 --EPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLgmMTRFT-----EADIIVVGLIGERGREVKEFIEHILGEEGL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 202 DKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQL 281
Cdd:PRK05688 223 KRSVVVASPADDAPLMRLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 282 QDRIVSTKKG--SVTSVQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILdPNIVGDDHYDT 359
Cdd:PRK05688 302 VERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRR 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 493410791 360 AQAVKQLLQRYKDLQDIIAILGMDELSD-EDKLVVSRARKVQRFLSQ 405
Cdd:PRK05688 381 AQRFKQLWSRYQQSRDLISVGAYVAGGDpETDLAIARFPHLVQFLRQ 427
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-406 |
3.62e-48 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 171.10 E-value: 3.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 4 GKISQIIGPVVDVDFPEGRLPSILdalTITRPDGTklVLETQQHLGEERvrTVSMES----TDGLVRGTSVANTGMPIQV 79
Cdd:PRK09099 26 GKVVEVIGTLLRVSGLDVTLGELC---ELRQRDGT--LLQRAEVVGFSR--DVALLSpfgeLGGLSRGTRVIGLGRPLSV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 80 PVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKfdeiSTKAEMFE----TGIKVIDLLEPYSRGGKTGLFGGAGV 155
Cdd:PRK09099 99 PVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPD----PMSRRMVEaplpTGVRIVDGLMTLGEGQRMGIFAPAGV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 156 GKTVLIMELINNiakQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDE 235
Cdd:PRK09099 175 GKSTLMGMFARG---TQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 236 eGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPATAF 315
Cdd:PRK09099 252 -GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESGSDPIAEEVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 316 AHLDATTVLSRQIAELGIYPAVDPLDSTSRILdPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAI----LGMDELSDEdkl 391
Cdd:PRK09099 331 GILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVADE--- 406
|
410
....*....|....*
gi 493410791 392 VVSRARKVQRFLSQP 406
Cdd:PRK09099 407 AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
44-381 |
1.43e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 167.10 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 44 TQQHLGE------ERVRTVSMESTDGLVRGTSVANTGmPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTA-KTYSIHRSAP 116
Cdd:PRK06002 59 GGTHLGEvvrvdpDGVTVKPFEPRIEIGLGDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPLAPGtRPMSIDATAP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 117 KFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLIMELinniaKQQSGFS--VFAGVGERTREGNDLWHE 194
Cdd:PRK06002 138 PAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML-----ARADAFDtvVIALVGERGREVREFLED 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 195 MMeSGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTL 274
Cdd:PRK06002 213 TL-ADNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDR-GENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 275 ATEMGQLQDRI--VSTKKGSVTSVQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDPNIV 352
Cdd:PRK06002 291 FSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWT 370
|
330 340
....*....|....*....|....*....
gi 493410791 353 GDDHyDTAQAVKQLLQRYKDLQDIIAILG 381
Cdd:PRK06002 371 PEQR-KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
59-405 |
5.32e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 165.15 E-value: 5.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 59 ESTDGLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGrgPVHTAKTYSIHRSAPKFDEISTK--AEMFETGIKVID 136
Cdd:PRK06793 71 EQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHAFEREeiTDVFETGIKSID 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 137 LLEPYSRGGKTGLFGGAGVGKTVLIMELINNiakQQSGFSVFAGVGERTREGND-LWHEMMESGvIDKTALVFGQMNEPP 215
Cdd:PRK06793 149 SMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN---AKADINVISLVGERGREVKDfIRKELGEEG-MRKSVVVVATSDESH 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 216 GARQRVALTGLSIAEYFRDEeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAvGYQPTLATEMGQLQDRIVSTKKGSVTS 295
Cdd:PRK06793 225 LMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 296 VQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDpNIVGDDHYDTAQAVKQLLQRYKDlQD 375
Cdd:PRK06793 303 IYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYKE-NE 380
|
330 340 350
....*....|....*....|....*....|...
gi 493410791 376 IIAILGMDELSDEDKLVVSRARKVQ---RFLSQ 405
Cdd:PRK06793 381 LYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
9-413 |
1.10e-45 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 164.01 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 9 IIGPVVDVDFPEGRLPSILDaltITRPDGTKLVLETQQHLGEERVRTV--SMESTDGLVRGTSVANTGMPIQVPVGPEVL 86
Cdd:PRK08149 13 IQGPIIEAELPDVAIGEICE---IRAGWHSNEVIARAQVVGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 87 SRMMNVVGEpIDGR--GPVhTAKTYSIHR----SAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVL 160
Cdd:PRK08149 90 GAVLDPTGK-IVERfdAPP-TVGPISEERvidvAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 161 IMELINNiakQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDeEGRDV 240
Cdd:PRK08149 168 MNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 241 LLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAIYVPADDLTDPAPATAFAHLDA 320
Cdd:PRK08149 244 VLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 321 TTVLSRQIAELGIYPAVDPLDSTSRILDpNIVGDDHYDTAQAVKQLLQRYKDLQDIIAiLG---MDELSDEDKlVVSRAR 397
Cdd:PRK08149 324 HIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEELQLFID-LGeyrRGENADNDR-AMDKRP 400
|
410
....*....|....*.
gi 493410791 398 KVQRFLSQPFFVAEAF 413
Cdd:PRK08149 401 ALEAFLKQDVAEKSSF 416
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-407 |
2.22e-45 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 164.23 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 5 KISQIIGPVVdvdFPEGRLPSILDAL-TITRPDGTKL---VLETQqhlgEERVRTVSMESTDGL-VRGTSVANTGMPIQV 79
Cdd:PRK04196 6 TVSEIKGPLL---FVEGVEGVAYGEIvEIELPNGEKRrgqVLEVS----EDKAVVQVFEGTTGLdLKDTKVRFTGEPLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 80 PVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIH--------RSAPKfdeistkaEMFETGIKVIDLLEPYSRGGKTGLFG 151
Cdd:PRK04196 79 PVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINgapinpvaREYPE--------EFIQTGISAIDGLNTLVRGQKLPIFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 152 GAGVGKTvlimELINNIAKQ------QSGFS-VFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQ---RV 221
Cdd:PRK04196 151 GSGLPHN----ELAAQIARQakvlgeEENFAvVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERIltpRM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 222 ALTglsIAEYFRDEEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDR--IVSTKKGSVTSVQAI 299
Cdd:PRK04196 227 ALT---AAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 300 YVPADDLTDPAPatafahlDAT-------TVLSRQIAELGIYPAVDPLDSTSRILDPNIvG-----DDHYDTAQavkQLL 367
Cdd:PRK04196 304 TMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLMKDGI-GegktrEDHKDVAN---QLY 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 493410791 368 QRY---KDLQDIIAILGMDELSDEDKLVVSRARKV-QRFLSQPF 407
Cdd:PRK04196 373 AAYargKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGF 416
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
3-429 |
2.89e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 160.53 E-value: 2.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 3 EGKISQIIGPVVDVDFPEGRLpSILDALTITRPDGTKLVLETqqhLGEERVRTVSM--ESTDGLVRGTSVANTGMPIQVP 80
Cdd:PRK08927 18 YGRVVAVRGLLVEVAGPIHAL-SVGARIVVETRGGRPVPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAAAAVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 81 VGPEVLSRMMNVVGEPIDGRGPVHTAKT-YSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTV 159
Cdd:PRK08927 94 PSRAWLGRVVNALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 160 LIMELINNIAkqqSGFSVFAGVGERTRE-----GNDLWHEMMESGVIdktalVFGQMNEPPGARQRVALTGLSIAEYFRD 234
Cdd:PRK08927 174 LLSMLARNAD---ADVSVIGLIGERGREvqeflQDDLGPEGLARSVV-----VVATSDEPALMRRQAAYLTLAIAEYFRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 235 EeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIV--STKKGSVTSVQAIYVPADDLTDPAPA 312
Cdd:PRK08927 246 Q-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGpgPIGEGTITGLFTVLVDGDDHNEPVAD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 313 TAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILdPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAI----LGMDELSDE 388
Cdd:PRK08927 325 AVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRLgayrAGSDPEVDE 403
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 493410791 389 dklVVSRARKVQRFLSQPffVAEAfTGLAGKYVKLEETIKG 429
Cdd:PRK08927 404 ---AIRLNPALEAFLRQG--KDEA-TSLAEGYARLAQILGG 438
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
60-388 |
9.61e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 150.87 E-value: 9.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 60 STDGLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRG-PVHTAKTYSIHRSAPKFDEISTKAEMfeTGIKVIDLL 138
Cdd:PRK07594 72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRElPDVCWKDYDAMPPPAMVRQPITQPLM--TGIRAIDSV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 139 EPYSRGGKTGLFGGAGVGKTVLIMELINniaKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGAR 218
Cdd:PRK07594 150 ATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALER 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 219 QRVALTGLSIAEYFRDEeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQA 298
Cdd:PRK07594 227 VRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYT 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 299 IYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILdPNIVGDDHYDTAQAVKQLLQRYKDLQDIIA 378
Cdd:PRK07594 306 VLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVELLIR 384
|
330
....*....|....
gi 493410791 379 I----LGMDELSDE 388
Cdd:PRK07594 385 IgeyqRGVDTDTDK 398
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
63-405 |
4.10e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 149.27 E-value: 4.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 63 GLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHrsAPKFDEISTKA--EMFETGIKVIDLLEP 140
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQ--LPQIHPLQRRAvdTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 141 YSRGGKTGLFGGAGVGKTVLIMELINNiakQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQR 220
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVLLGMITRY---TQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 221 VALTGLSIAEYFRDEeGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRI-VSTKKGSVTSVQAI 299
Cdd:PRK07196 229 ATELCHAIATYYRDK-GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTMTAIYTV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 300 YVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDpNIVGDDHYDTAQAVKQLLQRYKDLQDIIA- 378
Cdd:PRK07196 308 LAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAIKPLIPl 386
|
330 340 350
....*....|....*....|....*....|
gi 493410791 379 ---ILGMDELSDEdklVVSRARKVQRFLSQ 405
Cdd:PRK07196 387 ggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
26-408 |
6.59e-39 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 146.47 E-value: 6.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 26 ILDALTITRPDGTKLVLETQQHLGEERVRT------------VSMESTDGLVRGTSV-------ANTGMPIQVPVGPEVL 86
Cdd:PRK07960 38 VLEATGLQLPLGATCVIERQNGSETHEVESevvgfngqrlflMPLEEVEGILPGARVyarnisgEGLQSGKQLPLGPALL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 87 SRMMNVVGEPIDGRGPVHTakTYSIHRSAPKFDEISTKA--EMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLImel 164
Cdd:PRK07960 118 GRVLDGSGKPLDGLPAPDT--GETGALITPPFNPLQRTPieHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLL--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 165 iNNIAK-QQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEeGRDVLLF 243
Cdd:PRK07960 193 -GMMARyTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFRDR-GQHVLLI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 244 IDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVS--TKKGSVTSVQAIYVPADDLTDPAPATAFAHLDAT 321
Cdd:PRK07960 271 MDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQDPIADSARAILDGH 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 322 TVLSRQIAELGIYPAVDPLDSTSRILdPNIVGDDHYDTAQAVKQLLQRYKDLQDIIAI----LGMDELSDEdklVVSRAR 397
Cdd:PRK07960 351 IVLSRRLAEAGHYPAIDIEASISRAM-TALIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSDPMLDK---AIALWP 426
|
410
....*....|.
gi 493410791 398 KVQRFLSQPFF 408
Cdd:PRK07960 427 QLEAFLQQGIF 437
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
2-77 |
6.57e-36 |
|
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: 127.25 E-value: 6.57e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493410791 2 QEGKISQIIGPVVDVDFPEGRLPSILDALTITRPDGTKLVLETQQHLGEERVRTVSMESTDGLVRGTSVANTGMPI 77
Cdd:cd18115 1 NTGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
47-346 |
1.36e-33 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 132.35 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 47 HLGEERVRTVSMESTDGLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAE 126
Cdd:PRK13343 65 NLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 127 MFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLIMELINNiAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTAL 206
Cdd:PRK13343 145 PLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 207 VFGQMNEPPGArQRVA-LTGLSIAEYFRDeEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYqP------------- 272
Cdd:PRK13343 224 VVAEASDPPGL-QYLApFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY-Pgdifylhsrller 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493410791 273 --TLATEMGqlqdrivstkKGSVTSVQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRI 346
Cdd:PRK13343 301 aaKLSPELG----------GGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRV 366
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
76-351 |
1.43e-33 |
|
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: 127.72 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 76 PIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIH--------RSAPKfdeistkaEMFETGIKVIDLLEPYSRGGKT 147
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYPE--------EMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 148 GLFGGAGVGKTvlimELINNIAKQ------QSGFS-VFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGAR-- 218
Cdd:cd01135 73 PIFSGSGLPHN----ELAAQIARQagvvgsEENFAiVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERii 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 219 -QRVALTglsIAEYFRDEEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDR--IVSTKKGSVTS 295
Cdd:cd01135 149 tPRMALT---TAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493410791 296 VQAIYVPADDLTDPAPatafahlDAT-------TVLSRQIAELGIYPAVDPLDSTSRILDPNI 351
Cdd:cd01135 226 IPILTMPNDDITHPIP-------DLTgyitegqIYLDRDLHNKGIYPPIDVLPSLSRLMKSGI 281
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
6-405 |
2.88e-31 |
|
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: 125.22 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 6 ISQIIGPVVDVDfpEGRLPSILDALTITRPDGTK---LVLETQqhlGEERVRTVsMESTDGL-VRGTSVANTGMPIQVPV 81
Cdd:TIGR01040 5 VSGVNGPLVILD--NVKFPRFAEIVNLTLPDGTVrsgQVLEVS---GNKAVVQV-FEGTSGIdAKKTTCEFTGDILRTPV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 82 GPEVLSRMMNVVGEPIDgRGPVHTAKTY------SIHRSAPKFDEistkaEMFETGIKVIDLLEPYSRGGKTGLFGGAGV 155
Cdd:TIGR01040 79 SEDMLGRVFNGSGKPID-KGPPVLAEDYldingqPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKIPIFSAAGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 156 GKtvlimeliNNIAKQ---QSG----------------FS-VFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPP 215
Cdd:TIGR01040 153 PH--------NEIAAQicrQAGlvklptkdvhdghednFAiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 216 GAR---QRVALTglsIAEYFRDEEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRI--VSTKK 290
Cdd:TIGR01040 225 IERiitPRLALT---TAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 291 GSVTSVQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDPNI----VGDDHYDTAQavkQL 366
Cdd:TIGR01040 302 GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmTRKDHSDVSN---QL 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 493410791 367 LQRY---KDLQDIIAILGMDELSDEDKLVVSRARKVQR-FLSQ 405
Cdd:TIGR01040 379 YACYaigKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
46-406 |
4.26e-31 |
|
proton translocating ATP synthase, F1 alpha 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. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 125.19 E-value: 4.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 46 QHLGEERVRTVSMESTDGLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKA 125
Cdd:TIGR00962 63 LNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 126 EMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLIMELINNiAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTA 205
Cdd:TIGR00962 143 EPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIIN-QKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTI 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 206 LVFGQMNEPPGARQRVALTGLSIAEYFRDeEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRI 285
Cdd:TIGR00962 222 VVAATASDSASLQYLAPYTGCTMGEYFRD-NGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 286 --VSTKK--GSVTSVQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRildpniVGddhyDTAQ 361
Cdd:TIGR00962 301 akLNDEKggGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSR------VG----GAAQ 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 493410791 362 --AVKQL-------LQRYKDLqDIIAILGMDeLSDEDKLVVSRARKVQRFLSQP 406
Cdd:TIGR00962 371 ikAMKQVagslrleLAQYREL-EAFSQFASD-LDEATKKQLERGQRVVELLKQP 422
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
67-428 |
1.55e-29 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 119.62 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 67 GTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGK 146
Cdd:PRK05922 80 GAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 147 TGLFGGAGVGKTvlimELINNIAK-QQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTG 225
Cdd:PRK05922 160 IGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 226 LSIAEYFRDeEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKKGSVTSVQAI-YVP-- 302
Cdd:PRK05922 236 MTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAIlHYPnh 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 303 ADDLTDPAPATafahLDATTVLSRQIAELGiYPAVDPLDSTSRILDpNIVGDDHYDTAQAVKQLLQRYKDLQDIIAI--- 379
Cdd:PRK05922 315 PDIFTDYLKSL----LDGHFFLTPQGKALA-SPPIDILTSLSRSAR-QLALPHHYAAAEELRSLLKAYHEALDIIQLgay 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 493410791 380 -LGMD-ELSDEDKLVVSrarkVQRFLSQPFfvaeaftglaGKYVKLEETIK 428
Cdd:PRK05922 389 vPGQDaHLDRAVKLLPS----IKQFLSQPL----------SSYCALHNTLK 425
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
128-345 |
3.51e-26 |
|
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: 107.28 E-value: 3.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 128 FETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVlimeLINNIAKQ-QSGFSVFAGVGERtreGNDLWHEMME--------- 197
Cdd:cd01134 60 LLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTV----ISQSLSKWsNSDVVIYVGCGER---GNEMAEVLEEfpelkdpit 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 198 -SGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDeEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLAT 276
Cdd:cd01134 133 gESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 277 EMGQLQDR--IVST-----KKGSVTSVQAIYVPADDLTDP-APAT-----AFAHLDATTVLSRQiaelgiYPAVDPLDST 343
Cdd:cd01134 212 RLAEFYERagRVRClgspgREGSVTIVGAVSPPGGDFSEPvTQATlrivqVFWGLDKKLAQRRH------FPSINWLISY 285
|
..
gi 493410791 344 SR 345
Cdd:cd01134 286 SK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
126-397 |
1.10e-25 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 109.87 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 126 EMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVlimeLINNIAKQ-QSGFSVFAGVGERtreGNdlwhEMME------- 197
Cdd:PRK04192 209 EPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTV----TQHQLAKWaDADIVIYVGCGER---GN----EMTEvleefpe 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 198 -----SG--VIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDeEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGY 270
Cdd:PRK04192 278 lidpkTGrpLMERTVLIANTSNMPVAAREASIYTGITIAEYYRD-MGYDVLLMADSTSRWAEALREISGRLEEMPGEEGY 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 271 QPTLATEMGQLQDR--IVST---KKGSVTSVQAIYVPADDLTDP-APAT-----AFAHLDATTVLSRQiaelgiYPAVDP 339
Cdd:PRK04192 357 PAYLASRLAEFYERagRVKTlggEEGSVTIIGAVSPPGGDFSEPvTQNTlrivkVFWALDAELADRRH------FPAINW 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493410791 340 LDSTSRILD------PNIVGDDHYDTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLVVSRAR 397
Cdd:PRK04192 431 LTSYSLYLDqvapwwEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVAR 494
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
77-346 |
5.57e-24 |
|
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: 100.71 E-value: 5.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 77 IQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFDEISTKAEMFETGIKVIDLLEPYSRGGKTGLFGGAGVG 156
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 157 KTVLIMELINNiAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDeE 236
Cdd:cd01132 82 KTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD-N 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 237 GRDVLLFIDNIFRFTQAGSEVSALLGR------MPSAVGY-QPTLATEMGQLQDRIvstKKGSVTSVQAIYVPADDLTDP 309
Cdd:cd01132 160 GKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlHSRLLERAAKLSDEL---GGGSLTALPIIETQAGDVSAY 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 493410791 310 APATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRI 346
Cdd:cd01132 237 IPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-390 |
1.49e-21 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 96.64 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 5 KISQIIGPVVDVdfpEGRLPSILDALTITRPDGTKL--VLetqqHLGEERVRTVSMESTDGLVRGTSVANTGMPIQVPVG 82
Cdd:PRK02118 7 KITDITGNVITV---EAEGVGYGELATVERKDGSSLaqVI----RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 83 PEVLSRMMNVVGEPIDGrGPVHTAKTYSIhrSAPKFDEISTK--AEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVL 160
Cdd:PRK02118 80 ESLLGRRFNGSGKPIDG-GPELEGEPIEI--GGPSVNPVKRIvpREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 161 IMelinNIAKQ-QSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDEEGRD 239
Cdd:PRK02118 157 LA----RIALQaEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 240 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQDRIVSTKK-GSVTSVQAIYVPADDLTDPAPatafahl 318
Cdd:PRK02118 233 VLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDgGSITIIAVTTMPGDDVTHPVP------- 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493410791 319 DATTVlsrqIAELGIY---PAVDPLDSTSRiLDPNIVG----DDHYDTAQAVKQLLQRYKDLQDIIAiLGMDeLSDEDK 390
Cdd:PRK02118 306 DNTGY----ITEGQFYlrrGRIDPFGSLSR-LKQLVIGkktrEDHGDLMNAMIRLYADSREAKEKMA-MGFK-LSNWDE 377
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-74 |
3.48e-21 |
|
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: 86.83 E-value: 3.48e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493410791 6 ISQIIGPVVDVDFPEGRLPSILDALTITRPDGTKLVLETQQHLGEERVRTVSMESTDGLVRGTSVANTG 74
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
177-408 |
1.27e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 92.01 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 177 VFAGVGERTREGNDLWHEMME-------SGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDeEGRDVLLFIDNIFR 249
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKlkdpktgKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYDVALMADSTSR 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 250 FTQAGSEVSALLGRMPSAVGYQPTLATEMGQLQD---RIVST----KKGSVTSVQAIYVPADDLTDPAPATAFAHLDATT 322
Cdd:PRK14698 765 WAEALREISGRLEEMPGEEGYPAYLASKLAEFYEragRVVTLgsdyRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFW 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 323 VLSRQIAELGIYPAVDPLDSTSRILDP------NIVGDDHYDTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLVVSRA 396
Cdd:PRK14698 845 ALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVA 924
|
250
....*....|...
gi 493410791 397 RKVQR-FLSQPFF 408
Cdd:PRK14698 925 RMLREdYLQQDAF 937
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
356-415 |
2.81e-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: 78.64 E-value: 2.81e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 356 HYDTAQAVKQLLQRYKDLQDIIAILGMDELSDEDKLVVSRARKVQRFLSQPFFVAEAFTG 415
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIED 60
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
62-265 |
1.16e-17 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 85.01 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 62 DGL--VRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHRSAPKFdeISTKA--EMFETGIKVIDL 137
Cdd:CHL00059 57 DGLmiQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGI--ISRRSvyEPLQTGLIAIDS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 138 LEPYSRGGKTGLFGGAGVGKTVLIMELINNiAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTALVFGQMNEpPGA 217
Cdd:CHL00059 135 MIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADS-PAT 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493410791 218 RQRVA-LTGLSIAEYFRdEEGRDVLLFIDNIFRFTQAGSEVSALLGRMP 265
Cdd:CHL00059 213 LQYLApYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
35-265 |
1.87e-17 |
|
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: 84.71 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 35 PDGTK-LVLetqqHLGEERVRTVSMESTDGLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHR 113
Cdd:COG0056 56 PGGVYgMAL----NLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVER 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 114 SAPkfdEISTKA---EMFETGIKVIDLLEPYSRG-----------GKTglfggagvgkTVLIMELINNIAKQ-------- 171
Cdd:COG0056 132 PAP---GVIDRQpvhEPLQTGIKAIDAMIPIGRGqreliigdrqtGKT----------AIAIDTIINQKGKDviciyvai 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 172 -QSGFSVfAGVGERTREGndlwhemmesGVIDKTALVFGQMNEPPGArQRVA-LTGLSIAEYFRDeEGRDVLLFIDNIFR 249
Cdd:COG0056 199 gQKASTV-AQVVETLEEH----------GAMEYTIVVAATASDPAPL-QYIApYAGCAMGEYFMD-QGKDVLIVYDDLSK 265
|
250
....*....|....*.
gi 493410791 250 FTQAGSEVSALLGRMP 265
Cdd:COG0056 266 HAVAYRELSLLLRRPP 281
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
35-265 |
3.69e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 80.49 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 35 PDGTK-LVLetqqHLGEERVRTVSMESTDGLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPIDGRGPVHTAKTYSIHR 113
Cdd:PRK09281 56 PGGVYgIAL----NLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVER 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 114 SAPKFdeISTKA--EMFETGIKVIDLLEPYSRG-----------GKTglfggagvgkTVLIMELINNIAKQ--------- 171
Cdd:PRK09281 132 KAPGV--IDRKSvhEPLQTGIKAIDAMIPIGRGqreliigdrqtGKT----------AIAIDTIINQKGKDviciyvaig 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 172 QSGFSVfAGVGERTREgndlwHEMME-SGVIDKTAlvfgqmNEPPGArQRVA-LTGLSIAEYFRDeEGRDVLLFIDNIFR 249
Cdd:PRK09281 200 QKASTV-AQVVRKLEE-----HGAMEyTIVVAATA------SDPAPL-QYLApYAGCAMGEYFMD-NGKDALIVYDDLSK 265
|
250
....*....|....*.
gi 493410791 250 FTQAGSEVSALLGRMP 265
Cdd:PRK09281 266 QAVAYRQLSLLLRRPP 281
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
52-346 |
2.80e-12 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 68.53 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 52 RVRTVSMESTDGLVRGTSVANTGMPIQVPVGPEVLSRMMNVVGEPID------GRGPVHTAKTY-SIHRSAPKFDEISTK 124
Cdd:PTZ00185 90 RIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTLgKVDAGAPNIVSRSPV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 125 AEMFETGIKVIDLLEPYSRGGKTGLFGGAGVGKTVLIMELINN-------IAKQQSGFSVFAGVGERTREGNDLWHEMME 197
Cdd:PTZ00185 170 NYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 198 SGVIDKTALVFGQMNEPPGARQRVALTGLSIAEYFRDeEGRDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 277
Cdd:PTZ00185 250 YGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYL 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493410791 278 MGQLQDR--IVSTKK--GSVTSVQAIYVPADDLTDPAPATAFAHLDATTVLSRQIAELGIYPAVDPLDSTSRI 346
Cdd:PTZ00185 329 HSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRV 401
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
143-264 |
8.18e-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: 45.44 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 143 RGGKTGLFGGAGVGKTVLIMELINNIAKQQSGFSVFAGVGERTREGNDLWHEMMESGVIDKTalvfgqmnepPGARQRVA 222
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 493410791 223 LTGLsiaeyfrdEEGRDVLLFIDNIFRFTQAGSEVSALLGRM 264
Cdd:smart00382 71 LALA--------RKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-74 |
8.57e-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: 40.76 E-value: 8.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493410791 4 GKISQIIGPVVDVDFPEGrlPSILDALTITRPDGTKLVLETQQHLG--EERVRTVSMESTDGLVRGTSVANTG 74
Cdd:cd01426 2 GRVIRVNGPLVEAELEGE--VAIGEVCEIERGDGNNETVLKAEVIGfrGDRAILQLFESTRGLSRGALVEPTG 72
|
|
| ATP-synt_V_A-type_beta_C |
cd18112 |
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ... |
354-405 |
1.26e-04 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 40.88 E-value: 1.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 493410791 354 DDHYDTAQavkQLLQRY---KDLQDIIAILGMDELSDEDKLVVSRARKV-QRFLSQ 405
Cdd:cd18112 5 EDHRDVSN---QLYAAYargKDVRALAAIVGEEALSEEDRLYLEFADRFeREFINQ 57
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
352-428 |
2.63e-04 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 39.34 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493410791 352 VGDDHYDTAQAVKQLLQRYKDLQDIIAI----LGMDELSDEdklVVSRARKVQRFLSQPffVAEAFTglagkyvkLEETI 427
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRIgayqAGSDPEIDE---AIAKRPAINAFLRQG--VDEPVS--------FEETL 67
|
.
gi 493410791 428 K 428
Cdd:pfam18269 68 A 68
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
130-197 |
6.33e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 39.23 E-value: 6.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493410791 130 TGIKVIDLLEPYSRGGKTGLFGGAGVGKTV----LIMELINNIAKQQSGFSVFAGVGERTREGNDLWHEMME 197
Cdd:PRK14698 213 TGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdgdtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| |
