|
Name |
Accession |
Description |
Interval |
E-value |
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-367 |
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: 859.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 1 RAHGLENAMSGELLEFSNGSYGMAQNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLG 80
Cdd:COG0056 40 RVYGLPNAMAGELLEFPGGVYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 81 EIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIG 160
Cdd:COG0056 120 PIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 161 QKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRR 240
Cdd:COG0056 200 QKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 241 PPGREAYPGDVFYLHSRLLERAAKLSDDLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDA 320
Cdd:COG0056 280 PPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINV 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 63091953 321 GLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFGSDLDAAT 367
Cdd:COG0056 360 GLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEAT 406
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-367 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 855.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 1 RAHGLENAMSGELLEFSNGSYGMAQNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLG 80
Cdd:PRK09281 40 RVYGLDNVMAGELLEFPGGVYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 81 EIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIG 160
Cdd:PRK09281 120 PIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIINQKGKDVICIYVAIG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 161 QKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRR 240
Cdd:PRK09281 200 QKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 241 PPGREAYPGDVFYLHSRLLERAAKLSDDLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDA 320
Cdd:PRK09281 280 PPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINV 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 63091953 321 GLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFGSDLDAAT 367
Cdd:PRK09281 360 GISVSRVGGAAQIKAMKKVAGTLRLDLAQYRELEAFAQFGSDLDEAT 406
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
1-367 |
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: 724.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 1 RAHGLENAMSGELLEFSNGSYGMAQNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLG 80
Cdd:TIGR00962 39 RVYGLENVMSGELIEFEGGVQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 81 EIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIG 160
Cdd:TIGR00962 119 PIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKDSDVYCIYVAIG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 161 QKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRR 240
Cdd:TIGR00962 199 QKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 241 PPGREAYPGDVFYLHSRLLERAAKLSDDLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDA 320
Cdd:TIGR00962 279 PPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINV 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 63091953 321 GLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFGSDLDAAT 367
Cdd:TIGR00962 359 GLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELEAFSQFASDLDEAT 405
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-367 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 673.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 1 RAHGLENAMSGELLEFSNGSYGMAQNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLG 80
Cdd:PRK13343 40 FVSGLPDAALDELLRFEGGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 81 EIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIG 160
Cdd:PRK13343 120 PLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIINQKDSDVICVYVAIG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 161 QKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRR 240
Cdd:PRK13343 200 QKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 241 PPGREAYPGDVFYLHSRLLERAAKLSDDLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDA 320
Cdd:PRK13343 280 PPGREAYPGDIFYLHSRLLERAAKLSPELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDV 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 63091953 321 GLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFGSDLDAAT 367
Cdd:PRK13343 360 GLSVSRVGGKAQHPAIRKESGRLRLDYAQFLELEAFTRFGGLLDAGT 406
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
1-367 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 667.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 1 RAHGLENAMSGELLEFSNGSYGMAQNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLG 80
Cdd:CHL00059 19 RIYGLDEVMAGELVEFEDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 81 EIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIG 160
Cdd:CHL00059 99 EISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQKGQNVICVYVAIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 161 QKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRR 240
Cdd:CHL00059 179 QKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 241 PPGREAYPGDVFYLHSRLLERAAKLSDDLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDA 320
Cdd:CHL00059 259 PPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINV 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 63091953 321 GLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFGSDLDAAT 367
Cdd:CHL00059 339 GISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKAT 385
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
55-328 |
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: 573.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 55 IMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKT 134
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 135 GKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNG 214
Cdd:cd01132 81 GKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 215 KHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDLGGGSMTALPFVETQAGDISAYIPTN 294
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTN 240
|
250 260 270
....*....|....*....|....*....|....
gi 63091953 295 VISITDGQIFLESDLFYAGTRPAVDAGLSVSRVG 328
Cdd:cd01132 241 VISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
22-363 |
4.57e-118 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 353.58 E-value: 4.57e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 22 GMAQNLESND-VGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDgLGEIVTDKAR--------PVEA 92
Cdd:PTZ00185 80 GLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRALleseqtlgKVDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 93 MAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQ--------KGQDMICIYVAIGQKDS 164
Cdd:PTZ00185 159 GAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQvrinqqilSKNAVISIYVSIGQRCS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 165 TVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGR 244
Cdd:PTZ00185 239 NVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 245 EAYPGDVFYLHSRLLERAAKLSDDLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSV 324
Cdd:PTZ00185 319 EAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSV 398
|
330 340 350
....*....|....*....|....*....|....*....
gi 63091953 325 SRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFGSDL 363
Cdd:PTZ00185 399 SRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQV 437
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
110-325 |
1.16e-111 |
|
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: 324.31 E-value: 1.16e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 110 GLKAIDALVPIGRGQRELVIGDRKTGKTSIAiDTIINQKGQDmICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGA 189
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD-VVVYALIGERGREVREFIEELLGSGALKRTVVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 190 SQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdl 269
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKG-- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 63091953 270 GGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVS 325
Cdd:pfam00006 157 KGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
94-343 |
2.09e-107 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 324.23 E-value: 2.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 94 APGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETL 173
Cdd:PRK07165 114 AHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIYETL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 174 KKYGAMDYTIVVNAGASQPAPlLYIAPYAGTAMGEEFMYNgKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFY 253
Cdd:PRK07165 194 KEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAENISYN-DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFF 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 254 LHSRLLERAAKLsddLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQI 333
Cdd:PRK07165 272 AHSKLLERAGKF---KNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRTGSSVQS 348
|
250
....*....|
gi 63091953 334 KAMKKVAGTL 343
Cdd:PRK07165 349 KTITKVAGEI 358
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
58-327 |
1.33e-106 |
|
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: 313.62 E-value: 1.33e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 58 VPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKT 137
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 138 SIAIDTIINQKGQD-MICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKH 216
Cdd:cd19476 82 VLAMQLARNQAKAHaGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 217 VLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdlGGGSMTALPFVETQAGDISAYIPTNVI 296
Cdd:cd19476 162 VLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 63091953 297 SITDGQIFLESDLFYAGTRPAVDAGLSVSRV 327
Cdd:cd19476 240 AILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
57-327 |
2.31e-52 |
|
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: 174.67 E-value: 2.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 57 EVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGK 136
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 137 TSIaIDTIINQKGQDMICIyVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKH 216
Cdd:cd01136 81 STL-LGMIARNTDADVNVI-ALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 217 VLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdlggGSMTALPFVETQAGDISAYIPTNVI 296
Cdd:cd01136 159 VLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEK----GSITAFYTVLVEGDDFNDPIADEVR 234
|
250 260 270
....*....|....*....|....*....|.
gi 63091953 297 SITDGQIFLESDLFYAGTRPAVDAGLSVSRV 327
Cdd:cd01136 235 SILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
37-366 |
5.19e-49 |
|
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: 170.60 E-value: 5.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 37 LGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDA 116
Cdd:COG1157 71 LGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 117 LVPIGRGQRelvIGdr---ktGKTSIaIDTIINQKGQDMICIyvA-IGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQP 192
Cdd:COG1157 151 LLTVGRGQR---IGifagsgvGKSTL-LGMIARNTEADVNVI--AlIGERGREVREFIEDDLGEEGLARSVVVVATSDEP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 193 APLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlsddLGGG 272
Cdd:COG1157 225 PLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN----GGKG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 273 SMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRE 352
Cdd:COG1157 301 SITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEE 380
|
330 340
....*....|....*....|..
gi 63091953 353 LE------AFTQfGSD--LDAA 366
Cdd:COG1157 381 NEdlirigAYQP-GSDpeLDEA 401
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
37-360 |
1.10e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 169.93 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 37 LGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGlGEIVTDKAR-PVEAMAPGVMQRKSVNEPMQTGLKAID 115
Cdd:PRK06936 76 LGEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDG-GHPPEPAAWyPVYADAPAPMSRRLIETPLSLGVRVID 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 116 ALVPIGRGQRELVIGDRKTGKTSIaIDTIINQKGQDmICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPL 195
Cdd:PRK06936 155 GLLTCGEGQRMGIFAAAGGGKSTL-LASLIRSAEVD-VTVLALIGERGREVREFIESDLGEEGLRKAVLVVATSDRPSME 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 196 LYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSDDlggGSMT 275
Cdd:PRK06936 233 RAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDK---GSIT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 276 ALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEA 355
Cdd:PRK06936 309 ALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVEL 388
|
....*
gi 63091953 356 FTQFG 360
Cdd:PRK06936 389 LLQIG 393
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
1-360 |
2.55e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 163.79 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 1 RAHGLENAMsGELLEFSNGSYGMAQNLE----SNDVGIII-LGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQP 75
Cdd:PRK09099 37 RVSGLDVTL-GELCELRQRDGTLLQRAEvvgfSRDVALLSpFGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 76 IDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTsiaidTIINQKGQDMIC- 154
Cdd:PRK09099 116 IDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCd 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 155 --IYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYR 232
Cdd:PRK09099 191 vnVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 233 ELSLLLRRPPGREAYPGDVFYLHSRLLERAAklsddLGG-GSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFY 311
Cdd:PRK09099 271 EIGLAAGEPPARRGFPPSVFAELPRLLERAG-----MGEtGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAA 345
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 63091953 312 AGTRPAVDAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFG 360
Cdd:PRK09099 346 RNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVG 394
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
5-360 |
2.27e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 161.14 E-value: 2.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 5 LENAMSGELLEFSNgsygmaQNLESNDVGI----IILGDFES---IREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPID 77
Cdd:PRK06820 45 LPGVAQGELCRIEP------QGMLAEVVSIeqemALLSPFASsdgLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 78 GlGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIaIDTIINQKGQDMIcIYV 157
Cdd:PRK06820 119 G-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTL-LGMLCADSAADVM-VLA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 158 AIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLL 237
Cdd:PRK06820 196 LIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLA 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 238 LRRPPGREAYPGDVFYLHSRLLERAAKLSDdlggGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPA 317
Cdd:PRK06820 276 AGEPPAAGSFPPSVFANLPRLLERTGNSDR----GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPA 351
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 63091953 318 VDAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFG 360
Cdd:PRK06820 352 IDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVG 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
35-361 |
2.96e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 155.27 E-value: 2.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 35 IILGDFESIRE---GDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGL 111
Cdd:PRK07721 67 VLLMPYTEVAEiapGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 112 KAIDALVPIGRGQRELVIGDRKTGKTSIaIDTIINQKGQDMICIYVaIGQKDSTVRTQVET------LKKygamdyTIVV 185
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTL-MGMIARNTSADLNVIAL-IGERGREVREFIERdlgpegLKR------SIVV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 186 NAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKl 265
Cdd:PRK07721 219 VATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGT- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 266 sddLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQIKAMKKVAGTLRL 345
Cdd:PRK07721 298 ---NASGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRE 374
|
330
....*....|....*.
gi 63091953 346 DLASYRELEAFTQFGS 361
Cdd:PRK07721 375 LLSTYQNSEDLINIGA 390
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
49-360 |
2.47e-41 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 150.14 E-value: 2.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 49 VKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTD----KARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQ 124
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVgpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 125 RELVIGDRKTGKTSIaIDTIINQKGQDmicIYVA--IGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYA 202
Cdd:PRK08149 153 RMGIFASAGCGKTSL-MNMLIEHSEAD---VFVIglIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 203 GTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdlggGSMTALPFVET 282
Cdd:PRK08149 229 ATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLA----GSITAFYTVLL 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63091953 283 QAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFG 360
Cdd:PRK08149 305 ESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLG 382
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
5-360 |
1.88e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 147.79 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 5 LENAMSGELLEFSNGSyGMAQ--NLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLgEI 82
Cdd:PRK07594 37 LPGVFMGELCCIKPGE-ELAEvvGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGR-EL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 83 VTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIaIDTIINQKGQDmICIYVAIGQK 162
Cdd:PRK07594 115 PDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL-LAMLCNAPDAD-SNVLVLIGER 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 163 DSTVRTQVE-TLKKYGAMDYTIVVnAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRP 241
Cdd:PRK07594 193 GREVREFIDfTLSEETRKRCVIVV-ATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGET 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 242 PGREAYPGDVFYLHSRLLERAAklsddLGG-GSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDA 320
Cdd:PRK07594 272 AVSGEYPPGVFSALPRLLERTG-----MGEkGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDV 346
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 63091953 321 GLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFG 360
Cdd:PRK07594 347 LATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIG 386
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
22-366 |
3.66e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 144.44 E-value: 3.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 22 GMAQNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRK 101
Cdd:PRK08472 56 GMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 102 SVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIINQKGQdmICIYVAIGQKDSTVRTQVE-TLKkyGAMD 180
Cdd:PRK08472 136 LIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGCLAP--IKVVALIGERGREIPEFIEkNLG--GDLE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 181 YTIVVNAgASQPAPLL--YIApYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRL 258
Cdd:PRK08472 212 NTVIVVA-TSDDSPLMrkYGA-FCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 259 LERAAKlsdDLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQIKAMKK 338
Cdd:PRK08472 290 MERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKL 366
|
330 340 350
....*....|....*....|....*....|....*
gi 63091953 339 VAGTLRLDLASYRELEAFTQFGS-------DLDAA 366
Cdd:PRK08472 367 AARKFKRLYSLLKENEVLIRIGAyqkgndkELDEA 401
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
55-331 |
9.35e-38 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 136.97 E-value: 9.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 55 IMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQR--------- 125
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKlpifsgsgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 126 ---ELVIgdrktgktSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYA 202
Cdd:cd01135 81 phnELAA--------QIARQAGVVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 203 GTAMGEEFMY-NGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDDlgGGSMTALP 278
Cdd:cd01135 153 ALTTAEYLAYeKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--KGSITQIP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 63091953 279 FVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSA 331
Cdd:cd01135 228 ILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSG 280
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
23-366 |
1.79e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 134.44 E-value: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 23 MAQNLESNDVG----IIILGDFESIR---EGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAP 95
Cdd:PRK08972 55 MAGELEAEVVGfdgdLLYLMPIEELRgvlPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 96 GVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKtSIAIDTIINQKGQDMICIYVaIGQKDSTVRTQVETLKK 175
Cdd:PRK08972 135 NPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGK-SVLLGMMTRGTTADVIVVGL-VGERGREVKEFIEEILG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 176 YGAMDYTIVVNAGASQpAPLLYI-APYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYL 254
Cdd:PRK08972 213 EEGRARSVVVAAPADT-SPLMRLkGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 255 HSRLLERAAKLSDdlGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVG----GS 330
Cdd:PRK08972 292 LPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMpmviSE 369
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 63091953 331 AQIKAMKKVAGTLRL-----DLASyreLEAFTQfGSD--LDAA 366
Cdd:PRK08972 370 EHLEAMRRVKQVYSLyqqnrDLIS---IGAYKQ-GSDprIDNA 408
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
4-326 |
1.40e-33 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 129.56 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 4 GLENAMSGELLEF--SNGSYGMAQNLESNDvGIIILGDFESIR----EGDKVKRTGKIMEVPVGEALIGRVVNPLGQPID 77
Cdd:PRK04196 19 GVEGVAYGEIVEIelPNGEKRRGQVLEVSE-DKAVVQVFEGTTgldlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPID 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 78 GLGEIVTDKARPV--EAMAPgvMQRKSVNEPMQTGLKAIDALVPIGRGQR------------ELVigdrktgkTSIAIDT 143
Cdd:PRK04196 98 GGPEIIPEKRLDIngAPINP--VAREYPEEFIQTGISAIDGLNTLVRGQKlpifsgsglphnELA--------AQIARQA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 144 IINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYN-GKHVLIIFD 222
Cdd:PRK04196 168 KVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAFEkGMHVLVILT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 223 DLSKQAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSDDlgGGSMTALPFVETQAGDISAYIPTNVISIT 299
Cdd:PRK04196 248 DMTNYCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGK--KGSITQIPILTMPDDDITHPIPDLTGYIT 322
|
330 340
....*....|....*....|....*..
gi 63091953 300 DGQIFLESDLFYAGTRPAVDAGLSVSR 326
Cdd:PRK04196 323 EGQIVLSRELHRKGIYPPIDVLPSLSR 349
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
13-358 |
2.58e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 128.75 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 13 LLEFSNGsyGMAQNLESNDVG-------IIILGDFESIREGDKV---------KRTGKimEVPVGEALIGRVVNPLGQPI 76
Cdd:PRK07960 53 VIERQNG--SETHEVESEVVGfngqrlfLMPLEEVEGILPGARVyarnisgegLQSGK--QLPLGPALLGRVLDGSGKPL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 77 DGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKtSIAIDTIINQKGQDMICIY 156
Cdd:PRK07960 129 DGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK-SVLLGMMARYTQADVIVVG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 157 VaIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQpAPLLYI--APYAgTAMGEEFMYNGKHVLIIFDDLSKQAVAYREL 234
Cdd:PRK07960 208 L-IGERGREVKDFIENILGAEGRARSVVIAAPADV-SPLLRMqgAAYA-TRIAEDFRDRGQHVLLIMDSLTRYAMAQREI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 235 SLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdlGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGT 314
Cdd:PRK07960 285 ALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGH 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 63091953 315 RPAVDAGLSVSRvggsaqikAMkkvagTLRLDLASYRELEAFTQ 358
Cdd:PRK07960 363 YPAIDIEASISR--------AM-----TALIDEQHYARVRQFKQ 393
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
37-327 |
2.40e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 126.00 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 37 LGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDA 116
Cdd:PRK05688 82 VGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSING 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 117 LVPIGRGQRELVIGDRKTGKtSIAIDTIINQKGQDMICIYVaIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQpAPL- 195
Cdd:PRK05688 162 LLTVGRGQRLGLFAGTGVGK-SVLLGMMTRFTEADIIVVGL-IGERGREVKEFIEHILGEEGLKRSVVVASPADD-APLm 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 196 -LYIAPYAgTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDDLGGGSM 274
Cdd:PRK05688 239 rLRAAMYC-TRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSI 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 63091953 275 TALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRV 327
Cdd:PRK05688 316 TAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRV 368
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
57-341 |
1.24e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 123.85 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 57 EVPVGEALIGRVVNPLGQPIDGLGEIVTDKarPVEAMAPGV--MQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKT 134
Cdd:PRK07196 89 ELLIGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIhpLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 135 GKtSIAIDTIINQKGQDMICIYVaIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQpAPLLYI-APYAGTAMGEEFMYN 213
Cdd:PRK07196 167 GK-SVLLGMITRYTQADVVVVGL-IGERGREVKEFIEHSLQAAGMAKSVVVAAPADE-SPLMRIkATELCHAIATYYRDK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 214 GKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklsDDLGGGSMTALPFVETQAGDISAYIPT 293
Cdd:PRK07196 244 GHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQDPIVD 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 63091953 294 NVISITDGQIFLESDLFYAGTRPAVDAGLSVSR----VGGSAQIKAMKKVAG 341
Cdd:PRK07196 321 CARAVLDGHIVLSRKLAEAGHYPAIDISQSISRcmsqVIGSQQAKAASLLKQ 372
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
46-352 |
2.66e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 120.10 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 46 GDKVKRTGKiMEVPVGEALIGRVVNPLGQPIDGLGEIVT-DKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQ 124
Cdd:PRK06002 88 GDAVFRKGP-LRIRPDPSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQ 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 125 RELVIGDRKTGKTSI--------AIDTIInqkgqdmiciyVA-IGQKDSTVRTQVE-TLKkyGAMDYTIVVNAGASQPAP 194
Cdd:PRK06002 167 RIGIFAGSGVGKSTLlamlaradAFDTVV-----------IAlVGERGREVREFLEdTLA--DNLKKAVAVVATSDESPM 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 195 LLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdlGGGSM 274
Cdd:PRK06002 234 MRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAE--GGGSI 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63091953 275 TALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRE 352
Cdd:PRK06002 312 TGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEE 389
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
38-354 |
2.30e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 117.39 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 38 GDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVT-DKARPVEAMAPGVMQRKSVNEPMQTGLKAIDA 116
Cdd:PRK08927 72 GPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 117 LVPIGRGQRELVIGDRKTGKtSIAIDTIINQKGQDMICIYVaIGQKDSTVRTQVE-TLKKYGaMDYTIVVNAGASQPAPL 195
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGK-SVLLSMLARNADADVSVIGL-IGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALM 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 196 LYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDDLGGGSMT 275
Cdd:PRK08927 229 RRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTIT 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63091953 276 ALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELE 354
Cdd:PRK08927 307 GLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
58-366 |
5.73e-28 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 113.46 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 58 VPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKT 137
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 138 SIAidTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHV 217
Cdd:PRK05922 172 SLL--STIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 218 LIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDDlgGGSMTALPFVETQAG--DI-SAYIPtn 294
Cdd:PRK05922 250 LFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG--NND--KGSITALYAILHYPNhpDIfTDYLK-- 323
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63091953 295 viSITDGQIFLeSDLFYAGTRPAVDAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFTQFGS-------DLDAA 366
Cdd:PRK05922 324 --SLLDGHFFL-TPQGKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAyvpgqdaHLDRA 399
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
24-354 |
2.44e-26 |
|
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: 109.42 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 24 AQNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSV 103
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 104 NEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIIN-QKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYT 182
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNiAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 183 IVVNAGASQPAPLLYIAPYAGTAMGEEFM-YNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLER 261
Cdd:TIGR01039 204 ALVYGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 262 AAKLSddlgGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSR-----VGGSAQIKAM 336
Cdd:TIGR01039 284 ITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRlldpsVVGEEHYDVA 359
|
330
....*....|....*...
gi 63091953 337 KKVAGTLRldlaSYRELE 354
Cdd:TIGR01039 360 RGVQQILQ----RYKELQ 373
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
48-336 |
9.75e-25 |
|
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: 104.80 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 48 KVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQREL 127
Cdd:TIGR01040 66 TCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 128 VIGD-------------RKTGKTSIAIDTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAP 194
Cdd:TIGR01040 146 IFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 195 LLYIAPYAGTAMGEEFMYN-GKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDDlgGGS 273
Cdd:TIGR01040 226 ERIITPRLALTTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGR--NGS 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 63091953 274 MTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQIKAM 336
Cdd:TIGR01040 304 ITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
6-308 |
1.15e-24 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 104.35 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 6 ENAMSGELLEFSN---GSYGMAQNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEI 82
Cdd:PRK02118 21 EGVGYGELATVERkdgSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 83 VTDkarPVEAMAPGV--MQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDrkTGKTSIAI-DTIINQKGQDMIcIYVAI 159
Cdd:PRK02118 101 EGE---PIEIGGPSVnpVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSV--SGEPYNALlARIALQAEADII-ILGGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 160 GQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNG-KHVLIIFDDLSKQAVAYRELSLLL 238
Cdd:PRK02118 175 GLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGkKKVLVLLTDMTNFADALKEISITM 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 239 RRPPGREAYPGDvfyLHSRLLERAAKLSDDLGGGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESD 308
Cdd:PRK02118 255 DQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYLRRG 321
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
41-361 |
4.44e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 99.67 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 41 ESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPI 120
Cdd:PRK06793 74 EKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTI 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 121 GRGQRELVIGDRKTGKTSIAidTIINQKGQDMICIYVAIGQKDSTVRTQVETLKKYGAMDYTIVVNAGASQPAPLLYIAP 200
Cdd:PRK06793 154 GIGQKIGIFAGSGVGKSTLL--GMIAKNAKADINVISLVGERGREVKDFIRKELGEEGMRKSVVVVATSDESHLMQLRAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 201 YAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYRELSLLLRRPPgreaYPGDVFYLHS---RLLERAAKLSDdlggGSMTAL 277
Cdd:PRK06793 232 KLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLLMESymkKLLERSGKTQK----GSITGI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 278 PFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRVGGSAQIKAMKKVAGTLRLDLASYRELEAFT 357
Cdd:PRK06793 304 YTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYF 383
|
....
gi 63091953 358 QFGS 361
Cdd:PRK06793 384 KLGT 387
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
332-367 |
3.09e-22 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 90.58 E-value: 3.09e-22
10 20 30
....*....|....*....|....*....|....*.
gi 63091953 332 QIKAMKKVAGTLRLDLASYRELEAFTQFGSDLDAAT 367
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEAT 36
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
1-54 |
3.14e-22 |
|
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: 88.66 E-value: 3.14e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 63091953 1 RAHGLENAMSGELLEFSNGSYGMAQNLESNDVGIIILGDFESIREGDKVKRTGK 54
Cdd:cd18116 14 RVYGLPNVMAGELVEFPGGVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
57-327 |
2.09e-20 |
|
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: 89.59 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 57 EVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGK 136
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 137 TSIAIDTIIN-QKGQDMICIYVAIGQkdstvRTQvETLKKYGAMDYTIVVNAGASQPAPLLY-----------IAPYAGT 204
Cdd:cd01133 81 TVLIMELINNiAKAHGGYSVFAGVGE-----RTR-EGNDLYHEMKESGVINLDGLSKVALVYgqmneppgaraRVALTGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 205 AMGEEFM-YNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDdlggGSMTALPFVETQ 283
Cdd:cd01133 155 TMAEYFRdEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYVP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 63091953 284 AGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVSRV 327
Cdd:cd01133 231 ADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
24-123 |
7.87e-20 |
|
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: 90.53 E-value: 7.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 24 AQNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSV 103
Cdd:COG0055 47 AQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTK 126
|
90 100
....*....|....*....|
gi 63091953 104 NEPMQTGLKAIDALVPIGRG 123
Cdd:COG0055 127 TEILETGIKVIDLLAPYAKG 146
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
336-367 |
3.02e-19 |
|
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: 82.41 E-value: 3.02e-19
10 20 30
....*....|....*....|....*....|..
gi 63091953 336 MKKVAGTLRLDLASYRELEAFTQFGSDLDAAT 367
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEAT 32
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
25-354 |
7.77e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 75.46 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 25 QNLESNDVGIIILGDFESIREGDKVKRTGKIMEVPVGEALIGRVVNPLGQPIDGLGEIVTDKARPVEAMAPGVMQRKSVN 104
Cdd:CHL00060 63 QLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 105 EPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTSIAIDTIIN-QKGQDMICIYVAIGQkdstvRTQvETLKKYGAMDYTI 183
Cdd:CHL00060 143 SIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGVGE-----RTR-EGNDLYMEMKESG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 184 VVNA---GASQPApLLY------------IAPYAGTaMGEEFM-YNGKHVLIIFDDLSKQAVAYRELSLLLRRPPGREAY 247
Cdd:CHL00060 217 VINEqniAESKVA-LVYgqmneppgarmrVGLTALT-MAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 248 PGDVFYLHSRLLERAAKLSDdlggGSMTALPFVETQAGDISAYIPTNVISITDGQIFLESDLFYAGTRPAVDAGLSVS-- 325
Cdd:CHL00060 295 QPTLSTEMGSLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTStm 370
|
330 340 350
....*....|....*....|....*....|..
gi 63091953 326 ---RVGGSAQIKAMKKVAGTLRldlaSYRELE 354
Cdd:CHL00060 371 lqpRIVGEEHYETAQRVKQTLQ----RYKELQ 398
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
89-326 |
7.25e-14 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 71.07 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 89 PVEAMAPgVMQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKTsiaidtIINQK----GQDMICIYVAIGQKDS 164
Cdd:cd01134 43 PVRQPRP-VKEKLPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKT------VISQSlskwSNSDVVIYVGCGERGN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 165 TVrtqVETLKKY----------GAMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLSKQAVAYREL 234
Cdd:cd01134 116 EM---AEVLEEFpelkdpitgeSLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 235 SLLLRRPPGREAYPGdvfYLHSRL---LERAAK---LSDDLGGGSMTALPFVETQAGDISAYIPTNVISITdgQIF--LE 306
Cdd:cd01134 193 SGRLEEMPAEEGYPA---YLGARLaefYERAGRvrcLGSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLD 267
|
250 260
....*....|....*....|
gi 63091953 307 SDLFYAGTRPAVDAGLSVSR 326
Cdd:cd01134 268 KKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
1-53 |
1.67e-12 |
|
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: 62.18 E-value: 1.67e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 63091953 1 RAHGLENAMSGELLEFSNGSYGMAQNLESNDVGIIILGDFESIREGDKVKRTG 53
Cdd:pfam02874 17 RLPGLLNALEVELVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
153-319 |
9.40e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 57.34 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 153 ICIYVAIGQKDSTVRTQVETLKKYG-------AMDYTIVVNAGASQPAPLLYIAPYAGTAMGEEFMYNGKHVLIIFDDLS 225
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFPKLKdpktgkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 226 KQAVAYRELSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKLSDDLGGGSMTALPFVETQAGDISAYIPTNVISIT 299
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVV 840
|
170 180
....*....|....*....|
gi 63091953 300 DGQIFLESDLFYAGTRPAVD 319
Cdd:PRK14698 841 KVFWALDADLARRRHFPAIN 860
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
86-288 |
2.17e-06 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 49.40 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 86 KARPVEamapgvmQRKSVNEPMQTGLKAIDALVPIGRGQRELVIGDRKTGKT----SIAidtiinqKGQDM-ICIYVAIG 160
Cdd:PRK04192 197 RPRPYK-------EKLPPVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTvtqhQLA-------KWADAdIVIYVGCG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63091953 161 QKDSTVrtqVETLK--------KYGA--MDYTIVVNAGASQPapllyIAP-----YAGTAMGEEFMYNGKHVLIIFDDLS 225
Cdd:PRK04192 263 ERGNEM---TEVLEefpelidpKTGRplMERTVLIANTSNMP-----VAAreasiYTGITIAEYYRDMGYDVLLMADSTS 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63091953 226 KQAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSdDLGG--GSMTALPFVETQAGDIS 288
Cdd:PRK04192 335 RWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRVK-TLGGeeGSVTIIGAVSPPGGDFS 398
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
336-367 |
6.51e-04 |
|
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: 37.81 E-value: 6.51e-04
10 20 30
....*....|....*....|....*....|....
gi 63091953 336 MKKVAGTLRLDLASYRELEAFTQFGSD--LDAAT 367
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEAD 34
|
|
| |
