|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-502 |
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: 1033.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 1 MSIKAEEISSLIKQQLEHYDDKLDINEVGVVTYIGDGIARAHGLNNVLANELLEFDNGSYGIAQNLEANDVGIIILGNFD 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 81 NIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIG 160
Cdd:COG0056 81 GIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 161 RGQRELIIGDRKTGKTSLAIDTILNQKGQDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPY 240
Cdd:COG0056 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 241 AGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDELGGGSMTALPFIQ 320
Cdd:COG0056 241 AGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 321 TEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFGS 400
Cdd:COG0056 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 401 DLDQATQAKLNRGRRVVEVLKQPLHDPIPVEKQVLILYALTHGYLDSIPVEDIARFEKEMYDNFDSSHADLLKQIRETGE 480
Cdd:COG0056 401 DLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDLLKEIRETGK 480
|
490 500
....*....|....*....|....
gi 2469845588 481 LPDE--KELQAAISKFADSFSPSN 502
Cdd:COG0056 481 LDDEieEKLKAAIEEFKKTFAASA 504
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-500 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1030.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 1 MSIKAEEISSLIKQQLEHYDDKLDINEVGVVTYIGDGIARAHGLNNVLANELLEFDNGSYGIAQNLEANDVGIIILGNFD 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 81 NIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIG 160
Cdd:PRK09281 81 DIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 161 RGQRELIIGDRKTGKTSLAIDTILNQKGQDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPY 240
Cdd:PRK09281 161 RGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 241 AGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDELGGGSMTALPFIQ 320
Cdd:PRK09281 241 AGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 321 TEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFGS 400
Cdd:PRK09281 321 TQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 401 DLDQATQAKLNRGRRVVEVLKQPLHDPIPVEKQVLILYALTHGYLDSIPVEDIARFEKEMYDNFDSSHADLLKQIRETGE 480
Cdd:PRK09281 401 DLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADLLEEIRETKD 480
|
490 500
....*....|....*....|..
gi 2469845588 481 LPDE--KELQAAISKFADSFSP 500
Cdd:PRK09281 481 LSDEieAKLKAAIEEFKKTFAA 502
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
2-500 |
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: 866.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 2 SIKAEEISSLIKQQLEHYDDKLDINEVGVVTYIGDGIARAHGLNNVLANELLEFDNGSYGIAQNLEANDVGIIILGNFDN 81
Cdd:TIGR00962 1 QLKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 82 IREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGR 161
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 162 GQRELIIGDRKTGKTSLAIDTILNQKGQDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYA 241
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 242 GTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDELGGGSMTALPFIQT 321
Cdd:TIGR00962 241 GCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 322 EAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFGSD 401
Cdd:TIGR00962 321 QAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 402 LDQATQAKLNRGRRVVEVLKQPLHDPIPVEKQVLILYALTHGYLDSIPVEDIARFEKEMYDNFDSSHADLLKQIRETGEL 481
Cdd:TIGR00962 401 LDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILEEINTTKKL 480
|
490 500
....*....|....*....|.
gi 2469845588 482 PDEKE--LQAAISKFADSFSP 500
Cdd:TIGR00962 481 TEELEakLKEALKNFKKTFAW 501
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-500 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 792.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 1 MSIKAEEISSLIKQQLEHYDDKLDINEVGVVTYIGDGIARAHGLNNVLANELLEFDNGSYGIAQNLEANDVGIIILGNFD 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 81 NIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIG 160
Cdd:PRK13343 81 DILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 161 RGQRELIIGDRKTGKTSLAIDTILNQKGQDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPY 240
Cdd:PRK13343 161 RGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 241 AGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDELGGGSMTALPFIQ 320
Cdd:PRK13343 241 AGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 321 TEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFGS 400
Cdd:PRK13343 321 TLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 401 DLDQATQAKLNRGRRVVEVLKQPLHDPIPVEKQVLILYALTHGYLDSIPVEDIARFEKEMYDNFDSSHADLLKQIRETGE 480
Cdd:PRK13343 401 LLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAALSLALESPRE 480
|
490 500
....*....|....*....|..
gi 2469845588 481 LPDE--KELQAAISKFADSFSP 500
Cdd:PRK13343 481 LDEAwlAALEEILREAGERFAA 502
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
25-503 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 745.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 25 INEVGVVTYIGDGIARAHGLNNVLANELLEFDNGSYGIAQNLEANDVGIIILGNFDNIREGDQVKRTGQIMRVPVGDALI 104
Cdd:CHL00059 4 IVNTGTVLQVGDGIARIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 105 GRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLAIDTIL 184
Cdd:CHL00059 84 GRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 185 NQKGQDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFDDLS 264
Cdd:CHL00059 164 NQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 265 KQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDELGGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFL 344
Cdd:CHL00059 244 KQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 345 QSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFGSDLDQATQAKLNRGRRVVEVLKQPL 424
Cdd:CHL00059 324 SADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLARGQRLRELLKQSQ 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 425 HDPIPVEKQVLILYALTHGYLDSIPVEDIARFEKEMYDNFDSSHADLLKQIRETGELPDEKE--LQAAISKFADSFSPSN 502
Cdd:CHL00059 404 SAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEalLKEAIQEQLELFLLQE 483
|
.
gi 2469845588 503 K 503
Cdd:CHL00059 484 Q 484
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-367 |
0e+00 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 555.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 94 IMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKT 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 174 GKTSLAIDTILNQKGQDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNG 253
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 254 KDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDELGGGSMTALPFIQTEAGDISAYIPTN 333
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 2469845588 334 VISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVG 367
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
61-457 |
9.44e-117 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 355.50 E-value: 9.44e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 61 GIAQNLEAND-VGIIILGNFDNIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQ--PVDGLGE----IKTDKTR-PIESN 132
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHevPVGLLTRsralLESEQTLgKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 133 APGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLAIDTILNQ--------KGQDVICIYVFIGQKEST 204
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCSN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 205 VRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGRE 284
Cdd:PTZ00185 240 VARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGRE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 285 AYPGDVFYLHSRLLERSAKLSDELGGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVS 364
Cdd:PTZ00185 320 AYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVS 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 365 RVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFGSdldQATQAKLNRGRRVVEVLKQplHDPIPVEKQVLILYALTHGY 444
Cdd:PTZ00185 400 RVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGS---QVQTVPMIRGARFVALFNQ--KNPSFFMNALVSLYACLNGY 474
|
410
....*....|...
gi 2469845588 445 LDSIPVEDIARFE 457
Cdd:PTZ00185 475 LDDVKVNYAKLYE 487
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-364 |
1.66e-108 |
|
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: 321.23 E-value: 1.66e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 149 GIKAIDALVPIGRGQRELIIGDRKTGKTSLAiDTILNQKGQDViCIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGP 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASADV-VVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 229 SEPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDEl 308
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKGK- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2469845588 309 gGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVS 364
Cdd:pfam00006 158 -GGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
128-423 |
1.44e-104 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 321.92 E-value: 1.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 128 PIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLAIDTILNQKGQDVICIYVFIGQKESTVRT 207
Cdd:PRK07165 109 SIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 208 EVETLKRFGAMDYTIVVEAgPSEPAPMLYIAPYAGTAMGEEFMYNgKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYP 287
Cdd:PRK07165 189 IYETLKEHDALKNTIIIDA-PSTSPYEQYLAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 288 GDVFYLHSRLLERSAKLsdeLGGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVG 367
Cdd:PRK07165 267 GDMFFAHSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTG 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2469845588 368 GSAQIKAMKKVAGTLRTDLAAFHELESFAQFGSDLDQATQAKLNRGRRVVEVLKQP 423
Cdd:PRK07165 344 SSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQK 399
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
96-366 |
4.90e-102 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 307.07 E-value: 4.90e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 96 RVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGK 175
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 176 TSLAIDTILNQKGQDV-ICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGK 254
Cdd:cd19476 81 TVLAMQLARNQAKAHAgVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 255 DVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDelGGGSMTALPFIQTEAGDISAYIPTNV 334
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 2469845588 335 ISITDGQIFLQSDLFFAGTRPAIDAGNSVSRV 366
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
375-498 |
9.55e-66 |
|
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: 208.37 E-value: 9.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 375 MKKVAGTLRTDLAAFHELESFAQFGSDLDQATQAKLNRGRRVVEVLKQPLHDPIPVEKQVLILYALTHGYLDSIPVEDIA 454
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2469845588 455 RFEKEMYDNFDSSHADLLKQIRETGEL--PDEKELQAAISKFADSF 498
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLsdELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
371-494 |
1.51e-64 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 204.98 E-value: 1.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 371 QIKAMKKVAGTLRTDLAAFHELESFAQFGSDLDQATQAKLNRGRRVVEVLKQPLHDPIPVEKQVLILYALTHGYLDSIPV 450
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2469845588 451 EDIARFEKEMYDNFDSSHADLLKQIRETGELPDE--KELQAAISKF 494
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDEleEKLKEAIEEF 126
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-366 |
1.32e-56 |
|
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: 189.31 E-value: 1.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 96 RVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGK 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 176 TSLaIDTILNQKGQDVICIyVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKD 255
Cdd:cd01136 81 STL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 256 VLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDelggGSMTALPFIQTEAGDISAYIPTNVI 335
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 2469845588 336 SITDGQIFLQSDLFFAGTRPAIDAGNSVSRV 366
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
76-431 |
7.16e-52 |
|
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: 181.77 E-value: 7.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 76 LGNFDNIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDA 155
Cdd:COG1157 71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 156 LVPIGRGQReliIGdr---ktGKTSLaIDTILNQKGQDVICIyVFIGQKEstvRtEV----------ETLKRfgamdyTI 222
Cdd:COG1157 151 LLTVGRGQR---IGifagsgvGKSTL-LGMIARNTEADVNVI-ALIGERG---R-EVrefieddlgeEGLAR------SV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 223 VVEAgPS-EPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERS 301
Cdd:COG1157 216 VVVA-TSdEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 302 AKlsdeLGGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGT 381
Cdd:COG1157 295 GN----GGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARR 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2469845588 382 LRTDLAAFHELESF----A-QFGSD--LDQAtqakLNRGRRVVEVLKQPLHDPIPVE 431
Cdd:COG1157 371 LRRLLARYEENEDLirigAyQPGSDpeLDEA----IALIPAIEAFLRQGMDERVSFE 423
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-440 |
1.01e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 176.54 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 29 GVVTYIGDGIARAhGLNNVLANELLEFDNgsygiaQNLEANDVGI----IILGNFDN---IREGDQVKRTGQIMRVPVGD 101
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEP------QGMLAEVVSIeqemALLSPFASsdgLRCGQWVTPLGHMHQVQVGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 102 ALIGRVVNPLGQPVDGlGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLaID 181
Cdd:PRK06820 104 DLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 182 TILNQKGQDVIcIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFD 261
Cdd:PRK06820 182 MLCADSAADVM-VLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 262 DLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKlSDElggGSMTALPFIQTEAGDISAYIPTNVISITDGQ 341
Cdd:PRK06820 261 SLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLLDGH 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 342 IFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFG---SDLDQATQAKLNRGRRVVE 418
Cdd:PRK06820 337 IVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGeyqAGEDLQADEALQRYPAICA 416
|
410 420
....*....|....*....|..
gi 2469845588 419 VLKQPLHDPIPVEKQVLILYAL 440
Cdd:PRK06820 417 FLQQDHSETAHLETTLEHLAQV 438
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
76-441 |
3.83e-49 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 174.94 E-value: 3.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 76 LGNFDNIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDA 155
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 156 LVPIGRGQRELIIGDRKTGKTSLAIDTIlnqKGQDV-ICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPM 234
Cdd:PRK06936 156 LLTCGEGQRMGIFAAAGGGKSTLLASLI---RSAEVdVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSME 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 235 LYIAPYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERsAKLSDElggGSMT 314
Cdd:PRK06936 233 RAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMER-AGQSDK---GSIT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 315 ALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELES 394
Cdd:PRK06936 309 ALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVEL 388
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2469845588 395 FAQFGS---DLDQATQAKLNRGRRVVEVLKQPLHDPIPVEKQVLILYALT 441
Cdd:PRK06936 389 LLQIGEyqkGQDKEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETLT 438
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
74-443 |
2.49e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 172.60 E-value: 2.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 74 IILGNFDNIRE---GDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGI 150
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 151 KAIDALVPIGRGQRELIIGDRKTGKTSLaIDTILNQKGQDVICIyVFIGQKESTVRTEVET------LKRfgamdyTIVV 224
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADLNVI-ALIGERGREVREFIERdlgpegLKR------SIVV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 225 EAGPSEPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAkl 304
Cdd:PRK07721 219 VATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG-- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 305 SDELggGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRT 384
Cdd:PRK07721 297 TNAS--GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRE 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2469845588 385 DLAAFHELESFAQFGS-------DLDQATQAKlnrgRRVVEVLKQPLHDPIPVEKQVLILYALTHG 443
Cdd:PRK07721 375 LLSTYQNSEDLINIGAykrgssrEIDEAIQFY----PQIISFLKQGTDEKATFEESIQALLSLFGK 436
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
30-441 |
2.45e-47 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 169.95 E-value: 2.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 30 VVTYIGDGIaRAHGLNNVLAnELLEFDNGSYGIAQNLE----ANDVGIII-LGNFDNIREGDQVKRTGQIMRVPVGDALI 104
Cdd:PRK09099 28 VVEVIGTLL-RVSGLDVTLG-ELCELRQRDGTLLQRAEvvgfSRDVALLSpFGELGGLSRGTRVIGLGRPLSVPVGPALL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 105 GRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLAidTIL 184
Cdd:PRK09099 106 GRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLM--GMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 185 NQKGQDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFDDLS 264
Cdd:PRK09099 184 ARGTQCDVNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 265 KQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERsAKLSDElggGSMTALPFIQTEAGDISAYIPTNVISITDGQIFL 344
Cdd:PRK09099 264 RFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER-AGMGET---GSITALYTVLAEDESGSDPIAEEVRGILDGHMIL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 345 QSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFG---SDLDQATQAKLNRGRRVVEVLK 421
Cdd:PRK09099 340 SREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGeyrAGSDPVADEAIAKIDAIRDFLS 419
|
410 420
....*....|....*....|
gi 2469845588 422 QPLHDPIPVEKQVLILYALT 441
Cdd:PRK09099 420 QRTDEYSDPDATLAALAELS 439
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
88-399 |
1.44e-43 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 159.39 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 88 VKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKT----RPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQ 163
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGPiseeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 164 RELIIGDRKTGKTSLaIDTILNQKGQDViciYV--FIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYA 241
Cdd:PRK08149 153 RMGIFASAGCGKTSL-MNMLIEHSEADV---FVigLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 242 GTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDelggGSMTALPFIQT 321
Cdd:PRK08149 229 ATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA----GSITAFYTVLL 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2469845588 322 EAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFG 399
Cdd:PRK08149 305 ESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLG 382
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
16-438 |
3.98e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 158.31 E-value: 3.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 16 LEHYDDKLD----INEVGVVTYIGDGIARAHGLNNVLAN--ELLEFDNGSYGIAQNLEANDVGIII--LGNFDNIREGDQ 87
Cdd:PRK08472 3 LESLKNKLQkfnlSPRFGSITKISPTIIEADGLNPSVGDivKIESSDNGKECLGMVVVIEKEQFGIspFSFIEGFKIGDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 88 VKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELI 167
Cdd:PRK08472 83 VFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 168 IGDRKTGKTSLAIDTILNQKGQdvICIYVFIGQKESTVRTEVE-TLKrfGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMG 246
Cdd:PRK08472 163 FAGSGVGKSTLMGMIVKGCLAP--IKVVALIGERGREIPEFIEkNLG--GDLENTVIVVATSDDSPLMRKYGAFCAMSVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 247 EEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKlsdELGGGSMTALPFIQTEAGDI 326
Cdd:PRK08472 239 EYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 327 SAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFGS------ 400
Cdd:PRK08472 316 SDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRLYSLLKENEVLIRIGAyqkgnd 395
|
410 420 430
....*....|....*....|....*....|....*....
gi 2469845588 401 -DLDQAtqakLNRGRRVVEVLKQPLHDPIPVEKQVLILY 438
Cdd:PRK08472 396 kELDEA----ISKKEFMEQFLKQNPNELFPFEQTFEQLE 430
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
85-399 |
1.93e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 148.18 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 85 GDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLgEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQR 164
Cdd:PRK07594 79 GQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 165 ELIIGDRKTGKTSLaIDTILNQKGQDViCIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTA 244
Cdd:PRK07594 158 VGIFSAPGVGKSTL-LAMLCNAPDADS-NVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 245 MGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAklsdeLGG-GSMTALPFIQTEA 323
Cdd:PRK07594 236 IAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEG 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2469845588 324 GDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFG 399
Cdd:PRK07594 311 DDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIG 386
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
85-440 |
1.53e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 143.30 E-value: 1.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 85 GDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQR 164
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 165 ELIIGDRKTGKtSLAIDTILNQKGQDVICIYVfIGQKESTVRTEVETL------KRfgamdytIVVEAGPSEPAPMLYI- 237
Cdd:PRK08972 165 MGLFAGSGVGK-SVLLGMMTRGTTADVIVVGL-VGERGREVKEFIEEIlgeegrAR-------SVVVAAPADTSPLMRLk 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 238 APYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDelGGGSMTALP 317
Cdd:PRK08972 236 GCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 318 FIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVG----GSAQIKAMKKVAGTLRT-----DLAA 388
Cdd:PRK08972 314 TVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRVKQVYSLyqqnrDLIS 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2469845588 389 fheLESFAQfGSD--LDQATQAKlnrgRRVVEVLKQPLHDPIPVEKQVLILYAL 440
Cdd:PRK08972 394 ---IGAYKQ-GSDprIDNAIRLQ----PAMNAFLQQTMKEAVPYDMSVNMLKQL 439
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
41-440 |
3.27e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 139.48 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 41 AHGLNNVLANELLEFDNGSYGIAQnLEANDVG-------IIILGNFDNIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQ 113
Cdd:PRK05688 41 AEGLRAAVGSRCLVINDDSYHPVQ-VEAEVMGfsgdkvfLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 114 PVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKtSLAIDTILNQKGQDVIC 193
Cdd:PRK05688 120 ALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGK-SVLLGMMTRFTEADIIV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 194 IYVfIGQKESTVRTEVETLKRFGAMDYTIVVeAGPSEPAPM--LYIAPYAgTAMGEEFMYNGKDVLVVFDDLSKQAVAYR 271
Cdd:PRK05688 199 VGL-IGERGREVKEFIEHILGEEGLKRSVVV-ASPADDAPLmrLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 272 ELSLLLRRPPGREAYPGDVFYLHSRLLERSAklSDELGGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFA 351
Cdd:PRK05688 276 EIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 352 GTRPAIDAGNSVSRVggSAQIKAMKKVAGTLRtdlaaFHELESFAQFGSDL----------DQATQAKLNRGRRVVEVLK 421
Cdd:PRK05688 354 GHYPAIDIEASISRV--MPQVVDPEHLRRAQR-----FKQLWSRYQQSRDLisvgayvaggDPETDLAIARFPHLVQFLR 426
|
410
....*....|....*....
gi 2469845588 422 QPLHDPIPVEKQVLILYAL 440
Cdd:PRK05688 427 QGLRENVSLAQSREQLAAI 445
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
16-427 |
7.19e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 138.59 E-value: 7.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 16 LEHY-DDKLDINEVGVVTYIGDGIARAHGLNN-VLANELLEF--DNGSYgIAQNLEANDVGIII--LGNFDNIREGDQVK 89
Cdd:PRK06002 14 VERYaAPEPLVRIGGTVSEVTASHYRVRGLSRfVRLGDFVAIraDGGTH-LGEVVRVDPDGVTVkpFEPRIEIGLGDAVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 90 RTGQiMRVPVGDALIGRVVNPLGQPVDGLGEIKT-DKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELII 168
Cdd:PRK06002 93 RKGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 169 GDRKTGKTSL--------AIDTIlnqkgqdVICIyvfIGQKESTVRTEVE-TLKrfGAMDYTIVVEAGPSEPAPMLYIAP 239
Cdd:PRK06002 172 AGSGVGKSTLlamlaradAFDTV-------VIAL---VGERGREVREFLEdTLA--DNLKKAVAVVATSDESPMMRRLAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 240 YAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDelGGGSMTALPFI 319
Cdd:PRK06002 240 LTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 320 QTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHE-----LES 394
Cdd:PRK06002 318 LVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdlrLIG 397
|
410 420 430
....*....|....*....|....*....|....*
gi 2469845588 395 FAQFGSD--LDQATQaklnRGRRVVEVLKQPLHDP 427
Cdd:PRK06002 398 GYRAGSDpdLDQAVD----LVPRIYEALRQSPGDP 428
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
90-429 |
7.65e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 138.10 E-value: 7.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 90 RTGQIMrvpVGDALIGRVVNPLGQPVDGLGEIKTDKtrPIESNAPGV--MQRQSVNQPLQTGIKAIDALVPIGRGQRELI 167
Cdd:PRK07196 86 QDGELL---IGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 168 IGDRKTGKtSLAIDTILNQKGQDVICIYVfIGQKESTVRTEVETLKRFGAMDYTIVVeAGPSEPAPMLYI-APYAGTAMG 246
Cdd:PRK07196 161 MAGSGVGK-SVLLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVV-AAPADESPLMRIkATELCHAIA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 247 EEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAklsDELGGGSMTALPFIQTEAGDI 326
Cdd:PRK07196 238 TYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQ 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 327 SAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSR----VGGSAQIKAMKKVAGTLrTDLAAFHELESFAQFGSDL 402
Cdd:PRK07196 315 QDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQCY-ADYMAIKPLIPLGGYVAGA 393
|
330 340
....*....|....*....|....*..
gi 2469845588 403 DQATQAKLNRGRRVVEVLKQPLHDPIP 429
Cdd:PRK07196 394 DPMADQAVHYYPAITQFLRQEVGHPAL 420
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
96-408 |
9.41e-35 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 135.68 E-value: 9.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 96 RVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGK 175
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 176 tSLAIDTILNQKGQDVICIYVfIGQKESTVRTEVETLKRFGAMDYTIVVeAGPSEPAPMLYI--APYAgTAMGEEFMYNG 253
Cdd:PRK07960 189 -SVLLGMMARYTQADVIVVGL-IGERGREVKDFIENILGAEGRARSVVI-AAPADVSPLLRMqgAAYA-TRIAEDFRDRG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 254 KDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLSDelGGGSMTALPFIQTEAGDISAYIPTN 333
Cdd:PRK07960 265 QHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 334 VISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGS-------AQIKAMKK-----------------VAGT---LRTDL 386
Cdd:PRK07960 343 ARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQllssfqrnrdlvsvgayAKGSdpmLDKAI 422
|
330 340
....*....|....*....|....*.
gi 2469845588 387 AAFHELESFAQFG----SDLDQATQA 408
Cdd:PRK07960 423 ALWPQLEAFLQQGiferADWEDSLQA 448
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-380 |
1.47e-34 |
|
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: 131.19 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 94 IMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKT 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 174 GKTSLAIDTILN----QKGQDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEF 249
Cdd:cd01135 81 PHNELAAQIARQagvvGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 250 MY-NGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERSAKLSDElgGGSMTALPFIQTEAGD 325
Cdd:cd01135 161 AYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPNDD 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2469845588 326 ISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVggsaqikaMKKVAG 380
Cdd:cd01135 236 ITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRL--------MKSGIG 282
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
97-428 |
1.72e-32 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 128.87 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 97 VPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKT 176
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 177 SLaIDTIlnQKG-QDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKD 255
Cdd:PRK05922 172 SL-LSTI--AKGsKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 256 VLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKlSDElggGSMTALPFIQTEAG--DI-SAYIPt 332
Cdd:PRK05922 249 VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN-NDK---GSITALYAILHYPNhpDIfTDYLK- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 333 nviSITDGQIFL--QSDLFFAgtrPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELESFAQFGSdLDQATQAKL 410
Cdd:PRK05922 324 ---SLLDGHFFLtpQGKALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGA-YVPGQDAHL 396
|
330
....*....|....*...
gi 2469845588 411 NRGRRVVEVLKQPLHDPI 428
Cdd:PRK05922 397 DRAVKLLPSIKQFLSQPL 414
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
77-399 |
7.83e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 127.02 E-value: 7.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 77 GNFDNIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKT-RPIESNAPGVMQRQSVNQPLQTGIKAIDA 155
Cdd:PRK08927 72 GPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRARVGEPLDLGVRALNT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 156 LVPIGRGQRELIIGDRKTGKTSLaIDTILNQKGQDVICIYVfIGQKESTVRTEV------ETLKRfgamdyTIVVEAGPS 229
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGKSVL-LSMLARNADADVSVIGL-IGERGREVQEFLqddlgpEGLAR------SVVVVATSD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 230 EPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAklSDELG 309
Cdd:PRK08927 224 EPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 310 GGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAF 389
Cdd:PRK08927 302 EGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATY 381
|
330
....*....|
gi 2469845588 390 HELESFAQFG 399
Cdd:PRK08927 382 ADMEELIRLG 391
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
62-425 |
8.53e-32 |
|
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: 127.14 E-value: 8.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 62 IAQNLEANDVGIIILGNFDNIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQS 141
Cdd:TIGR01039 43 VAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQST 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 142 VNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLaIDTILNQKGQDVICIYVFIGQKESTVRTE---VEtLKRFGAM 218
Cdd:TIGR01039 123 KVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVL-IQELINNIAKEHGGYSVFAGVGERTREGNdlyHE-MKESGVI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 219 DYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFM-YNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRL 297
Cdd:TIGR01039 201 DKTALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGEL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 298 LER--SAKlsdelgGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSR-----VGGSA 370
Cdd:TIGR01039 281 QERitSTK------TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRlldpsVVGEE 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2469845588 371 QIKAMKKVAGTLRTdlaaFHELES-FAQFGSD-LDQATQAKLNRGRRVVEVLKQPLH 425
Cdd:TIGR01039 355 HYDVARGVQQILQR----YKELQDiIAILGMDeLSEEDKLTVERARRIQRFLSQPFF 407
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
27-93 |
2.60e-29 |
|
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: 109.47 E-value: 2.60e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2469845588 27 EVGVVTYIGDGIARAHGLNNVLANELLEFDNGSYGIAQNLEANDVGIIILGNFDNIREGDQVKRTGQ 93
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
43-365 |
2.31e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 108.37 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 43 GLNNVLANELLEF--DNGSYGIAQNLEAND--VGIIILGNFDNI-REGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDG 117
Cdd:PRK04196 19 GVEGVAYGEIVEIelPNGEKRRGQVLEVSEdkAVVQVFEGTTGLdLKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 118 LGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLAIDtILNQ---KGQDVICI 194
Cdd:PRK04196 99 GPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ-IARQakvLGEEENFA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 195 YVF--IGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYN-GKDVLVVFDDLSKQAVAYR 271
Cdd:PRK04196 178 VVFaaMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEkGMHVLVILTDMTNYCEALR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 272 ELSLLLRRPPGREAYPGdvfYLHSRL---LERSAKLSDElgGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDL 348
Cdd:PRK04196 258 EISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSREL 332
|
330
....*....|....*..
gi 2469845588 349 FFAGTRPAIDAGNSVSR 365
Cdd:PRK04196 333 HRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
80-434 |
1.40e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 105.83 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 80 DNIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPI 159
Cdd:PRK06793 74 EKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 160 GRGQRELIIGDRKTGKTSLAIDTILNQKGQdvICIYVFIGQKESTVRTEVEtlKRFG--AMDYTIVVEAGPSEPAPMLYI 237
Cdd:PRK06793 154 GIGQKIGIFAGSGVGKSTLLGMIAKNAKAD--INVISLVGERGREVKDFIR--KELGeeGMRKSVVVVATSDESHLMQLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 238 APYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPgreaYPGDVFYLHS---RLLERSAKLSDelggGSMT 314
Cdd:PRK06793 230 AAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSIT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 315 ALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAMKKVAGTLRTDLAAFHELES 394
Cdd:PRK06793 302 GIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENEL 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2469845588 395 FAQFGSDLDQATQAKL----NRGRRVVEVLKQPLHDPIPVEKQV 434
Cdd:PRK06793 382 YFKLGTIQENAENAYIfeckNKVEGINTFLKQGRSDSFQFDDIV 425
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
56-365 |
1.94e-24 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 105.50 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 56 DNGSYGIAQNLEANDVGIIILGNFDNIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDktrPIESNAPG 135
Cdd:PRK02118 35 DGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGE---PIEIGGPS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 136 V--MQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLAIdTILNQKGQDVIcIYVFIGQKESTVRTEVETLK 213
Cdd:PRK02118 112 VnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-RIALQAEADII-ILGGMGLTFDDYLFFKDTFE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 214 RFGAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNG-KDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDvfy 292
Cdd:PRK02118 190 NAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGS--- 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2469845588 293 LHSRLLERSAKLSDELGGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDlffagtrpAIDAGNSVSR 365
Cdd:PRK02118 267 LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG--------RIDPFGSLSR 331
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-366 |
7.93e-24 |
|
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: 100.76 E-value: 7.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 96 RVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGK 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 176 TSLAIDTILN-QKGQDVICIYVFIGQ------------KESTVRTEVETLKR---FGAMDytivveagpsEPAPMLYIAP 239
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGErtregndlyhemKESGVINLDGLSKValvYGQMN----------EPPGARARVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 240 YAGTAMGEEFM-YNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLER--SAKlsdelgGGSMTAL 316
Cdd:cd01133 151 LTGLTMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERitSTK------KGSITSV 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2469845588 317 PFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRV 366
Cdd:cd01133 225 QAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
91-375 |
6.41e-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: 6.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 91 TGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGD 170
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 171 -------------RKTGKTSLAIDTILNQKGQDVICIYVFIGQKESTVRTEVETLKRFGAMDYTIVVEAGPSEPAPMLYI 237
Cdd:TIGR01040 150 aglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 238 APYAGTAMGEEFMYN-GKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERSAKLsdELGGGSMTAL 316
Cdd:TIGR01040 230 TPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV--EGRNGSITQI 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2469845588 317 PFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQIKAM 375
Cdd:TIGR01040 308 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
64-423 |
4.30e-18 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 87.02 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 64 QNLEANDVGIIILGNFDNIREGDQVKRTGQIMRVPVGDALIGRVVNPLGQPVDGLGEIKTDKTRPIESNAPGVMQRQSVN 143
Cdd:CHL00060 63 QLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 144 QPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLAIDTILN----QKGqdvicIYVFIG--------------QKESTV 205
Cdd:CHL00060 143 SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakaHGG-----VSVFGGvgertregndlymeMKESGV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 206 RTEVETLKRFGAMDYTIVVEAgpsePAPMLYIAPYAGTaMGEEFM-YNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGRE 284
Cdd:CHL00060 218 INEQNIAESKVALVYGQMNEP----PGARMRVGLTALT-MAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 285 AYPGDVFYLHSRLLERSAKLSDelggGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVS 364
Cdd:CHL00060 293 GYQPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2469845588 365 -----RVGGSAQIKAMKKVAGTLR-----TDLAAFHELESFaqfgSDLDQATQAklnRGRRVVEVLKQP 423
Cdd:CHL00060 369 tmlqpRIVGEEHYETAQRVKQTLQrykelQDIIAILGLDEL----SEEDRLTVA---RARKIERFLSQP 430
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
27-92 |
3.62e-16 |
|
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: 72.96 E-value: 3.62e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2469845588 27 EVGVVTYIGDGIARAHGLNNVLANELLEFDNGSYGIAQNLEANDVGIIILGNFDNIREGDQVKRTG 92
Cdd:pfam02874 4 VIGPVVDVEFGIGRLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
136-365 |
4.85e-12 |
|
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: 66.44 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 136 VMQRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKTSLaIDTILNQKGQDVIcIYVFIGQKESTVrteVETLKRF 215
Cdd:cd01134 50 VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVI-SQSLSKWSNSDVV-IYVGCGERGNEM---AEVLEEF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 216 ----------GAMDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREA 285
Cdd:cd01134 125 pelkdpitgeSLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 286 YPGdvfYLHSRL---LERSAK---LSDELGGGSMTALPFIQTEAGDISAYIPTNVISITdgQIF--LQSDLFFAGTRPAI 357
Cdd:cd01134 205 YPA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSI 279
|
....*...
gi 2469845588 358 DAGNSVSR 365
Cdd:cd01134 280 NWLISYSK 287
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-441 |
9.44e-12 |
|
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: 60.54 E-value: 9.44e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2469845588 375 MKKVAGTLRTDLAAFHELESFAQFGSD--LDQATQAKLNRGRRVVEVLKQPLHDPIPVEKQVLILYALT 441
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
218-456 |
7.42e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 58.49 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 218 MDYTIVVEAGPSEPAPMLYIAPYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYRELSLLLRRPPGREAYPGdvfYLHSRL 297
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKL 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 298 LE------RSAKLSDELGGGSMTALPFIQTEAGDISAYIPTNVISITDGQIFLQSDLFFAGTRPAIDAGNSVSRVGGSAQ 371
Cdd:PRK14698 794 AEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAVK 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 372 ----------IKAMKKVAGTLRTDLAAFHELESFAqfGSD-LDQATQAKLNRGRRVVE-VLKQPLHDPI----PVEKQVL 435
Cdd:PRK14698 874 dwwhknvdpeWKAMRDKAMELLQKEAELQEIVRIV--GPDaLPERERAILLVARMLREdYLQQDAFDEVdtycPPEKQVT 951
|
250 260
....*....|....*....|....*...
gi 2469845588 436 ILYALTHGY---LDSI----PVEDIARF 456
Cdd:PRK14698 952 MMRVLLNFYdktMDAIsrgvPLEEIAKL 979
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
138-299 |
1.31e-05 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 47.85 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 138 QRQSVNQPLQTGIKAIDALVPIGRGQRELIIGDRKTGKT----SLAidtilnqKGQDV-ICIYVFIGQKESTVrteVETL 212
Cdd:PRK04192 203 EKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTvtqhQLA-------KWADAdIVIYVGCGERGNEM---TEVL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2469845588 213 KRF--------GA--MDYTIVV-----------EAgpsepapmlyiAPYAGTAMGEEFMYNGKDVLVVFDDLSKQAVAYR 271
Cdd:PRK04192 273 EEFpelidpktGRplMERTVLIantsnmpvaarEA-----------SIYTGITIAEYYRDMGYDVLLMADSTSRWAEALR 341
|
170 180
....*....|....*....|....*...
gi 2469845588 272 ELSLLLRRPPGREAYPGdvfYLHSRLLE 299
Cdd:PRK04192 342 EISGRLEEMPGEEGYPA---YLASRLAE 366
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
29-93 |
2.47e-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: 36.52 E-value: 2.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2469845588 29 GVVTYIGDGIARAHGLNNVLANELLEF-----DNGSYGIAQ--NLEANDVGIIILGNFDNIREGDQVKRTGQ 93
Cdd:cd01426 2 GRVIRVNGPLVEAELEGEVAIGEVCEIergdgNNETVLKAEviGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
151-178 |
2.64e-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: 39.50 E-value: 2.64e-03
10 20
....*....|....*....|....*...
gi 2469845588 151 KAIDALVPIGRGQRELIIGDRKTGKTSL 178
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTL 32
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
153-178 |
2.66e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 40.12 E-value: 2.66e-03
10 20
....*....|....*....|....*.
gi 2469845588 153 IDALVPIGRGQRELIIGDRKTGKTSL 178
Cdd:PRK09376 160 IDLIAPIGKGQRGLIVAPPKAGKTVL 185
|
|
| |
