|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
48-550 |
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: 1016.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 48 AEVSSILEEKILGADTGAELEETGRVLSIGDGIARVYGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEG 127
Cdd:COG0056 6 EEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 128 DIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRE 207
Cdd:COG0056 86 DTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 208 LIIGDRQTGKTAIAIDTIINQKrfnegteeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYL 287
Cdd:COG0056 166 LIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 288 APYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDNFGGGSLTALP 367
Cdd:COG0056 238 APYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 368 VIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQ 447
Cdd:COG0056 318 IIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 448 FGSDLDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGHLDKMEPSKITKFEKAFLQHVISQHQDLLAAIRS 527
Cdd:COG0056 398 FGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRE 477
|
490 500
....*....|....*....|...
gi 116325975 528 DGKISEASDAKLKEIVLNFLSSF 550
Cdd:COG0056 478 TGKLDDEIEEKLKAAIEEFKKTF 500
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
48-550 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1014.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 48 AEVSSILEEKILGADTGAELEETGRVLSIGDGIARVYGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEG 127
Cdd:PRK09281 6 EEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 128 DIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRE 207
Cdd:PRK09281 86 DTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 208 LIIGDRQTGKTAIAIDTIINQKrfnegteeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYL 287
Cdd:PRK09281 166 LIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 288 APYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDNFGGGSLTALP 367
Cdd:PRK09281 238 APYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 368 VIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQ 447
Cdd:PRK09281 318 IIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 448 FGSDLDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGHLDKMEPSKITKFEKAFLQHVISQHQDLLAAIRS 527
Cdd:PRK09281 398 FGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRE 477
|
490 500
....*....|....*....|...
gi 116325975 528 DGKISEASDAKLKEIVLNFLSSF 550
Cdd:PRK09281 478 TKDLSDEIEAKLKAAIEEFKKTF 500
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
49-550 |
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: 834.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 49 EVSSILEEKILGADTGAELEETGRVLSIGDGIARVYGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGD 128
Cdd:TIGR00962 6 EISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 129 IVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQREL 208
Cdd:TIGR00962 86 TVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQREL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 209 IIGDRQTGKTAIAIDTIINQKrfnegteeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLA 288
Cdd:TIGR00962 166 IIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 289 PYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDNFGGGSLTALPV 368
Cdd:TIGR00962 238 PYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 369 IETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQF 448
Cdd:TIGR00962 318 IETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 449 GSDLDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGHLDKMEPSKITKFEKAFLQHVISQHQDLLAAIRSD 528
Cdd:TIGR00962 398 ASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTT 477
|
490 500
....*....|....*....|..
gi 116325975 529 GKISEASDAKLKEIVLNFLSSF 550
Cdd:TIGR00962 478 KKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
70-550 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 762.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 70 TGRVLSIGDGIARVYGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRV 149
Cdd:CHL00059 7 TGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 150 VDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTIINQK 229
Cdd:CHL00059 87 VNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 230 rfnegteeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALII 309
Cdd:CHL00059 167 --------GQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 310 YDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDNFGGGSLTALPVIETQAGDVSAYIPTNVISITD 389
Cdd:CHL00059 239 YDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 390 GQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTEL 469
Cdd:CHL00059 319 GQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLREL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 470 LKQGQYSPMAIEEQVAVIYAGVRGHLDKMEPSKITKFEKAFLQHVISQHQDLLAAIRSDGKISEASDAKLKEIVLNFLSS 549
Cdd:CHL00059 399 LKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEAIQEQLEL 478
|
.
gi 116325975 550 F 550
Cdd:CHL00059 479 F 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
44-550 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 744.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 44 KTGTAEVSSILEEKILGADTGAELEETGRVLSIGDGIARVYGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKL 123
Cdd:PRK13343 2 KSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 124 IKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGR 203
Cdd:PRK13343 82 ILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 204 GQRELIIGDRQTGKTAIAIDTIINQKrfnegteeKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAP 283
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 284 LQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDNFGGGSL 363
Cdd:PRK13343 234 LQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 364 TALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVA 443
Cdd:PRK13343 314 TALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 444 AFAQFGSDLDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGHLDKMEPSKITKFEKAFLQHVISQHQDLLA 523
Cdd:PRK13343 394 AFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSL 473
|
490 500
....*....|....*....|....*..
gi 116325975 524 AIRSDGKISEASDAKLKEIVLNFLSSF 550
Cdd:PRK13343 474 ALESPRELDEAWLAALEEILREAGERF 500
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
136-417 |
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: 620.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 136 IVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQT 215
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 216 GKTAIAIDTIINQKRfnegteekKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSM 295
Cdd:cd01132 81 GKTAIAIDTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 296 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDNFGGGSLTALPVIETQAGD 375
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 116325975 376 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVG 417
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
66-533 |
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: 556.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 66 ELEETGRVLSIGDGIARVYGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL 145
Cdd:TIGR03324 24 TVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 146 LGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTI 225
Cdd:TIGR03324 104 LGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 226 INQKRFNegteekkkLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH 305
Cdd:TIGR03324 184 LNQKGRN--------VLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 306 ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDNFGGGSLTALPVIETQAGDVSAYIPTNVI 385
Cdd:TIGR03324 256 VLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQNISAYIPTNLI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 386 SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVR 465
Cdd:TIGR03324 336 SITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGARLDENTRKTIEHGRR 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116325975 466 LTELLKQGQYSPMAIEEQVAVIYAGVRGHLDKMEPSKITKFEKAFLQHVISQHQDLLAAIRSDGKISE 533
Cdd:TIGR03324 416 IRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKKLSD 483
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
138-416 |
9.12e-136 |
|
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: 394.90 E-value: 9.12e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 138 DVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGK 217
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 218 TAIAIDTIINQKrfnegteEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGE 297
Cdd:cd19476 81 TVLAMQLARNQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 298 YFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDnfGGGSLTALPVIETQAGDVS 377
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 116325975 378 AYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 416
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
103-507 |
4.65e-125 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 378.61 E-value: 4.65e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 103 GMSLNLEPDN-VGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPIdgkgPLGSKERRR----------- 170
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEV----PVGLLTRSRalleseqtlgk 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 171 VGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTIINQKRFNEGTEEKKKLYCIYVAIGQ 250
Cdd:PTZ00185 156 VDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVSIGQ 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 251 KRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRP 330
Cdd:PTZ00185 236 RCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRP 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 331 PGREAYPGDVFYLHSRLLERAAKMNDNFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVG 410
Cdd:PTZ00185 316 PGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 411 LSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATqqlLNRGVRLTELLKQGQysPMAIEEQVAVIYAG 490
Cdd:PTZ00185 396 LSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSLYAC 470
|
410
....*....|....*..
gi 116325975 491 VRGHLDKMEPSKITKFE 507
Cdd:PTZ00185 471 LNGYLDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
191-414 |
2.14e-116 |
|
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: 343.18 E-value: 2.14e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 191 GIKAVDSLVPIGRGQRELIIGDRQTGKTAIAiDTIINQKRFNegteekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKY 270
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD---------VVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 271 TIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 350
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116325975 351 AAKMNDnfGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVS 414
Cdd:pfam00006 151 AGRVKG--KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
72-477 |
4.05e-102 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 317.30 E-value: 4.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 72 RVLSIGDGIARVYGLRNVQAEEMVEFSS--GLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRV 149
Cdd:PRK07165 4 KIKSIFDYIVEVKGEYDYQQNQFFTLKNnpNVKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 150 VDALGNPI--DGKGPLGSKERRRVG---LKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDT 224
Cdd:PRK07165 84 IDIDGNIIypEAQNPLSKKFLPNTSsifNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 225 IINQKrfNEGTEekkklyCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSAtASDAAPLQYLAPYSGCSMGE---YFRD 301
Cdd:PRK07165 164 IINQK--NTNVK------CIYVAIGQKRENLSRIYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAEnisYNDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 302 ngkhALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNdnfGGGSLTALPVIETQAGDVSAYIP 381
Cdd:PRK07165 235 ----VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFK---NRKTITALPILQTVDNDITSLIS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 382 TNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLN 461
Cdd:PRK07165 308 SNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLF 387
|
410
....*....|....*.
gi 116325975 462 RGVRLTELLKQGQYSP 477
Cdd:PRK07165 388 KGKMIEKMFNQKGFSL 403
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
425-550 |
6.57e-68 |
|
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: 214.92 E-value: 6.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 425 MKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGHLDKMEPSKIT 504
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 116325975 505 KFEKAFLQHVISQHQDLLAAIRSDGKISEASDAKLKEIVLNFLSSF 550
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
421-546 |
2.35e-65 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 208.45 E-value: 2.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 421 QTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGHLDKMEP 500
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 116325975 501 SKITKFEKAFLQHVISQHQDLLAAIRSDGKISEASDAKLKEIVLNF 546
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
139-416 |
1.76e-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: 171.59 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 139 VPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 218
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 219 aiaidTIINQkrFNEGTEEKKKlycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEY 298
Cdd:cd01136 82 -----TLLGM--IARNTDADVN---VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 299 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmndNFGGGSLTALPVIETQAGDVSA 378
Cdd:cd01136 152 FRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG----NGEKGSITAFYTVLVEGDDFND 227
|
250 260 270
....*....|....*....|....*....|....*...
gi 116325975 379 YIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 416
Cdd:cd01136 228 PIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
115-482 |
1.57e-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: 171.37 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 115 VVVFGNDKL----------IKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISV 184
Cdd:COG1157 58 VVGFRGDRVllmplgdlegISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 185 REPMQTGIKAVDSLVPIGRGQReliIG----------------DRQTgkTAiaiDTIInqkrfnegteekkklyciyVA- 247
Cdd:COG1157 138 TEPLDTGVRAIDGLLTVGRGQR---IGifagsgvgkstllgmiARNT--EA---DVNV-------------------IAl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 248 IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLL 327
Cdd:COG1157 191 IGERGREVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 328 RRPPGREAYPGDVFYLHSRLLERAAkmndNFGGGSLTAL------------PVIETqagdvsayiptnVISITDGQIFLE 395
Cdd:COG1157 271 GEPPATRGYPPSVFALLPRLLERAG----NGGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 396 TELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVA------AFAQfGSD--LDAAtqqlLNRGVRLT 467
Cdd:COG1157 335 RKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEdlirigAYQP-GSDpeLDEA----IALIPAIE 409
|
410
....*....|....*
gi 116325975 468 ELLKQGQYSPMAIEE 482
Cdd:COG1157 410 AFLRQGMDERVSFEE 424
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
130-492 |
1.99e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 168.39 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 130 VKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELI 209
Cdd:PRK06936 88 VSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 210 IGDRQTGKTAIaIDTIInqkrfnEGTEEKkklYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAP 289
Cdd:PRK06936 168 FAAAGGGKSTL-LASLI------RSAEVD---VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKAG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 290 YSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDNfggGSLTALPVI 369
Cdd:PRK06936 238 FVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-QSDK---GSITALYTV 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 370 ETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG 449
Cdd:PRK06936 314 LVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIG 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 116325975 450 S---DLDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIYAGVR 492
Cdd:PRK06936 394 EyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLTQ 439
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
46-449 |
9.50e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 166.48 E-value: 9.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 46 GTAEVSSILEEKILGAdtgAELEETGRVLSIGDGIARVYGL---------------RNVQAEEMVEFSSGLKGMSlnlep 110
Cdd:PRK09099 4 ELSRLADALERELAAL---PAVRRTGKVVEVIGTLLRVSGLdvtlgelcelrqrdgTLLQRAEVVGFSRDVALLS----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 111 dnvgvvVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQT 190
Cdd:PRK09099 76 ------PFGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 191 GIKAVDSLVPIGRGQRELIIGDRQTGKTaiaidTIINQkrFNEGTEekkklyC---IYVAIGQKRSTVAQLVKRLTDADA 267
Cdd:PRK09099 150 GVRIVDGLMTLGEGQRMGIFAPAGVGKS-----TLMGM--FARGTQ------CdvnVIALIGERGREVREFIELILGEDG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 268 MKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRL 347
Cdd:PRK09099 217 MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 348 LERAAkMNDNfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQ 427
Cdd:PRK09099 297 LERAG-MGET---GSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQ 372
|
410 420
....*....|....*....|..
gi 116325975 428 VAGTMKLELAQYREVAAFAQFG 449
Cdd:PRK09099 373 AAGRLRQLLAKHREVETLLQVG 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
124-487 |
1.27e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 163.35 E-value: 1.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 124 IKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKG-PLG----SKERrrvglKAPGIIPRISVREPMQTGIKAVDSL 198
Cdd:PRK07721 78 IAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSAlPKGlapvSTDQ-----DPPNPLKRPPIREPMEVGVRAIDSL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 199 VPIGRGQRELIIGDRQTGKTA----IAIDTiinQKRFNegteekkklycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVV 274
Cdd:PRK07721 153 LTVGKGQRVGIFAGSGVGKSTlmgmIARNT---SADLN-----------VIALIGERGREVREFIERDLGPEGLKRSIVV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 275 SATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKm 354
Cdd:PRK07721 219 VATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 355 NDNfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKL 434
Cdd:PRK07721 298 NAS---GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRE 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 435 ELAQYREVAAFAQFGS-------DLDAATQqllnRGVRLTELLKQGQYSPMAIEEQVAVI 487
Cdd:PRK07721 375 LLSTYQNSEDLINIGAykrgssrEIDEAIQ----FYPQIISFLKQGTDEKATFEESIQAL 430
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
71-478 |
1.35e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 163.45 E-value: 1.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 71 GRVLSIGDGIARVyGLRNVQAEEMVEFS-SGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRV 149
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEpQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 150 VDALGNPIDGKGPLGSKERRRVGlKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAI--------A 221
Cdd:PRK06820 110 LDGLGAPIDGGPPLTGQWRELDC-PPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLlgmlcadsA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 222 IDTIInqkrfnegteekkklyciYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATaSDAAPLQYL-APYSGCSMGEYFR 300
Cdd:PRK06820 189 ADVMV------------------LALIGERGREVREFLEQVLTPEARARTVVVVAT-SDRPALERLkGLSTATTIAEYFR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 301 DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmndNFGGGSLTALPVIETQAGDVSAYI 380
Cdd:PRK06820 250 DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTG----NSDRGSITAFYTVLVEGDDMNEPV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 381 PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFG---SDLDAATQ 457
Cdd:PRK06820 326 ADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQAD 405
|
410 420
....*....|....*....|...
gi 116325975 458 QLLNRGVRLTELLKQ--GQYSPM 478
Cdd:PRK06820 406 EALQRYPAICAFLQQdhSETAHL 428
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
67-473 |
1.45e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 154.84 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 67 LEETGRVLSIGDgIARVyglrnvqaeEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELL 146
Cdd:PRK08472 30 IEADGLNPSVGD-IVKI---------ESSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 147 GRVVDALGNPIDGKGPLGSKERRRVgLKAP------GIIprisvREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAI 220
Cdd:PRK08472 100 GRVVDPLGRPIDGKGAIDYERYAPI-MKAPiaamkrGLI-----DEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 221 aIDTIInqkrfnEGTEEKKKLyciyVA-IGQKRSTVAQLVKRLTDADaMKYTIVVSATASDAAPLQYLAPYSGCSMGEYF 299
Cdd:PRK08472 174 -MGMIV------KGCLAPIKV----VAlIGERGREIPEFIEKNLGGD-LENTVIVVATSDDSPLMRKYGAFCAMSVAEYF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 300 RDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmndNFGGGSLTALPVIETQAGDVSAY 379
Cdd:PRK08472 242 KNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 380 IPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFaQFGSD-- 451
Cdd:PRK08472 319 IADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKEnevlirIGAY-QKGNDke 397
|
410 420
....*....|....*....|..
gi 116325975 452 LDAAtqqlLNRGVRLTELLKQG 473
Cdd:PRK08472 398 LDEA----ISKKEFMEQFLKQN 415
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
139-493 |
2.37e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 151.81 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 139 VPVGEELLGRVVDALGNPIDGKGPLGSKERrrVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 216
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 217 KTAIaidtIINQKRFNEGTeekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAaPLQYLAPYSGCS 294
Cdd:PRK05688 181 KSVL----LGMMTRFTEAD--------IIVVglIGERGREVKEFIEHILGEEGLKRSVVVASPADDA-PLMRLRAAMYCT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 295 -MGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDNFGGGSLTALPVIETQA 373
Cdd:PRK05688 248 rIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 374 GDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFAQ 447
Cdd:PRK05688 326 DDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQsrdlisVGAYVA 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 116325975 448 FGsdlDAATQQLLNRGVRLTELLKQG--QYSPMA-IEEQVAVIYAGVRG 493
Cdd:PRK05688 406 GG---DPETDLAIARFPHLVQFLRQGlrENVSLAqSREQLAAIFAPAAG 451
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
139-473 |
9.84e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 147.15 E-value: 9.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 139 VPVGEELLGRVVDALGNPIDGKGPLGSKErrRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 216
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQ--RASRHSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 217 KTAIAidtiinqKRFNEGTEEKkklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYLapySGC-- 293
Cdd:PRK08972 175 KSVLL-------GMMTRGTTAD----VIVVGlVGERGREVKEFIEEILGEEGRARSVVVAAPA-DTSPLMRL---KGCet 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 294 --SMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDNFGGGSLTALPVIET 371
Cdd:PRK08972 240 atTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAG--NGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 372 QAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAF 445
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQnrdlisIGAY 397
|
330 340
....*....|....*....|....*...
gi 116325975 446 AQfGSdlDAATQQLLNRGVRLTELLKQG 473
Cdd:PRK08972 398 KQ-GS--DPRIDNAIRLQPAMNAFLQQT 422
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
71-472 |
2.82e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 146.30 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 71 GRVLSIGDGIARVYGL-RNVQAEEMVEFSSGlKGMSL----NLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPvGEEL 145
Cdd:PRK06002 28 GTVSEVTASHYRVRGLsRFVRLGDFVAIRAD-GGTHLgevvRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRP-DPSW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 146 LGRVVDALGNPIDGKGPLGSKERRR-VGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT------ 218
Cdd:PRK06002 106 KGRVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKStllaml 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 219 --AIAIDTIInqkrfnegteekkklyciyVA-IGQKRSTVAQLVKRlTDADAMKYTIVVSATASDAAPLQYLAPYSGCSM 295
Cdd:PRK06002 186 arADAFDTVV-------------------IAlVGERGREVREFLED-TLADNLKKAVAVVATSDESPMMRRLAPLTATAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 296 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDnfGGGSLTALPVIETQAGD 375
Cdd:PRK06002 246 AEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 376 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYRE------VAAFaQFG 449
Cdd:PRK06002 324 HNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdlrlIGGY-RAG 402
|
410 420
....*....|....*....|....*
gi 116325975 450 SD--LDAATQQLlnrgVRLTELLKQ 472
Cdd:PRK06002 403 SDpdLDQAVDLV----PRIYEALRQ 423
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
139-481 |
1.28e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 141.24 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 139 VPVGEELLGRVVDALGNPIDGKgPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 218
Cdd:PRK07594 91 VPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 219 AI------AIDTIINqkrfnegteekkklycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSG 292
Cdd:PRK07594 170 TLlamlcnAPDADSN----------------VLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 293 CSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMNDNfggGSLTALPVIETQ 372
Cdd:PRK07594 234 TTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITAFYTVLVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 373 AGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGS-- 450
Cdd:PRK07594 310 GDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEyq 389
|
330 340 350
....*....|....*....|....*....|..
gi 116325975 451 -DLDAATQQLLNRGVRLTELLKQGQYSPMAIE 481
Cdd:PRK07594 390 rGVDTDTDKAIDTYPDICTFLRQSKDEVCGPE 421
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
129-489 |
4.42e-36 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 139.36 E-value: 4.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 129 IVKRTGAIVDVPVGEELLGRVVDALGNpIDGK-----GPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGR 203
Cdd:PRK08149 72 VLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 204 GQRELIIGDRQTGKTAIaIDTIINQKRFNegteekkklycIYVA--IGQKRSTVAQLVKRLTDADAMKYTIVVSATaSDA 281
Cdd:PRK08149 151 GQRMGIFASAGCGKTSL-MNMLIEHSEAD-----------VFVIglIGERGREVTEFVESLRASSRREKCVLVYAT-SDF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 282 APLQYL-APYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmndNFGG 360
Cdd:PRK08149 218 SSVDRCnAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPG----ATLA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 361 GSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYR 440
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLE 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 116325975 441 EVAAFAQFG-------SDLDAAtqqlLNRGVRLTELLKQGQYSPMAIEEQVAVIYA 489
Cdd:PRK08149 374 ELQLFIDLGeyrrgenADNDRA----MDKRPALEAFLKQDVAEKSSFSDTLERLNE 425
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
139-430 |
2.61e-35 |
|
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: 133.89 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 139 VPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGlkAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTG 216
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDIN--GPPINPvaRIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 217 KTAIAIdTIINQKRFnEGTEEKKKLycIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMG 296
Cdd:cd01135 82 HNELAA-QIARQAGV-VGSEENFAI--VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 297 EYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNDNfgGGSLTALPVIETQ 372
Cdd:cd01135 158 EYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 116325975 373 AGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVgsaaqtraMKQVAG 430
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
69-135 |
3.27e-35 |
|
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: 126.41 E-value: 3.27e-35
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116325975 69 ETGRVLSIGDGIARVYGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGA 135
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
141-472 |
2.14e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 135.02 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 141 VGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAI 220
Cdd:PRK07196 92 IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 221 aidtiinqkrFNEGTEEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYLAPYSGC-SMGEYF 299
Cdd:PRK07196 172 ----------LGMITRYTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 300 RDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnDNFGGGSLTALPVIETQAGDVSAY 379
Cdd:PRK07196 241 RDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDP 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 380 IPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDL---DAAT 456
Cdd:PRK07196 318 IVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVagaDPMA 397
|
330
....*....|....*.
gi 116325975 457 QQLLNRGVRLTELLKQ 472
Cdd:PRK07196 398 DQAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
63-459 |
9.95e-32 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 127.59 E-value: 9.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 63 TGAELEETGRVLSIGDG--IARVYG--LRNVQAEEMvefssGLKGMSLNLEP-DNVGVVVFGNdKLIKEGDIVKRTGAIV 137
Cdd:PRK07960 35 TGLVLEATGLQLPLGATcvIERQNGseTHEVESEVV-----GFNGQRLFLMPlEEVEGILPGA-RVYARNISGEGLQSGK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 138 DVPVGEELLGRVVDALGNPIDGKGPlgSKERRRVGLKAPGIIP--RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQT 215
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPA--PDTGETGALITPPFNPlqRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 216 GKTAIaidtIINQKRFNEGTeekkklyCIYVA-IGQKRSTVAQLVKRLTDADAMKYTIVVSATAsDAAPLQYL--APYSg 292
Cdd:PRK07960 187 GKSVL----LGMMARYTQAD-------VIVVGlIGERGREVKDFIENILGAEGRARSVVIAAPA-DVSPLLRMqgAAYA- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 293 CSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmNDNFGGGSLTALPVIETQ 372
Cdd:PRK07960 254 TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAG--NGISGGGSITAFYTVLTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 373 AGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSA-------AQTRAMKQ-----------------V 428
Cdd:PRK07960 332 GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQllssfqrnrdlvsvgayA 411
|
410 420 430
....*....|....*....|....*....|....*...
gi 116325975 429 AGTMKL---ELAQYREVAAFAQFG----SDLDAATQQL 459
Cdd:PRK07960 412 KGSDPMldkAIALWPQLEAFLQQGiferADWEDSLQAL 449
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
139-479 |
9.23e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 124.63 E-value: 9.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 139 VPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 218
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 219 AIaIDTIinqkrfnegTEEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEY 298
Cdd:PRK05922 172 SL-LSTI---------AKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 299 FRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmNDNfggGSLTALPVIETQAGDVSA 378
Cdd:PRK05922 242 FRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILHYPNHPDI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 379 YIPTnVISITDGQIFL---ETELFykgiRPAINVGLSVSRvgSAAQTRAMKQVAGTMKLE--LAQYREVAAFAQFGSDLD 453
Cdd:PRK05922 318 FTDY-LKSLLDGHFFLtpqGKALA----SPPIDILTSLSR--SARQLALPHHYAAAEELRslLKAYHEALDIIQLGAYVP 390
|
330 340
....*....|....*....|....*.
gi 116325975 454 AATQQlLNRGVRLTELLKQGQYSPMA 479
Cdd:PRK05922 391 GQDAH-LDRAVKLLPSIKQFLSQPLS 415
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
106-488 |
1.43e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 123.93 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 106 LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGkgPLGSKERRRVGLKAPGI--IPRIS 183
Cdd:PRK06793 58 IAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNE--EAENIPLQKIKLDAPPIhaFEREE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 184 VREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTaiaidTIINQKRFNEgteeKKKLYCIYVaIGQKRSTVAQLVKRLT 263
Cdd:PRK06793 136 ITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS-----TLLGMIAKNA----KADINVISL-VGERGREVKDFIRKEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 264 DADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFYL 343
Cdd:PRK06793 206 GEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 344 HS---RLLERAAKMNDnfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA 420
Cdd:PRK06793 282 ESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEI 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116325975 421 QTRAMKQVAGTMKLELAQYREVAAFAQFGS----DLDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIY 488
Cdd:PRK06793 358 VSPNHWQLANEMRKILSIYKENELYFKLGTiqenAENAYIFECKNKVEGINTFLKQGRSDSFQFDDIVEAMH 429
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
83-482 |
4.58e-30 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 123.01 E-value: 4.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 83 VYGLRNVQAEEMVEFSSG----LKGMSLNLEPDNVGVVVF-GNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPI 157
Cdd:PRK04196 17 VEGVEGVAYGEIVEIELPngekRRGQVLEVSEDKAVVQVFeGTTGLDLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 158 DGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQReLII--GdrqTGKTA--IAIDtIINQKRFNE 233
Cdd:PRK04196 97 DGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQK-LPIfsG---SGLPHneLAAQ-IARQAKVLG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 234 GTEEkkkLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDD 312
Cdd:PRK04196 172 EEEN---FAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 313 LSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNDNfgGGSLTALPVIETQAGDVSAYIPTNVISITD 389
Cdd:PRK04196 249 MTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYITE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 390 GQIFLETELFYKGIRPAINVGLSVSR-----VGsAAQTRA-MKQVAGTMKLELAQYREVAAFAQF-GSD-LDAATQQLLN 461
Cdd:PRK04196 324 GQIVLSRELHRKGIYPPIDVLPSLSRlmkdgIG-EGKTREdHKDVANQLYAAYARGKDLRELAAIvGEEaLSERDRKYLK 402
|
410 420
....*....|....*....|..
gi 116325975 462 RGVRL-TELLKQGQYSPMAIEE 482
Cdd:PRK04196 403 FADAFeREFVNQGFDENRSIEE 424
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
121-483 |
8.11e-30 |
|
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: 122.13 E-value: 8.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 121 DKLIKeGDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVP 200
Cdd:TIGR01039 61 DGLVR-GLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 201 IGRGQRELIIGDRQTGKTAIAIDTIINQKRFNEGteekkklYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASD 280
Cdd:TIGR01039 140 YAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG-------YSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 281 AAPLQYLAPYSGCSMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNdnfg 359
Cdd:TIGR01039 213 PPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTK---- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 360 GGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQT-RAMKQVAGTMKLELAQ 438
Cdd:TIGR01039 289 TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVgEEHYDVARGVQQILQR 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 116325975 439 YREVA-AFAQFGSD-LDAATQQLLNRGVRLTELLKQgqysPMAIEEQ 483
Cdd:TIGR01039 369 YKELQdIIAILGMDeLSEEDKLTVERARRIQRFLSQ----PFFVAEV 411
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
146-482 |
4.02e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 117.00 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 146 LGRVVDALGNPIDGKGPLGSKERRRVgLKA--PGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAI--- 220
Cdd:PRK08927 99 LGRVVNALGEPIDGKGPLPQGPVPYP-LRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLlsm 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 221 -----AIDTIInqkrfnegteekkklycIYVaIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSM 295
Cdd:PRK08927 178 larnaDADVSV-----------------IGL-IGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 296 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKmnDNFGGGSLTALPVIETQAGD 375
Cdd:PRK08927 240 AEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGP--GPIGEGTITGLFTVLVDGDD 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 376 VSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSdLDAA 455
Cdd:PRK08927 318 HNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGA-YRAG 396
|
330 340 350
....*....|....*....|....*....|.
gi 116325975 456 TQQLLNRGVR----LTELLKQGQYSPMAIEE 482
Cdd:PRK08927 397 SDPEVDEAIRlnpaLEAFLRQGKDEATSLAE 427
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
133-425 |
2.49e-24 |
|
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: 105.96 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 133 TGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGD 212
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 213 RQTGKTAIAIDtIINQ--------KRFNEGTEEKkklYCI-YVAIGQKRSTvAQLVKR-LTDADAMKYTIVVSATASDAA 282
Cdd:TIGR01040 150 AGLPHNEIAAQ-ICRQaglvklptKDVHDGHEDN---FAIvFAAMGVNMET-ARFFKQdFEENGSMERVCLFLNLANDPT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 283 PLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDNfgGG 361
Cdd:TIGR01040 225 IERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NG 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116325975 362 SLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM 425
Cdd:TIGR01040 303 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
425-492 |
5.40e-22 |
|
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: 89.81 E-value: 5.40e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 425 MKQVAGTMKLELAQYREVAAFAQFGSD--LDAATQQLLNRGVRLTELLKQGQYSPMAIEEQVAVIYAGVR 492
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
139-416 |
6.82e-22 |
|
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: 95.75 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 139 VPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKT 218
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 219 AIAIDTIINQKRFNEG----------TEEKKKLYciyvaigqkrstvaqlvkrltdaDAMKYTIVVSATASDAAPLQY-- 286
Cdd:cd01133 82 VLIMELINNIAKAHGGysvfagvgerTREGNDLY-----------------------HEMKESGVINLDGLSKVALVYgq 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 287 ---------LAPYSGCSMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmnd 356
Cdd:cd01133 139 mneppgaraRVALTGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT---- 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 357 NFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRV 416
Cdd:cd01133 215 STKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
106-394 |
2.67e-21 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 96.64 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 106 LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGkGPlgSKERRRVGLKAPGIIP--RIS 183
Cdd:PRK02118 43 IRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GP--ELEGEPIEIGGPSVNPvkRIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 184 VREPMQTGIKAVD---SLVpigRGQReliigdrqtgktaIAIDTIINQKrFNE-------GTEEKKklyCIYVAIGQKRS 253
Cdd:PRK02118 120 PREMIRTGIPMIDvfnTLV---ESQK-------------IPIFSVSGEP-YNAllarialQAEADI---IILGGMGLTFD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 254 TVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPG 332
Cdd:PRK02118 180 DYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPS 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116325975 333 REAYPGDvfyLHSRLLERAAKMNDNFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL 394
Cdd:PRK02118 260 NRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
127-204 |
2.08e-18 |
|
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: 87.84 E-value: 2.08e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116325975 127 GDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRG 204
Cdd:COG0055 69 GMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKG 146
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
68-134 |
2.96e-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: 76.04 E-value: 2.96e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116325975 68 EETGRVLSIGDGIARVYGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTG 134
Cdd:pfam02874 3 QVIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
186-415 |
1.45e-15 |
|
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: 77.23 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 186 EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTAI--AI----DTIINqkrfnegteekkklycIYVAIGQKRSTVA--- 256
Cdd:cd01134 58 VPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVIsqSLskwsNSDVV----------------IYVGCGERGNEMAevl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 257 ----QLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPG 332
Cdd:cd01134 122 eefpELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 333 REAYPGdvfYLHSRL---LERA--AKMNDNFG-GGSLTALPVIETQAGDVSAYIPTNVISITdgQIF--LETELFYKGIR 404
Cdd:cd01134 202 EEGYPA---YLGARLaefYERAgrVRCLGSPGrEGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHF 276
|
250
....*....|.
gi 116325975 405 PAINVGLSVSR 415
Cdd:cd01134 277 PSINWLISYSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
124-408 |
2.21e-12 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 69.30 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 124 IKEGDIVKRTGAIVDVPVGEELLGRVVDALGNPIDGKGPLGSKERRRVGLKAPGII---PRISVREpmqTGIKAVDSLVP 200
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIFE---TGIKVVDLLAP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 201 IGRGQRELIIGDRQTGKTAIAIDTIINQKRFNEG----------TEEKKKLYciyvaIGQKRSTVAQLVKRLTDADAMKY 270
Cdd:CHL00060 158 YRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGvsvfggvgerTREGNDLY-----MEMKESGVINEQNIAESKVALVY 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 271 ---------TIVVSATASdaaplqylapysgcSMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDV 340
Cdd:CHL00060 233 gqmneppgaRMRVGLTAL--------------TMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTL 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116325975 341 FYLHSRLLERAAKMNDnfggGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAIN 408
Cdd:CHL00060 299 STEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVD 362
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
244-428 |
6.63e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 65.43 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 244 IYVAIGQKRSTVAQLVK---RLTDADA----MKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQ 316
Cdd:PRK14698 686 IYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRW 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 317 AVAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKMNDNFGGGSLTALPVIETQAGDVSAYIPTNVISITDG 390
Cdd:PRK14698 766 AEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKV 842
|
170 180 190
....*....|....*....|....*....|....*...
gi 116325975 391 QIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQV 428
Cdd:PRK14698 843 FWALDADLARRRHFPAINWLTSYSLYVDAVKDWWHKNV 880
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
290-365 |
1.08e-08 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 57.87 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 290 YSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMNdNFGG--GSLT 364
Cdd:PRK04192 310 YTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRVK-TLGGeeGSVT 385
|
.
gi 116325975 365 A 365
Cdd:PRK04192 386 I 386
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
70-135 |
4.02e-03 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 36.14 E-value: 4.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116325975 70 TGRVLSIGDGIARVYGLRNVQAEEMVEF-------SSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGA 135
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIergdgnnETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| DUF4142 |
pfam13628 |
Domain of unknown function (DUF4142); This is a bacterial family of unknown function. |
419-541 |
6.17e-03 |
|
Domain of unknown function (DUF4142); This is a bacterial family of unknown function.
Pssm-ID: 433361 Cd Length: 138 Bit Score: 37.21 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116325975 419 AAQTRAMKQV-AGTMKLELAQYREVAAFAQF-GSDLDAATQQLlnrgvrlTELLKQgqyspMAIEEQVAVIYAGVRGHLD 496
Cdd:pfam13628 9 KAAQAGLFEIeAAKLALQKSTNPEVKAFAQQmVADHTKANAEL-------KALASK-----KGVTLPDTTLDADQQAKLD 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 116325975 497 KMEPSKITKFEKAFLQHVISQHQDLLAAIrsDGKISEASDAKLKE 541
Cdd:pfam13628 77 KLSALSGAAFDKAYLDQQVAAHQKAVELF--EKYAASGDDPELKA 119
|
|
| |
