|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
122-588 |
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: 954.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 122 GIIHSVIGPVVDVYFE-DELPDILNAMEVEDAPIGHLVLEVFHHLGNNTVRCVAMDATEGLRRGQKVIDTGFPIRVAVGK 200
Cdd:COG0055 6 GKIVQVIGPVVDVEFPeGELPAIYNALEVENEGGGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 201 SVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTVLIME 280
Cdd:COG0055 86 ATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIME 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 281 LINNIAKSHGGYSVFVGAGERTREGNDLYYEMIESKVISldddtsKVALVYGQMNEPPGARNRVVLTGLTIAEYFRDIEG 360
Cdd:COG0055 166 LIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD------KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 361 QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITSVQAVYVPADDLSDPAPSATFSH 440
Cdd:COG0055 240 QDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 441 LDATTVLSRPIAELGIYPAVDPLDSSSRVLDPEVVGEDHYNVARAVQKTLQGYKSLQDIIAILGMDELSEEDKLTVARAR 520
Cdd:COG0055 320 LDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARAR 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820303933 521 KIQRFLSQPFSVAEIFTGHPGKMVPVEKSVDGFKRLLNGEYDDIPEIAFYMVGDIDEVLAKANQMAAS 588
Cdd:COG0055 400 KIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKKLKAE 467
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
121-585 |
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: 835.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 121 EGIIHSVIGPVVDVYFE-DELPDILNAMEVEDAPIGHLVLEVFHHLGNNTVRCVAMDATEGLRRGQKVIDTGFPIRVAVG 199
Cdd:TIGR01039 2 KGKVVQVIGPVVDVEFEqGELPRIYNALKVQNRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 200 KSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTVLIM 279
Cdd:TIGR01039 82 KETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 280 ELINNIAKSHGGYSVFVGAGERTREGNDLYYEMIESKVISldddtsKVALVYGQMNEPPGARNRVVLTGLTIAEYFRDIE 359
Cdd:TIGR01039 162 ELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID------KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 360 GQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITSVQAVYVPADDLSDPAPSATFS 439
Cdd:TIGR01039 236 GQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 440 HLDATTVLSRPIAELGIYPAVDPLDSSSRVLDPEVVGEDHYNVARAVQKTLQGYKSLQDIIAILGMDELSEEDKLTVARA 519
Cdd:TIGR01039 316 HLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1820303933 520 RKIQRFLSQPFSVAEIFTGHPGKMVPVEKSVDGFKRLLNGEYDDIPEIAFYMVGDIDEVLAKANQM 585
Cdd:TIGR01039 396 RRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAKKL 461
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
122-585 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 805.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 122 GIIHSVIGPVVDVYF-EDELPDILNAMEVEDA-PIGH---LVLEVFHHLGNNTVRCVAMDATEGLRRGQKVIDTGFPIRV 196
Cdd:CHL00060 17 GRITQIIGPVLDVAFpPGKMPNIYNALVVKGRdTAGQeinVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 197 AVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTV 276
Cdd:CHL00060 97 PVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 277 LIMELINNIAKSHGGYSVFVGAGERTREGNDLYYEMIESKVISLDD-DTSKVALVYGQMNEPPGARNRVVLTGLTIAEYF 355
Cdd:CHL00060 177 LIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNiAESKVALVYGQMNEPPGARMRVGLTALTMAEYF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 356 RDIEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITSVQAVYVPADDLSDPAPS 435
Cdd:CHL00060 257 RDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 436 ATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLDPEVVGEDHYNVARAVQKTLQGYKSLQDIIAILGMDELSEEDKLT 515
Cdd:CHL00060 337 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLT 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 516 VARARKIQRFLSQPFSVAEIFTGHPGKMVPVEKSVDGFKRLLNGEYDDIPEIAFYMVGDIDEVLAKANQM 585
Cdd:CHL00060 417 VARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANL 486
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
195-472 |
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: 579.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 195 RVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGK 274
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 275 TVLIMELINNIAKSHGGYSVFVGAGERTREGNDLYYEMIESKVISLDDDtSKVALVYGQMNEPPGARNRVVLTGLTIAEY 354
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGL-SKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 355 FRDIEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITSVQAVYVPADDLSDPAP 434
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1820303933 435 SATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLDP 472
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
122-577 |
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: 579.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 122 GIIHSVIGPVVDVYFEDELPDILNAMEVEDApiGHLVLEVFHHLGNNTVRCVAMDATEGLRRGQKVIDTGFPIRVAVGKS 201
Cdd:TIGR03305 1 GHVVAVRGSIVDVRFDGELPAIHSVLRAGRE--GEVVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 202 VLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTVLIMEL 281
Cdd:TIGR03305 79 TLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 282 INNIAKSHGGYSVFVGAGERTREGNDLYYEMIESKVIsldDDTskvALVYGQMNEPPGARNRVVLTGLTIAEYFRDIEGQ 361
Cdd:TIGR03305 159 IHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVL---DNT---VMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 362 DVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITSVQAVYVPADDLSDPAPSATFSHL 441
Cdd:TIGR03305 233 DVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 442 DATTVLSRPIAELGIYPAVDPLDSSSRVLDPEVVGEDHYNVARAVQKTLQGYKSLQDIIAILGMDELSEEDKLTVARARK 521
Cdd:TIGR03305 313 SASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1820303933 522 IQRFLSQPFSVAEIFTGHPGKMVPVEKSVDGFKRLLNGEYDDIPEIAFYMVGDIDE 577
Cdd:TIGR03305 393 LERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
195-469 |
1.94e-125 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 372.17 E-value: 1.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 195 RVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGK 274
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 275 TVLIMELINNIAKSHGGYSVFVGAGERTREGNDLYYEMIESkvisldDDTSKVALVYGQMNEPPGARNRVVLTGLTIAEY 354
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKS------GAMERTVVVANTANDPPGARMRVPYTGLTIAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 355 FRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKN--GSITSVQAVYVPADDLSDP 432
Cdd:cd19476 155 FRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDP 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 1820303933 433 APSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRV 469
Cdd:cd19476 234 IPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
248-467 |
1.08e-92 |
|
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: 285.40 E-value: 1.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 248 GIKVIDLLAPYVKGGKIGLFGGAGVGKTVLIMELINNIAKshgGYSVFVGAGERTREGNDLYYEMIESKVISldddtsKV 327
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALK------RT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 328 ALVYGQMNEPPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQER 407
Cdd:pfam00006 72 VVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820303933 408 ISST--KNGSITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSS 467
Cdd:pfam00006 151 AGRVkgKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
474-581 |
3.77e-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: 222.74 E-value: 3.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 474 VVGEDHYNVARAVQKTLQGYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFSVAEIFTGHPGKMVPVEKSVDGF 553
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 1820303933 554 KRLLNGEYDDIPEIAFYMVGDIDEVLAK 581
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
119-529 |
1.74e-63 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 216.44 E-value: 1.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 119 RREGIIHSVIGPVVDVyfedELPDilnamevedAPIGHLVL-----------EV--FHhlgNNTVRCVAMDATEGLRRGQ 185
Cdd:COG1157 18 RVSGRVTRVVGLLIEA----VGPD---------ASIGELCEietadgrpvlaEVvgFR---GDRVLLMPLGDLEGISPGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 186 KVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPD-LQELSVKpEVLVTGIKVIDLLAPYVKGGKI 264
Cdd:COG1157 82 RVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNpLERARIT-EPLDTGVRAIDGLLTVGRGQRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 265 GLFGGAGVGKTVLI-MelinnIAKshggYS---VFVGA--GERTREGNdlyyEMIESkviSLDDDT-SKVALVYGQMNEP 337
Cdd:COG1157 161 GIFAGSGVGKSTLLgM-----IAR----NTeadVNVIAliGERGREVR----EFIED---DLGEEGlARSVVVVATSDEP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 338 PGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSIT 417
Cdd:COG1157 225 PLMRLRAAYTATAIAEYFRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 418 SVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLdPEVVGEDHYNVARAVQKTLQGYKSLQ 497
Cdd:COG1157 304 AFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENE 382
|
410 420 430
....*....|....*....|....*....|....*.
gi 1820303933 498 DIIAI----LGMDELSEEdklTVARARKIQRFLSQP 529
Cdd:COG1157 383 DLIRIgayqPGSDPELDE---AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
195-469 |
6.28e-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: 193.55 E-value: 6.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 195 RVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGK 274
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 275 TVLIMELINNIAKShggYSVFVGAGERTREGNdlyyEMIESKvisLDDDT-SKVALVYGQMNEPPGARNRVVLTGLTIAE 353
Cdd:cd01136 81 STLLGMIARNTDAD---VNVIALIGERGREVR----EFIEKD---LGEEGlKRSVLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 354 YFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITSVQAVYVPADDLSDPA 433
Cdd:cd01136 151 YFRD-QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 1820303933 434 PSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRV 469
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
179-528 |
6.89e-52 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 185.27 E-value: 6.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 179 EGLRRGQKVI--DTGFPIrvAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLA 256
Cdd:PRK08472 75 EGFKIGDKVFisKEGLNI--PVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 257 PYVKGGKIGLFGGAGVGKTVLiMELInnIAKSHGGYSVFVGAGERTREgndlYYEMIESkviSLDDDTSKVALVYGQMNE 336
Cdd:PRK08472 153 TCGKGQKLGIFAGSGVGKSTL-MGMI--VKGCLAPIKVVALIGERGRE----IPEFIEK---NLGGDLENTVIVVATSDD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 337 PPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKN-GS 415
Cdd:PRK08472 223 SPLMRKYGAFCAMSVAEYFKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 416 ITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLDpEVVGEDHYNVARAVQKTLQGYKS 495
Cdd:PRK08472 302 ITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKE 380
|
330 340 350
....*....|....*....|....*....|....*...
gi 1820303933 496 LQDIIAI----LGMD-ELSEedklTVARARKIQRFLSQ 528
Cdd:PRK08472 381 NEVLIRIgayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
176-534 |
7.13e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 185.40 E-value: 7.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 176 DATEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSfIHNEPPDlqELSVKP--EVLVTGIKVID 253
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQWRE-LDCPPPS--PLTRQPieQMLTTGIRAID 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 254 LLAPYVKGGKIGLFGGAGVGKTVLIMELInniakSHGGYSVFVGA--GERTREgndlYYEMIESKVIslDDDTSKVALVY 331
Cdd:PRK06820 156 GILSCGEGQRIGIFAAAGVGKSTLLGMLC-----ADSAADVMVLAliGERGRE----VREFLEQVLT--PEARARTVVVV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 332 GQMNEPPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISST 411
Cdd:PRK06820 225 ATSDRPALERLKGLSTATTIAEYFRD-RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 412 KNGSITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLdPEVVGEDHYNVARAVQKTLQ 491
Cdd:PRK06820 304 DRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLA 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1820303933 492 GYKSLQDIIAI----LGMDELSEEdklTVARARKIQRFLSQpfSVAE 534
Cdd:PRK06820 383 CYQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ--DHSE 424
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
155-502 |
3.94e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 180.67 E-value: 3.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 155 GHLVLEVFHHLGNNTVrCVAMDATEGLRRGQKVI----DTGFPirvaVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHN 230
Cdd:PRK08972 57 GELEAEVVGFDGDLLY-LMPIEELRGVLPGARVTplgeQSGLP----VGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 231 EPpdLQELSVKP--EVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTVLI-MELINNIAKShggysVFVG-AGERTREgn 306
Cdd:PRK08972 132 PP--INPLSRRPitEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV-----IVVGlVGERGRE-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 307 dlYYEMIESkvISLDDDTSKVALVYGQMNEPPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGR 386
Cdd:PRK08972 203 --VKEFIEE--ILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 387 IPSAVGYQPTLSTDMGAMQERIS--STKNGSITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLD 464
Cdd:PRK08972 278 PPATKGYPPSVFAKLPALVERAGngGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEA 357
|
330 340 350
....*....|....*....|....*....|....*...
gi 1820303933 465 SSSRVLdPEVVGEDHYNVARAVQKTLQGYKSLQDIIAI 502
Cdd:PRK08972 358 SISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
184-471 |
1.68e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 170.95 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 184 GQKVIDTGfPIRVAVGKSVLGRIVNVVGDPIDERGEIK--SEFYSFIHNEPPDLQELSVKpEVLVTGIKVIDLLAPYVKG 261
Cdd:PRK06002 88 GDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPLApgTRPMSIDATAPPAMTRARVE-TGLRTGVRVIDIFTPLCAG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 262 GKIGLFGGAGVGKTVLIMELinniAKSHGGYSVFVG-AGERTREgndlYYEMIESkviSLDDDTSKVALVYGQMNEPPGA 340
Cdd:PRK06002 166 QRIGIFAGSGVGKSTLLAML----ARADAFDTVVIAlVGERGRE----VREFLED---TLADNLKKAVAVVATSDESPMM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 341 RNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERI--SSTKNGSITS 418
Cdd:PRK06002 235 RRLAPLTATAIAEYFRD-RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITG 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1820303933 419 VQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLD 471
Cdd:PRK06002 314 IFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLAR 366
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
129-530 |
6.81e-44 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 162.86 E-value: 6.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 129 GPVVDVYFED----ELPDILNAMeVEDAPIGHLVLEVFHHlgNNTVRCVAMDAtEGLRRGQKVIDTGFPIRVAVGKSVLG 204
Cdd:PRK08149 15 GPIIEAELPDvaigEICEIRAGW-HSNEVIARAQVVGFQR--ERTILSLIGNA-QGLSRQVVLKPTGKPLSVWVGEALLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 205 RIVNVVG-------DPIDERGEIKsefYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTVL 277
Cdd:PRK08149 91 AVLDPTGkiverfdAPPTVGPISE---ERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 278 IMELINniaksHGGYSVFVGA--GERTREgndlYYEMIESkvISLDDDTSKVALVYGQMNEPPGARNRVVLTGLTIAEYF 355
Cdd:PRK08149 168 MNMLIE-----HSEADVFVIGliGERGRE----VTEFVES--LRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 356 RDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITSVQAVYVPADDLSDPAPS 435
Cdd:PRK08149 237 RD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLLESEEEPDPIGD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 436 ATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLDpEVVGEDHYNVARAVQKTLQGYKSLQDIIailgmdELSE----- 510
Cdd:PRK08149 316 EIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAAAFRKLLTRLEELQLFI------DLGEyrrge 388
|
410 420
....*....|....*....|..
gi 1820303933 511 --EDKLTVARARKIQRFLSQPF 530
Cdd:PRK08149 389 naDNDRAMDKRPALEAFLKQDV 410
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
177-528 |
6.90e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 163.36 E-value: 6.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 177 ATEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEfySFIHNEPPDLQELSVKP--EVLVTGIKVIDL 254
Cdd:PRK05688 84 SVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAE--DWVPMDGPTINPLNRHPisEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 255 LAPYVKGGKIGLFGGAGVGKTVLImelinniakshGGYSVFVGA--------GERTREgndlYYEMIESkvISLDDDTSK 326
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGKSVLL-----------GMMTRFTEAdiivvgliGERGRE----VKEFIEH--ILGEEGLKR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 327 VALVYGQMNEPPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQE 406
Cdd:PRK05688 225 SVVVASPADDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 407 RISSTK--NGSITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLdPEVVGEDHYNVAR 484
Cdd:PRK05688 304 RAGNAEpgGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQ 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1820303933 485 AVQKTLQGYKSLQDIIAI----LGMDelsEEDKLTVARARKIQRFLSQ 528
Cdd:PRK05688 383 RFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
177-502 |
3.77e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 160.89 E-value: 3.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 177 ATEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKpEVLVTGIKVIDLLA 256
Cdd:PRK07594 72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVCWKDYDAMPPPAMVRQPIT-QPLMTGIRAIDSVA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 257 PYVKGGKIGLFGGAGVGKTVLIMELINniaKSHGGYSVFVGAGERTREgndlYYEMIEskvISLDDDTSK-VALVYGQMN 335
Cdd:PRK07594 151 TCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGRE----VREFID---FTLSEETRKrCVIVVATSD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 336 EPPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGS 415
Cdd:PRK07594 221 RPALERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 416 ITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLdPEVVGEDHYNVARAVQKTLQGYKS 495
Cdd:PRK07594 300 ITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQE 378
|
....*..
gi 1820303933 496 LQDIIAI 502
Cdd:PRK07594 379 VELLIRI 385
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
179-529 |
1.30e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 159.55 E-value: 1.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 179 EGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPY 258
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 259 VKGGKIGLFGGAGVGKTVLIMELINNIAKShggYSVFVGAGERTREgndlYYEMIEskVISLDDDTSKVALVYGQMNEPP 338
Cdd:PRK09099 161 GEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGRE----VREFIE--LILGEDGMARSVVVCATSDRSS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 339 GARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITS 418
Cdd:PRK09099 232 IERAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 419 VQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLdPEVVGEDHYNVARAVQKTLQGYKSLQD 498
Cdd:PRK09099 311 LYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVET 389
|
330 340 350
....*....|....*....|....*....|....*
gi 1820303933 499 IIAI----LGMDELSEEdklTVARARKIQRFLSQP 529
Cdd:PRK09099 390 LLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
179-528 |
2.55e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 158.76 E-value: 2.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 179 EGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPY 258
Cdd:PRK06936 80 YGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 259 VKGGKIGLFGGAGVGKTVLIMELINNIAKShggYSVFVGAGERTREgndlYYEMIESKVisLDDDTSKVALVYGQMNEPP 338
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRSAEVD---VTVLALIGERGRE----VREFIESDL--GEEGLRKAVLVVATSDRPS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 339 GARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITS 418
Cdd:PRK06936 231 MERAKAGFVATSIAEYFRD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 419 VQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLDpEVVGEDHYNVARAVQKTLQGYKSLQD 498
Cdd:PRK06936 310 LYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVEL 388
|
330 340 350
....*....|....*....|....*....|....
gi 1820303933 499 IIAI----LGMDELSEEdklTVARARKIQRFLSQ 528
Cdd:PRK06936 389 LLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
190-502 |
4.10e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 158.35 E-value: 4.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 190 TGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGG 269
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 270 AGVGK-TVLIMelinnIAK-SHGGYSVFVGAGERTREgndlYYEMIESKVisLDDDTSKVALVYGQMNEPPGARNRVVLT 347
Cdd:PRK07721 167 SGVGKsTLMGM-----IARnTSADLNVIALIGERGRE----VREFIERDL--GPEGLKRSIVVVATSDQPALMRIKGAYT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 348 GLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISSTKNGSITSVQAVYVPAD 427
Cdd:PRK07721 236 ATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGD 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820303933 428 DLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLdPEVVGEDHYNVARAVQKTLQGYKSLQDIIAI 502
Cdd:PRK07721 315 DMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
104-502 |
3.29e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 150.13 E-value: 3.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 104 GKVVGDNTFGKLVGKRreGIIHSVIGPVvdvyfedelpdilNAMEVEDapigHLVLEVfhhLGNNTVRC----------V 173
Cdd:PRK08927 10 GDIDTLVIYGRVVAVR--GLLVEVAGPI-------------HALSVGA----RIVVET---RGGRPVPCevvgfrgdraL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 174 AM--DATEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSF-IHNEPPDLQELSVKPEVLVTGIK 250
Cdd:PRK08927 68 LMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYpLRAPPPPAHSRARVGEPLDLGVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 251 VIDLLAPYVKGGKIGLFGGAGVGKTVLIMELINNIAKShggYSVFVGAGERTREGNdlyyEMIEskvisldDD-----TS 325
Cdd:PRK08927 148 ALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQ----EFLQ-------DDlgpegLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 326 KVALVYGQMNEPPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQ 405
Cdd:PRK08927 214 RSVVVVATSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 406 ERIS--STKNGSITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLdPEVVGEDHYNVA 483
Cdd:PRK08927 293 ERAGpgPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLV 371
|
410
....*....|....*....
gi 1820303933 484 RAVQKTLQGYKSLQDIIAI 502
Cdd:PRK08927 372 RRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
176-528 |
7.54e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 145.89 E-value: 7.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 176 DATEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEiKSEFYSFIHNEPP----DLQELSvkpEVLVTGIKV 251
Cdd:PRK06793 71 EQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAE-NIPLQKIKLDAPPihafEREEIT---DVFETGIKS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 252 IDLLAPYVKGGKIGLFGGAGVGKTVLIMELINNiAKSHggYSVFVGAGERTREGNDLYYEMIEskvislDDDTSKVALVY 331
Cdd:PRK06793 147 IDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKDFIRKELG------EEGMRKSVVVV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 332 GQMNEPPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAvGYQPTLSTDMGAMQERISST 411
Cdd:PRK06793 218 ATSDESHLMQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 412 KNGSITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLDpEVVGEDHYNVARAVQKTLQ 491
Cdd:PRK06793 296 QKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILS 374
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1820303933 492 GYKSlQDIIAILGMDELSEEDKLTVARARK---IQRFLSQ 528
Cdd:PRK06793 375 IYKE-NELYFKLGTIQENAENAYIFECKNKvegINTFLKQ 413
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
180-528 |
1.12e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 145.42 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 180 GLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEfySFIHNEPPDLQELSVKP--EVLVTGIKVIDLLAP 257
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGS--TPLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 258 YVKGGKIGLFGGAGVGKTVLImeliNNIAKSHGGYSVFVG-AGERTREgndlYYEMIESKVISldDDTSKVALVYGQMNE 336
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVLL----GMITRYTQADVVVVGlIGERGRE----VKEFIEHSLQA--AGMAKSVVVAAPADE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 337 PPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERI-SSTKNGS 415
Cdd:PRK07196 222 SPLMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 416 ITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLDpEVVGEDHYNVARAVQKTLQGYKS 495
Cdd:PRK07196 301 MTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMA 379
|
330 340 350
....*....|....*....|....*....|....*..
gi 1820303933 496 LQDIIA----ILGMDELSEEdklTVARARKIQRFLSQ 528
Cdd:PRK07196 380 IKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
121-194 |
7.37e-32 |
|
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: 118.00 E-value: 7.37e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1820303933 121 EGIIHSVIGPVVDVYF-EDELPDILNAMEVEDAPIGHLVLEVFHHLGNNTVRCVAMDATEGLRRGQKVIDTGFPI 194
Cdd:cd18115 2 TGKIVQVIGPVVDVEFpEGELPPIYNALEVKGDDGKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
195-502 |
1.92e-30 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 124.90 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 195 RVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPD-LQELSVKpEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVG 273
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNpLQRTPIE-HVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 274 KTVLImeliNNIAKSHGGYSVFVG-AGERTREGNDlYYEMI-------ESKVISLDDDTSkvalvygqmnepPGARNRVV 345
Cdd:PRK07960 188 KSVLL----GMMARYTQADVIVVGlIGERGREVKD-FIENIlgaegraRSVVIAAPADVS------------PLLRMQGA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 346 LTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISS--TKNGSITSVQAVY 423
Cdd:PRK07960 251 AYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVL 329
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820303933 424 VPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLdPEVVGEDHYNVARAVQKTLQGYKSLQDIIAI 502
Cdd:PRK07960 330 TEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM-TALIDEQHYARVRQFKQLLSSFQRNRDLVSV 407
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
193-468 |
2.54e-30 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 120.76 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 193 PIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYS---FIHNEP-----PDLQELS-VKPevLVTGIKVIDLLAPYVKGGK 263
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGSIFIPrgvNVQRWPvrqprPVKEKLPpNVP--LLTGQRVLDTLFPVAKGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 264 IGLFGGAGVGKTVlimeLINNIAKshggYS-----VFVGAGERtreGNDL------YYEM-IESKVISLDDDTskvALVY 331
Cdd:cd01134 79 AAIPGPFGCGKTV----ISQSLSK----WSnsdvvIYVGCGER---GNEMaevleeFPELkDPITGESLMERT---VLIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 332 GQMNEPPGARNRVVLTGLTIAEYFRDIeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERI--- 408
Cdd:cd01134 145 NTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrv 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820303933 409 ----SSTKNGSITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSR 468
Cdd:cd01134 224 rclgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
178-530 |
1.10e-29 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 122.63 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 178 TEGL-RRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEP--PDLQElsvKP-EVLVTGIKVID 253
Cdd:PRK04196 59 TTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVARE---YPeEFIQTGISAID 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 254 LLAPYVKGGKIGLFGGAGVGKTVLIMELINNiAKSHGGYS----VFVGAGERTREGNDLYYEMIESKVIsldddtSKVAL 329
Cdd:PRK04196 136 GLNTLVRGQKLPIFSGSGLPHNELAAQIARQ-AKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGAL------ERSVV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 330 VYGQMNEPpgARNRVVL--TGLTIAEYFRDIEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQER 407
Cdd:PRK04196 209 FLNLADDP--AIERILTprMALTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 408 --ISSTKNGSITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRVLD----PEVVGEDHYN 481
Cdd:PRK04196 287 agRIKGKKGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKdgigEGKTREDHKD 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1820303933 482 VARAVQKTLQGYKSLQDIIAILGMDELSEEDKLTVARARKI-QRFLSQPF 530
Cdd:PRK04196 367 VANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGF 416
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
240-528 |
2.02e-28 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 120.27 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 240 VKPevLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTVLImeliNNIAKshggYS-----VFVGAGERtreGNdlyyEMIE 314
Cdd:PRK04192 208 VEP--LITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQ----HQLAK----WAdadivIYVGCGER---GN----EMTE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 315 skVIS----LDD---------------DTSkvalvygqmNEPPGARNRVVLTGLTIAEYFRDIeGQDVLLFIDNIFRFTQ 375
Cdd:PRK04192 271 --VLEefpeLIDpktgrplmertvliaNTS---------NMPVAAREASIYTGITIAEYYRDM-GYDVLLMADSTSRWAE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 376 AGSEVSALLGRIPSAVGYQPTLSTDMGAMQER--ISSTKN---GSITSVQAVYVPADDLSDPAPSATfshLDATTV---L 447
Cdd:PRK04192 339 ALREISGRLEEMPGEEGYPAYLASRLAEFYERagRVKTLGgeeGSVTIIGAVSPPGGDFSEPVTQNT---LRIVKVfwaL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 448 SRPIAELGIYPAVDPLDSSSRVLD------PEVVGEDHYNVARAVQKTLQGYKSLQDIIAILGMDELSEEDKLTVARARK 521
Cdd:PRK04192 416 DAELADRRHFPAINWLTSYSLYLDqvapwwEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARL 495
|
....*...
gi 1820303933 522 I-QRFLSQ 528
Cdd:PRK04192 496 IrEDFLQQ 503
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
193-468 |
1.60e-27 |
|
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: 112.70 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 193 PIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGV 272
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 273 GKTVLIMELINNiAKSHGGYS----VFVGAGERTREGNDLYYEMIESKVISldddtsKVALVYGQMNEPPGARNRVVLTG 348
Cdd:cd01135 81 PHNELAAQIARQ-AGVVGSEEnfaiVFAAMGVTMEEARFFKDDFEETGALE------RVVLFLNLANDPTIERIITPRMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 349 LTIAEYFRDIEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISST--KNGSITSVQAVYVPA 426
Cdd:cd01135 154 LTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVegRKGSITQIPILTMPN 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1820303933 427 DDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSR 468
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
163-469 |
1.68e-23 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 104.61 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 163 HHLGNNTVRCVAMDATEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQELSVKP 242
Cdd:PRK13343 64 FNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 243 EVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTVLIMELINNiAKSHGGYSVFVGAGERT----------REGNDLYYEM 312
Cdd:PRK13343 144 EPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN-QKDSDVICVYVAIGQKAsavarvietlREHGALEYTT 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 313 IeskvisldddtskvalVYGQMNEPPGARNRVVLTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVG 392
Cdd:PRK13343 223 V----------------VVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 393 YqP---------------TLSTDMGAmqerisstknGSITSVQAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIY 457
Cdd:PRK13343 286 Y-PgdifylhsrlleraaKLSPELGG----------GSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQR 354
|
330
....*....|..
gi 1820303933 458 PAVDPLDSSSRV 469
Cdd:PRK13343 355 PAVDVGLSVSRV 366
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
162-531 |
2.24e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 103.45 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 162 FHhlgNNTVRCVAMDATEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPdlQELSVK 241
Cdd:PRK05922 61 FH---NRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPP--SPMSRQ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 242 P--EVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTvlimELINNIAK-SHGGYSVFVGAGERTREGNDlYYEMIESKVi 318
Cdd:PRK05922 136 PiqEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEGL- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 319 slddDTSKVALVYGQMNEPPGARnrvVLTG---LTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQP 395
Cdd:PRK05922 210 ----AAQRTIIIASPAHETAPTK---VIAGraaMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 396 TLSTDMGAMQERISSTKNGSITSVQAV-YVP--ADDLSDPAPSAtfshLDATTVLSrPIAELGIYPAVDPLDSSSRVLDp 472
Cdd:PRK05922 282 SVFHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSL----LDGHFFLT-PQGKALASPPIDILTSLSRSAR- 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820303933 473 EVVGEDHYNVARAVQKTLQGYKSLQDIIAiLGMDELSEEDKLTvaRARK----IQRFLSQPFS 531
Cdd:PRK05922 356 QLALPHHYAAAEELRSLLKAYHEALDIIQ-LGAYVPGQDAHLD--RAVKllpsIKQFLSQPLS 415
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
158-537 |
6.90e-21 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 96.33 E-value: 6.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 158 VLEVFhhlGNNTVRCVaMDATEGLRRGQKVID-TGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQ 236
Cdd:TIGR01040 41 VLEVS---GNKAVVQV-FEGTSGIDAKKTTCEfTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 237 ELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKtvlimeliNNIAKShggysVFVGAGERTREGNDLyyemiesk 316
Cdd:TIGR01040 117 ARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH--------NEIAAQ-----ICRQAGLVKLPTKDV-------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 317 visLDDDTSKVALVYGQMN-------------EPPGARNRVVL-----------------TGLTIAEYFRDIEGQDVLLF 366
Cdd:TIGR01040 176 ---HDGHEDNFAIVFAAMGvnmetarffkqdfEENGSMERVCLflnlandptieriitprLALTTAEYLAYQCEKHVLVI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 367 IDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERISST--KNGSITSVQAVYVPADDLSDPAPSATFSHLDAT 444
Cdd:TIGR01040 253 LTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRNGSITQIPILTMPNDDITHPIPDLTGYITEGQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 445 TVLSRPIAELGIYPAVDPLDSSSRVLDpEVVGE-----DHYNVARAVQKTLQGYKSLQDIIAILGMDELSEEDKLTVARA 519
Cdd:TIGR01040 333 IYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVGEEALSSEDLLYLEFL 411
|
410 420
....*....|....*....|
gi 1820303933 520 RKIQR-FLSQ-PFSVAEIFT 537
Cdd:TIGR01040 412 DKFEKnFIAQgPYENRTIFE 431
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
479-548 |
2.78e-20 |
|
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: 85.19 E-value: 2.78e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 479 HYNVARAVQKTLQGYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFSVAEIFTGHPGKMVPVEK 548
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
294-558 |
4.13e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 95.47 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 294 VFVGAGERTREGNDLYYEMIESKvislDDDTSK-----VALVYGQMNEPPGARNRVVLTGLTIAEYFRDIeGQDVLLFID 368
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEEFPKLK----DPKTGKplmerTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYDVALMAD 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 369 NIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQERI-------SSTKNGSITSVQAVYVPADDLSDPAPSATFSHL 441
Cdd:PRK14698 761 STSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 442 DATTVLSRPIAELGIYPAVDPLDSSSRVLDPeVVGEDHYNVA---RAVQ----KTLQGYKSLQDIIAILGMDELSEEDKL 514
Cdd:PRK14698 841 KVFWALDADLARRRHFPAINWLTSYSLYVDA-VKDWWHKNVDpewKAMRdkamELLQKEAELQEIVRIVGPDALPERERA 919
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1820303933 515 TVARARKIQRFLSQPFSVAEIFTghpgkMVPVEKSVDGFKRLLN 558
Cdd:PRK14698 920 ILLVARMLREDYLQQDAFDEVDT-----YCPPEKQVTMMRVLLN 958
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
196-469 |
4.92e-19 |
|
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: 87.61 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 196 VAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNEPPDLQE-LSVKpEVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGK 274
Cdd:cd01132 4 VPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPrQSVN-EPLQTGIKAIDSLIPIGRGQRELIIGDRQTGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 275 TVLIMELINNiAKSHGGYSVFVGAGERTREGNDLYYEMIESKVIsldDDTSKVAlvyGQMNEPPGARNRVVLTGLTIAEY 354
Cdd:cd01132 83 TAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAM---EYTIVVA---ATASDPAPLQYLAPYAGCAMGEY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 355 FRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYqP---------------TLSTDMGAmqerisstknGSITSV 419
Cdd:cd01132 156 FRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAY-PgdvfylhsrlleraaKLSDELGG----------GSLTAL 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1820303933 420 QAVYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRV 469
Cdd:cd01132 224 PIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRV 273
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
124-191 |
1.53e-18 |
|
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: 79.90 E-value: 1.53e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1820303933 124 IHSVIGPVVDVYF-EDELPDILNAMEVEDAPIGHLVLEVFHHLGNNTVRCVAMDATEGLRRGQKVIDTG 191
Cdd:pfam02874 1 IVQVIGPVVDVEFgIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
178-513 |
3.43e-16 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 81.23 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 178 TEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKsefysfihNEPPDLQELSVKP-------EVLVTGIK 250
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELE--------GEPIEIGGPSVNPvkrivprEMIRTGIP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 251 VIDLLAPYVKGGKIGLFGGAGVGKTVLIMelinNIA-KSHGGYSVFVGAGERtregNDLYYEMIE--SKVISLDddtsKV 327
Cdd:PRK02118 130 MIDVFNTLVESQKIPIFSVSGEPYNALLA----RIAlQAEADIIILGGMGLT----FDDYLFFKDtfENAGALD----RT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 328 ALVYGQMNEPPGARNRVVLTGLTIAEYFRDIEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQER 407
Cdd:PRK02118 198 VMFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 408 -ISSTKNGSITSVQAVYVPADDLSDPAPsatfshlDATTVlsrpIAELGIY---PAVDPLDSSSRvLDPEVVG----EDH 479
Cdd:PRK02118 278 aVDFEDGGSITIIAVTTMPGDDVTHPVP-------DNTGY----ITEGQFYlrrGRIDPFGSLSR-LKQLVIGkktrEDH 345
|
330 340 350
....*....|....*....|....*....|....
gi 1820303933 480 YNVARAVQKTLQGYKSLQDIIAiLGMDeLSEEDK 513
Cdd:PRK02118 346 GDLMNAMIRLYADSREAKEKMA-MGFK-LSNWDE 377
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
168-388 |
1.07e-15 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 80.11 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 168 NTVRCVAMDATEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSFIHNE-PPDLQELSVKpEVLV 246
Cdd:PRK09281 69 DNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKaPGVIDRKSVH-EPLQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 247 TGIKVIDLLAPyvkggkIG------LFGGAGVGKTVLIMELINNiAKSHGGYSVFVGAGERtregndlyyemieskvisl 320
Cdd:PRK09281 148 TGIKAIDAMIP------IGrgqrelIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQK------------------- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 321 dddTSKVALV------YGQM----------NEPPGarnrvvL------TGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGS 378
Cdd:PRK09281 202 ---ASTVAQVvrkleeHGAMeytivvaataSDPAP------LqylapyAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYR 271
|
250
....*....|
gi 1820303933 379 EVSALLGRIP 388
Cdd:PRK09281 272 QLSLLLRRPP 281
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
148-469 |
6.71e-14 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 74.61 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 148 EVEDAPIGhLVLevfhHLGNNTVRCVAMDATEGLRRGQKVIDTGFPIRVAVGKSVLGRIVNVVGDPIDERGEIKSEFYSF 227
Cdd:CHL00059 33 EFEDGTIG-IAL----NLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 228 IhnEPPDLQELSVKP--EVLVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTVLIMELINNiAKSHGGYSVFVGAGERT--- 302
Cdd:CHL00059 108 I--ESPAPGIISRRSvyEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKAssv 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 303 -------REGNDLYYEMIeskvisldddtskvalVYGQMNEPPGARNRVVLTGLTIAEYFRdIEGQDVLLFIDNIFRFTQ 375
Cdd:CHL00059 185 aqvvttlQERGAMEYTIV----------------VAETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 376 AGSEVSALLGRIPSAVGYqP---------------TLSTDMGAmqerisstknGSITSVQAVYVPADDLSDPAPSATFSH 440
Cdd:CHL00059 248 AYRQMSLLLRRPPGREAY-PgdvfylhsrlleraaKLSSQLGE----------GSMTALPIVETQAGDVSAYIPTNVISI 316
|
330 340
....*....|....*....|....*....
gi 1820303933 441 LDATTVLSRPIAELGIYPAVDPLDSSSRV 469
Cdd:CHL00059 317 TDGQIFLSADLFNAGIRPAINVGISVSRV 345
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
122-492 |
2.42e-10 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 63.52 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 122 GIIHSVIGPVVDVYFEDELPDIL--NAMEVEDAPIGHLVLEVFHHLGNNTVRCVAMDATEGLRRGQKVIDTGFPIRVAVG 199
Cdd:PTZ00185 41 GYVHSIDGTIATLIPAPGNPGVAynTIIMIQVSPTTFAAGLVFNLEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPVG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 200 KSVLGRIVNVVGDPID------ERGEIKSEF-YSFIHNEPPDLQELSVKPEVLVTGIKVIDLLAPYVKGGKIGLFGGAGV 272
Cdd:PTZ00185 121 AGVLGKVVNPLGHEVPvglltrSRALLESEQtLGKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 273 GKTVLIMELINN-------IAKSHGGYSVFVGAGERTREGNDLYyemiesKVISLDDDTSKVALVYGQMNEPPGARNRVV 345
Cdd:PTZ00185 201 GKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIH------RLLRSYGALRYTTVMAATAAEPAGLQYLAP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 346 LTGLTIAEYFRDiEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLSTDMGAMQER---ISSTK-NGSITSVQA 421
Cdd:PTZ00185 275 YSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERaamLSPGKgGGSVTALPI 353
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820303933 422 VYVPADDLSDPAPSATFSHLDATTVLSRPIAELGIYPAVDPLDSSSRvldpevVGEDHYNVA-RAVQKTLQG 492
Cdd:PTZ00185 354 VETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR------VGSSAQNVAmKAVAGKLKG 419
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
180-468 |
1.91e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 57.02 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 180 GLRRGQKVIDTgfpIRVAVGKSVLGRIVNVVGDPIDERGEiksefysfihnEPPDLQELSVKPE---VLVTG-----IKV 251
Cdd:PRK12608 58 NLRTGDVVEGV---ARPRERYRVLVRVDSVNGTDPEKLAR-----------RPHFDDLTPLHPRerlRLETGsddlsMRV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 252 IDLLAPYVKGGKIGLFGGAGVGKTVLIMELINNIAKSHGG---YSVFVGagERTREGNDLYYEmIESKVISLDDDtskva 328
Cdd:PRK12608 124 VDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEvhlMVLLID--ERPEEVTDMRRS-VKGEVYASTFD----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 329 lvygqmnEPPgaRNRVVLTGLTIAEYFRDIE-GQDVLLFIDNIFRFTQAGSEVSALLGRipsavgyqpTLS--TDMGAMQ 405
Cdd:PRK12608 196 -------RPP--DEHIRVAELVLERAKRLVEqGKDVVILLDSLTRLARAYNNEVESSGR---------TLSggVDARALQ 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820303933 406 --ERI-SSTKN----GSITSVQAVYVpadDLSDPAPSATFSHLDAT----TVLSRPIAELGIYPAVDPLDSSSR 468
Cdd:PRK12608 258 rpKRLfGAARNieegGSLTIIATALV---DTGSRMDEVIFEEFKGTgnmeIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
260-386 |
3.41e-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: 47.37 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 260 KGGKIGLFGGAGVGKTVLIMELINNIAKSHGGysVFVGAGERTREGNDLYYEMIeskvisldddtskvalvYGQMNEPPG 339
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--VIYIDGEDILEEVLDQLLLI-----------------IVGGKKASG 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1820303933 340 ARNRVVLTGLTIAEYFRDIegqdvLLFIDNIFRFTQAGSEVSALLGR 386
Cdd:smart00382 62 SGELRLRLALALARKLKPD-----VLILDEITSLLDAEQEALLLLLE 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
580-659 |
4.40e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 580 AKANQMAASMAPEEGAPKteQKDDGKDKTDETKGEGRETKGDDKKARGDDEETKGNDKVERKAEKGKK-DEAENKKDDKD 658
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEK--KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKaDEAKKKAEEKK 1431
|
.
gi 1820303933 659 K 659
Cdd:PTZ00121 1432 K 1432
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
580-659 |
7.84e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 580 AKANQMAASMAPEEGAPKTEQKDDGKDKTDETKGEGRETKGDDKKARGDDEETKGNDKVERKAEKGKKDEAENKKDDKDK 659
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
576-659 |
8.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 576 DEVLAKANQMAASMAPEEGAPKTEQKDDGKDKTDETKGEGRETKGDDKkARGDDEETKGNDKVERKAEKGKK-DEAENKK 654
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKAEEAKKKAEEAKKaDEAKKKA 1479
|
....*
gi 1820303933 655 DDKDK 659
Cdd:PTZ00121 1480 EEAKK 1484
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
580-659 |
9.14e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820303933 580 AKANQMAASMAPEEGAPKTE---QKDDGKDKTDETKGEGRETKGDDKKARGDDEETKGNDKVERKAEKGKK-DEAENKKD 655
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADaakKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKaDEAKKKAE 1441
|
....
gi 1820303933 656 DKDK 659
Cdd:PTZ00121 1442 EAKK 1445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
595-658 |
2.08e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820303933 595 APKTEQKDDGKDKTDETKGEGRETKGDDKKARGDDEETKGNDKVERKAEKGKKDEAENKKDDKD 658
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
242-314 |
2.48e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 41.16 E-value: 2.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1820303933 242 PEV-LVTGIKVIDLLAPYVKGGKIGLFGGAGVGKTV----LIMELINNIAKSHGGYSVFVGAGERTREGNDLYYEMIE 314
Cdd:PRK14698 207 PEVpLITGQRVIDTFFPQAKGGTAAIPGPFGSGKCVdgdtLILTKEFGLIKIKDLYEILDGKGKKTVEGNEEWTELEE 284
|
|
| Ribosomal_L12p |
cd05832 |
Ribosomal protein L12p. This subfamily includes archaeal L12p, the protein that is ... |
574-618 |
6.71e-03 |
|
Ribosomal protein L12p. This subfamily includes archaeal L12p, the protein that is functionally equivalent to L7/L12 in bacteria and the P1 and P2 proteins in eukaryotes. L12p is homologous to P1 and P2 but is not homologous to bacterial L7/L12. It is located in the L12 stalk, with proteins L10, L11, and 23S rRNA. L12p is the only protein in the ribosome to occur as multimers, always appearing as sets of dimers. Recent data indicate that most archaeal species contain six copies of L12p (three homodimers), while eukaryotes have four copies (two heterodimers), and bacteria may have four or six copies (two or three homodimers), depending on the species. The organization of proteins within the stalk has been characterized primarily in bacteria, where L7/L12 forms either two or three homodimers and each homodimer binds to the extended C-terminal helix of L10. L7/L12 is attached to the ribosome through L10 and is the only ribosomal protein that does not directly interact with rRNA. Archaeal L12p is believed to function in a similar fashion. However, hybrid ribosomes containing the large subunit from E. coli with an archaeal stalk are able to bind archaeal and eukaryotic elongation factors but not bacterial elongation factors. In several mesophilic and thermophilic archaeal species, the binding of 23S rRNA to protein L11 and to the L10/L12p pentameric complex was found to be temperature-dependent and cooperative.
Pssm-ID: 100110 [Multi-domain] Cd Length: 106 Bit Score: 36.71 E-value: 6.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1820303933 574 DIDEVLAKANQMAASMAPEEGAPKTEQKDDGKDKTDETKGEGRET 618
Cdd:cd05832 49 NIDEAIKKAAVAAAAAAPAAAAAAAAEEKAEEKEEEKKKEEEKEE 93
|
|
| 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 ... |
477-528 |
8.18e-03 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 36.26 E-value: 8.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1820303933 477 EDHYNVARavqktlQGY------KSLQDIIAILGMDELSEEDKLTVARARKI-QRFLSQ 528
Cdd:cd18112 5 EDHRDVSN------QLYaayargKDVRALAAIVGEEALSEEDRLYLEFADRFeREFINQ 57
|
|
| |
