|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
2-505 |
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: 726.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 2 LEDRLEAFFQKLYSKLKEYSFEPYLEEEGTAVSVGDDIVFLRGLPNATLFELVVFEREDTGLIFDLDVETAGVVLLQKRG 81
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 82 GIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIG 161
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 162 RGQRELILGDPATGKTALAVDTVVNQKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPY 241
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 242 TATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDELGGGSITALPIVE 321
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 322 TQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGM 401
Cdd:COG0056 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 402 KLEEETLKLIQRGHRYREIFKQKPLHPRSLEEHILHLMLVDTGVLDEVPLEKVTEISSTLIKKLQESLPEITKNIKTLGR 481
Cdd:COG0056 401 DLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGK 480
|
490 500
....*....|....*....|....
gi 1057117146 482 LTTKEREIIKKFFSNLFQELYAGQ 505
Cdd:COG0056 481 LDDEIEEKLKAAIEEFKKTFAASA 504
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
7-492 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 635.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 7 EAFFQKLYSKLKEYSFEPYLEEEGTAVSVGDDIVFLRGLPNATLFELVVFEREDTGLIFDLDVETAGVVLLQKRGGIKAG 86
Cdd:PRK13343 6 DEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 87 DKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRE 166
Cdd:PRK13343 86 TEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 167 LILGDPATGKTALAVDTVVNQKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAI 246
Cdd:PRK13343 166 LIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 247 AEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDELGGGSITALPIVETQQGN 326
Cdd:PRK13343 246 AEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 327 ISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKLEEE 406
Cdd:PRK13343 326 LSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 407 TLKLIQRGHRYREIFKQKPLHPRSLEEHILHLMLVDTGVLDEVPLEKVTEISSTLIKKLQESLPEITKNIKTLGRLTTKE 486
Cdd:PRK13343 406 TQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRELDEAW 485
|
....*.
gi 1057117146 487 REIIKK 492
Cdd:PRK13343 486 LAALEE 491
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
15-497 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 619.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 15 SKLKEYSFEPYLEEEGTAVSVGDDIVFLRGLPNATLFELVVFEREDTGLIFDLDVETAGVVLLQKRGGIKAGDKAYRTGR 94
Cdd:PRK09281 14 QQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 95 MVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPAT 174
Cdd:PRK09281 94 ILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 175 GKTALAVDTVVNQKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKG 254
Cdd:PRK09281 174 GKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 255 KSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDELGGGSITALPIVETQQGNISAFIPTN 334
Cdd:PRK09281 254 KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 335 LISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKLEEETLKLIQRG 414
Cdd:PRK09281 334 VISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEATRAQLERG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 415 HRYREIFKQKPLHPRSLEEHILHLMLVDTGVLDEVPLEKVTEISSTLIKKLQESLPEITKNIKTLGRLTTKEREIIKKFF 494
Cdd:PRK09281 414 QRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKDLSDEIEAKLKAAI 493
|
...
gi 1057117146 495 SNL 497
Cdd:PRK09281 494 EEF 496
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
16-499 |
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: 550.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 16 KLKEYSFEPYLEEEGTAVSVGDDIVFLRGLPNATLFELVVFEREDTGLIFDLDVETAGVVLLQKRGGIKAGDKAYRTGRM 95
Cdd:TIGR00962 14 EIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 96 VSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATG 175
Cdd:TIGR00962 94 LEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 176 KTALAVDTVVNQKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGK 255
Cdd:TIGR00962 174 KTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 256 SVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDELGGGSITALPIVETQQGNISAFIPTNL 335
Cdd:TIGR00962 254 HALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQAGDVSAYIPTNV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 336 ISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKLEEETLKLIQRGH 415
Cdd:TIGR00962 334 ISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEATKKQLERGQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 416 RYREIFKQKPLHPRSLEEHILHLMLVDTGVLDEVPLEKVTEISSTLIKKLQESLPEITKNIKTLGRLTTKEREIIKKFFS 495
Cdd:TIGR00962 414 RVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKLTEELEAKLKEALK 493
|
....
gi 1057117146 496 NLFQ 499
Cdd:TIGR00962 494 NFKK 497
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
2-490 |
2.93e-180 |
|
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: 515.09 E-value: 2.93e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 2 LEDRLEAFFQKLYSKLKEYSFEPYLEEEGTAVSVGDDIVFLRGLPNATLFELVVFEREDTGLIFDLDVETAGVVLLQKRG 81
Cdd:TIGR03324 1 LTEVLDKAFQQLDQARESFQPQLTVQEVGTVESVSTGIARVHGLPGVGFEELLRFPGGLLGIAFNVDEDEVGVVLLGEYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 82 GIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIG 161
Cdd:TIGR03324 81 HLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIERPAPPIMDRAPVTVPLQTGLKVIDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 162 RGQRELILGDPATGKTALAVDTVVNQKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPY 241
Cdd:TIGR03324 161 RGQRELILGDRQTGKTAIAIDTILNQKGRNVLCIYCAIGQRASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 242 TATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDELGGGSITALPIVE 321
Cdd:TIGR03324 241 AATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPPGREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 322 TQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGM 401
Cdd:TIGR03324 321 TEAQNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGKSVSRVGGKAQLAAYRAVAGDLKLAYAQFEELETFARFGA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 402 KLEEETLKLIQRGHRYREIFKQKPLHPRSLEEHILHLMLVDTGVLDEVPLEKVTEISSTLIKKLQESLPEITKNIKTLGR 481
Cdd:TIGR03324 401 RLDENTRKTIEHGRRIRACLKQTQSSPLTVPQQIAILLALTNGLFDGVDLDAMPEAESAIRAAVTSLPADLRERLQSGKK 480
|
....*....
gi 1057117146 482 LTTKEREII 490
Cdd:TIGR03324 481 LSDEDREQI 489
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
30-492 |
1.13e-169 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 487.55 E-value: 1.13e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 30 GTAVSVGDDIVFLRGLPNATLFELVVFEREDTGLIFDLDVETAGVVLLQKRGGIKAGDKAYRTGRMVSVPVGEFILGKVL 109
Cdd:CHL00059 8 GTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 110 DGLGSPLE-------EEFSRkieiyypVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTALAVD 182
Cdd:CHL00059 88 NALAKPIDgkgeisaSESRL-------IESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 183 TVVNQKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGKSVLIIYD 262
Cdd:CHL00059 161 TILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 263 DLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDELGGGSITALPIVETQQGNISAFIPTNLISITDGQ 342
Cdd:CHL00059 241 DLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 343 IYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKLEEETLKLIQRGHRYREIFK 422
Cdd:CHL00059 321 IFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 423 QKPLHPRSLEEHILHLMLVDTGVLDEVPLEKVTEISSTLIKKLQESLPEITKNIKTLGRLTTKEREIIKK 492
Cdd:CHL00059 401 QSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKE 470
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-368 |
4.24e-150 |
|
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: 429.67 E-value: 4.24e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 96 VSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATG 175
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 176 KTALAVDTVVNQKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGK 255
Cdd:cd01132 82 KTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 256 SVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDELGGGSITALPIVETQQGNISAFIPTNL 335
Cdd:cd01132 162 HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNV 241
|
250 260 270
....*....|....*....|....*....|...
gi 1057117146 336 ISITDGQIYLDVELFNKNIRPAVDVGKSVSRIG 368
Cdd:cd01132 242 ISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-464 |
2.13e-96 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 303.12 E-value: 2.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 62 GLIFDLDVE-TAGVVLLQKRGGIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEF---SRKI----EIYYPVERE 133
Cdd:PTZ00185 80 GLVFNLEKDgRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVGLltrSRALleseQTLGKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 134 APPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTALAVDTVVNQKKSD--------VISIYVSIGQKREH 205
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINqqilsknaVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 206 IQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGRE 285
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 286 AFPGDIFYLHSRLLERAGKLKDELGGGSITALPIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVS 365
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVS 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 366 RIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKLeeETLKLIqRGHRYREIFKQKplHPRSLEEHILHLMLVDTGV 445
Cdd:PTZ00185 400 RVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQV--QTVPMI-RGARFVALFNQK--NPSFFMNALVSLYACLNGY 474
|
410
....*....|....*....
gi 1057117146 446 LDEVPLEKVTEISSTLIKK 464
Cdd:PTZ00185 475 LDDVKVNYAKLYEYLLVNK 493
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
106-500 |
2.53e-95 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 298.04 E-value: 2.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 106 GKVLDGLGSPLEEEfSRKIEIYYPVEREAPP------LLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTAL 179
Cdd:PRK07165 81 GKIIDIDGNIIYPE-AQNPLSKKFLPNTSSIfnlahgLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 180 AVDTVVNQKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGlQYLAPYTATAIAEFLrDKGKSVLI 259
Cdd:PRK07165 160 ALNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENI-SYNDDVLI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 260 IYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKdelGGGSITALPIVETQQGNISAFIPTNLISIT 339
Cdd:PRK07165 238 VFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFK---NRKTITALPILQTVDNDITSLISSNIISIT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 340 DGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKLEEETLKLIQRGHRYRE 419
Cdd:PRK07165 315 DGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEK 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 420 IFKQKPLHPRSLEEHILHLMLVDTGVldevpLEKVTEISSTL--IKKLQESLPEITKNIKTLGRLTTKEREIIKKFFSNL 497
Cdd:PRK07165 395 MFNQKGFSLYSYRFVLLISKLISWGL-----LKDVKDEQKALdfIDYLIENDPDAKKIFNKIKNNEDVDDELMKNYFAFL 469
|
...
gi 1057117146 498 FQE 500
Cdd:PRK07165 470 LNQ 472
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-365 |
3.69e-93 |
|
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: 281.94 E-value: 3.69e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 150 GITVIDALIPIGRGQRELILGDPATGKTALAvDTVVNQKKSDVIsIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEA 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADVV-VYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 230 GEPLGLQYLAPYTATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDEl 309
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1057117146 310 gGGSITALPIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVS 365
Cdd:pfam00006 158 -GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-367 |
8.70e-85 |
|
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: 262.78 E-value: 8.70e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 97 SVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 177 TALAVDTVVNQKKSDV-ISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGK 255
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 256 SVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDelGGGSITALPIVETQQGNISAFIPTNL 335
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 1057117146 336 ISITDGQIYLDVELFNKNIRPAVDVGKSVSRI 367
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-367 |
1.48e-53 |
|
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: 181.60 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 97 SVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGK 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 177 TALaVDTVVNQKKSDVISIyVSIGQK-REhiqrVYQFIANYGD---LSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRD 252
Cdd:cd01136 81 STL-LGMIARNTDADVNVI-ALIGERgRE----VREFIEKDLGeegLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 253 KGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDelggGSITALPIVETQQGNISAFIP 332
Cdd:cd01136 155 QGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIA 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1057117146 333 TNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRI 367
Cdd:cd01136 231 DEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
82-438 |
3.64e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 169.55 E-value: 3.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 82 GIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIG 161
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 162 RGQRELILGDPATGKTALaVDTVVNQKKSDVISIYVsIGQK-REhiqrVYQFI-ANYGD--LSKTIFLKVEAGEPLGLQY 237
Cdd:PRK06936 161 EGQRMGIFAAAGGGKSTL-LASLIRSAEVDVTVLAL-IGERgRE----VREFIeSDLGEegLRKAVLVVATSDRPSMERA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 238 LAPYTATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDelggGSITAL 317
Cdd:PRK06936 235 KAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDK----GSITAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 318 PIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFT 397
Cdd:PRK06936 311 YTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLL 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1057117146 398 KFG---MKLEEETLKLIQRGHRYREIFKQKPLHPRSLEEHILHL 438
Cdd:PRK06936 391 QIGeyqKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLL 434
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
25-366 |
1.10e-43 |
|
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: 159.81 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 25 YLEEEGTAVSVGDdIVFLRGLPNATLF-ELVVFEREDTGLifdldvetagvVLLQKRGGIKAGDKAYRTGRMVSVPVGEF 103
Cdd:COG1157 30 LIEAVGPDASIGE-LCEIETADGRPVLaEVVGFRGDRVLL-----------MPLGDLEGISPGARVVPTGRPLSVPVGDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 104 ILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTAL---- 179
Cdd:COG1157 98 LLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLlgmi 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 180 ----AVDTVvnqkksdVISIyvsIGQK-REhiqrVYQFIANygDL-----SKTIFLKVEAGEPLGLQYLAPYTATAIAEF 249
Cdd:COG1157 178 arntEADVN-------VIAL---IGERgRE----VREFIED--DLgeeglARSVVVVATSDEPPLMRLRAAYTATAIAEY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 250 LRDKGKSVLIIYDDLTK--HAssyrslslllKR--------PPGREAFPGDIFYLHSRLLERAGKlkdeLGGGSITAL-- 317
Cdd:COG1157 242 FRDQGKNVLLLMDSLTRfaMA----------QReiglaagePPATRGYPPSVFALLPRLLERAGN----GGKGSITAFyt 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1057117146 318 ----------PIVETqqgnisafiptnLISITDGQIYLDVELFNKNIRPAVDVGKSVSR 366
Cdd:COG1157 308 vlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISR 354
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
45-441 |
2.88e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 148.04 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 45 LPNATLFELVVFEreDTGLIFDLDVETAGVVLL---QKRGGIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFS 121
Cdd:PRK06820 45 LPGVAQGELCRIE--PQGMLAEVVSIEQEMALLspfASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 122 RKIEiYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTALaVDTVVNQKKSDVISIYVsIGQ 201
Cdd:PRK06820 123 LTGQ-WRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLCADSAADVMVLAL-IGE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 202 K----REHIQRVYQFIANygdlSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLL 277
Cdd:PRK06820 200 RgrevREFLEQVLTPEAR----ARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 278 LKRPPGREAFPGDIFYLHSRLLERAGKLKDelggGSITALPIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPA 357
Cdd:PRK06820 276 AGEPPAAGSFPPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 358 VDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKL---EEETLKLIQRGHRYREIFKQKPLHPRSLEEH 434
Cdd:PRK06820 352 IDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQageDLQADEALQRYPAICAFLQQDHSETAHLETT 431
|
....*..
gi 1057117146 435 ILHLMLV 441
Cdd:PRK06820 432 LEHLAQV 438
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
92-439 |
4.61e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 147.18 E-value: 4.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 92 TGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGD 171
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 172 PATGKTALaVDTVVNQKKSDVISIYVsIGQK-REhiqrVYQFIAN-YGD--LSKTIFLKVEAGEPLGLQYLAPYTATAIA 247
Cdd:PRK07721 167 SGVGKSTL-MGMIARNTSADLNVIAL-IGERgRE----VREFIERdLGPegLKRSIVVVATSDQPALMRIKGAYTATAIA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 248 EFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKlkdeLGGGSITALPIVETQQGNI 327
Cdd:PRK07721 241 EYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT----NASGSITAFYTVLVDGDDM 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 328 SAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKLEEET 407
Cdd:PRK07721 317 NEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSS 396
|
330 340 350
....*....|....*....|....*....|....*
gi 1057117146 408 LKLIQRGHRYREI---FKQKPLHPRSLEEHILHLM 439
Cdd:PRK07721 397 REIDEAIQFYPQIisfLKQGTDEKATFEESIQALL 431
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
18-400 |
8.09e-37 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 141.06 E-value: 8.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 18 KEYSFEPYLEEEGTAVSVGDDIVFLRGLpNATLFELVVFEREDTGLIFDLDVE--TAGVVLLQKRGGIKAGDKAYRT--- 92
Cdd:PRK09099 14 RELAALPAVRRTGKVVEVIGTLLRVSGL-DVTLGELCELRQRDGTLLQRAEVVgfSRDVALLSPFGELGGLSRGTRVigl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 93 GRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDP 172
Cdd:PRK09099 93 GRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 173 ATGKTALaVDTVVNQKKSDViSIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRD 252
Cdd:PRK09099 173 GVGKSTL-MGMFARGTQCDV-NVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 253 KGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGklkdeLGG-GSITALPIVETQQGNISAFI 331
Cdd:PRK09099 251 RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-----MGEtGSITALYTVLAEDESGSDPI 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057117146 332 PTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFG 400
Cdd:PRK09099 326 AEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
11-443 |
1.15e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 140.59 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 11 QKLYSKLKEYSFEPYLeeeGTAVSVGDDIVFLRGLpNATLFELVVFEREDT-----GLIFDLDVETAGVVLLQKRGGIKA 85
Cdd:PRK08472 4 ESLKNKLQKFNLSPRF---GSITKISPTIIEADGL-NPSVGDIVKIESSDNgkeclGMVVVIEKEQFGISPFSFIEGFKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 86 GDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQR 165
Cdd:PRK08472 80 GDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 166 ELILGDPATGKTALAVDTVVNQKKSdvISIYVSIGQK-REhiqrVYQFIANY--GDLSKTIFLKVEAGE-PLGLQYLApY 241
Cdd:PRK08472 160 LGIFAGSGVGKSTLMGMIVKGCLAP--IKVVALIGERgRE----IPEFIEKNlgGDLENTVIVVATSDDsPLMRKYGA-F 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 242 TATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKlkdELGGGSITALPIVE 321
Cdd:PRK08472 233 CAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 322 TQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFG- 400
Cdd:PRK08472 310 VEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGa 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1057117146 401 --MKLEEETLKLIQRGHRYREIFKQKPLHPRSLEEHILHLMLVDT 443
Cdd:PRK08472 390 yqKGNDKELDEAISKKEFMEQFLKQNPNELFPFEQTFEQLEEILR 434
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
4-392 |
6.36e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 135.90 E-value: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 4 DRLEAFfqklyskLKEYSFEPYLEEEGTAVS-VGDDIVFLRGL-PNATLFELVVFeREDTGLIFD--LDVETAGVVLLQK 79
Cdd:PRK06002 8 ARLAAL-------VERYAAPEPLVRIGGTVSeVTASHYRVRGLsRFVRLGDFVAI-RADGGTHLGevVRVDPDGVTVKPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 80 RGGIKA--GDKAYRTGRMVSVPV----GEFI--LGKVLDGLGSPLEEEFSRkieiyyPVEREAPPLLHRDFVREPLYTGI 151
Cdd:PRK06002 80 EPRIEIglGDAVFRKGPLRIRPDpswkGRVInaLGEPIDGLGPLAPGTRPM------SIDATAPPAMTRARVETGLRTGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 152 TVIDALIPIGRGQRELILGDPATGKTAL--------AVDTVVnqkksdvISIyvsIGQK-REhiqrVYQFIANY--GDLS 220
Cdd:PRK06002 154 RVIDIFTPLCAGQRIGIFAGSGVGKSTLlamlaradAFDTVV-------IAL---VGERgRE----VREFLEDTlaDNLK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 221 KTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLE 300
Cdd:PRK06002 220 KAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 301 RAGKLKDelGGGSITAL------------PIVETQQGnisafiptnlisITDGQIYLDVELFNKNIRPAVDVGKSVSRIG 368
Cdd:PRK06002 300 RAGPGAE--GGGSITGIfsvlvdgddhndPVADSIRG------------TLDGHIVLDRAIAEQGRYPAVDPLASISRLA 365
|
410 420
....*....|....*....|....
gi 1057117146 369 GKAQVPIMKEVAGKLKIEYAQFLE 392
Cdd:PRK06002 366 RHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
98-381 |
2.08e-33 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 128.11 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 98 VPVGEFILGKVLDGLGSP-------LEEEFsrkIEI----YYPVEREAPpllhrdfvREPLYTGITVIDALIPIGRGQRE 166
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPidggppiLPEDY---LDIngppINPVARIYP--------EEMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 167 LILGDPATGKTALAVD-----TVVNQKKSDVIsIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPY 241
Cdd:cd01135 73 PIFSGSGLPHNELAAQiarqaGVVGSEENFAI-VFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 242 TATAIAEFLR-DKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGdifYLHSRL---LERAGKLKDElgGGSITAL 317
Cdd:cd01135 152 MALTTAEYLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQI 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057117146 318 PIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRiggkaqvpIMKEVAG 381
Cdd:cd01135 227 PILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR--------LMKSGIG 282
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
92-370 |
4.31e-33 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 130.50 E-value: 4.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 92 TGRMVSVPVGEFILGKVLDGLGSpLEEEFSRKIEI-----YYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRE 166
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGK-IVERFDAPPTVgpiseERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 167 LILGDPATGKTALaVDTVVNQKKSDVisiYVsIGQKREHIQRVYQFI---ANYGDLSKTIFLKVEAGEPLGLQYLAPYTA 243
Cdd:PRK08149 155 GIFASAGCGKTSL-MNMLIEHSEADV---FV-IGLIGERGREVTEFVeslRASSRREKCVLVYATSDFSSVDRCNAALVA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 244 TAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDelggGSITALPIVETQ 323
Cdd:PRK08149 230 TTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA----GSITAFYTVLLE 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1057117146 324 QGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGK 370
Cdd:PRK08149 306 SEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ 352
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
82-400 |
1.17e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 126.61 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 82 GIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIeIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIG 161
Cdd:PRK07594 75 GLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDV-CWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 162 RGQRELILGDPATGKTALaVDTVVNQKKSDViSIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPY 241
Cdd:PRK07594 154 EGQRVGIFSAPGVGKSTL-LAMLCNAPDADS-NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 242 TATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGklkdeLGG-GSITALPIV 320
Cdd:PRK07594 232 VATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 321 ETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFG 400
Cdd:PRK07594 307 LVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIG 386
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
376-500 |
1.31e-31 |
|
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: 117.85 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 376 MKEVAGKLKIEYAQFLEKEIFTKFGMKLEEETLKLIQRGHRYREIFKQKPLHPRSLEEHILHLMLVDTGVLDEVPLEKVT 455
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1057117146 456 EISSTLIKKLQESLPEITKNIKTLGRLTTKEREIIKKFFSNLFQE 500
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKS 125
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
92-367 |
3.48e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 125.61 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 92 TGRMvsvPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGD 171
Cdd:PRK05688 100 TGRL---PMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 172 PATGKTALaVDTVVNQKKSDVISIYVsIGQK-REhiqrVYQFIAN-YGD--LSKTIFLKVEAGEPLGLQYLAPYTATAIA 247
Cdd:PRK05688 177 TGVGKSVL-LGMMTRFTEADIIVVGL-IGERgRE----VKEFIEHiLGEegLKRSVVVASPADDAPLMRLRAAMYCTRIA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 248 EFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGklKDELGGGSITALPIVETQQGNI 327
Cdd:PRK05688 251 EYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQ 328
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1057117146 328 SAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRI 367
Cdd:PRK05688 329 QDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
23-406 |
6.55e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 124.32 E-value: 6.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 23 EPYLEEEGTAVSVGDdiVFLRGlPNATLFELVVFEREDTGLIfdldvetagvvLLQKRGGIKAGDKAYRTGRMVSVPVGE 102
Cdd:PRK06793 30 EQFFVAKGPKAKIGD--VCFVG-EHNVLCEVIAIEKENNMLL-----------PFEQTEKVCYGDSVTLIAEDVVIPRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 103 FILGKVLDGLGSPLEEEfSRKIEIYyPVEREAPPL--LHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTALa 180
Cdd:PRK06793 96 HLLGKVLSANGEVLNEE-AENIPLQ-KIKLDAPPIhaFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTL- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 181 VDTVVNQKKSDvISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGKSVLII 260
Cdd:PRK06793 173 LGMIAKNAKAD-INVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 261 YDDLTKHASSYRSLSLLLKRPPgreaFPGDIFYLHS---RLLERAGKLKDelggGSITALPIVETQQGNISAFIPTNLIS 337
Cdd:PRK06793 252 MDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDLARG 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057117146 338 ITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKLEEE 406
Cdd:PRK06793 324 ILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENA 392
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
372-494 |
1.79e-28 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 109.45 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 372 QVPIMKEVAGKLKIEYAQFLEKEIFTKFGMKLEEETLKLIQRGHRYREIFKQKPLHPRSLEEHILHLMLVDTGVLDEVPL 451
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1057117146 452 EKVTEISSTLIKKLQESLPEITKNIKTLGRLTTKEREIIKKFF 494
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAI 123
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
82-367 |
4.29e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 116.34 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 82 GIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPveREAPPL--LHRDFVREPLYTGITVIDALIP 159
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRAS--RHSPPInpLSRRPITEPLDVGVRAINAMLT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 160 IGRGQRELILGDPATGKTALaVDTVVNQKKSDVISIYVsIGQK-REhiqrVYQFIAN-YGDLSKTIFLKVEA---GEPLg 234
Cdd:PRK08972 159 VGKGQRMGLFAGSGVGKSVL-LGMMTRGTTADVIVVGL-VGERgRE----VKEFIEEiLGEEGRARSVVVAApadTSPL- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 235 LQYLAPYTATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDelGGGSI 314
Cdd:PRK08972 232 MRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSI 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1057117146 315 TALPIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRI 367
Cdd:PRK08972 310 TAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRV 362
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
17-366 |
5.02e-28 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 116.46 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 17 LKEYSfepyleeegTAVSVGDDIVFLRGLPNATLFELVVFERED----TGLIFDLDVETAGVVLLQKRGGIKAGDKAYR- 91
Cdd:PRK04196 1 LKEYR---------TVSEIKGPLLFVEGVEGVAYGEIVEIELPNgekrRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRf 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 92 TGRMVSVPVGEFILGKVLDGLGSPLEE------EFSRKI--EIYYPVEREAPpllhrdfvREPLYTGITVIDALIPIGRG 163
Cdd:PRK04196 72 TGEPLKLPVSEDMLGRIFDGLGRPIDGgpeiipEKRLDIngAPINPVAREYP--------EEFIQTGISAIDGLNTLVRG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 164 QRELIL---GDPATgktALAVDtVVNQKK-----SDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGL 235
Cdd:PRK04196 144 QKLPIFsgsGLPHN---ELAAQ-IARQAKvlgeeENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 236 QYLAPYTATAIAEFLR-DKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGdifYLHSRL---LERAGKLKDElgG 311
Cdd:PRK04196 220 RILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--K 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1057117146 312 GSITALPIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSR 366
Cdd:PRK04196 295 GSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
55-366 |
1.45e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 112.18 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 55 VFEREDTGLIFDLDVETAG-------VVLLQKRGGIKAGDKAYrtGRMVS---------VPVGEFILGKVLDGLGSPLEE 118
Cdd:PRK07960 53 VIERQNGSETHEVESEVVGfngqrlfLMPLEEVEGILPGARVY--ARNISgeglqsgkqLPLGPALLGRVLDGSGKPLDG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 119 EFSRkiEIYYPVEREAPPL--LHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTALaVDTVVNQKKSDVISIY 196
Cdd:PRK07960 131 LPAP--DTGETGALITPPFnpLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVL-LGMMARYTQADVIVVG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 197 VsIGQK-REhiqrVYQFIAN-YGD--LSKTIFLKVEAG-EPLGLQYLAPYtATAIAEFLRDKGKSVLIIYDDLTKHASSY 271
Cdd:PRK07960 208 L-IGERgRE----VKDFIENiLGAegRARSVVIAAPADvSPLLRMQGAAY-ATRIAEDFRDRGQHVLLIMDSLTRYAMAQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 272 RSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDelGGGSITALPIVETQQGNISAFIPTNLISITDGQIYLDVELFN 351
Cdd:PRK07960 282 REIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAE 359
|
330
....*....|....*
gi 1057117146 352 KNIRPAVDVGKSVSR 366
Cdd:PRK07960 360 AGHYPAIDIEASISR 374
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
52-392 |
8.64e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 109.60 E-value: 8.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 52 ELVVFEREDTGLIfdldvetagvvLLQKRGGIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEfsRKIEIYYPVE 131
Cdd:PRK07196 55 QVVGFDRDITYLM-----------PFKHPGGVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGK--GQLGGSTPLQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 132 REAPPL--LHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTALaVDTVVNQKKSDVISIYVsIGQKREHIQRV 209
Cdd:PRK07196 122 QQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGL-IGERGREVKEF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 210 YQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPG 289
Cdd:PRK07196 200 IEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 290 DIFYLHSRLLERAGklkDELGGGSITALPIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRIGG 369
Cdd:PRK07196 280 SAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS 356
|
330 340
....*....|....*....|...
gi 1057117146 370 KAQVPIMKEVAGKLKIEYAQFLE 392
Cdd:PRK07196 357 QVIGSQQAKAASLLKQCYADYMA 379
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
82-427 |
3.05e-22 |
|
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: 99.41 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 82 GIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIG 161
Cdd:TIGR01039 62 GLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 162 RGQRELILGDPATGKTALAVDTVVN-QKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAP 240
Cdd:TIGR01039 142 KGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 241 YTATAIAEFLRD-KGKSVLIIYDDLTKHASSYRSLSLLLKRppgreaFPGDIFYlHSRLLERAGKLKDELG---GGSITA 316
Cdd:TIGR01039 222 LTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGR------MPSAVGY-QPTLATEMGELQERITstkTGSITS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 317 LPIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSR-----IGGKAQVPIMKEVAGKLKiEYAQFl 391
Cdd:TIGR01039 295 VQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRlldpsVVGEEHYDVARGVQQILQ-RYKEL- 372
|
330 340 350
....*....|....*....|....*....|....*..
gi 1057117146 392 eKEIFTKFGM-KLEEETLKLIQRGHRYREIFKQkPLH 427
Cdd:TIGR01039 373 -QDIIAILGMdELSEEDKLTVERARRIQRFLSQ-PFF 407
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
92-367 |
6.40e-22 |
|
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: 98.26 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 92 TGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELIL-- 169
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFsa 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 170 -GDP----------ATGKTALAVDTVVNQKKSDVISIYVSIGQKREHIQRVYQFIANYGDLSKT-IFLKVeAGEPLGLQY 237
Cdd:TIGR01040 150 aGLPhneiaaqicrQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVcLFLNL-ANDPTIERI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 238 LAPYTATAIAEFLR-DKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKLKDElgGGSITA 316
Cdd:TIGR01040 229 ITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NGSITQ 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1057117146 317 LPIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSRI 367
Cdd:TIGR01040 307 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRL 357
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
94-384 |
1.62e-21 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 96.90 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 94 RMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPA 173
Cdd:PRK05922 88 RPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 174 TGKTALaVDTVVNQKKSdVISIYVSIGQK----REHIQRVYQFIANYgdlsKTIFLKVEAGEPLGLQYLAPYTATAIAEF 249
Cdd:PRK05922 168 SGKSSL-LSTIAKGSKS-TINVIALIGERgrevREYIEQHKEGLAAQ----RTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 250 LRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGKlKDElggGSITALPIVeTQQGNISA 329
Cdd:PRK05922 242 FRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAI-LHYPNHPD 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1057117146 330 FIPTNLISITDGQIYLDVElfNKNI-RPAVDVGKSVSRIGGKAQVPIMKEVAGKLK 384
Cdd:PRK05922 317 IFTDYLKSLLDGHFFLTPQ--GKALaSPPIDILTSLSRSARQLALPHHYAAAEELR 370
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
10-345 |
1.82e-20 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 93.56 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 10 FQKLYSKLKEYSfepyleeeGTAVSVGDDivflrglpNATLFELVVFEREDTGL---IFDLDVETAGVVLLQKRGGIKAG 86
Cdd:PRK02118 1 MQKIYTKITDIT--------GNVITVEAE--------GVGYGELATVERKDGSSlaqVIRLDGDKVTLQVFGGTRGISTG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 87 DKAYRTGRMVSVPVGEFILGKVLDGLGSPLE---EEFSRKIEI----YYPVEREAPpllhRDFVReplyTGITVIDALIP 159
Cdd:PRK02118 65 DEVVFLGRPMQVTYSESLLGRRFNGSGKPIDggpELEGEPIEIggpsVNPVKRIVP----REMIR----TGIPMIDVFNT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 160 IGRGQRELILGDPATGKTALAVdTVVNQKKSDVIsIYVSIGQKREHIQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLA 239
Cdd:PRK02118 137 LVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 240 PYTATAIAE-FLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDifyLHSRLLERAGKLKDELGGGSITALP 318
Cdd:PRK02118 215 PDMALAVAEkFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIA 291
|
330 340
....*....|....*....|....*..
gi 1057117146 319 IVETQQGNISAFIPTNLISITDGQIYL 345
Cdd:PRK02118 292 VTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
31-382 |
1.22e-19 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 91.19 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 31 TAVSVGDDIVFLRGLPNATLFELVVFeREDTGLIF---DLDvetagvvllqkrgGIKAGDKAYRTGRMVSVPVGEFILGK 107
Cdd:PRK08927 36 HALSVGARIVVETRGGRPVPCEVVGF-RGDRALLMpfgPLE-------------GVRRGCRAVIANAAAAVRPSRAWLGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 108 VLDGLGSP------LEEEFSRkieiyYPVeREAPPLLH-RDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTALa 180
Cdd:PRK08927 102 VVNALGEPidgkgpLPQGPVP-----YPL-RAPPPPAHsRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 181 VDTVVNQKKSDVISIYVsIGQK-REhiqrVYQFI-ANYGD--LSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGKS 256
Cdd:PRK08927 175 LSMLARNADADVSVIGL-IGERgRE----VQEFLqDDLGPegLARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 257 VLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGDIFYLHSRLLERAGklKDELGGGSITALPIVETQQGNISAFIPTNLI 336
Cdd:PRK08927 250 VLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVR 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1057117146 337 SITDGQIYLDVELFNKNIRPAVDVGKSVSRIGGKAQVPIMKEVAGK 382
Cdd:PRK08927 328 GILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRR 373
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-262 |
2.77e-19 |
|
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: 87.66 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 97 SVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGK 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 177 TALAVDTVVN-QKKSDVISIYVSIGQK-REHIQRVYQFIA----NYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFL 250
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGERtREGNDLYHEMKEsgviNLDGLSKVALVYGQMNEPPGARARVALTGLTMAEYF 160
|
170
....*....|...
gi 1057117146 251 RD-KGKSVLIIYD 262
Cdd:cd01133 161 RDeEGQDVLLFID 173
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
38-262 |
6.55e-17 |
|
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: 83.22 E-value: 6.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 38 DIVFLRG-LPNatLFELVVFEREDTGLIF-----DLDVETAGVVLLQKRGGIKAGDKAYRTGRMVSVPVGEFILGKVLDG 111
Cdd:COG0055 17 DVEFPEGeLPA--IYNALEVENEGGGELVlevaqHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 112 LGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRELILGDPATGKTALAVDTVVN-QKKS 190
Cdd:COG0055 95 LGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNiAKEH 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1057117146 191 DVISIYVSIGQK-REHiQRVYQFIANYGDLSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRD-KGKSVLIIYD 262
Cdd:COG0055 175 GGVSVFAGVGERtREG-NDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDeEGQDVLLFID 247
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
28-94 |
3.77e-15 |
|
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: 69.79 E-value: 3.77e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057117146 28 EEGTAVSVGDDIVFLRGLPNATLFELVVFEREDTGLIFDLDVETAGVVLLQKRGGIKAGDKAYRTGR 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
95-366 |
1.24e-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: 71.45 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 95 MVSVPVGEFILGKVLDGLGSPLEEEF-------SRKIEI-YYPVeREAPPLLHRDFVREPLYTGITVIDALIPIGRGQRE 166
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAetgsifiPRGVNVqRWPV-RQPRPVKEKLPPNVPLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 167 LILGDPATGKTalavdtVVNQ---KKSDV-ISIYVSIGQKREHIQRVYQ-------------------FIANygdlskTI 223
Cdd:cd01134 80 AIPGPFGCGKT------VISQslsKWSNSdVVIYVGCGERGNEMAEVLEefpelkdpitgeslmertvLIAN------TS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 224 FLKVEAGEPlglqylAPYTATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGdifYLHSRL---LE 300
Cdd:cd01134 148 NMPVAAREA------SIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYE 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057117146 301 RAGKLKdELGG----GSITALPIVETQQGNISAFIPTNLISITdgQIY--LDVELFNKNIRPAVDVGKSVSR 366
Cdd:cd01134 219 RAGRVR-CLGSpgreGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
82-264 |
5.09e-11 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 64.68 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 82 GIKAGDKAYRTGRMVSVPVGEFILGKVLDGLGSPLEEEFSRKIEIYYPVEREAPPLLHRDFVREPLYTGITVIDALIPIG 161
Cdd:CHL00060 80 GLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 162 RGQRELILGDPATGKTALAVDTVVNQKKSDV-ISIYVSIGQKREHIQRVY-----------QFIANygdlSKTIFLKVEA 229
Cdd:CHL00060 160 RGGKIGLFGGAGVGKTVLIMELINNIAKAHGgVSVFGGVGERTREGNDLYmemkesgvineQNIAE----SKVALVYGQM 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 1057117146 230 GEPLGLQYLAPYTATAIAEFLRDKGKS-VLIIYDDL 264
Cdd:CHL00060 236 NEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNI 271
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
193-359 |
2.14e-06 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 50.41 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 193 ISIYVSIGQKREHIQRVYQFIANYGD-------LSKTIFLKVEAGEPLGLQYLAPYTATAIAEFLRDKGKSVLIIYDDLT 265
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKLKDpktgkplMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 266 KHASSYRSLSLLLKRPPGREAFPGdifYLHSRL---LERAGK---LKDELGGGSITALPIVETQQGNISAFIPTNLISIT 339
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLaefYERAGRvvtLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180
....*....|....*....|
gi 1057117146 340 DGQIYLDVELFNKNIRPAVD 359
Cdd:PRK14698 841 KVFWALDADLARRRHFPAIN 860
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
153-366 |
6.12e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 48.54 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 153 VIDALIPIGRGQRELILGDPATGKTAL--AVDTVVNQKKSDVISIYVSIGQKREHIQrvyqfianygDLSKTIflkveAG 230
Cdd:PRK12608 123 VVDLVAPIGKGQRGLIVAPPRAGKTVLlqQIAAAVAANHPEVHLMVLLIDERPEEVT----------DMRRSV-----KG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 231 EPLGLQYLAPYT-----ATAIAEFLR---DKGKSVLIIYDDLTKHASSYRSLSlllkRPPGREAFPGdifyLHSRLLERA 302
Cdd:PRK12608 188 EVYASTFDRPPDehirvAELVLERAKrlvEQGKDVVILLDSLTRLARAYNNEV----ESSGRTLSGG----VDARALQRP 259
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1057117146 303 GKL-----KDElGGGSIT--ALPIVETQQgNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGKSVSR 366
Cdd:PRK12608 260 KRLfgaarNIE-EGGSLTiiATALVDTGS-RMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTR 328
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
376-435 |
9.53e-06 |
|
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: 43.59 E-value: 9.53e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1057117146 376 MKEVAGKLKIEYAQFLEKEIFTKFG--MKLEEETLKLIQRGHRYREIFKQKPLHPRSLEEHI 435
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVgdDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTL 62
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
27-328 |
5.29e-05 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 45.93 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 27 EEEGTAVSVGDDIVFLRGLPNATLFELV-VFEREDTGLIFDLDVETAGVVLLQKRGGIKAGDKAYRTGRMVSVPVGEFIL 105
Cdd:PRK04192 2 MTKGKIVRVSGPLVVAEGMGGARMYEVVrVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 106 GKVLDGLGSPLEE------EF-SRKIEIYyPVEREA-----------------------------------PP------- 136
Cdd:PRK04192 82 GSIFDGIQRPLDElaeksgDFlERGVYVP-ALDREKkweftptvkvgdkveagdilgtvqetpsiehkimvPPgvsgtvk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 137 ----------------------------LLHRDFVR------------EPLYTGITVIDALIPIGRGQRELILGDPATGK 176
Cdd:PRK04192 161 eivsegdytvddtiavlededgegveltMMQKWPVRrprpykeklppvEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 177 TalavdtVVNQ---KKSDV-ISIYVSIGQK--------------------REHIQRVYqFIANygdlskTIFLKVEAGEp 232
Cdd:PRK04192 241 T------VTQHqlaKWADAdIVIYVGCGERgnemtevleefpelidpktgRPLMERTV-LIAN------TSNMPVAARE- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 233 lglqylAP-YTATAIAEFLRDKGKSVLIIYDDLTKHASSYRSLSLLLKRPPGREAFPGdifYLHSRL---LERAGKLKDe 308
Cdd:PRK04192 307 ------ASiYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRVKT- 376
|
410 420
....*....|....*....|..
gi 1057117146 309 LGG--GSITALPIVETQQGNIS 328
Cdd:PRK04192 377 LGGeeGSVTIIGAVSPPGGDFS 398
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
149-362 |
3.00e-04 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 42.21 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 149 TGITVIDALIPIG--RGQRELILGDPATGKTALAVDTVVNQKKSDVISIYVSIgqkREHIQRVYQFIANYG-DLSKTI-- 223
Cdd:COG0467 4 TGIPGLDELLGGGlpRGSSTLLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSF---EESPEQLLRRAESLGlDLEEYIes 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 224 -FLKVEAGEPLGLQYLAPYTATAIAEFLRDKGKSVLIIyDDLTkhassyrslslllkrppGREAFPGDIFYLHSRLLEra 302
Cdd:COG0467 81 gLLRIIDLSPEELGLDLEELLARLREAVEEFGAKRVVI-DSLS-----------------GLLLALPDPERLREFLHR-- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 303 gkLKDELGGGSITALpIVETQQGNISAFIPTNLISITDGQIYLDVELFNKNIRPAVDVGK 362
Cdd:COG0467 141 --LLRYLKKRGVTTL-LTSETGGLEDEATEGGLSYLADGVILLRYVELGGELRRALSVLK 197
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
153-179 |
1.52e-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: 40.27 E-value: 1.52e-03
10 20
....*....|....*....|....*..
gi 1057117146 153 VIDALIPIGRGQRELILGDPATGKTAL 179
Cdd:cd01128 6 VIDLIAPIGKGQRGLIVAPPKAGKTTL 32
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
153-179 |
3.98e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 39.74 E-value: 3.98e-03
10 20
....*....|....*....|....*..
gi 1057117146 153 VIDALIPIGRGQRELILGDPATGKTAL 179
Cdd:PRK09376 159 IIDLIAPIGKGQRGLIVAPPKAGKTVL 185
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
153-177 |
4.22e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 39.89 E-value: 4.22e-03
10 20
....*....|....*....|....*
gi 1057117146 153 VIDALIPIGRGQRELILGDPATGKT 177
Cdd:PRK12678 406 VIDLIMPIGKGQRGLIVSPPKAGKT 430
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
29-117 |
6.80e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 39.23 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057117146 29 EGTAVSVGDDIVFLRGLPNATLFELV-VFEREDTGLIFDLDVETAGVVLLQKRGGIKAGDKAYRTGRMVSVPVGEFILGK 107
Cdd:PRK14698 4 KGRIIRVTGPLVIADGMKGAKMYEVVrVGELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTS 83
|
90
....*....|
gi 1057117146 108 VLDGLGSPLE 117
Cdd:PRK14698 84 IYDGIQRPLE 93
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
153-179 |
6.98e-03 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 38.90 E-value: 6.98e-03
10 20
....*....|....*....|....*..
gi 1057117146 153 VIDALIPIGRGQRELILGDPATGKTAL 179
Cdd:TIGR00767 158 VLDLFAPIGKGQRGLIVAPPKAGKTVL 184
|
|
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
153-179 |
9.26e-03 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 38.47 E-value: 9.26e-03
10 20
....*....|....*....|....*..
gi 1057117146 153 VIDALIPIGRGQRELILGDPATGKTAL 179
Cdd:COG1158 114 VIDLVAPIGKGQRGLIVAPPKAGKTTL 140
|
|
| |
