|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
4-513 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1013.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 4 LTINADDVRNALNDFAASYEPSgTDRTEVGRVISAADGIARVEGLPSVMANELLRFENGIQGLAQNLDTREIGVVVLGEF 83
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAE-AEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 84 QEIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPI 163
Cdd:PRK09281 80 EDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 164 GRGQRQLIIGDRQTGKTAIAVDTILNQKanwesgdvEKQVRCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDP 243
Cdd:PRK09281 160 GRGQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 244 AGFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDEMGAG 323
Cdd:PRK09281 232 APLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 324 SMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDLAQYRD 403
Cdd:PRK09281 312 SLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 404 QQAFSMFASDLDPATRRQLARGERLMELLKQPQYSPYPVEEQVVSIWAGSKGHLDEVPVQDVLRFEREFIDHLRR-HTSV 482
Cdd:PRK09281 392 LEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSnHADL 471
|
490 500 510
....*....|....*....|....*....|.
gi 738382901 483 LTDIASTGKLEDGTVSALESAVAEFSKGFQS 513
Cdd:PRK09281 472 LEEIRETKDLSDEIEAKLKAAIEEFKKTFAA 502
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
4-515 |
0e+00 |
|
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: 1002.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 4 LTINADDVRNALNDFAASYEPSgTDRTEVGRVISAADGIARVEGLPSVMANELLRFENGIQGLAQNLDTREIGVVVLGEF 83
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPE-VEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 84 QEIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPI 163
Cdd:COG0056 80 EGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 164 GRGQRQLIIGDRQTGKTAIAVDTILNQKanwesgdvEKQVRCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDP 243
Cdd:COG0056 160 GRGQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 244 AGFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDEMGAG 323
Cdd:COG0056 232 APLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 324 SMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDLAQYRD 403
Cdd:COG0056 312 SLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 404 QQAFSMFASDLDPATRRQLARGERLMELLKQPQYSPYPVEEQVVSIWAGSKGHLDEVPVQDVLRFEREFIDHLR-RHTSV 482
Cdd:COG0056 392 LEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRaKHPDL 471
|
490 500 510
....*....|....*....|....*....|...
gi 738382901 483 LTDIASTGKLEDGTVSALESAVAEFSKGFQSSE 515
Cdd:COG0056 472 LKEIRETGKLDDEIEEKLKAAIEEFKKTFAASA 504
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
5-511 |
0e+00 |
|
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: 827.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 5 TINADDVRNALNDFAASYEPSgTDRTEVGRVISAADGIARVEGLPSVMANELLRFENGIQGLAQNLDTREIGVVVLGEFQ 84
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVD-SEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 85 EIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIG 164
Cdd:TIGR00962 80 DIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 165 RGQRQLIIGDRQTGKTAIAVDTILNQKANWesgdvekqVRCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDPA 244
Cdd:TIGR00962 160 RGQRELIIGDRQTGKTAVAIDTIINQKDSD--------VYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 245 GFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDEMGAGS 324
Cdd:TIGR00962 232 SLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 325 MTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDLAQYRDQ 404
Cdd:TIGR00962 312 LTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYREL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 405 QAFSMFASDLDPATRRQLARGERLMELLKQPQYSPYPVEEQVVSIWAGSKGHLDEVPVQDVLRFEREFIDHLRR-HTSVL 483
Cdd:TIGR00962 392 EAFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDAnHPDIL 471
|
490 500
....*....|....*....|....*...
gi 738382901 484 TDIASTGKLEDGTVSALESAVAEFSKGF 511
Cdd:TIGR00962 472 EEINTTKKLTEELEAKLKEALKNFKKTF 499
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
20-513 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 745.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 20 ASYEPsGTDRTEVGRVISAADGIARVEGLPSVMANELLRFENGIQGLAQNLDTREIGVVVLGEFQEIREGMEVQRTGEIL 99
Cdd:PRK13343 17 ARYEP-QPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 100 SVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:PRK13343 96 EVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 180 TAIAVDTILNQKanwesgdvEKQVRCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDPAGFKYLAPYAGSAIGQ 259
Cdd:PRK13343 176 TAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 260 HWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDEMGAGSMTGLPIIETKANDVS 339
Cdd:PRK13343 248 YFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGELS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 340 AYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDLAQYRDQQAFSMFASDLDPATR 419
Cdd:PRK13343 328 AYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 420 RQLARGERLMELLKQPQYSPYPVEEQVVSIWAGSKGHLDEVPVQDVLRFEREFIDHLR-RHTSVLTDIASTGKLEDGTVS 498
Cdd:PRK13343 408 KQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDaRFAALSLALESPRELDEAWLA 487
|
490
....*....|....*
gi 738382901 499 ALESAVAEFSKGFQS 513
Cdd:PRK13343 488 ALEEILREAGERFAA 502
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
32-515 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 735.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 32 VGRVISAADGIARVEGLPSVMANELLRFENGIQGLAQNLDTREIGVVVLGEFQEIREGMEVQRTGEILSVPVGDAFLGRV 111
Cdd:CHL00059 7 TGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 112 VDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGKTAIAVDTILNQK 191
Cdd:CHL00059 87 VNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 192 AnwesgdveKQVRCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDPAGFKYLAPYAGSAIGQHWMYGGKHVLII 271
Cdd:CHL00059 167 G--------QNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 272 FDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDEMGAGSMTGLPIIETKANDVSAYIPTNVISITD 351
Cdd:CHL00059 239 YDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 352 GQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDLAQYRDQQAFSMFASDLDPATRRQLARGERLMEL 431
Cdd:CHL00059 319 GQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLREL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 432 LKQPQYSPYPVEEQVVSIWAGSKGHLDEVPVQDVLRFEREFIDHLRRHTSVLTD-IASTGKLEDGTVSALESAVAEFSKG 510
Cdd:CHL00059 399 LKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEiISSTKTFTEEAEALLKEAIQEQLEL 478
|
....*
gi 738382901 511 FQSSE 515
Cdd:CHL00059 479 FLLQE 483
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
98-379 |
0e+00 |
|
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: 551.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 98 ILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQT 177
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 178 GKTAIAVDTILNQKanwesgdvEKQVRCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDPAGFKYLAPYAGSAI 257
Cdd:cd01132 81 GKTAIAIDTIINQK--------GKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 258 GQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDEMGAGSMTGLPIIETKAND 337
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 738382901 338 VSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVG 379
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
65-469 |
4.00e-121 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 368.21 E-value: 4.00e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 65 GLAQNLDTR-EIGVVVLGEFQEIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDdLGPIeAEGRRALELQ------- 136
Cdd:PTZ00185 80 GLVFNLEKDgRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLL-TRSRALLESEqtlgkvd 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 137 --APTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGKTAIAVDTILNQKANWESGDVEKQVRCVYVAVGQKA 214
Cdd:PTZ00185 158 agAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQRC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 215 STIAGVRATLEEHGALEYTTIVASPASDPAGFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPG 294
Cdd:PTZ00185 238 SNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPG 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 295 REAYPGDVFYLHSRLLERCAKLSDEMGAGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGIS 374
Cdd:PTZ00185 318 REAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLS 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 375 VSRVGGAAQVKAMKKVSGTLKLDLAQYRDQQAFSMFASDLDPATrrqLARGERLMELLKQPQysPYPVEEQVVSIWAGSK 454
Cdd:PTZ00185 398 VSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYACLN 472
|
410
....*....|....*
gi 738382901 455 GHLDEVPVQDVLRFE 469
Cdd:PTZ00185 473 GYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
153-376 |
1.31e-105 |
|
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: 315.06 E-value: 1.31e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 153 GMKAIDAMIPIGRGQRQLIIGDRQTGKTAIAvDTIlnqkANWESGDVekqvrCVYVAVGQKASTIAGVRATLEEHGALEY 232
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMI----ARQASADV-----VVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 233 TTIVASPASDPAGFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLER 312
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738382901 313 CAKLSDEmgAGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVS 376
Cdd:pfam00006 151 AGRVKGK--GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
142-509 |
3.61e-103 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 319.61 E-value: 3.61e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 142 ERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGKTAIAVDTILNQKANwesgdvekQVRCVYVAVGQKASTIAGVR 221
Cdd:PRK07165 119 TVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNT--------NVKCIYVAIGQKRENLSRIY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 222 ATLEEHGALEYTTIVASPASDPAGfKYLAPYAGSAIGQHWMYGgKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGD 301
Cdd:PRK07165 191 ETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGD 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 302 VFYLHSRLLERCAKLSDEMgagSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGA 381
Cdd:PRK07165 269 MFFAHSKLLERAGKFKNRK---TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 382 AQVKAMKKVSGTLKLDLAQYRDQQAFSMFASDLDPATRRQLARGERLMELLKQPQYSPYPVEEQVVSIWAGSKGHLDEVP 461
Cdd:PRK07165 346 VQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLISKLISWGLLKDVK 425
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 738382901 462 -VQDVLRFEREFIDHLRRHTSVLTDIASTGKLEDGTVSA-LESAVAEFSK 509
Cdd:PRK07165 426 dEQKALDFIDYLIENDPDAKKIFNKIKNNEDVDDELMKNyFAFLLNQYSD 475
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
100-378 |
3.23e-93 |
|
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: 285.89 E-value: 3.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 100 SVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 180 TAIAVDTILNQKAnwESGDVekqvrCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDPAGFKYLAPYAGSAIGQ 259
Cdd:cd19476 81 TVLAMQLARNQAK--AHAGV-----VVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 260 HWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDemGAGSMTGLPIIETKANDVS 339
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 738382901 340 AYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
383-507 |
2.47e-62 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 200.36 E-value: 2.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 383 QVKAMKKVSGTLKLDLAQYRDQQAFSMFASDLDPATRRQLARGERLMELLKQPQYSPYPVEEQVVSIWAGSKGHLDEVPV 462
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 738382901 463 QDVLRFEREFIDHLR-RHTSVLTDIASTGKLEDGTVSALESAVAEF 507
Cdd:pfam00306 81 EKVKEFEKELLEYLRsNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
387-511 |
9.03e-62 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) 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 alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 198.74 E-value: 9.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 387 MKKVSGTLKLDLAQYRDQQAFSMFASDLDPATRRQLARGERLMELLKQPQYSPYPVEEQVVSIWAGSKGHLDEVPVQDVL 466
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 738382901 467 RFEREFIDHLR-RHTSVLTDIASTGKLEDGTVSALESAVAEFSKGF 511
Cdd:cd18113 81 EFEKELLEYLRsNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
100-378 |
5.14e-49 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 170.43 E-value: 5.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 100 SVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 180 TaiavdTILNQKANWESGDVEkqvrcVYVAVGQKASTiagVRATLEEH---GALEYTTIVASPASDPAGFKYLAPYAGSA 256
Cdd:cd01136 81 S-----TLLGMIARNTDADVN-----VIALIGERGRE---VREFIEKDlgeEGLKRSVLVVATSDESPLLRVRAAYTATA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 257 IGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSdemgAGSMTGLPIIETKAN 336
Cdd:cd01136 148 IAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGE----KGSITAFYTVLVEGD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 738382901 337 DVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:cd01136 224 DFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
80-444 |
1.55e-45 |
|
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: 165.59 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 80 LGEFQEIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDA 159
Cdd:COG1157 71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 160 MIPIGRGQRQLIIGDRQTGKTaiavdTILNQKANWESGDVekqvrcVYVA-VGQKastiaG--VRATLEEH---GALEYT 233
Cdd:COG1157 151 LLTVGRGQRIGIFAGSGVGKS-----TLLGMIARNTEADV------NVIAlIGER-----GreVREFIEDDlgeEGLARS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 234 TIVASPASDPAGFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERC 313
Cdd:COG1157 215 VVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 314 AKlsdeMGAGSMTGL------------PIIETkandvsayiptnVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGA 381
Cdd:COG1157 295 GN----GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPD 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738382901 382 AQVKAMKKVSGTLKLDLAQYRDqqafsmfASDL----------DPATRRQLARGERLMELLKQPQYSPYPVEE 444
Cdd:COG1157 359 IVSPEHRALARRLRRLLARYEE-------NEDLirigayqpgsDPELDEAIALIPAIEAFLRQGMDERVSFEE 424
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
80-449 |
2.87e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 154.14 E-value: 2.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 80 LGEFQEIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDA 159
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 160 MIPIGRGQRQLIIGDRQTGKTaiavdTILNQKANWESGDVekqvrCVYVAVGQKASTIAG-VRATLEEHGaLEYTTIVAS 238
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKS-----TLLASLIRSAEVDV-----TVLALIGERGREVREfIESDLGEEG-LRKAVLVVA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 239 PASDPAGFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERcAKLSD 318
Cdd:PRK06936 225 TSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMER-AGQSD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 319 EmgaGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDL 398
Cdd:PRK06936 304 K---GSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELL 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 738382901 399 AQYRDQQ---AFSMFASDLDPATRRQLARGERLMELLKQPQYSPYPVEEQVVSI 449
Cdd:PRK06936 381 AKYEEVElllQIGEYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLL 434
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
98-377 |
3.10e-38 |
|
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: 141.59 E-value: 3.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 98 ILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQT 177
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 178 GKTAIAVdTILNQKANWESGDVEKqvrCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDPAGFKYLAPYAGSAI 257
Cdd:cd01135 81 PHNELAA-QIARQAGVVGSEENFA---IVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 258 GQHWMY-GGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGdvfYLHSRL---LERCAKLSDEmgAGSMTGLPIIET 333
Cdd:cd01135 157 AEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTM 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 738382901 334 KANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSR 377
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
33-440 |
3.67e-38 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 145.68 E-value: 3.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 33 GRVISAADGIARVEGLpSVMANELLRFENGIQGLAQNLD----TREIGVVV-LGEFQEIREGMEVQRTGEILSVPVGDAF 107
Cdd:PRK09099 26 GKVVEVIGTLLRVSGL-DVTLGELCELRQRDGTLLQRAEvvgfSRDVALLSpFGELGGLSRGTRVIGLGRPLSVPVGPAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 108 LGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGKTaiavdTI 187
Cdd:PRK09099 105 LGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS-----TL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 188 LNQKANWESGDVEkqvrcVYVAVGQKASTIAG-VRATLEEHGALEytTIVASPASDPAGFKYL-APYAGSAIGQHWMYGG 265
Cdd:PRK09099 180 MGMFARGTQCDVN-----VIALIGERGREVREfIELILGEDGMAR--SVVVCATSDRSSIERAkAAYVATAIAEYFRDRG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 266 KHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAklsdeMGA-GSMTGLPIIETKANDVSAYIPT 344
Cdd:PRK09099 253 LRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-----MGEtGSITALYTVLAEDESGSDPIAE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 345 NVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDLAQYRDQQAF---SMFASDLDPATRRQ 421
Cdd:PRK09099 328 EVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLlqvGEYRAGSDPVADEA 407
|
410 420
....*....|....*....|.
gi 738382901 422 LARGERLMELLKQP--QYSPY 440
Cdd:PRK09099 408 IAKIDAIRDFLSQRtdEYSDP 428
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
30-451 |
5.40e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 144.96 E-value: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 30 TEVGRVISAADgiarvegLPSVMANELLRFENgiQGLAQNLDTREIGVVVLGEFQE---IREGMEVQRTGEILSVPVGDA 106
Cdd:PRK06820 34 VEIGPTLLRAS-------LPGVAQGELCRIEP--QGMLAEVVSIEQEMALLSPFASsdgLRCGQWVTPLGHMHQVQVGAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 107 FLGRVVDPLGQPIDDlGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGKTaiavdT 186
Cdd:PRK06820 105 LAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKS-----T 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 187 ILNQKANWESGDVekqvrCVYVAVGQKASTiagVRATLEEH---GALEYTTIVASPASDPAGFKYLAPYAGSAIGQHWMY 263
Cdd:PRK06820 179 LLGMLCADSAADV-----MVLALIGERGRE---VREFLEQVltpEARARTVVVVATSDRPALERLKGLSTATTIAEYFRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 264 GGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERcAKLSDEmgaGSMTGLPIIETKANDVSAYIP 343
Cdd:PRK06820 251 RGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLER-TGNSDR---GSITAFYTVLVEGDDMNEPVA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 344 TNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDLAQYRDQQAF---SMFASDLDPATRR 420
Cdd:PRK06820 327 DEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLvrvGEYQAGEDLQADE 406
|
410 420 430
....*....|....*....|....*....|.
gi 738382901 421 QLARGERLMELLKQPQYSPYPVEEQVVSIWA 451
Cdd:PRK06820 407 ALQRYPAICAFLQQDHSETAHLETTLEHLAQ 437
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
82-446 |
1.23e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 129.84 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 82 EFQEIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDD------LGPIEAEGrralelQAPTVTERKSVHEPLQTGMK 155
Cdd:PRK07721 74 EVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGsalpkgLAPVSTDQ------DPPNPLKRPPIREPMEVGVR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 156 AIDAMIPIGRGQRQLIIGDRQTGKTaiavdTILNQKANWESGDVEkqvrcVYVAVGQKASTiagVRATLE----EHGaLE 231
Cdd:PRK07721 148 AIDSLLTVGKGQRVGIFAGSGVGKS-----TLMGMIARNTSADLN-----VIALIGERGRE---VREFIErdlgPEG-LK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 232 YTTIVASPASDPAGFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLE 311
Cdd:PRK07721 214 RSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 312 RcaklSDEMGAGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVS 391
Cdd:PRK07721 294 R----TGTNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAA 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738382901 392 GTLKLDLAQYRDQQ------AFSMFAS-DLDPATRRQlargERLMELLKQPQYSPYPVEEQV 446
Cdd:PRK07721 370 NRFRELLSTYQNSEdlinigAYKRGSSrEIDEAIQFY----PQIISFLKQGTDEKATFEESI 427
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
92-406 |
5.97e-32 |
|
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: 128.30 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 92 VQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLI 171
Cdd:TIGR01040 67 CEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 172 IGD-------------RQTGKTAIAVDTILNQKanwesgdvEKQVRCVYVAVGQKASTIAGVRATLEEHGALEYTTIVAS 238
Cdd:TIGR01040 147 FSAaglphneiaaqicRQAGLVKLPTKDVHDGH--------EDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLN 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 239 PASDPAGFKYLAPYAGSAIGQHWMYG-GKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLs 317
Cdd:TIGR01040 219 LANDPTIERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 318 dEMGAGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKK-----VSG 392
Cdd:TIGR01040 298 -EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRkdhsdVSN 376
|
330
....*....|....
gi 738382901 393 TLKLDLAQYRDQQA 406
Cdd:TIGR01040 377 QLYACYAIGKDVQA 390
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
45-377 |
1.17e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 127.25 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 45 VEGLPSVMANELLRFE--NGIQGLAQNLDTREIGVV--VLGEFQEI-REGMEVQRTGEILSVPVGDAFLGRVVDPLGQPI 119
Cdd:PRK04196 17 VEGVEGVAYGEIVEIElpNGEKRRGQVLEVSEDKAVvqVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 120 DDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQR----------------QLIigdRQTgktaia 183
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnelaaQIA---RQA------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 184 vdTILNQkanwesgdvEKQVRCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDPAGFKYLAPYAGSAIGQHWMY 263
Cdd:PRK04196 168 --KVLGE---------EENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 264 G-GKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGdvfYLHSRL---LERCAKLSDEmgAGSMTGLPIIETKANDVS 339
Cdd:PRK04196 237 EkGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDIT 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 738382901 340 AYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSR 377
Cdd:PRK04196 312 HPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
89-434 |
2.16e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 126.35 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 89 GMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQR 168
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 169 QLIIGDRQTGKTaiavdTILNQKANWESGDVekqvrCVYVAVGQKASTIAG-VRATLEEHGaLEYTTIVASPASDPAGFK 247
Cdd:PRK08972 165 MGLFAGSGVGKS-----VLLGMMTRGTTADV-----IVVGLVGERGREVKEfIEEILGEEG-RARSVVVAAPADTSPLMR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 248 YLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDemGAGSMTG 327
Cdd:PRK08972 234 LKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 328 LPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVG----GAAQVKAMKKVSGTLKLdLAQYRD 403
Cdd:PRK08972 312 FYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRVKQVYSL-YQQNRD 390
|
330 340 350
....*....|....*....|....*....|.
gi 738382901 404 QQAFSMFASDLDPATRRQLARGERLMELLKQ 434
Cdd:PRK08972 391 LISIGAYKQGSDPRIDNAIRLQPAMNAFLQQ 421
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
93-446 |
4.41e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 125.39 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 93 QRTGEILsvpVGDAFLGRVVDPLGQPIDDLGPIEaeGRRALELQAPTVT--ERKSVHEPLQTGMKAIDAMIPIGRGQRQL 170
Cdd:PRK07196 85 EQDGELL---IGDSWLGRVINGLGEPLDGKGQLG--GSTPLQQQLPQIHplQRRAVDTPLDVGVNAINGLLTIGKGQRVG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 171 IIGDRQTGKTaiavdTILNQKANWESGDVekqvrCVYVAVGQKASTIAG-VRATLEEHGaLEYTTIVASPASDPAGFKYL 249
Cdd:PRK07196 160 LMAGSGVGKS-----VLLGMITRYTQADV-----VVVGLIGERGREVKEfIEHSLQAAG-MAKSVVVAAPADESPLMRIK 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 250 APYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAklsDEMGAGSMTGLP 329
Cdd:PRK07196 229 ATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIY 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 330 IIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSR----VGGAAQVKAMKKVSGTLKlDLAQYRDQQ 405
Cdd:PRK07196 306 TVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCYA-DYMAIKPLI 384
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 738382901 406 AFSMFASDLDPATRRQLARGERLMELLKQPQYSPYPVEEQV 446
Cdd:PRK07196 385 PLGGYVAGADPMADQAVHYYPAITQFLRQEVGHPALFSASV 425
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
24-439 |
1.70e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 123.52 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 24 PSGTDRTevGRVISAADGIARVEgLPSVMANELLRFENGiQGLAQ--NLDTREIGVVVLGEFQEIREGMEVQRTGEILSV 101
Cdd:PRK07594 16 PDGYCRW--GRIQDVSATLLNAW-LPGVFMGELCCIKPG-EELAEvvGINGSKALLSPFTSTIGLHCGQQVMALRRRHQV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 102 PVGDAFLGRVVDPLGQPIDDLgPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGKTa 181
Cdd:PRK07594 92 PVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 182 iavdTILNQKANWESGDVEkqvrcVYVAVGQKASTIAG-VRATLEEHGALEYTTIVASpaSD-PAGFKYLAPYAGSAIGQ 259
Cdd:PRK07594 170 ----TLLAMLCNAPDADSN-----VLVLIGERGREVREfIDFTLSEETRKRCVIVVAT--SDrPALERVRALFVATTIAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 260 HWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAklsdeMGA-GSMTGLPIIETKANDV 338
Cdd:PRK07594 239 FFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 339 SAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDLAQYRDQQAF---SMFASDLD 415
Cdd:PRK07594 314 NEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLiriGEYQRGVD 393
|
410 420
....*....|....*....|....
gi 738382901 416 PATRRQLARGERLMELLKQPQYSP 439
Cdd:PRK07594 394 TDTDKAIDTYPDICTFLRQSKDEV 417
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
95-402 |
2.37e-29 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 120.10 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 95 TGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEG----RRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQL 170
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGpiseERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 171 IIGDRQTGKTaiavdTILNQKANWESGDVekqvrCVYVAVGQKASTIAGVRATLEEHGALEYTTIVASPASDPAGFKYLA 250
Cdd:PRK08149 156 IFASAGCGKT-----SLMNMLIEHSEADV-----FVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 251 PYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSdemgAGSMTGLPI 330
Cdd:PRK08149 226 ALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATL----AGSITAFYT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 331 IETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGG-------AAQVKAMKKVSGTLK-----LDL 398
Cdd:PRK08149 302 VLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGqvtdpkhRQLAAAFRKLLTRLEelqlfIDL 381
|
....
gi 738382901 399 AQYR 402
Cdd:PRK08149 382 GEYR 385
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
99-380 |
3.73e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 119.79 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 99 LSVPVGDAFLGRVVDPLGQPIDDLGPIEAEgRRALELQAP-TVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQT 177
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYE-RYAPIMKAPiAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 178 GKTAIAVDTILNQKAnwesgdvekQVRCVYVaVGQKASTIAG-VRATLEehGALEYTTIVASPASDPAGFKYLAPYAGSA 256
Cdd:PRK08472 169 GKSTLMGMIVKGCLA---------PIKVVAL-IGERGREIPEfIEKNLG--GDLENTVIVVATSDDSPLMRKYGAFCAMS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 257 IGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKlsdEMGAGSMTGLPIIETKAN 336
Cdd:PRK08472 237 VAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGD 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 738382901 337 DVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGG 380
Cdd:PRK08472 314 DMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN 357
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
101-434 |
1.60e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 112.52 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 101 VPVGDAFLGRVVDPLGQPIDDLGPIEAEGRraLELQAPTVT--ERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTG 178
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINplNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 179 KTaiavdTILNQKANWESGDVekqvrCVYVAVGQKASTIAG-VRATLEEHGaLEYTTIVASPASDPAGFKYLAPYAGSAI 257
Cdd:PRK05688 181 KS-----VLLGMMTRFTEADI-----IVVGLIGERGREVKEfIEHILGEEG-LKRSVVVASPADDAPLMRLRAAMYCTRI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 258 GQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAklSDEMGAGSMTGLPIIETKAND 337
Cdd:PRK05688 250 AEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 338 VSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVggaaqvkaMKKVSGTLKLDLAQY-----------RDQQA 406
Cdd:PRK05688 328 QQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV--------MPQVVDPEHLRRAQRfkqlwsryqqsRDLIS 399
|
330 340
....*....|....*....|....*...
gi 738382901 407 FSMFASDLDPATRRQLARGERLMELLKQ 434
Cdd:PRK05688 400 VGAYVAGGDPETDLAIARFPHLVQFLRQ 427
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
31-96 |
3.09e-26 |
|
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) 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, in 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 alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349740 [Multi-domain] Cd Length: 67 Bit Score: 101.38 E-value: 3.09e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738382901 31 EVGRVISAADGIARVEGLPSVMANELLRFENGIQGLAQNLDTREIGVVVLGEFQEIREGMEVQRTG 96
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTG 66
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
33-403 |
7.53e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 110.47 E-value: 7.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 33 GRVISAADGIARVEGL-PSVMANELLRFE--NGIQgLAQNLDTREIGVVV--LGEFQEIREGMEVQRTGEiLSVPVGDAF 107
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIRadGGTH-LGEVVRVDPDGVTVkpFEPRIEIGLGDAVFRKGP-LRIRPDPSW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 108 LGRVVDPLGQPIDDLGPI-EAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGKTaiavdT 186
Cdd:PRK06002 106 KGRVINALGEPIDGLGPLaPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKS-----T 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 187 ILNQKANWESGDVekqvrcVYVA-VGQKASTiagVRATLEEH--GALEYTTIVASPASDPAGFKYLAPYAGSAIGQHWMY 263
Cdd:PRK06002 181 LLAMLARADAFDT------VVIAlVGERGRE---VREFLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 264 GGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDemGAGSMTGLPIIETKANDVSAYIP 343
Cdd:PRK06002 252 RGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVA 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 344 TNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGAAQVKAMKKVSGTLKLDLAQYRD 403
Cdd:PRK06002 330 DSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
101-434 |
1.33e-25 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 109.49 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 101 VPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGKT 180
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 181 aiavdTILNQKANWESGDVekqvrCVYVAVGQKASTIAG-VRATLEEHGaLEYTTIVASPAS-DPAGFKYLAPYAgSAIG 258
Cdd:PRK07960 190 -----VLLGMMARYTQADV-----IVVGLIGERGREVKDfIENILGAEG-RARSVVIAAPADvSPLLRMQGAAYA-TRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 259 QHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAKLSDemGAGSMTGLPIIETKANDV 338
Cdd:PRK07960 258 EDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQ 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 339 SAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRVGGA-------AQVKAMKKVsgtlkldLAQY---RDQQAFS 408
Cdd:PRK07960 336 QDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQL-------LSSFqrnRDLVSVG 408
|
330 340
....*....|....*....|....*.
gi 738382901 409 MFASDLDPATRRQLARGERLMELLKQ 434
Cdd:PRK07960 409 AYAKGSDPMLDKAIALWPQLEAFLQQ 434
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
67-476 |
4.87e-24 |
|
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: 105.19 E-value: 4.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 67 AQNLDTREIGVVVLGEFQEIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSV 146
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 147 HEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGKTAIAVDTIlNQKANWESGdvekqvRCVYVAVGQKASTIAGVRATLEE 226
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELI-NNIAKEHGG------YSVFAGVGERTREGNDLYHEMKE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 227 HGALEYTTIVASPASDPAGFKYLAPYAGSAIGQHWM-YGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPgdvfyl 305
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQ------ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 306 hsrllercAKLSDEMG----------AGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISV 375
Cdd:TIGR01039 271 --------PTLATEMGelqeritstkTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDST 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 376 SR-----VGGAAQVKAMKKVSGTLKldlaQYRD-QQAFSMFASD-LDPATRRQLARGERLMELLKQpqysPYPVEEQvvs 448
Cdd:TIGR01039 343 SRlldpsVVGEEHYDVARGVQQILQ----RYKElQDIIAILGMDeLSEEDKLTVERARRIQRFLSQ----PFFVAEV--- 411
|
410 420 430
....*....|....*....|....*....|..
gi 738382901 449 iWAGSKGHLdeVPVQDVLRFEREFI----DHL 476
Cdd:TIGR01039 412 -FTGQPGKY--VPLKDTIRGFKEILegkyDHL 440
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
89-378 |
1.15e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 103.52 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 89 GMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDlgPIEAEGRRALELQAPTVT--ERKSVHEPLQTGMKAIDAMIPIGRG 166
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIHafEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 167 QRQLIIGDRQTGKTaiavdTILNQKANWESGDVEkqvrcVYVAVGQKASTIAG-VRATLEEHGaLEYTTIVASPASDPAG 245
Cdd:PRK06793 157 QKIGIFAGSGVGKS-----TLLGMIAKNAKADIN-----VISLVGERGREVKDfIRKELGEEG-MRKSVVVVATSDESHL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 246 FKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPgreaYPGDVFYLHS---RLLERCAKLSDemga 322
Cdd:PRK06793 226 MQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK---- 297
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 738382901 323 GSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:PRK06793 298 GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 353
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
100-377 |
3.60e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 102.29 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 100 SVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:PRK05922 91 SLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 180 TAIaVDTIlnqkanwESGdvEKQVRCVYVAVGQKASTiagVRATLEEHG---ALEYTTIVASPASDPAGFKYLAPYAGSA 256
Cdd:PRK05922 171 SSL-LSTI-------AKG--SKSTINVIALIGERGRE---VREYIEQHKeglAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 257 IGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERcAKLSDEmgaGSMTGLPIIETKAN 336
Cdd:PRK05922 238 IAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTER-AGNNDK---GSITALYAILHYPN 313
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 738382901 337 DVSAYIPTnVISITDGQIFLqSDLFNANQRPAVDVGISVSR 377
Cdd:PRK05922 314 HPDIFTDY-LKSLLDGHFFL-TPQGKALASPPIDILTSLSR 352
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
86-377 |
3.60e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 99.28 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 86 IREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIeAEGRRALELQA--PTVTERKSVHEPLQTGMKAIDAMIPI 163
Cdd:PRK08927 77 VRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPL-PQGPVPYPLRAppPPAHSRARVGEPLDLGVRALNTFLTC 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 164 GRGQRQLIIGDRQTGKTaiavdTILNQKANWESGDVekqvrCVYVAVGQKASTIAG-VRATLEEHGALEYTTIVASpaSD 242
Cdd:PRK08927 156 CRGQRMGIFAGSGVGKS-----VLLSMLARNADADV-----SVIGLIGERGREVQEfLQDDLGPEGLARSVVVVAT--SD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 243 -PAGFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGDVFYLHSRLLERCAklSDEMG 321
Cdd:PRK08927 224 ePALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIG 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 738382901 322 AGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSR 377
Cdd:PRK08927 302 EGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
46-166 |
1.41e-20 |
|
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: 94.77 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 46 EGLPSVmaNELLRFENGIQG-----LAQNLDTREIGVVVLGEFQEIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPID 120
Cdd:COG0055 23 GELPAI--YNALEVENEGGGelvleVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPID 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 738382901 121 DLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRG 166
Cdd:COG0055 101 GKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
66-359 |
3.53e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 87.01 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 66 LAQ--NLDTREIGVVVLGEFQEIREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDlGPiEAEGRRaLELQAPTV--T 141
Cdd:PRK02118 39 LAQviRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GP-ELEGEP-IEIGGPSVnpV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 142 ERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDrqTGKTAIAVdtiLNQKANWESGDVekqvrCVYVAVGQKASTIAGVR 221
Cdd:PRK02118 116 KRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNAL---LARIALQAEADI-----IILGGMGLTFDDYLFFK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 222 ATLEEHGALEYTTIVASPASDPAGFKYLAPYAGSAIGQHW-MYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPG 300
Cdd:PRK02118 186 DTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFaLEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPG 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 738382901 301 DvfyLHSRLLERCAKLSDEMGAGSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSD 359
Cdd:PRK02118 266 S---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
100-378 |
6.54e-17 |
|
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: 81.11 E-value: 6.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 100 SVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQLIIGDRQTGK 179
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 180 TAIAVDTIlNQKANWESGDVekqvrcVYVAVGQKasTIAG-------VRATLEEHGALEYTTIVASPASDPAGFKYLAPY 252
Cdd:cd01133 81 TVLIMELI-NNIAKAHGGYS------VFAGVGER--TREGndlyhemKESGVINLDGLSKVALVYGQMNEPPGARARVAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 253 AGSAIGQHWM-YGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPgdvfylhsrllercAKLSDEMGA--------- 322
Cdd:cd01133 152 TGLTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQ--------------PTLATEMGSlqeritstk 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 738382901 323 -GSMTGLPIIETKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVDVGISVSRV 378
Cdd:cd01133 218 kGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
86-189 |
6.73e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 77.00 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 86 IREGMEVQRTGEILSVPVGDAFLGRVVDPLGQPIDDLGPIEAEGRRALELQAPTVTERKSVHEPLQTGMKAIDAMIPIGR 165
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRR 160
|
90 100
....*....|....*....|....
gi 738382901 166 GQRQLIIGDRQTGKTAIAVDTILN 189
Cdd:CHL00060 161 GGKIGLFGGAGVGKTVLIMELINN 184
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
387-454 |
7.54e-15 |
|
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: 69.40 E-value: 7.54e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 387 MKKVSGTLKLDLAQYRDQQAFSMFASD--LDPATRRQLARGERLMELLKQPQYSPYPVEEQVVSIWAGSK 454
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
99-377 |
2.42e-13 |
|
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: 70.68 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 99 LSVPVGDAFLGRVVDPLGQPIDDLGpiEAEG---RRALELQ------APTVTERKSVHEPLQTGMKAIDAMIPIGRGQRQ 169
Cdd:cd01134 2 LSVELGPGLLGSIFDGIQRPLEVIA--ETGSifiPRGVNVQrwpvrqPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 170 LIIGDRQTGKTaiavdTILNQKANWESGDVekqvrCVYVAVGQKASTIAGV-----RATLEEHGA--LEYTTIVASPASD 242
Cdd:cd01134 80 AIPGPFGCGKT-----VISQSLSKWSNSDV-----VIYVGCGERGNEMAEVleefpELKDPITGEslMERTVLIANTSNM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 243 PAGFKYLAPYAGSAIGQHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGdvfYLHSRLLE------RCAKL 316
Cdd:cd01134 150 PVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLAEfyeragRVRCL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738382901 317 SDEMGAGSMTGLPIIETKANDVSAYIPTNVISITdgQIF--LQSDLFNANQRPAVDVGISVSR 377
Cdd:cd01134 227 GSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
31-96 |
2.40e-12 |
|
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: 62.18 E-value: 2.40e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738382901 31 EVGRVISAADGIARVEGLPSVMANELLRFENGIQGLAQNLDTREIGVVVLGEFQEIREGMEVQRTG 96
Cdd:pfam02874 4 VIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
189-370 |
1.01e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 58.11 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 189 NQKANWESGDVekqvrCVYVAVGQKASTIAGVratLEEHGAL----------EYTTIVASPASDPAGFKYLAPYAGSAIG 258
Cdd:PRK14698 674 HQLAKWSDAQV-----VIYIGCGERGNEMTDV---LEEFPKLkdpktgkplmERTVLIANTSNMPVAAREASIYTGITIA 745
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738382901 259 QHWMYGGKHVLIIFDDLSKQAEAYRAVSLLLRRPPGREAYPGdvfYLHSRLLE------RCAKLSDEMGAGSMTGLPIIE 332
Cdd:PRK14698 746 EYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVS 822
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170 180 190
....*....|....*....|....*....|....*...
gi 738382901 333 TKANDVSAYIPTNVISITDGQIFLQSDLFNANQRPAVD 370
Cdd:PRK14698 823 PPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAIN 860
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| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
33-97 |
9.01e-04 |
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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: 38.06 E-value: 9.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738382901 33 GRVISAADGIARVEGLPSVMANELLRFENGIQGLAQNLDTREIG-------VVVLGEFQEIREGMEVQRTGE 97
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIERGDGNNETVLKAEVIGfrgdraiLQLFESTRGLSRGALVEPTGR 73
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