|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-509 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 1031.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 1 MEIRPAEISEILKRQIADFDTEANVAETGQVLSVGDGIARVFGLANVQAGELVDFPGaGLKGMALNLEADNVGVVIFGDD 80
Cdd:PRK09281 1 MQINPEEISAIIKQQIENFDAEAEVEEVGTVISVGDGIARVYGLDNVMAGELLEFPG-GVYGIALNLEEDNVGAVILGDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 81 KSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPI 160
Cdd:PRK09281 80 EDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 161 GRGQRELIIGDRQTGKTALIIDTIINQKavnaqgdeSKKLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDP 240
Cdd:PRK09281 160 GRGQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 241 APMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDEKGAG 320
Cdd:PRK09281 232 APLQYLAPYAGCAMGEYFMDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 321 SLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYRE 400
Cdd:PRK09281 312 SLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGISVSRVGGAAQIKAMKKVAGTLRLDLAQYRE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 401 MAAFAQFASDLDPATQKLLARGARLTELLKQPQYAPLSVAEQVISVFAGTKGYLDNLPVADVQKFESALIAALKANDPSI 480
Cdd:PRK09281 392 LEAFAQFGSDLDEATRAQLERGQRLVELLKQPQYSPLPVEEQVVILYAGTNGYLDDVPVEKVRRFEAELLAYLRSNHADL 471
|
490 500
....*....|....*....|....*....
gi 2541254387 481 VAAIEADQQIKPETETKLVAFIENLLRTF 509
Cdd:PRK09281 472 LEEIRETKDLSDEIEAKLKAAIEEFKKTF 500
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
1-509 |
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: 1028.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 1 MEIRPAEISEILKRQIADFDTEANVAETGQVLSVGDGIARVFGLANVQAGELVDFPGaGLKGMALNLEADNVGVVIFGDD 80
Cdd:COG0056 1 MQIRPEEISSIIKQQIENYDPEVEVEEVGTVLSVGDGIARVYGLPNAMAGELLEFPG-GVYGMALNLEEDNVGVVLLGDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 81 KSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPI 160
Cdd:COG0056 80 EGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 161 GRGQRELIIGDRQTGKTALIIDTIINQKavnaqgdeSKKLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDP 240
Cdd:COG0056 160 GRGQRELIIGDRQTGKTAIAIDTIINQK--------GKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 241 APMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDEKGAG 320
Cdd:COG0056 232 APLQYIAPYAGCAMGEYFMDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 321 SLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYRE 400
Cdd:COG0056 312 SLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNAGIRPAINVGLSVSRVGGAAQIKAMKKVAGTLRLDLAQYRE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 401 MAAFAQFASDLDPATQKLLARGARLTELLKQPQYAPLSVAEQVISVFAGTKGYLDNLPVADVQKFESALIAALKANDPSI 480
Cdd:COG0056 392 LEAFAQFGSDLDEATRAQLERGERLVELLKQPQYSPLSVEEQVAILYAGTNGYLDDVPVEKVREFEKELLEYLRAKHPDL 471
|
490 500
....*....|....*....|....*....
gi 2541254387 481 VAAIEADQQIKPETETKLVAFIENLLRTF 509
Cdd:COG0056 472 LKEIRETGKLDDEIEEKLKAAIEEFKKTF 500
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
3-509 |
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: 860.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 3 IRPAEISEILKRQIADFDTEANVAETGQVLSVGDGIARVFGLANVQAGELVDFPGaGLKGMALNLEADNVGVVIFGDDKS 82
Cdd:TIGR00962 2 LKLEEISELIKQEIKNFNVDSEAEEVGTVVSVGDGIARVYGLENVMSGELIEFEG-GVQGIALNLEEDSVGAVIMGDYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 83 IREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGR 162
Cdd:TIGR00962 81 IREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 163 GQRELIIGDRQTGKTALIIDTIINQKavnaqgdeSKKLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAP 242
Cdd:TIGR00962 161 GQRELIIGDRQTGKTAVAIDTIINQK--------DSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSAS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 243 MQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDEKGAGSL 322
Cdd:TIGR00962 233 LQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAAKLNDEKGGGSL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 323 TALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYREMA 402
Cdd:TIGR00962 313 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAAQIKAMKQVAGSLRLELAQYRELE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 403 AFAQFASDLDPATQKLLARGARLTELLKQPQYAPLSVAEQVISVFAGTKGYLDNLPVADVQKFESALIAALKANDPSIVA 482
Cdd:TIGR00962 393 AFSQFASDLDEATKKQLERGQRVVELLKQPQYKPLSVEEQVVILFAGTKGYLDDIPVDKIRKFEQALLAYLDANHPDILE 472
|
490 500
....*....|....*....|....*..
gi 2541254387 483 AIEADQQIKPETETKLVAFIENLLRTF 509
Cdd:TIGR00962 473 EINTTKKLTEELEAKLKEALKNFKKTF 499
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
22-509 |
0e+00 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 781.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 22 EANVAETGQVLSVGDGIARVFGLANVQAGELVDFpGAGLKGMALNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTG 101
Cdd:CHL00059 1 EVKIVNTGTVLQVGDGIARIYGLDEVMAGELVEF-EDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 102 KGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALII 181
Cdd:CHL00059 80 EAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 182 DTIINQKAVNaqgdeskkLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRDN 261
Cdd:CHL00059 160 DTILNQKGQN--------VICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 262 GMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDEKGAGSLTALPVIETQAGDVSAYIPT 341
Cdd:CHL00059 232 GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 342 NVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYREMAAFAQFASDLDPATQKLLAR 421
Cdd:CHL00059 312 NVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFAQFASDLDKATQNQLAR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 422 GARLTELLKQPQYAPLSVAEQVISVFAGTKGYLDNLPVADVQKFESALIAALKANDPSIVAAIEADQQIKPETETKLVAF 501
Cdd:CHL00059 392 GQRLRELLKQSQSAPLTVEEQVATIYTGTNGYLDSLEIGQVRKFLVELRTYLKTNKPQFQEIISSTKTFTEEAEALLKEA 471
|
....*...
gi 2541254387 502 IENLLRTF 509
Cdd:CHL00059 472 IQEQLELF 479
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-510 |
0e+00 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 748.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 1 MEIRPAEISEILKRQIADFDTEANVAETGQVLSVGDGIARVFGLANVQAGELVDFPGaGLKGMALNLEADNVGVVIFGDD 80
Cdd:PRK13343 1 MKSNADEWLARIRQRIARYEPQPDAREIGRVESVGDGIAFVSGLPDAALDELLRFEG-GSRGFAFNLEEELVGAVLLDDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 81 KSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPI 160
Cdd:PRK13343 80 ADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 161 GRGQRELIIGDRQTGKTALIIDTIINQKavnaqgdeSKKLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDP 240
Cdd:PRK13343 160 GRGQRELIIGDRQTGKTAIAIDAIINQK--------DSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 241 APMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDEKGAG 320
Cdd:PRK13343 232 PGLQYLAPFAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPELGGG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 321 SLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYRE 400
Cdd:PRK13343 312 SLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSRVGGKAQHPAIRKESGRLRLDYAQFLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 401 MAAFAQFASDLDPATQKLLARGARLTELLKQPQYAPLSVAEQVISVFAGTKGYLDNLPVADVQKFESALIAALKANDPSI 480
Cdd:PRK13343 392 LEAFTRFGGLLDAGTQKQITRGRRLRELLKQPRFSPLSVEEQIALLYALNEGLLDAVPLANIQAFEERLLEKLDARFAAL 471
|
490 500 510
....*....|....*....|....*....|
gi 2541254387 481 VAAIEADQQIKPETETKLVAFIENLLRTFG 510
Cdd:PRK13343 472 SLALESPRELDEAWLAALEEILREAGERFA 501
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
95-376 |
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: 596.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 95 IVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQT 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 175 GKTALIIDTIINQKAvnaqgdesKKLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAM 254
Cdd:cd01132 81 GKTAIAIDTIINQKG--------KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 255 GEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDEKGAGSLTALPVIETQAGD 334
Cdd:cd01132 153 GEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGD 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2541254387 335 VSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVG 376
Cdd:cd01132 233 VSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSRVG 274
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
56-470 |
2.97e-129 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 387.86 E-value: 2.97e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 56 PGAGLKGMALNLEADN-VGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDgKGPVMFSERRL----- 129
Cdd:PTZ00185 74 PTTFAAGLVFNLEKDGrIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVP-VGLLTRSRALLeseqt 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 130 ---VETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALIIDTIINQKAVNAQGDESKKLYCIYVA 206
Cdd:PTZ00185 153 lgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVISIYVS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 207 VGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLL 286
Cdd:PTZ00185 233 IGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 287 RRPPGREAYPGDVFYLHSRLLERAAKMSDEKGAGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAI 366
Cdd:PTZ00185 313 RRPPGREAYPGDVFYLHSRLLERAAMLSPGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 367 NVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYREMAAFAQFASDLDPATqklLARGARLTELLKQPQyaPLSVAEQVISV 446
Cdd:PTZ00185 393 NIGLSVSRVGSSAQNVAMKAVAGKLKGILAEYRKLAADSVGGSQVQTVP---MIRGARFVALFNQKN--PSFFMNALVSL 467
|
410 420
....*....|....*....|....
gi 2541254387 447 FAGTKGYLDNLPVADVQKFESALI 470
Cdd:PTZ00185 468 YACLNGYLDDVKVNYAKLYEYLLV 491
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
97-375 |
7.65e-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: 350.22 E-value: 7.65e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 97 DVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGK 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 177 TALIIDTIINQKavnaqgdESKKLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAMGE 256
Cdd:cd19476 81 TVLAMQLARNQA-------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 257 FFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDekGAGSLTALPVIETQAGDVS 336
Cdd:cd19476 154 YFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKD--GGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 2541254387 337 AYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRV 375
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-373 |
1.20e-115 |
|
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: 339.72 E-value: 1.20e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 150 GIKAIDVLVPIGRGQRELIIGDRQTGKTALIiDTIINQKAVNaqgdeskklYCIYVAVGQKRSTVAQLVRTLEEYGVMEY 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLA-GMIARQASAD---------VVVYALIGERGREVREFIEELLGSGALKR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 230 SIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLER 309
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLER 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541254387 310 AAKMSDEKgaGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVS 373
Cdd:pfam00006 151 AGRVKGKG--GSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
60-509 |
7.91e-105 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 322.69 E-value: 7.91e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 60 LKGMALNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPI-------------DGKGPVMFse 126
Cdd:PRK07165 35 VKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKIIDIDGNIIypeaqnplskkflPNTSSIFN-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 127 rrlvetKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALIIDTIINQKAVNAQgdeskklyCIYVA 206
Cdd:PRK07165 113 ------LAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIINQKNTNVK--------CIYVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 207 VGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPmQYLAPYTGAAMGE---FFRDngmhALIAFDDLSKQAVAYRQMS 283
Cdd:PRK07165 179 IGQKRENLSRIYETLKEHDALKNTIIIDAPSTSPYE-QYLAPYVAMAHAEnisYNDD----VLIVFDDLTKHANIYREIA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 284 LLLRRPPGREAYPGDVFYLHSRLLERAAKMSDEKgagSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIR 363
Cdd:PRK07165 254 LLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK---TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 364 PAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYREMAAFAQFASDLDPATQKLLARGARLTELLKQPQYAPLSVAeqv 443
Cdd:PRK07165 331 PAIDIDLSVSRTGSSVQSKTITKVAGEISKIYRAYKRQLKLSMLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYSYR--- 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541254387 444 iSVFAGTK----GYLDNlpVADVQKfesAL--IAALKANDPS---IVAAIEADQqikpETETKLV-AFIENLLRTF 509
Cdd:PRK07165 408 -FVLLISKliswGLLKD--VKDEQK---ALdfIDYLIENDPDakkIFNKIKNNE----DVDDELMkNYFAFLLNQY 473
|
|
| ATP-synt_F1_alpha_C |
cd18113 |
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex ... |
384-509 |
9.93e-66 |
|
F1-ATP synthase alpha (A) subunit, C-terminal domain; The alpha (A) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic.
Pssm-ID: 349748 [Multi-domain] Cd Length: 126 Bit Score: 208.37 E-value: 9.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 384 MKQVAGKIKLELAQYREMAAFAQFASDLDPATQKLLARGARLTELLKQPQYAPLSVAEQVISVFAGTKGYLDNLPVADVQ 463
Cdd:cd18113 1 MKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKKQLERGERLTELLKQPQYSPLSVEEQVAILYAATNGYLDDIPVEKIK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2541254387 464 KFESALIAALKANDPSIVAAIEADQQIKPETETKLVAFIENLLRTF 509
Cdd:cd18113 81 EFEKELLEYLRSNHPDLLEEIEKTKKLSDELEEKLKEAIEEFKKSF 126
|
|
| ATP-synt_ab_C |
pfam00306 |
ATP synthase alpha/beta chain, C terminal domain; |
380-503 |
1.89e-65 |
|
ATP synthase alpha/beta chain, C terminal domain;
Pssm-ID: 425595 [Multi-domain] Cd Length: 126 Bit Score: 207.68 E-value: 1.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 380 QIKAMKQVAGKIKLELAQYREMAAFAQFASDLDPATQKLLARGARLTELLKQPQYAPLSVAEQVISVFAGTKGYLDNLPV 459
Cdd:pfam00306 1 QTKAMKKVAGSLRLDLAQYRELEAFAQFGSDLDEATKAQLDRGERLVELLKQPQYSPLSVEEQVIILYAATNGLLDDIPV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2541254387 460 ADVQKFESALIAALKANDPSIVAAIEADQQIKPETETKLVAFIE 503
Cdd:pfam00306 81 EKVKEFEKELLEYLRSNHPEILEEIEETKKLSDELEEKLKEAIE 124
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
98-375 |
1.78e-49 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 170.82 E-value: 1.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 98 VPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKT 177
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 178 ALIIDTIINQKA-VNaqgdeskklycIYVAVGQK-RSTVAQLVRTLEEYGvMEYSIVVAATASDPAPMQYLAPYTGAAMG 255
Cdd:cd01136 82 TLLGMIARNTDAdVN-----------VIALIGERgREVREFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 256 EFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMSDEkgaGSLTALPVIETQAGDV 335
Cdd:cd01136 150 EYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAG-NGEK---GSITAFYTVLVEGDDF 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2541254387 336 SAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRV 375
Cdd:cd01136 226 NDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
10-441 |
1.17e-48 |
|
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: 173.29 E-value: 1.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 10 EILKRQIADFDTEANVAETGQVLSVGDGIARVFGLaNVQAGELVDF---PGAGLKGMALNLEADNVGVVIFGDDKSIREG 86
Cdd:COG1157 2 DRLARLLARLEELPPVRVSGRVTRVVGLLIEAVGP-DASIGELCEIetaDGRPVLAEVVGFRGDRVLLMPLGDLEGISPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 87 DTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRe 166
Cdd:COG1157 81 ARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQR- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 167 liIGdr---qtGKTaliidTIINQKAVNAQGDeskklyciyVAVgqkrstVAqLV------------RTLEEYGvMEYSI 231
Cdd:COG1157 160 --IGifagsgvGKS-----TLLGMIARNTEAD---------VNV------IA-LIgergrevrefieDDLGEEG-LARSV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 232 VVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAA 311
Cdd:COG1157 216 VVVATSDEPPLMRLRAAYTATAIAEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 312 KMsdekGAGSLTAL------------PVIETqagdvsayiptnVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAA 379
Cdd:COG1157 296 NG----GKGSITAFytvlvegddmndPIADA------------VRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDI 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541254387 380 QIKAMKQVAGKIKLELAQYREMAafaqfasDL----------DPATQKLLARGARLTELLKQPQYAPLSVAE 441
Cdd:COG1157 360 VSPEHRALARRLRRLLARYEENE-------DLirigayqpgsDPELDEAIALIPAIEAFLRQGMDERVSFEE 424
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-436 |
1.02e-47 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 171.10 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 4 RPAEISEILKRQIADFDTEANVAETGQVLSVGDGIARVFGLaNVQAGELVDFPGAglKGmALNLEADNVG-------VVI 76
Cdd:PRK09099 1 ALAELSRLADALERELAALPAVRRTGKVVEVIGTLLRVSGL-DVTLGELCELRQR--DG-TLLQRAEVVGfsrdvalLSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 77 FGDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDV 156
Cdd:PRK09099 77 FGELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 157 LVPIGRGQRELIIGDRQTGKTaliidTIINQKAVNAQGDESkklycIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAAT 236
Cdd:PRK09099 157 LMTLGEGQRMGIFAPAGVGKS-----TLMGMFARGTQCDVN-----VIALIGERGREVREFIELILGEDGMARSVVVCAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 237 ASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMSDe 316
Cdd:PRK09099 227 SDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGE- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 317 kgAGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELA 396
Cdd:PRK09099 305 --TGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLA 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2541254387 397 QYREMAAFAQ---FASDLDPATQKLLARGARLTELLKQP--QYAP 436
Cdd:PRK09099 383 KHREVETLLQvgeYRAGSDPVADEAIAKIDAIRDFLSQRtdEYSD 427
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
78-443 |
2.12e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 164.93 E-value: 2.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 78 GDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVL 157
Cdd:PRK06936 77 GEMYGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 158 VPIGRGQRELIIGDRQTGKTALiIDTIINQKAVNAqgdeskklyCIYVAVGQKRSTVAQLV-RTLEEYGvMEYSIVVAAT 236
Cdd:PRK06936 157 LTCGEGQRMGIFAAAGGGKSTL-LASLIRSAEVDV---------TVLALIGERGREVREFIeSDLGEEG-LRKAVLVVAT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 237 ASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMSDE 316
Cdd:PRK06936 226 SDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG-QSDK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 317 kgaGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELA 396
Cdd:PRK06936 305 ---GSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLA 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2541254387 397 QYREMAAFAQ---FASDLDPATQKLLARGARLTELLKQPQYAPLSVAEQV 443
Cdd:PRK06936 382 KYEEVELLLQigeYQKGQDKEADQAIERIGAIRGFLRQGTHELSHFNETL 431
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
77-443 |
1.59e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 162.58 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 77 FGDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDG----KGPVMFSerrlVETKAPGIIPRKSVHEPMQTGIK 152
Cdd:PRK07721 72 YTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGsalpKGLAPVS----TDQDPPNPLKRPPIREPMEVGVR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 153 AIDVLVPIGRGQRELIIGDRQTGKTaliidTIINQKAVNAQGDESkklycIYVAVGQKRSTVAQLV-RTLEEYGvMEYSI 231
Cdd:PRK07721 148 AIDSLLTVGKGQRVGIFAGSGVGKS-----TLMGMIARNTSADLN-----VIALIGERGREVREFIeRDLGPEG-LKRSI 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 232 VVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAA 311
Cdd:PRK07721 217 VVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 312 kmSDEKgaGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKI 391
Cdd:PRK07721 297 --TNAS--GSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRF 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2541254387 392 KLELAQYRE------MAAFAQFAS-DLDPATQkllaRGARLTELLKQPQYAPLSVAEQV 443
Cdd:PRK07721 373 RELLSTYQNsedlinIGAYKRGSSrEIDEAIQ----FYPQIISFLKQGTDEKATFEESI 427
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
29-442 |
2.24e-44 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 161.91 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 29 GQVLSVGDGIARVfGLANVQAGELVDFPGAGLKGMALNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGLLGRV 108
Cdd:PRK06820 31 GPIVEIGPTLLRA-SLPGVAQGELCRIEPQGMLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 109 VDALGNPIDGkGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTaliidTIINQK 188
Cdd:PRK06820 110 LDGLGAPIDG-GPPLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKS-----TLLGML 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 189 AVNAQGDeskklyCIYVAVGQKRstvAQLVRTLEEYGVME----YSIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMH 264
Cdd:PRK06820 184 CADSAAD------VMVLALIGER---GREVREFLEQVLTPearaRTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 265 ALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSdekgAGSLTALPVIETQAGDVSAYIPTNVI 344
Cdd:PRK06820 255 VLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD----RGSITAFYTVLVEGDDMNEPVADEVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 345 SITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYREMAAFAQ---FASDLDPATQKLLAR 421
Cdd:PRK06820 331 SLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRvgeYQAGEDLQADEALQR 410
|
410 420
....*....|....*....|...
gi 2541254387 422 GARLTELLKQP--QYAPLSVAEQ 442
Cdd:PRK06820 411 YPAICAFLQQDhsETAHLETTLE 433
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
62-392 |
2.10e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 156.38 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 62 GMALNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRK 141
Cdd:PRK08472 56 GMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 142 SVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALIiDTIInqKAVNAQgdeskklycIYVA--VGQKRSTVAQLVr 219
Cdd:PRK08472 136 LIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLM-GMIV--KGCLAP---------IKVValIGERGREIPEFI- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 220 tleEY---GVMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYP 296
Cdd:PRK08472 203 ---EKnlgGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 297 GDVFYLHSRLLERAAKmsdEKGAGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVG 376
Cdd:PRK08472 280 PSVLSLLPQLMERAGK---EEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVM 356
|
330
....*....|....*.
gi 2541254387 377 SAAQIKAMKQVAGKIK 392
Cdd:PRK08472 357 NDIISPEHKLAARKFK 372
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
20-438 |
3.48e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 153.61 E-value: 3.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 20 DTEANVAETGQVLSVGDGIARVFGLAN-VQAGELVDFPGAG--LKGMALNLEADNVGVVIFGDDKSIREGDTVTRTG--Q 94
Cdd:PRK06002 19 APEPLVRIGGTVSEVTASHYRVRGLSRfVRLGDFVAIRADGgtHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKGplR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 95 IVDVPTGKGllgRVVDALGNPIDGKGPVMFSERRL-VETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQ 173
Cdd:PRK06002 99 IRPDPSWKG---RVINALGEPIDGLGPLAPGTRPMsIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 174 TGKTALIidtiinqkAVNAQGDESKKlycIYVA-VGQKRSTVAQLvrtLEEY--GVMEYSIVVAATaSDPAPM-QYLAPY 249
Cdd:PRK06002 176 VGKSTLL--------AMLARADAFDT---VVIAlVGERGREVREF---LEDTlaDNLKKAVAVVAT-SDESPMmRRLAPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 250 TGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmSDEKGAGSLTALPVIE 329
Cdd:PRK06002 241 TATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAG--PGAEGGGSITGIFSVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 330 TQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYRE------MAA 403
Cdd:PRK06002 319 VDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEEtrdlrlIGG 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 2541254387 404 FAQFA-SDLDPATQKLlargARLTELLKQPQYAPLS 438
Cdd:PRK06002 399 YRAGSdPDLDQAVDLV----PRIYEALRQSPGDPPS 430
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
63-431 |
3.23e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 147.92 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 63 MALNLEADNVGvviFGDD----------KSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVmFSERRlVET 132
Cdd:PRK08972 55 MAGELEAEVVG---FDGDllylmpieelRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPI-YTDQR-ASR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 133 KAPGIIP--RKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALIidtiinqkAVNAQGDESKklyCIYVA-VGQ 209
Cdd:PRK08972 130 HSPPINPlsRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLL--------GMMTRGTTAD---VIVVGlVGE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 210 KRSTVAQLVR-TLEEYGvMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRR 288
Cdd:PRK08972 199 RGREVKEFIEeILGEEG-RARSVVVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQAQREIALAVGE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 289 PPGREAYPGDVFYLHSRLLERAAKMSDekGAGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINV 368
Cdd:PRK08972 278 PPATKGYPPSVFAKLPALVERAGNGGP--GQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDI 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541254387 369 GLSVSRVG----SAAQIKAMKQVAGKIKLeLAQYREMAAFAQFASDLDPATQKLLARGARLTELLKQ 431
Cdd:PRK08972 356 EASISRVMpmviSEEHLEAMRRVKQVYSL-YQQNRDLISIGAYKQGSDPRIDNAIRLQPAMNAFLQQ 421
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
98-374 |
2.92e-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: 141.21 E-value: 2.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 98 VPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDrqtgkT 177
Cdd:cd01135 4 LPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSG-----S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 178 ALIIDTIINQKAVNAQ-GDESKKLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAMGE 256
Cdd:cd01135 79 GLPHNELAAQIARQAGvVGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 257 FFR-DNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMSDEKGagSLTALPVIETQA 332
Cdd:cd01135 159 YLAyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGRKG--SITQIPILTMPN 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2541254387 333 GDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSR 374
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
74-404 |
1.03e-35 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 137.82 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 74 VVIFGDDKSIRE--GDTVTRTGQIVDVPTGK--------GLLGRVVDALGNpIDGK-----GPVMFSERRLVETKAPGII 138
Cdd:PRK08149 48 VVGFQRERTILSliGNAQGLSRQVVLKPTGKplsvwvgeALLGAVLDPTGK-IVERfdappTVGPISEERVIDVAPPSYA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 139 PRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALiIDTIINQkavnAQGDeskklycIYVA--VGQKRSTVAQ 216
Cdd:PRK08149 127 ERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL-MNMLIEH----SEAD-------VFVIglIGERGREVTE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 217 LVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYP 296
Cdd:PRK08149 195 FVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 297 GDVFYLHSRLLERAAKMSdekgAGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVG 376
Cdd:PRK08149 275 ASVFDSLPRLLERPGATL----AGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVF 350
|
330 340
....*....|....*....|....*...
gi 2541254387 377 SAAQIKAMKQVAGKIKLELAQYREMAAF 404
Cdd:PRK08149 351 GQVTDPKHRQLAAAFRKLLTRLEELQLF 378
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
43-374 |
2.63e-35 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 137.26 E-value: 2.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 43 GLANVQAGELVDF---PGAGLKGMALNLEADNVGVVIFGDDKSIREGDTVTR-TGQIVDVPTGKGLLGRVVDALGNPIDG 118
Cdd:PRK04196 19 GVEGVAYGEIVEIelpNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRfTGEPLKLPVSEDMLGRIFDGLGRPIDG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 119 kGPVMFSERRLVETKAPgIIP--RKSVHEPMQTGIKAIDVLVPIGRGQRELIIgdrqTGkTALIIDTIINQKAVNAQ-GD 195
Cdd:PRK04196 99 -GPEIIPEKRLDINGAP-INPvaREYPEEFIQTGISAIDGLNTLVRGQKLPIF----SG-SGLPHNELAAQIARQAKvLG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 196 ESKKLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFR-DNGMHALIAFDDLSK 274
Cdd:PRK04196 172 EEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMHVLVILTDMTN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 275 QAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKMSDEKGagSLTALPVIETQAGDVSAYIPTNVISITDGQI 351
Cdd:PRK04196 252 YCEALREISAAREEVPGRRGYPG---YMYTDLatiYERAGRIKGKKG--SITQIPILTMPDDDITHPIPDLTGYITEGQI 326
|
330 340
....*....|....*....|...
gi 2541254387 352 FLETELFFKGIRPAINVGLSVSR 374
Cdd:PRK04196 327 VLSRELHRKGIYPPIDVLPSLSR 349
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
28-436 |
2.57e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 133.92 E-value: 2.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 28 TGQVLSVGDGIARVFgLANVQAGELVDF-PGAGLkGMALNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGLLG 106
Cdd:PRK07594 22 WGRIQDVSATLLNAW-LPGVFMGELCCIkPGEEL-AEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 107 RVVDALGNPIDGKgPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALIidtiin 186
Cdd:PRK07594 100 RVIDGFGRPLDGR-ELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLL------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 187 QKAVNAQGDESKKLyciyVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHAL 266
Cdd:PRK07594 173 AMLCNAPDADSNVL----VLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 267 IAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkMSDEkgaGSLTALPVIETQAGDVSAYIPTNVISI 346
Cdd:PRK07594 249 LLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEK---GSITAFYTVLVEGDDMNEPLADEVRSL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 347 TDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYRE---MAAFAQFASDLDPATQKLLARGA 423
Cdd:PRK07594 325 LDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEvelLIRIGEYQRGVDTDTDKAIDTYP 404
|
410
....*....|...
gi 2541254387 424 RLTELLKQPQYAP 436
Cdd:PRK07594 405 DICTFLRQSKDEV 417
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
98-452 |
3.07e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 134.09 E-value: 3.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 98 VPTGKGLLGRVVDALGNPIDGKGPVMFSERrlVETKAPGIIP--RKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTG 175
Cdd:PRK05688 103 LPMGMSMLGRVLDGAGRALDGKGPMKAEDW--VPMDGPTINPlnRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 176 KTALI-IDTIINQKAVNAQGdeskklyciyvAVGQKRSTVAQLV-RTLEEYGvMEYSIVVAATASDPAPMQYLAPYTGAA 253
Cdd:PRK05688 181 KSVLLgMMTRFTEADIIVVG-----------LIGERGREVKEFIeHILGEEG-LKRSVVVASPADDAPLMRLRAAMYCTR 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 254 MGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmSDEKGAGSLTALPVIETQAG 333
Cdd:PRK05688 249 IAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAG--NAEPGGGSITAFYTVLSEGD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 334 DVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQY---REMAAFAQFASD 410
Cdd:PRK05688 327 DQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYqqsRDLISVGAYVAG 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2541254387 411 LDPATQKLLARGARLTELLKQPQYAPLSVA---EQVISVFAGTKG 452
Cdd:PRK05688 407 GDPETDLAIARFPHLVQFLRQGLRENVSLAqsrEQLAAIFAPAAG 451
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
101-431 |
8.46e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 132.71 E-value: 8.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 101 GKGLLGRVVDALGNPIDGKGPVMFSErrLVETKAPGIIP--RKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTA 178
Cdd:PRK07196 93 GDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIHPlqRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 179 LI-IDTIINQKAVNAQGdeskklyciyvAVGQKRSTVAQLV-RTLEEYGvMEYSIVVAATASDPAPMQYLAPYTGAAMGE 256
Cdd:PRK07196 171 LLgMITRYTQADVVVVG-----------LIGERGREVKEFIeHSLQAAG-MAKSVVVAAPADESPLMRIKATELCHAIAT 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 257 FFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmsDEKGAGSLTALPVIETQAGDVS 336
Cdd:PRK07196 239 YYRDKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAG---NSSGNGTMTAIYTVLAEGDDQQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 337 AYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQY---REMAAFAQFASDLDP 413
Cdd:PRK07196 316 DPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYmaiKPLIPLGGYVAGADP 395
|
330
....*....|....*...
gi 2541254387 414 ATQKLLARGARLTELLKQ 431
Cdd:PRK07196 396 MADQAVHYYPAITQFLRQ 413
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
32-402 |
1.00e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 132.41 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 32 LSVGDGIARVFGLANVQAGELVDFPGaglkgmalnleaDNVGVVIFGDDKSIREG-DTVTRTGQIVDVPTgKGLLGRVVD 110
Cdd:PRK08927 38 LSVGARIVVETRGGRPVPCEVVGFRG------------DRALLMPFGPLEGVRRGcRAVIANAAAAVRPS-RAWLGRVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 111 ALGNPIDGKGPVMFSER-RLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALIidtiiNQKA 189
Cdd:PRK08927 105 ALGEPIDGKGPLPQGPVpYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLL-----SMLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 190 VNAQGDeskklyciyVAV----GQKRSTVAQLVR-TLEEYGvMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMH 264
Cdd:PRK08927 180 RNADAD---------VSVigliGERGREVQEFLQdDLGPEG-LARSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 265 ALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmSDEKGAGSLTALPVIETQAGDVSAYIPTNVI 344
Cdd:PRK08927 250 VLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAG--PGPIGEGTITGLFTVLVDGDDHNEPVADAVR 327
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541254387 345 SITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYREMA 402
Cdd:PRK08927 328 GILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADME 385
|
|
| ATP-synt_F1_alpha_N |
cd18116 |
F1-ATP synthase alpha (A) subunit, N-terminal domain; The alpha (A) subunit of the F1 complex ... |
27-94 |
3.62e-32 |
|
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: 117.55 E-value: 3.62e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541254387 27 ETGQVLSVGDGIARVFGLANVQAGELVDFPGaGLKGMALNLEADNVGVVIFGDDKSIREGDTVTRTGQ 94
Cdd:cd18116 1 EVGRVLSVGDGIARVYGLPNVMAGELVEFPG-GVKGMALNLEEDNVGVVLLGDYKLIKEGDSVKRTGR 67
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
64-469 |
8.81e-31 |
|
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: 124.45 E-value: 8.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 64 ALNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSV 143
Cdd:TIGR01039 44 AQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 144 HEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALIIDtIINQKAVNAQGdeskklYCIYVAVGQKRSTVAQLVRTLEE 223
Cdd:TIGR01039 124 VEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQE-LINNIAKEHGG------YSVFAGVGERTREGNDLYHEMKE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 224 YGVMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRD-NGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYL 302
Cdd:TIGR01039 197 SGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 303 HSRLLERAAKMSdekgAGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQI- 381
Cdd:TIGR01039 277 MGELQERITSTK----TGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVg 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 382 KAMKQVAGKIKLELAQYREMA-AFAQFASD-LDPATQKLLARGARLTELLKQPQYaplsVAEQvisvFAGTKGYLdnLPV 459
Cdd:TIGR01039 353 EEHYDVARGVQQILQRYKELQdIIAILGMDeLSEEDKLTVERARRIQRFLSQPFF----VAEV----FTGQPGKY--VPL 422
|
410
....*....|.
gi 2541254387 460 AD-VQKFESAL 469
Cdd:TIGR01039 423 KDtIRGFKEIL 433
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
65-400 |
1.48e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 120.47 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 65 LNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERrlVETKAPGI--IPRKS 142
Cdd:PRK06793 58 IAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQK--IKLDAPPIhaFEREE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 143 VHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTaliidTIINQKAVNAQGDESkklycIYVAVGQKRSTVAQLVRT-L 221
Cdd:PRK06793 136 ITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKS-----TLLGMIAKNAKADIN-----VISLVGERGREVKDFIRKeL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 222 EEYGvMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPgreaYPGDVFY 301
Cdd:PRK06793 206 GEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELP----IGGKTLL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 302 LHS---RLLERAAKMSDekgaGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSA 378
Cdd:PRK06793 281 MESymkKLLERSGKTQK----GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE 356
|
330 340
....*....|....*....|..
gi 2541254387 379 AQIKAMKQVAGKIKLELAQYRE 400
Cdd:PRK06793 357 IVSPNHWQLANEMRKILSIYKE 378
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
88-384 |
9.17e-29 |
|
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: 118.67 E-value: 9.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 88 TVTRTGQIVDVPTGKGLLGRVVDALGNPIDgKGPVMFSERRLVETKAPgIIPRKSVH--EPMQTGIKAIDVLVPIGRGQR 165
Cdd:TIGR01040 66 TCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPPVLAEDYLDINGQP-INPYARIYpeEMIQTGISAIDVMNSIARGQK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 166 ELIIGD-------------RQTGKTALIIDTIINQKAVNaqgdeskklYCI-YVAVGQKRSTVAQLVRTLEEYGVMEYSI 231
Cdd:TIGR01040 144 IPIFSAaglphneiaaqicRQAGLVKLPTKDVHDGHEDN---------FAIvFAAMGVNMETARFFKQDFEENGSMERVC 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 232 VVAATASDPAPMQYLAPYTGAAMGEFFR-DNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERA 310
Cdd:TIGR01040 215 LFLNLANDPTIERIITPRLALTTAEYLAyQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERA 294
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541254387 311 AKMsdEKGAGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSAAQIKAM 384
Cdd:TIGR01040 295 GRV--EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 366
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
98-438 |
1.98e-28 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 117.31 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 98 VPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKT 177
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 178 ALiIDTIinqkavnAQGdeSKKLYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAMGEF 257
Cdd:PRK05922 172 SL-LSTI-------AKG--SKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 258 FRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAkmSDEKgaGSLTALPVIETQAGDVSA 337
Cdd:PRK05922 242 FRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAG--NNDK--GSITALYAILHYPNHPDI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 338 YIPTnVISITDGQIFL--ETELFFKgirPAINVGLSVSRVGSAAQIKAMKQVAGKIKLELAQYREMAAFAQFASdLDPAT 415
Cdd:PRK05922 318 FTDY-LKSLLDGHFFLtpQGKALAS---PPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGA-YVPGQ 392
|
330 340
....*....|....*....|...
gi 2541254387 416 QKLLARGARLTELLKQPQYAPLS 438
Cdd:PRK05922 393 DAHLDRAVKLLPSIKQFLSQPLS 415
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
98-431 |
4.29e-28 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 116.81 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 98 VPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKT 177
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 178 ALiidtiINQKAVNAQGDeskklyCIYVA-VGQKRSTVAQLVRTLEEYGVMEYSIVVAAtasdPAPMQYLAPYTGAA--- 253
Cdd:PRK07960 190 VL-----LGMMARYTQAD------VIVVGlIGERGREVKDFIENILGAEGRARSVVIAA----PADVSPLLRMQGAAyat 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 254 -MGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDekGAGSLTALPVIETQA 332
Cdd:PRK07960 255 rIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGIS--GGGSITAFYTVLTEG 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 333 GDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRVGSA-------AQIKAMKQVagkikleLAQY---REMA 402
Cdd:PRK07960 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTAlideqhyARVRQFKQL-------LSSFqrnRDLV 405
|
330 340
....*....|....*....|....*....
gi 2541254387 403 AFAQFASDLDPATQKLLARGARLTELLKQ 431
Cdd:PRK07960 406 SVGAYAKGSDPMLDKAIALWPQLEAFLQQ 434
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
46-353 |
9.86e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 106.66 E-value: 9.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 46 NVQAGEL--VDFPGAGLKGMALNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGkGPVM 123
Cdd:PRK02118 22 GVGYGELatVERKDGSSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GPEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 124 FSERrlVETKAPGIIP--RKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKTALIIdtiinQKAVNAQGDeskklY 201
Cdd:PRK02118 101 EGEP--IEIGGPSVNPvkRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLA-----RIALQAEAD-----I 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 202 CIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFR-DNGMHALIAFDDLSKQAVAYR 280
Cdd:PRK02118 169 IILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTNFADALK 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541254387 281 QMSLLLRRPPGREAYPGDvfyLHSRLLERAAKMSDEKGAGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL 353
Cdd:PRK02118 249 EISITMDQIPSNRGYPGS---LYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYITEGQFYL 318
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
83-260 |
9.78e-21 |
|
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: 94.77 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 83 IREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGR 162
Cdd:COG0055 66 LVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 163 GQRELIIGDRQTGKTALIIDtIINQKAVNAQGdeskklYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSIVVAATASDPAP 242
Cdd:COG0055 146 GGKIGLFGGAGVGKTVLIME-LIHNIAKEHGG------VSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPG 218
|
170
....*....|....*...
gi 2541254387 243 MQYLAPYTGAAMGEFFRD 260
Cdd:COG0055 219 ARLRVALTALTMAEYFRD 236
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
98-375 |
6.31e-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: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 98 VPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGIIPRKSVHEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGKT 177
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 178 ALIIDtIINQKAVNAQGdeskklYCIYVAVGQKRSTVAQLVRTLEEYGVMEYSI-----VVAATASDPAPMQYLAPYTGA 252
Cdd:cd01133 82 VLIME-LINNIAKAHGG------YSVFAGVGERTREGNDLYHEMKESGVINLDGlskvaLVYGQMNEPPGARARVALTGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 253 AMGEFFRD-NGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMSDekgaGSLTALPVIETQ 331
Cdd:cd01133 155 TMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKK----GSITSVQAVYVP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2541254387 332 AGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSRV 375
Cdd:cd01133 231 ADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRI 274
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
101-374 |
2.70e-19 |
|
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: 88.02 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 101 GKGLLGRVVDALGNPI----DGKGPvmFSERRLVETKAPGIIPRKSV-----HEPMQTGIKAIDVLVPIGRGQRELIIGD 171
Cdd:cd01134 7 GPGLLGSIFDGIQRPLeviaETGSI--FIPRGVNVQRWPVRQPRPVKeklppNVPLLTGQRVLDTLFPVAKGGTAAIPGP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 172 RQTGKTaliidtIINQK-AVNAQGDeskklYCIYVAVGQKRSTVAQLVRTLEEY-------GVMEYSIVVAATASDPAPM 243
Cdd:cd01134 85 FGCGKT------VISQSlSKWSNSD-----VVIYVGCGERGNEMAEVLEEFPELkdpitgeSLMERTVLIANTSNMPVAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 244 QYLAPYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKM----SDE 316
Cdd:cd01134 154 REASIYTGITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPA---YLGARLaefYERAGRVrclgSPG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 317 KGaGSLTALPVIETQAGDVSAYIPTNVISITdgQIF--LETELFFKGIRPAINVGLSVSR 374
Cdd:cd01134 231 RE-GSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
384-451 |
1.63e-16 |
|
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: 74.02 E-value: 1.63e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 384 MKQVAGKIKLELAQYREMAAFAQFASD--LDPATQKLLARGARLTELLKQPQYAPLSVAEQVISVFAGTK 451
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDdaLSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
25-93 |
4.47e-16 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 72.58 E-value: 4.47e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541254387 25 VAETGQVLSVGDGIARVFGLANVQAGELVDFpGAGLKGMALNLEADNVGVVIFGDDKSIREGDTVTRTG 93
Cdd:pfam02874 2 VQVIGPVVDVEFGIGRLPGLLNALEVELVEF-GSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
83-458 |
7.87e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 76.62 E-value: 7.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 83 IREGDTVTRTGQIVDVPTGKGLLGRVVDALGNPIDGKGPVMFSERRLVETKAPGII---PRKSVHEpmqTGIKAIDVLVP 159
Cdd:CHL00060 81 LMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIqldTKLSIFE---TGIKVVDLLAP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 160 IGRGQRELIIGDRQTGKTALIIDtIINQKAvNAQGDESkklycIYVAVGQKRSTVAQLVRTLEEYGV-----MEYSIV-- 232
Cdd:CHL00060 158 YRRGGKIGLFGGAGVGKTVLIME-LINNIA-KAHGGVS-----VFGGVGERTREGNDLYMEMKESGVineqnIAESKVal 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 233 VAATASDPAPMQYLAPYTGAAMGEFFRD-NGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAA 311
Cdd:CHL00060 231 VYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERIT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 312 KMSDekgaGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFFKGIRPAINVGLSVSR------VGsaaqiKAMK 385
Cdd:CHL00060 311 STKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTmlqpriVG-----EEHY 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 386 QVAGKIKLELAQYREMA-AFAQFASDLDPATQKLL-ARGARLTELLKQPQYaplsVAEqvisVFAGT------------- 450
Cdd:CHL00060 382 ETAQRVKQTLQRYKELQdIIAILGLDELSEEDRLTvARARKIERFLSQPFF----VAE----VFTGSpgkyvglaetirg 453
|
410
....*....|...
gi 2541254387 451 -----KGYLDNLP 458
Cdd:CHL00060 454 fqlilSGELDGLP 466
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
25-324 |
5.40e-13 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 71.35 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 25 VAETGQVLSVGDGIARVFGLANVQAGELVDFPGAGLKGMALNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGL 104
Cdd:PRK04192 1 MMTKGKIVRVSGPLVVAEGMGGARMYEVVRVGEEGLIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 105 LGRVVDALGNPID----------GKG---------------------------------------------PVMFS---- 125
Cdd:PRK04192 81 LGSIFDGIQRPLDelaeksgdflERGvyvpaldrekkweftptvkvgdkveagdilgtvqetpsiehkimvPPGVSgtvk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 126 ------ERRLVETKA------------------PGIIPRKSV-----HEPMQTGIKAIDVLVPIGRGQRELIIGDRQTGK 176
Cdd:PRK04192 161 eivsegDYTVDDTIAvlededgegveltmmqkwPVRRPRPYKeklppVEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 177 TALIidtiiNQKAVNAQGDeskklYCIYVAVGQKRSTVAQlvrTLEEY--------G--VMEYSIVVAATASDPAPMQYL 246
Cdd:PRK04192 241 TVTQ-----HQLAKWADAD-----IVIYVGCGERGNEMTE---VLEEFpelidpktGrpLMERTVLIANTSNMPVAAREA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 247 APYTGAAMGEFFRDNGMHALIAFDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKM----SDEkga 319
Cdd:PRK04192 308 SIYTGITIAEYYRDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPA---YLASRLaefYERAGRVktlgGEE--- 381
|
....*
gi 2541254387 320 GSLTA 324
Cdd:PRK04192 382 GSVTI 386
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
203-367 |
1.04e-11 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 67.74 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 203 IYVAVGQKRStvaQLVRTLEEYG----------VMEYSIVVAATASDPAPMQYLAPYTGAAMGEFFRDNGMHALIAFDDL 272
Cdd:PRK14698 686 IYIGCGERGN---EMTDVLEEFPklkdpktgkpLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADST 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 273 SKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRLLE------RAAKMSDEKGAGSLTALPVIETQAGDVSAYIPTNVISI 346
Cdd:PRK14698 763 SRWAEALREISGRLEEMPGEEGYPA---YLASKLAEfyeragRVVTLGSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRV 839
|
170 180
....*....|....*....|.
gi 2541254387 347 TDGQIFLETELFFKGIRPAIN 367
Cdd:PRK14698 840 VKVFWALDADLARRRHFPAIN 860
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
28-94 |
1.72e-04 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 39.99 E-value: 1.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541254387 28 TGQVLSVGDGIARVFGLANVQAGELVDF------PGAGLKGMALNLEADNVGVVIFGDDKSIREGDTVTRTGQ 94
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIergdgnNETVLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
83-180 |
3.17e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 39.68 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 83 IREGDTVTrtGQIvDVPTGKGLLGRVVDALGNPIDGKG---------PVMFSERRLVETKAPGIIPRksvhepmqtgikA 153
Cdd:PRK12608 59 LRTGDVVE--GVA-RPRERYRVLVRVDSVNGTDPEKLArrphfddltPLHPRERLRLETGSDDLSMR------------V 123
|
90 100
....*....|....*....|....*..
gi 2541254387 154 IDVLVPIGRGQRELIIGDRQTGKTALI 180
Cdd:PRK12608 124 VDLVAPIGKGQRGLIVAPPRAGKTVLL 150
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
152-180 |
7.98e-03 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 37.96 E-value: 7.98e-03
10 20
....*....|....*....|....*....
gi 2541254387 152 KAIDVLVPIGRGQRELIIGDRQTGKTALI 180
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLL 33
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
32-117 |
9.17e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 38.85 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541254387 32 LSVGDGIARVFGLANVQAGELvdfpgaGLKGMALNLEADNVGVVIFGDDKSIREGDTVTRTGQIVDVPTGKGLLGRVVDA 111
Cdd:PRK14698 14 LVIADGMKGAKMYEVVRVGEL------GLIGEIIRLEGDKAVIQVYEETAGLKPGEPVEGTGSSLSVELGPGLLTSIYDG 87
|
....*.
gi 2541254387 112 LGNPID 117
Cdd:PRK14698 88 IQRPLE 93
|
|
| |
