|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-344 |
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: 738.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 1 AGEMVEFASGVKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRR 80
Cdd:COG0056 49 AGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 81 VEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNsratsesetLYCVYVAIG 160
Cdd:COG0056 129 VERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKD---------VICIYVAIG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 161 QKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRR 240
Cdd:COG0056 200 QKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 241 PPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINV 320
Cdd:COG0056 280 PPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINV 359
|
330 340
....*....|....*....|....
gi 302747434 321 GLSVSRVGSAAQLKTMKQVCGSLK 344
Cdd:COG0056 360 GLSVSRVGGAAQIKAMKKVAGTLR 383
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-344 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 738.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 1 AGEMVEFASGVKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRR 80
Cdd:PRK09281 49 AGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 81 VEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNsratsesetLYCVYVAIG 160
Cdd:PRK09281 129 VERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKD---------VICIYVAIG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 161 QKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRR 240
Cdd:PRK09281 200 QKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 241 PPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINV 320
Cdd:PRK09281 280 PPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINV 359
|
330 340
....*....|....*....|....
gi 302747434 321 GLSVSRVGSAAQLKTMKQVCGSLK 344
Cdd:PRK09281 360 GISVSRVGGAAQIKAMKKVAGTLR 383
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
1-344 |
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: 632.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 1 AGEMVEFASGVKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRR 80
Cdd:TIGR00962 48 SGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 81 VEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNsratsesetLYCVYVAIG 160
Cdd:TIGR00962 128 VEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSD---------VYCIYVAIG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 161 QKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRR 240
Cdd:TIGR00962 199 QKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 241 PPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINV 320
Cdd:TIGR00962 279 PPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINV 358
|
330 340
....*....|....*....|....
gi 302747434 321 GLSVSRVGSAAQLKTMKQVCGSLK 344
Cdd:TIGR00962 359 GLSVSRVGGAAQIKAMKQVAGSLR 382
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
1-344 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 601.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 1 AGEMVEFASGVKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRR 80
Cdd:CHL00059 28 AGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 81 VEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKqmnsratseSETLYCVYVAIG 160
Cdd:CHL00059 108 IESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQK---------GQNVICVYVAIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 161 QKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRR 240
Cdd:CHL00059 179 QKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 241 PPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINV 320
Cdd:CHL00059 259 PPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINV 338
|
330 340
....*....|....*....|....
gi 302747434 321 GLSVSRVGSAAQLKTMKQVCGSLK 344
Cdd:CHL00059 339 GISVSRVGSAAQIKAMKQVAGKLK 362
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
46-328 |
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: 580.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 46 IVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQT 125
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 126 GKTAIAIDTILNQKQMNsratsesetLYCVYVAIGQKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCA 205
Cdd:cd01132 81 GKTAIAIDTIINQKGKK---------VYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 206 MGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAG 285
Cdd:cd01132 152 MGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 302747434 286 DVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVG 328
Cdd:cd01132 232 DVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-344 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 569.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 1 AGEMVEFASGVKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRR 80
Cdd:PRK13343 49 LDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 81 VEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNsratsesetLYCVYVAIG 160
Cdd:PRK13343 129 LERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSD---------VICVYVAIG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 161 QKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRR 240
Cdd:PRK13343 200 QKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 241 PPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINV 320
Cdd:PRK13343 280 PPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDV 359
|
330 340
....*....|....*....|....
gi 302747434 321 GLSVSRVGSAAQLKTMKQVCGSLK 344
Cdd:PRK13343 360 GLSVSRVGGKAQHPAIRKESGRLR 383
|
|
| alt_F1F0_F1_al |
TIGR03324 |
alternate F1F0 ATPase, F1 subunit alpha; A small number of taxonomically diverse prokaryotic ... |
3-344 |
4.88e-152 |
|
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: 436.89 E-value: 4.88e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 3 EMVEFASGVKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVE 82
Cdd:TIGR03324 51 ELLRFPGGLLGIAFNVDEDEVGVVLLGEYSHLQAGDEVERTGRVMDVPVGDGLLGRVVDPLGRPLDGGGPLASSPRLPIE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 83 VKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNsratsesetLYCVYVAIGQK 162
Cdd:TIGR03324 131 RPAPPIMDRAPVTVPLQTGLKVIDALIPIGRGQRELILGDRQTGKTAIAIDTILNQKGRN---------VLCIYCAIGQR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 163 RSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPP 242
Cdd:TIGR03324 202 ASAVAKVVANLREHGAMDYTIVVVTEGNDPPGLQYIAPYAATSIGEHFMEQGRDVLIVYDDLTQHARAYRELSLLLRRPP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 243 GREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGL 322
Cdd:TIGR03324 282 GREAFPGDIFYVHSRLLERSTHLNEELGGGSLTALPIIETEAQNISAYIPTNLISITDGQIYLSPTLFELGVLPAVDVGK 361
|
330 340
....*....|....*....|..
gi 302747434 323 SVSRVGSAAQLKTMKQVCGSLK 344
Cdd:TIGR03324 362 SVSRVGGKAQLAAYRAVAGDLK 383
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
48-327 |
8.19e-119 |
|
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: 344.05 E-value: 8.19e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 48 DVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGK 127
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 128 TAIAIDTILNQKqmnsratsESETLYCVYVAIGQKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMG 207
Cdd:cd19476 81 TVLAMQLARNQA--------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 208 EYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRsdQTGAGSLTALPVIETQAGDV 287
Cdd:cd19476 153 EYFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKV--KDGGGSITAIPAVSTPGDDL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 302747434 288 SAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:cd19476 231 TDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
13-344 |
1.64e-115 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 346.26 E-value: 1.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 13 GIAFNLENEN-VGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALG--VPID----GRGAL-SDHERRRVEVK 84
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGheVPVGlltrSRALLeSEQTLGKVDAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 85 APGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRATSESETLyCVYVAIGQKRS 164
Cdd:PTZ00185 160 APNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVI-SIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 165 TVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGR 244
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 245 EAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSV 324
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340
....*....|....*....|
gi 302747434 325 SRVGSAAQLKTMKQVCGSLK 344
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLK 418
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
101-325 |
7.50e-114 |
|
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: 328.93 E-value: 7.50e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 101 GLKAVDSLVPIGRGQRELIIGDRQTGKTAIAiDTILNQKQMNsratsesetlYCVYVAIGQKRSTVAQLVQILSEGNALE 180
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD----------VVVYALIGERGREVREFIEELLGSGALK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 181 YSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLE 260
Cdd:pfam00006 70 RTVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302747434 261 RAAKRSDQTgaGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVS 325
Cdd:pfam00006 150 RAGRVKGKG--GSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
84-341 |
6.65e-99 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 301.51 E-value: 6.65e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 84 KAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRatsesetlyCVYVAIGQKR 163
Cdd:PRK07165 113 LAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVK---------CIYVAIGQKR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 164 STVAQLVQILSEGNALEYSILVAATASDPAPlQFLAPYSGCAMGE---YFRDngmhALIIYDDLSKQAVAYRQMSLLLRR 240
Cdd:PRK07165 184 ENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAEnisYNDD----VLIVFDDLTKHANIYREIALLTNK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 241 PPGREAFPGDVFYLHSRLLERAAKRSDQTgagSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINV 320
Cdd:PRK07165 259 PVGKEAFPGDMFFAHSKLLERAGKFKNRK---TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDI 335
|
250 260
....*....|....*....|.
gi 302747434 321 GLSVSRVGSAAQLKTMKQVCG 341
Cdd:PRK07165 336 DLSVSRTGSSVQSKTITKVAG 356
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
49-327 |
9.23e-50 |
|
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: 166.97 E-value: 9.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 49 VPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKT 128
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 129 aiaidTILNQKQMNSRATSEsetlycVYVAIGQKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGE 208
Cdd:cd01136 82 -----TLLGMIARNTDADVN------VIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 209 YFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKrsdqTGAGSLTALPVIETQAGDVS 288
Cdd:cd01136 151 YFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN----GEKGSITAFYTVLVEGDDFN 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 302747434 289 AYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:cd01136 227 DPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
20-327 |
1.79e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 149.87 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 20 NENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQ 99
Cdd:PRK07721 64 DEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPME 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 100 TGLKAVDSLVPIGRGQRELIIGDRQTGKTaiaidTILNqkqMNSRATSESETlycVYVAIGQKRSTVAQLVQ--ILSEGn 177
Cdd:PRK07721 144 VGVRAIDSLLTVGKGQRVGIFAGSGVGKS-----TLMG---MIARNTSADLN---VIALIGERGREVREFIErdLGPEG- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 178 aLEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSR 257
Cdd:PRK07721 212 -LKRSIVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPK 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 258 LLERAAkrsdQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:PRK07721 291 LLERTG----TNASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRV 356
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-327 |
3.85e-41 |
|
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: 149.03 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 28 FGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDS 107
Cdd:COG1157 71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 108 LVPIGRGQReliIGdr---qtGKTaiaidTILNqkqMNSRATSESetlycVYVaIGqkrstvaqLV------------QI 172
Cdd:COG1157 151 LLTVGRGQR---IGifagsgvGKS-----TLLG---MIARNTEAD-----VNV-IA--------LIgergrevrefieDD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 173 L-SEGnaLEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDV 251
Cdd:COG1157 206 LgEEG--LARSVVVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 252 FYLHSRLLERAAKrsdqTGAGSLTAL------------PVIETqagdvsayiptnVISITDGQICLETELFYRGIRPAIN 319
Cdd:COG1157 284 FALLPRLLERAGN----GGKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAID 347
|
....*...
gi 302747434 320 VGLSVSRV 327
Cdd:COG1157 348 VLASISRV 355
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
28-327 |
1.02e-40 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 147.99 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 28 FGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDS 107
Cdd:PRK09099 77 FGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 108 LVPIGRGQRELIIGDRQTGKTaiaidTILNqkqMNSRATSesetlyC---VYVAIGQKRSTVAQLVQILSEGNALEYSIL 184
Cdd:PRK09099 157 LMTLGEGQRMGIFAPAGVGKS-----TLMG---MFARGTQ------CdvnVIALIGERGREVREFIELILGEDGMARSVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 185 VAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAk 264
Cdd:PRK09099 223 VCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG- 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302747434 265 rsdQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:PRK09099 302 ---MGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRV 361
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
40-344 |
2.12e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 144.51 E-value: 2.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 40 VKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELI 119
Cdd:PRK06936 88 VSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 120 IGDRQTGKTaiaidTILnqkqmnSRATSESETLYCVYVAIGQKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLA 199
Cdd:PRK06936 168 FAAAGGGKS-----TLL------ASLIRSAEVDVTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSMERAKA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 200 PYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAkrsdQTGAGSLTALPV 279
Cdd:PRK06936 237 GFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG----QSDKGSITALYT 312
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302747434 280 IETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKTMKQVCGSLK 344
Cdd:PRK06936 313 VLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLR 377
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
9-327 |
4.79e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 143.42 E-value: 4.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 9 SGVKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGrGALSDHERRRVEVKAPGI 88
Cdd:PRK06820 59 QGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPPSP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 89 IERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTaiaidTILnqkqmnSRATSESETLYCVYVAIGQKRSTVAQ 168
Cdd:PRK06820 138 LTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKS-----TLL------GMLCADSAADVMVLALIGERGREVRE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 169 LV-QILSEgNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAF 247
Cdd:PRK06820 207 FLeQVLTP-EARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 248 PGDVFYLHSRLLERAAKrSDQtgaGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:PRK06820 286 PPSVFANLPRLLERTGN-SDR---GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI 361
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
13-327 |
1.82e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 141.75 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 13 GIAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVeVKAP-GIIER 91
Cdd:PRK08472 56 GMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPI-MKAPiAAMKR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 92 KSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTaiaidTILNQKQMNSRATSEsetlycVYVAIGQKRSTVAQLVQ 171
Cdd:PRK08472 135 GLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKS-----TLMGMIVKGCLAPIK------VVALIGERGREIPEFIE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 172 iLSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDV 251
Cdd:PRK08472 204 -KNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSV 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302747434 252 FYLHSRLLERAAKrsdQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:PRK08472 283 LSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRV 355
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
49-339 |
2.10e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 136.37 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 49 VPAGKAMLGRVVDALGVPIDGRGAL-SDHerrRVEVKAPGI--IERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQT 125
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIyTDQ---RASRHSPPInpLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 126 GKTAIAidtilnqkQMNSRATseseTLYCVYVA-IGQKRSTVAQLVQ-ILSEgNALEYSILVAATAsDPAPLQFLapySG 203
Cdd:PRK08972 174 GKSVLL--------GMMTRGT----TADVIVVGlVGERGREVKEFIEeILGE-EGRARSVVVAAPA-DTSPLMRL---KG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 204 C----AMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDqtGAGSLTALPV 279
Cdd:PRK08972 237 CetatTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYT 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302747434 280 IETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVG----SAAQLKTMKQV 339
Cdd:PRK08972 315 VLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSEEHLEAMRRV 378
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
49-326 |
9.63e-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: 125.80 E-value: 9.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 49 VPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDrqtgkT 128
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG-----S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 129 AIAIDTILNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGE 208
Cdd:cd01135 79 GLPHNELAAQIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 209 YFR-DNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGdvfYLHSRL---LERAAKRSDQtgAGSLTALPVIETQA 284
Cdd:cd01135 159 YLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIPILTMPN 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 302747434 285 GDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSR 326
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
29-327 |
3.39e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 124.84 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 29 GSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERrrVEVKAPGI--IERKSVHEPMQTGLKAVD 106
Cdd:PRK05688 83 GSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTInpLNRHPISEPLDVGIRSIN 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 107 SLVPIGRGQRELIIGDRQTGKTAIAidtilnqkQMNSRATsesETLYCVYVAIGQKRSTVAQLV-QILSEgNALEYSILV 185
Cdd:PRK05688 161 GLLTVGRGQRLGLFAGTGVGKSVLL--------GMMTRFT---EADIIVVGLIGERGREVKEFIeHILGE-EGLKRSVVV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 186 AATASDpAPLQFLAPYSGCA-MGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAk 264
Cdd:PRK05688 229 ASPADD-APLMRLRAAMYCTrIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG- 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302747434 265 rSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:PRK05688 307 -NAEPGGGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
28-344 |
1.21e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 123.14 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 28 FGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRgALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDS 107
Cdd:PRK07594 70 FTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 108 LVPIGRGQRELIIGDRQTGKTaiaidTILNqkqMNSRATSESETlycVYVAIGQKRSTVAQLVQILSEGNALEYSILVAA 187
Cdd:PRK07594 149 VATCGEGQRVGIFSAPGVGKS-----TLLA---MLCNAPDADSN---VLVLIGERGREVREFIDFTLSEETRKRCVIVVA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 188 TASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSd 267
Cdd:PRK07594 218 TSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGE- 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302747434 268 qtgAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKTMKQVCGSLK 344
Cdd:PRK07594 297 ---KGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILR 370
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
52-342 |
1.79e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 122.69 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 52 GKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIA 131
Cdd:PRK07196 93 GDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 132 idtilnqkQMNSRATsESETLycVYVAIGQKRSTVAQLVQILSEGNALEYSILVAATAsDPAPLQFLAPYSGC-AMGEYF 210
Cdd:PRK07196 173 --------GMITRYT-QADVV--VVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPA-DESPLMRIKATELChAIATYY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 211 RDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAkrsDQTGAGSLTALPVIETQAGDVSAY 290
Cdd:PRK07196 241 RDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDP 317
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 302747434 291 IPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVgsaaqlktMKQVCGS 342
Cdd:PRK07196 318 IVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRC--------MSQVIGS 361
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
2-336 |
2.00e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 122.80 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 2 GEMVEFASG---VKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAgKAMLGRVVDALGVPIDGRGALSDHER 78
Cdd:PRK06002 50 GDFVAIRADggtHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGPLRIRPD-PSWKGRVINALGEPIDGLGPLAPGTR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 79 RR-VEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTaiaidTILNqkqMNSRAtSESETlycVYV 157
Cdd:PRK06002 129 PMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKS-----TLLA---MLARA-DAFDT---VVI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 158 A-IGQKRSTVAQLvqiLSE--GNALEYSILVAATaSDPAP-LQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQ 233
Cdd:PRK06002 197 AlVGERGREVREF---LEDtlADNLKKAVAVVAT-SDESPmMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAARE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 234 MSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDqtGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRG 313
Cdd:PRK06002 273 VALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQG 350
|
330 340 350
....*....|....*....|....*....|...
gi 302747434 314 IRPAINVGLSVSRVGSAA----------QLKTM 336
Cdd:PRK06002 351 RYPAVDPLASISRLARHAwtpeqrklvsRLKSM 383
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
53-326 |
1.70e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 120.08 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 53 KAMLGRVVDALGVPIDGRGALSDHERRRVeVKA--PGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTai 130
Cdd:PRK08927 96 RAWLGRVVNALGEPIDGKGPLPQGPVPYP-LRAppPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 131 aidTILNqkqMNSRATSESETlycVYVAIGQKRSTVAQLVQ--ILSEGnaLEYSILVAATASDPAPLQFLAPYSGCAMGE 208
Cdd:PRK08927 173 ---VLLS---MLARNADADVS---VIGLIGERGREVQEFLQddLGPEG--LARSVVVVATSDEPALMRRQAAYLTLAIAE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 209 YFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAkrSDQTGAGSLTALPVIETQAGDVS 288
Cdd:PRK08927 242 YFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHN 319
|
250 260 270
....*....|....*....|....*....|....*...
gi 302747434 289 AYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSR 326
Cdd:PRK08927 320 EPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
39-327 |
1.14e-29 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 117.79 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 39 LVKRTGSIVDVPAGKAMLGRVVDALGVpIDGR-----GALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGR 113
Cdd:PRK08149 72 VLKPTGKPLSVWVGEALLGAVLDPTGK-IVERfdappTVGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 114 GQRELIIGDRQTGKTAIaIDTILNQkqmnsratSESEtlycVYVA--IGQKRSTVAQLVQILSEGNALEYSILVAATASD 191
Cdd:PRK08149 151 GQRMGIFASAGCGKTSL-MNMLIEH--------SEAD----VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 192 PAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKrsdqTGA 271
Cdd:PRK08149 218 SSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGA----TLA 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 302747434 272 GSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:PRK08149 294 GSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
2-326 |
3.05e-29 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 116.85 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 2 GEMVEF--ASG--VKGIAFNLENENVGIVVFGSDTAIK-EGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDH 76
Cdd:PRK04196 26 GEIVEIelPNGekRRGQVLEVSEDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 77 ERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIgdrqTGkTAIAIDTILNQKQMNSRATSESETLYCVY 156
Cdd:PRK04196 106 KRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIF----SG-SGLPHNELAAQIARQAKVLGEEENFAVVF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 157 VAIGQKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFR-DNGMHALIIYDDLSKQAVAYRQMS 235
Cdd:PRK04196 181 AAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTNYCEALREIS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 236 LLLRRPPGREAFPGdvfYLHSRL---LERAAKRSDQtgAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYR 312
Cdd:PRK04196 261 AAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYITEGQIVLSRELHRK 335
|
330
....*....|....
gi 302747434 313 GIRPAINVGLSVSR 326
Cdd:PRK04196 336 GIYPPIDVLPSLSR 349
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
18-327 |
2.74e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 111.22 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 18 LENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERrrVEVKAPGI--IERKSVH 95
Cdd:PRK06793 60 IEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQK--IKLDAPPIhaFEREEIT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 96 EPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTaiaidTILNQKQMNSRATSESETLycvyvaIGQKRSTVAQLVQILSE 175
Cdd:PRK06793 138 DVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS-----TLLGMIAKNAKADINVISL------VGERGREVKDFIRKELG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 176 GNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPgreaFPGDVFYLH 255
Cdd:PRK06793 207 EEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLME 282
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302747434 256 S---RLLERAAKrsdqTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:PRK06793 283 SymkKLLERSGK----TQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 353
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
14-327 |
3.14e-27 |
|
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: 111.35 E-value: 3.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 14 IAFNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKS 93
Cdd:TIGR01039 43 VAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQST 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 94 VHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRatsesetlYCVYVAIGQKRSTVAQLVQIL 173
Cdd:TIGR01039 123 KVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGG--------YSVFAGVGERTREGNDLYHEM 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 174 SEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRD-NGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVF 252
Cdd:TIGR01039 195 KESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLA 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302747434 253 YLHSRLLERAAkrsdQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:TIGR01039 275 TEMGELQERIT----STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRL 345
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
49-342 |
1.11e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 109.49 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 49 VPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKT 128
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 129 AIAidtilnqkQMNSRATSESetlYCVYVAIGQKRSTVAQLVQ-IL-SEGNAleYSILVAATAsDPAPLQFL--APYSgC 204
Cdd:PRK07960 190 VLL--------GMMARYTQAD---VIVVGLIGERGREVKDFIEnILgAEGRA--RSVVIAAPA-DVSPLLRMqgAAYA-T 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 205 AMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDqtGAGSLTALPVIETQA 284
Cdd:PRK07960 255 RIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEG 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302747434 285 GDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSA-------AQLKTMKQVCGS 342
Cdd:PRK07960 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQLLSS 397
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
49-333 |
3.75e-25 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 104.99 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 49 VPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKT 128
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 129 AIaIDTIlnqkqmnsraTSESETLYCVYVAIGQKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGE 208
Cdd:PRK05922 172 SL-LSTI----------AKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 209 YFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSdqtgAGSLTALPVIETQAGDVS 288
Cdd:PRK05922 241 YFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND----KGSITALYAILHYPNHPD 316
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 302747434 289 AYIPTnVISITDGQICL---ETELFyrgiRPAINVGLSVSRvgSAAQL 333
Cdd:PRK05922 317 IFTDY-LKSLLDGHFFLtpqGKALA----SPPIDILTSLSR--SARQL 357
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
43-331 |
4.37e-24 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 102.49 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 43 TGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGD 122
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 123 RQTGKTAIAIDTI----LNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQILSEGNALEYSILVAATASDPAPLQFL 198
Cdd:TIGR01040 150 AGLPHNEIAAQICrqagLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERII 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 199 APYSGCAMGEYFR-DNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQtgAGSLTAL 277
Cdd:TIGR01040 230 TPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NGSITQI 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 302747434 278 PVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAA 331
Cdd:TIGR01040 308 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 361
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
1-44 |
3.19e-19 |
|
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: 80.19 E-value: 3.19e-19
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 302747434 1 AGEMVEFASGVKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTG 44
Cdd:cd18116 23 AGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTG 66
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
17-305 |
1.95e-18 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 85.86 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 17 NLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHErrrVEVKAPGI--IERKSV 94
Cdd:PRK02118 44 RLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEP---IEIGGPSVnpVKRIVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 95 HEPMQTGLKAVD---SLVpigRGQReliigdrqtgktaIAIDTILNQK--QMNSRATSESETLYCVYVAIGQKRSTVAQL 169
Cdd:PRK02118 121 REMIRTGIPMIDvfnTLV---ESQK-------------IPIFSVSGEPynALLARIALQAEADIIILGGMGLTFDDYLFF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 170 VQILSEGNALEYSILVAATASDPAPLQFLAPYSGCAMGEYFR-DNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFP 248
Cdd:PRK02118 185 KDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYP 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 302747434 249 GDvfyLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICL 305
Cdd:PRK02118 265 GS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
49-327 |
6.72e-17 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 79.57 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 49 VPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKT 128
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 129 AIAIDTILNqkqmnsraTSESETLYCVYVAIGQ------------KRSTVAQLvqilsegNALEYSILVAATASDPAPLQ 196
Cdd:cd01133 82 VLIMELINN--------IAKAHGGYSVFAGVGErtregndlyhemKESGVINL-------DGLSKVALVYGQMNEPPGAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 197 FLAPYSGCAMGEYFRD-NGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAkrsdQTGAGSLT 275
Cdd:cd01133 147 ARVALTGLTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERIT----STKKGSIT 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 302747434 276 ALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRV 327
Cdd:cd01133 223 SVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
52-326 |
8.33e-17 |
|
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: 79.54 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 52 GKAMLGRVVDALGVPID----------GRGAlsDHERRRVEVKAPgIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIG 121
Cdd:cd01134 7 GPGLLGSIFDGIQRPLEviaetgsifiPRGV--NVQRWPVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 122 DRQTGKTAIaidtilnqkqmnSRATSE-SETLYCVYVAIGQKRSTVA-------QLVQILSEGNALEYSILVAATASDPA 193
Cdd:cd01134 84 PFGCGKTVI------------SQSLSKwSNSDVVIYVGCGERGNEMAevleefpELKDPITGESLMERTVLIANTSNMPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 194 PLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGdvfYLHSRL---LERAAK---RSD 267
Cdd:cd01134 152 AAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRvrcLGS 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 302747434 268 QTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSR 326
Cdd:cd01134 229 PGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
26-114 |
2.23e-16 |
|
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: 79.75 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 26 VVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAV 105
Cdd:COG0055 58 IAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVI 137
|
....*....
gi 302747434 106 DSLVPIGRG 114
Cdd:COG0055 138 DLLAPYAKG 146
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
90-276 |
4.40e-12 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 66.73 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 90 ERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIaidtilnQKQMnSRatsESETLYCVYVAIGQKRSTVaql 169
Cdd:PRK04192 203 EKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVT-------QHQL-AK---WADADIVIYVGCGERGNEM--- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 170 VQILSE---------GNAL-EYSILVAATASDP-----APLqflapYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQM 234
Cdd:PRK04192 269 TEVLEEfpelidpktGRPLmERTVLIANTSNMPvaareASI-----YTGITIAEYYRDMGYDVLLMADSTSRWAEALREI 343
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 302747434 235 SLLLRRPPGREAFPGdvfYLHSRL---LERAAK-RSDQTGAGSLTA 276
Cdd:PRK04192 344 SGRLEEMPGEEGYPA---YLASRLaefYERAGRvKTLGGEEGSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
134-319 |
7.18e-12 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 66.58 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 134 TILNQKQMNSRATSESETLYCVYVAIGQKRSTVAQLVQ---ILSEGNA----LEYSILVAATASDPAPLQFLAPYSGCAM 206
Cdd:PRK14698 665 TLLHNTVTQHQLAKWSDAQVVIYIGCGERGNEMTDVLEefpKLKDPKTgkplMERTVLIANTSNMPVAAREASIYTGITI 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 207 GEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGdvfYLHSRLLE------RAAKRSDQTGAGSLTALPVI 280
Cdd:PRK14698 745 AEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAV 821
|
170 180 190
....*....|....*....|....*....|....*....
gi 302747434 281 ETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAIN 319
Cdd:PRK14698 822 SPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAIN 860
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
18-319 |
4.28e-10 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 60.82 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 18 LENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGRGALSDHERRRVEVKAPGIIE---RKSV 94
Cdd:CHL00060 65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQldtKLSI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 95 HEpmqTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNS---------RATSESETLYcvyvaIGQKRST 165
Cdd:CHL00060 145 FE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGgvsvfggvgERTREGNDLY-----MEMKESG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 166 VAQLVQILSEGNALEYSIL---------VAATASdpaplqflapysgcAMGEYFRD-NGMHALIIYDDLSKQAVAYRQMS 235
Cdd:CHL00060 217 VINEQNIAESKVALVYGQMneppgarmrVGLTAL--------------TMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 236 LLLRRppgreaFPGDVFYLHSRLLERAA--KRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRG 313
Cdd:CHL00060 283 ALLGR------MPSAVGYQPTLSTEMGSlqERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKG 356
|
....*.
gi 302747434 314 IRPAIN 319
Cdd:CHL00060 357 IYPAVD 362
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
1-44 |
2.02e-09 |
|
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: 53.32 E-value: 2.02e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 302747434 1 AGEMVEFASGVKGIAFNLENENVGIVVFGSDTAIKEGDLVKRTG 44
Cdd:pfam02874 26 EVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
34-130 |
5.94e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 38.14 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302747434 34 IKEGDLVKrtgSIVDVPAGKAMLGRVVDALGVPIDGRGALSD---------HERRRVEVKAPGIIERksvhepmqtglkA 104
Cdd:PRK12608 59 LRTGDVVE---GVARPRERYRVLVRVDSVNGTDPEKLARRPHfddltplhpRERLRLETGSDDLSMR------------V 123
|
90 100
....*....|....*....|....*.
gi 302747434 105 VDSLVPIGRGQRELIIGDRQTGKTAI 130
Cdd:PRK12608 124 VDLVAPIGKGQRGLIVAPPRAGKTVL 149
|
|
| |
