|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-382 |
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: 865.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 1 IYIGDGIARAHGLDNALQGELLEFSNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPL 80
Cdd:COG0056 32 LSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 81 GQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILNQKDQDM 160
Cdd:COG0056 112 GRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 161 ICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYR 240
Cdd:COG0056 192 ICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 241 ELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYS 320
Cdd:COG0056 272 ELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNA 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284504904 321 GVRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFGSDLDAATQAKLNRG 382
Cdd:COG0056 352 GIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERG 413
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-382 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 862.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 1 IYIGDGIARAHGLDNALQGELLEFSNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPL 80
Cdd:PRK09281 32 ISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 81 GQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILNQKDQDM 160
Cdd:PRK09281 112 GQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 161 ICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYR 240
Cdd:PRK09281 192 ICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYR 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 241 ELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYS 320
Cdd:PRK09281 272 QLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNA 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284504904 321 GVRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFGSDLDAATQAKLNRG 382
Cdd:PRK09281 352 GIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERG 413
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
1-382 |
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: 733.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 1 IYIGDGIARAHGLDNALQGELLEFSNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPL 80
Cdd:TIGR00962 31 VSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 81 GQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILNQKDQDM 160
Cdd:TIGR00962 111 GEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 161 ICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYR 240
Cdd:TIGR00962 191 YCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 241 ELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYS 320
Cdd:TIGR00962 271 QISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNS 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284504904 321 GVRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFGSDLDAATQAKLNRG 382
Cdd:TIGR00962 351 GIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATKKQLERG 412
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
3-382 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 685.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 3 IGDGIARAHGLDNALQGELLEFSNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQ 82
Cdd:PRK13343 34 VGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 83 PVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILNQKDQDMIC 162
Cdd:PRK13343 114 PLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSDVIC 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 163 VYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYREL 242
Cdd:PRK13343 194 VYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYREL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 243 SLILRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGV 322
Cdd:PRK13343 274 SLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQ 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 323 RPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFGSDLDAATQAKLNRG 382
Cdd:PRK13343 354 RPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGTQKQITRG 413
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
3-382 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 677.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 3 IGDGIARAHGLDNALQGELLEFSNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQ 82
Cdd:CHL00059 13 VGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 83 PVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILNQKDQDMIC 162
Cdd:CHL00059 93 PIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVIC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 163 VYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYREL 242
Cdd:CHL00059 173 VYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 243 SLILRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGV 322
Cdd:CHL00059 253 SLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGI 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 323 RPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFGSDLDAATQAKLNRG 382
Cdd:CHL00059 333 RPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARG 392
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
63-336 |
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: 555.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 63 IMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKT 142
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 143 GKTSVAIDAILNQKDQDMICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNG 222
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 223 KHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDISAYIPTN 302
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 284504904 303 VISITDGQIFLDSDSFYSGVRPAIDAGASVSRVG 336
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
2-382 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic species, including Methanosarcina barkeri, 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 alpha subunit of this apparent second ATP synthase.
Pssm-ID: 132367 [Multi-domain] Cd Length: 497 Bit Score: 532.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 2 YIGDGIARAHGLDNALQGELLEFSNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLG 81
Cdd:TIGR03324 33 SVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLLGRVVDPLG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 82 QPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILNQKDQDMI 161
Cdd:TIGR03324 113 RPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTILNQKGRNVL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 162 CVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRE 241
Cdd:TIGR03324 193 CIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHARAYRE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 242 LSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSG 321
Cdd:TIGR03324 273 LSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQNISAYIPTNLISITDGQIYLSPTLFELG 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284504904 322 VRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFGSDLDAATQAKLNRG 382
Cdd:TIGR03324 353 VLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHG 413
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
30-371 |
1.03e-111 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 338.17 E-value: 1.03e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 30 GIVQNLESND-VGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVD--------GLGEIKTTNTRpIEH 100
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrsrALLESEQTLGK-VDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 101 KAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILNQ--------KDQDMICVYVAIGQKDS 172
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 173 TVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGR 252
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 253 EAYPGDVFYLHSRLLERAAKLSDELGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASV 332
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350
....*....|....*....|....*....|....*....
gi 284504904 333 SRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFGSDL 371
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQV 437
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
118-333 |
1.58e-107 |
|
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: 314.29 E-value: 1.58e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 118 GIKAIDALVPIGRGQRELIIGDRKTGKTSVAiDAILNQKDQDmICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGP 197
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 198 AEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDEl 277
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 284504904 278 gGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVS 333
Cdd:pfam00006 158 -GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
94-382 |
2.79e-102 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 311.52 E-value: 2.79e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 94 NTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILNQKDQDMICVYVAIGQKDST 173
Cdd:PRK07165 106 NTSSIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKREN 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 174 VRAQVETLKKLGAMDYTIVVTAgPAEPAPLLYLAPYAGAAMGEEFMMNgKHVLIVYDDLSKQATAYRELSLILRRPPGRE 253
Cdd:PRK07165 186 LSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 254 AYPGDVFYLHSRLLERAAKLsdeLGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVS 333
Cdd:PRK07165 264 AFPGDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVS 340
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 284504904 334 RVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFGSDLDAATQAKLNRG 382
Cdd:PRK07165 341 RTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKG 389
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
66-335 |
3.10e-102 |
|
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: 303.22 E-value: 3.10e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 66 VPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKT 145
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 146 SVAIDAILNQKDQD-MICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKH 224
Cdd:cd19476 82 VLAMQLARNQAKAHaGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 225 VLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDelGGGSMTALPIIETQAGDISAYIPTNVI 304
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 284504904 305 SITDGQIFLDSDSFYSGVRPAIDAGASVSRV 335
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
65-335 |
7.96e-51 |
|
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: 171.20 E-value: 7.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 65 EVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGK 144
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 145 tSVAIDAILNQKDQDMIcVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKH 224
Cdd:cd01136 81 -STLLGMIARNTDADVN-VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 225 VLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSMTALPIIETQAGDISAYIPTNVI 304
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 284504904 305 SITDGQIFLDSDSFYSGVRPAIDAGASVSRV 335
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
3-368 |
2.29e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 166.91 E-value: 2.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 3 IGDGIARAhGLDNALQGELLEFS-NGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLG 81
Cdd:PRK06820 36 IGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 82 QPVDGlGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKtSVAIDAILNQKDQDMI 161
Cdd:PRK06820 115 APIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGK-STLLGMLCADSAADVM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 162 cVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRE 241
Cdd:PRK06820 193 -VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAARE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 242 LSLILRRPPGREAYPGDVFYLHSRLLERAAKlSDElggGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSG 321
Cdd:PRK06820 272 IGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAG 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 284504904 322 VRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFG 368
Cdd:PRK06820 348 HYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVG 394
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
45-362 |
7.38e-47 |
|
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: 165.20 E-value: 7.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 45 LGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDA 124
Cdd:COG1157 71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 125 LVPIGRGQReliIGdr---ktGKtSVAIDAILNQKDQDmICVyVA-IGQKDSTVRAQVEtlKKLGA--MDYTIVVTAgPA 198
Cdd:COG1157 151 LLTVGRGQR---IGifagsgvGK-STLLGMIARNTEAD-VNV-IAlIGERGREVREFIE--DDLGEegLARSVVVVA-TS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 199 -EPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKlsdeL 277
Cdd:COG1157 222 dEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----G 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 278 GGGSMTAL------------PIIETqagdisayiptnVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVGGDAQIKAMK 345
Cdd:COG1157 298 GKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHR 365
|
330
....*....|....*..
gi 284504904 346 SVAGTLRLDLASYRELE 362
Cdd:COG1157 366 ALARRLRRLLARYEENE 382
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
9-368 |
8.27e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 162.63 E-value: 8.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 9 RAHGLDNALqGELLEFSNGVYGIVQNLE----SNDVGIVV-LGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQP 83
Cdd:PRK09099 37 RVSGLDVTL-GELCELRQRDGTLLQRAEvvgfSRDVALLSpFGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 84 VDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAidAILNQKDQDMICV 163
Cdd:PRK09099 116 IDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLM--GMFARGTQCDVNV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 164 YVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELS 243
Cdd:PRK09099 194 IALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 244 LILRRPPGREAYPGDVFYLHSRLLERAAklsdeLGG-GSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGV 322
Cdd:PRK09099 274 LAAGEPPARRGFPPSVFAELPRLLERAG-----MGEtGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQ 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 284504904 323 RPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFG 368
Cdd:PRK09099 349 YPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
45-368 |
1.39e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 162.23 E-value: 1.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 45 LGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDA 124
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 125 LVPIGRGQRELIIGDRKTGKtSVAIDAILNQKDQDmICVYVAIGQKDSTVRAQVEtlKKLGA--MDYTIVVTAGPAEPAP 202
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGK-STLLASLIRSAEVD-VTVLALIGERGREVREFIE--SDLGEegLRKAVLVVATSDRPSM 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 203 LLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKlSDElggGSM 282
Cdd:PRK06936 232 ERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 283 TALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELE 362
Cdd:PRK06936 308 TALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVE 387
|
....*.
gi 284504904 363 SFSQFG 368
Cdd:PRK06936 388 LLLQIG 393
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
43-377 |
6.29e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 154.88 E-value: 6.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 43 VVLGDFDGIRE---GDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGI 119
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 120 KAIDALVPIGRGQRELIIGDRKTGKtSVAIDAILNQKDQDmICVYVAIGQKDSTVRAQVEtlKKLGA--MDYTIVVTAGP 197
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGK-STLMGMIARNTSAD-LNVIALIGERGREVREFIE--RDLGPegLKRSIVVVATS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 198 AEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAklSDEL 277
Cdd:PRK07721 223 DQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG--TNAS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 278 ggGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLAS 357
Cdd:PRK07721 301 --GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLST 378
|
330 340
....*....|....*....|....*..
gi 284504904 358 YRELESFSQFGS-------DLDAATQA 377
Cdd:PRK07721 379 YQNSEDLINIGAykrgssrEIDEAIQF 405
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
30-378 |
8.08e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 146.37 E-value: 8.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 30 GIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQ 109
Cdd:PRK08472 56 GMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 110 SVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILNQKDQdmICVYVAIGQKDSTVRAQVEtlKKLGA-MD 188
Cdd:PRK08472 136 LIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAP--IKVVALIGERGREIPEFIE--KNLGGdLE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 189 YTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLE 268
Cdd:PRK08472 212 NTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLME 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 269 RAAKlsdELGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVGGDAQIKAMKSVA 348
Cdd:PRK08472 292 RAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAA 368
|
330 340 350
....*....|....*....|....*....|....*..
gi 284504904 349 GTLRLDLASYRELESFSQFGS-------DLDAATQAK 378
Cdd:PRK08472 369 RKFKRLYSLLKENEVLIRIGAyqkgndkELDEAISKK 405
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
13-368 |
2.00e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 142.78 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 13 LDNALQGELLEF-SNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLgEIK 91
Cdd:PRK07594 37 LPGVFMGELCCIkPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 92 TTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVaIDAILNQKDQDmICVYVAIGQKD 171
Cdd:PRK07594 116 DVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAPDAD-SNVLVLIGERG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 172 STVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPG 251
Cdd:PRK07594 194 REVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 252 REAYPGDVFYLHSRLLERAAklsdeLGG-GSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGA 330
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLA 348
|
330 340 350
....*....|....*....|....*....|....*...
gi 284504904 331 SVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFG 368
Cdd:PRK07594 349 TLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIG 386
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
21-366 |
2.36e-38 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 143.00 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 21 LLEFSNGvyGIVQNLESNDVG-------IVVLGDFDGIREGDTV---------KRTGRimEVPVGDAMIGRVVNPLGQPV 84
Cdd:PRK07960 53 VIERQNG--SETHEVESEVVGfngqrlfLMPLEEVEGILPGARVyarnisgegLQSGK--QLPLGPALLGRVLDGSGKPL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 85 DGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKtSVAIDAILNQKDQDMICVY 164
Cdd:PRK07960 129 DGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK-SVLLGMMARYTQADVIVVG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 165 VaIGQKDSTVRAQVETLkkLGAMDYT-IVVTAGPAEPAPLLYL--APYAgAAMGEEFMMNGKHVLIVYDDLSKQATAYRE 241
Cdd:PRK07960 208 L-IGERGREVKDFIENI--LGAEGRArSVVIAAPADVSPLLRMqgAAYA-TRIAEDFRDRGQHVLLIMDSLTRYAMAQRE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 242 LSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDelGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSG 321
Cdd:PRK07960 284 IALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAG 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 284504904 322 VRPAIDAGASVSRvggdaqikAMKSVagtlrLDLASYRELESFSQ 366
Cdd:PRK07960 362 HYPAIDIEASISR--------AMTAL-----IDEQHYARVRQFKQ 393
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
63-349 |
6.71e-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: 137.74 E-value: 6.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 63 IMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDrkT 142
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 143 G------KTSVAIDAILNQKDQDMICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGE 216
Cdd:cd01135 79 GlphnelAAQIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 217 EFMM-NGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGdvfYLHSRL---LERAAKLSDElgGGSMTALPIIETQA 292
Cdd:cd01135 159 YLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 284504904 293 GDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVggdaqikaMKSVAG 349
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
45-335 |
8.74e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 141.41 E-value: 8.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 45 LGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDA 124
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 125 LVPIGRGQRELIIGDRKTGKtSVAIDAILNQKDQDMICVYVaIGQKDSTVRAQVETLKKLGAMDYTIVVtAGPAEPAPLL 204
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGK-SVLLGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVV-ASPADDAPLM 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 205 YL-APYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAklSDELGGGSMT 283
Cdd:PRK05688 239 RLrAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSIT 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 284504904 284 ALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRV 335
Cdd:PRK05688 317 AFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
45-368 |
1.75e-37 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 140.13 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 45 LGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKT----TNTRPIEHKAPGIMQRQSVSEPLQTGIK 120
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTvgpiSEERVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 121 AIDALVPIGRGQRELIIGDRKTGKTSVaIDAILNQKDQDmICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEP 200
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEHSEAD-VFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 201 APLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDelggG 280
Cdd:PRK08149 219 SVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA----G 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 281 SMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRE 360
Cdd:PRK08149 295 SITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEE 374
|
....*...
gi 284504904 361 LESFSQFG 368
Cdd:PRK08149 375 LQLFIDLG 382
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
50-335 |
1.51e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 137.91 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 50 GIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIG 129
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 130 RGQRELIIGDRKTGKtSVAIDAILNQKDQDMICVYVaIGQKDSTVRAQVETLkkLGAMDYT-IVVTAGPAEPAPLLYL-A 207
Cdd:PRK08972 161 KGQRMGLFAGSGVGK-SVLLGMMTRGTTADVIVVGL-VGERGREVKEFIEEI--LGEEGRArSVVVAAPADTSPLMRLkG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 208 PYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDelGGGSMTALPI 287
Cdd:PRK08972 237 CETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYT 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 284504904 288 IETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRV 335
Cdd:PRK08972 315 VLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
54-339 |
8.26e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 124.72 E-value: 8.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 54 GDTVKRTGRiMEVPVGDAMIGRVVNPLGQPVDGLGEIKT-TNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQ 132
Cdd:PRK06002 88 GDAVFRKGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 133 RELIIGDRKTGKTSVAidAILNQKDqDMICVYVA-IGQKDSTVRAQVE-TLKklGAMDYTIVVTAGPAEPAPLLYLAPYA 210
Cdd:PRK06002 167 RIGIFAGSGVGKSTLL--AMLARAD-AFDTVVIAlVGERGREVREFLEdTLA--DNLKKAVAVVATSDESPMMRRLAPLT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 211 GAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDelGGGSMTALPIIET 290
Cdd:PRK06002 242 ATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLV 319
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 284504904 291 QAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVGGDA 339
Cdd:PRK06002 320 DGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
37-339 |
2.52e-31 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 123.78 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 37 SNDVGIV-VLGDFDGIREGDT-VKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEP 114
Cdd:PRK04196 47 SEDKAVVqVFEGTTGLDLKDTkVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 115 LQTGIKAIDALVPIGRGQR------------ELiigdrktgKTSVAIDAILNQKDQDMICVYVAIGQKDSTVRAQVETLK 182
Cdd:PRK04196 127 IQTGISAIDGLNTLVRGQKlpifsgsglphnEL--------AAQIARQAKVLGEEENFAVVFAAMGITFEEANFFMEDFE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 183 KLGAMDYTIVVTAGPAEPAPLLYLAPYAG--AAmgeEFMM--NGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGd 258
Cdd:PRK04196 199 ETGALERSVVFLNLADDPAIERILTPRMAltAA---EYLAfeKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 259 vfYLHSRL---LERAAKLSDElgGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRV 335
Cdd:PRK04196 275 --YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRL 350
|
....
gi 284504904 336 GGDA 339
Cdd:PRK04196 351 MKDG 354
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
50-377 |
4.20e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 122.69 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 50 GIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKttNTRPIEHKAPGI--MQRQSVSEPLQTGIKAIDALVP 127
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLG--GSTPLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 128 IGRGQRELIIGDRKTGKtSVAIDAILNQKDQDMICVYVaIGQKDSTVRAQVETLKKLGAMDYTIVVTAgPAEPAPLLYL- 206
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGK-SVLLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAA-PADESPLMRIk 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 207 APYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAklsDELGGGSMTALP 286
Cdd:PRK07196 229 ATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIY 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 287 IIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQ 366
Cdd:PRK07196 306 TVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIP 385
|
330
....*....|.
gi 284504904 367 FGSDLDAATQA 377
Cdd:PRK07196 386 LGGYVAGADPM 396
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
62-376 |
3.44e-30 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 120.01 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 62 RIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRK 141
Cdd:PRK05922 88 RPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 142 TGKTSVAidAILNQKDQDMICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMN 221
Cdd:PRK05922 168 SGKSSLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 222 GKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKlSDElggGSMTALPIIETQAG--DI-SAY 298
Cdd:PRK05922 246 GHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILHYPNhpDIfTDY 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 299 IPtnviSITDGQIFLDS--DSFYSgvrPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQFGS------- 369
Cdd:PRK05922 322 LK----SLLDGHFFLTPqgKALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAyvpgqda 394
|
....*..
gi 284504904 370 DLDAATQ 376
Cdd:PRK05922 395 HLDRAVK 401
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
46-362 |
7.87e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 119.31 E-value: 7.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 46 GDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEI-KTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDA 124
Cdd:PRK08927 72 GPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 125 LVPIGRGQRELIIGDRKTGKtSVAIDAILNQKDQDMIcVYVAIGQKDSTVRAQVEtlKKLGA--MDYTIVVTAGPAEPAP 202
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGK-SVLLSMLARNADADVS-VIGLIGERGREVQEFLQ--DDLGPegLARSVVVVATSDEPAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 203 LLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAklSDELGGGSM 282
Cdd:PRK08927 228 MRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 283 TALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELE 362
Cdd:PRK08927 306 TGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
15-362 |
2.86e-29 |
|
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: 117.90 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 15 NALQGELLEFSNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTN 94
Cdd:TIGR01039 27 NALKVQNRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 95 TRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILN-QKDQDMICVYVAIGQKDST 173
Cdd:TIGR01039 107 RWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTRE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 174 VRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFM-MNGKHVLIVYDDLSKQATAYRELSLILRRPPGR 252
Cdd:TIGR01039 187 GNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 253 EAYPGDVFYLHSRLLERAAKLSdelgGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASV 332
Cdd:TIGR01039 267 VGYQPTLATEMGELQERITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDST 342
|
330 340 350
....*....|....*....|....*....|....*
gi 284504904 333 SR-----VGGDAQIKAMKSVAGTLRldlaSYRELE 362
Cdd:TIGR01039 343 SRlldpsVVGEEHYDVARGVQQILQ----RYKELQ 373
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
19-334 |
2.09e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 115.13 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 19 GELLEFSN---GVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKttnT 95
Cdd:PRK02118 26 GELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELE---G 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 96 RPIEHKAPGI--MQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDrkTGKTSVAIDA-ILNQKDQDMIcVYVAIGQKDS 172
Cdd:PRK02118 103 EPIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALLArIALQAEADII-ILGGMGLTFD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 173 TVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNG-KHVLIVYDDLSKQATAYRELSLILRRPPG 251
Cdd:PRK02118 180 DYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQIPS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 252 REAYPGDvfyLHSRLLERAAKLSDELGGGSMTALPIIETQAGDISAYIPTNVISITDGQIFLDSDSfysgvrpaIDAGAS 331
Cdd:PRK02118 260 NRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRGR--------IDPFGS 328
|
...
gi 284504904 332 VSR 334
Cdd:PRK02118 329 LSR 331
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
1-62 |
6.43e-27 |
|
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: 101.76 E-value: 6.43e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284504904 1 IYIGDGIARAHGLDNALQGELLEFSNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGR 62
Cdd:cd18116 6 LSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
1-349 |
2.05e-26 |
|
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: 109.81 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 1 IYIGDGIARahgldnalQGELLEFSnGVYGIVQNLESNDvGIVVlgdfdgirEGDTVKRTGRIMEVPVGDAMIGRVVNPL 80
Cdd:TIGR01040 29 LTLPDGTVR--------SGQVLEVS-GNKAVVQVFEGTS-GIDA--------KKTTCEFTGDILRTPVSEDMLGRVFNGS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 81 GQPVDG----LGE-IKTTNTRPIEHKApgimqRQSVSEPLQTGIKAIDALVPIGRGQRELIIGD-------------RKT 142
Cdd:TIGR01040 91 GKPIDKgppvLAEdYLDINGQPINPYA-----RIYPEEMIQTGISAIDVMNSIARGQKIPIFSAaglphneiaaqicRQA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 143 GKTSVAIDAILNQKDQDMICVYVAIGQKDSTVRAQVETLKKLGAMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMN- 221
Cdd:TIGR01040 166 GLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQc 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 222 GKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLsdELGGGSMTALPIIETQAGDISAYIPT 301
Cdd:TIGR01040 246 EKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV--EGRNGSITQIPILTMPNDDITHPIPD 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 284504904 302 NVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVggdaqikaMKSVAG 349
Cdd:TIGR01040 324 LTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL--------MKSAIG 363
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
340-382 |
1.20e-25 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 100.21 E-value: 1.20e-25
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 284504904 340 QIKAMKSVAGTLRLDLASYRELESFSQFGSDLDAATQAKLNRG 382
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRG 43
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
344-382 |
4.39e-23 |
|
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: 93.20 E-value: 4.39e-23
10 20 30
....*....|....*....|....*....|....*....
gi 284504904 344 MKSVAGTLRLDLASYRELESFSQFGSDLDAATQAKLNRG 382
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERG 39
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
54-369 |
2.65e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 94.66 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 54 GDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEhkAPGI--MQRQSVSEPLQTGIKAIDALVPIGRG 131
Cdd:PRK06793 79 GDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLD--APPIhaFEREEITDVFETGIKSIDSMLTIGIG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 132 QRELIIGDRKTGKTSVaIDAILNQKDQDmICVYVAIGQKDSTVRAQVEtlKKLG--AMDYTIVVTAGPAEPAPLLYLAPY 209
Cdd:PRK06793 157 QKIGIFAGSGVGKSTL-LGMIAKNAKAD-INVISLVGERGREVKDFIR--KELGeeGMRKSVVVVATSDESHLMQLRAAK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 210 AGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPgreaYPGDVFYLHS---RLLERAAKLSDelggGSMTALP 286
Cdd:PRK06793 233 LATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 287 IIETQAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRVGGDAQIKAMKSVAGTLRLDLASYRELESFSQ 366
Cdd:PRK06793 305 TVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFK 384
|
...
gi 284504904 367 FGS 369
Cdd:PRK06793 385 LGT 387
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
65-335 |
2.71e-21 |
|
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: 92.28 E-value: 2.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 65 EVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGK 144
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 145 TSVAIDAILN-QKDQDMICVYVAIGQ------------KDSTVraqvetlKKLGAMDYTIVVTAGPAEPAPLLYLAPYAG 211
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGErtregndlyhemKESGV-------INLDGLSKVALVYGQMNEPPGARARVALTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 212 AAMGEEFM-MNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSMTALPIIET 290
Cdd:cd01133 154 LTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 284504904 291 QAGDISAYIPTNVISITDGQIFLDSDSFYSGVRPAIDAGASVSRV 335
Cdd:cd01133 230 PADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
33-154 |
5.65e-18 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 85.09 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 33 QNLESNDVGIVVLGDFDGIREGDTVKRTGRIMEVPVGDAMIGRVVNPLGQPVDGLGEIKTTNTRPIEHKAPGIMQRQSVS 112
Cdd:CHL00060 63 QLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKL 142
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 284504904 113 EPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSVAIDAILN 154
Cdd:CHL00060 143 SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN 184
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
1-61 |
7.72e-17 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 74.12 E-value: 7.72e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284504904 1 IYIGDGIARAHGLDNALQGELLEFSNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTG 61
Cdd:pfam02874 9 VDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
48-327 |
5.45e-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: 68.76 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 48 FDGIRegdtvKRTGRIMEVpvGDAMIGRVVN----PLGQPvdglgeikttntRPIEHKAPGimqrqsvSEPLQTGIKAID 123
Cdd:cd01134 15 FDGIQ-----RPLEVIAET--GSIFIPRGVNvqrwPVRQP------------RPVKEKLPP-------NVPLLTGQRVLD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 124 ALVPIGRGQRELIIGDRKTGKTsVAIDAILNQKDQDMIcVYVAIGQKDSTVraqVETLKKL----------GAMDYTIVV 193
Cdd:cd01134 69 TLFPVAKGGTAAIPGPFGCGKT-VISQSLSKWSNSDVV-IYVGCGERGNEM---AEVLEEFpelkdpitgeSLMERTVLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 194 TAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILRRPPGREAYPGdvfYLHSRL---LERA 270
Cdd:cd01134 144 ANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERA 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 284504904 271 AK---LSDELGGGSMTALPIIETQAGDISAYIPTNVISITdgQIF--LDSDSFYSGVRPAID 327
Cdd:cd01134 221 GRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSIN 280
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
161-333 |
4.77e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 55.03 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 161 ICVYVAIGQKDSTVRAQVETLKKLG-------AMDYTIVVTAGPAEPAPLLYLAPYAGAAMGEEFMMNGKHVLIVYDDLS 233
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKLKdpktgkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 234 KQATAYRELSLILRRPPGREAYPGdvfYLHSRLLE------RAAKLSDELGGGSMTALPIIETQAGDISAYIPTNVISIT 307
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180
....*....|....*....|....*.
gi 284504904 308 DGQIFLDSDSFYSGVRPAIDAGASVS 333
Cdd:PRK14698 841 KVFWALDADLARRRHFPAINWLTSYS 866
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
107-284 |
9.61e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 54.02 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 107 QRQSVSEPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTsVAIDAILNQKDQDmICVYVAIGQkdstvRAQ--VETL--- 181
Cdd:PRK04192 203 EKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKT-VTQHQLAKWADAD-IVIYVGCGE-----RGNemTEVLeef 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284504904 182 ---------KKLgaMDYTIVV--TAG-P--AEPAPLlylapYAGAAMGEEFMMNGKHVLIVYDDLSKQATAYRELSLILR 247
Cdd:PRK04192 276 pelidpktgRPL--MERTVLIanTSNmPvaAREASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLE 348
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 284504904 248 RPPGREAYPGdvfYLHSRL---LERAAKLSdELGG--GSMTA 284
Cdd:PRK04192 349 EMPGEEGYPA---YLASRLaefYERAGRVK-TLGGeeGSVTI 386
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
3-62 |
2.74e-05 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 41.91 E-value: 2.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 284504904 3 IGDGIARAHGLDNALQGELLEF-------SNGVYGIVQNLESNDVGIVVLGDFDGIREGDTVKRTGR 62
Cdd:cd01426 7 VNGPLVEAELEGEVAIGEVCEIergdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
344-382 |
9.00e-05 |
|
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: 40.51 E-value: 9.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 284504904 344 MKSVAGTLRLDLASYRELESFSQFGSD--LDAATQAKLNRG 382
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRG 41
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
120-161 |
4.44e-03 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 38.34 E-value: 4.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 284504904 120 KAIDALVPIGRGQRELIIGDRKTGKT----SVAIDAILNQKDQDMI 161
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTtllqNIANAIAKNHPEVELI 50
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
122-145 |
5.22e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 38.58 E-value: 5.22e-03
10 20
....*....|....*....|....
gi 284504904 122 IDALVPIGRGQRELIIGDRKTGKT 145
Cdd:PRK09376 160 IDLIAPIGKGQRGLIVAPPKAGKT 183
|
|
| |
