|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-376 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 911.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 1 VSMNPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDLDTRLSIFETGIKVV 80
Cdd:CHL00060 73 VAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSIFETGIKVV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 81 DLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFAGVGERTREGNDLYAEMKESGVIVEKNLSDSKVALVY 160
Cdd:CHL00060 153 DLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIAESKVALVY 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 161 GQMNEPPGARMRVALTALTMAEYFRDVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITST 240
Cdd:CHL00060 233 GQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITST 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 241 KDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPWIVGEKHYEKAQSVKKTLQ 320
Cdd:CHL00060 313 KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQ 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4519356 321 RYKELQDIIAILGLDELSEEDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVSLA 376
Cdd:CHL00060 393 RYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLA 448
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-376 |
0e+00 |
|
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: 831.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 1 VSMNPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDLDTRLSIFETGIKVV 80
Cdd:COG0055 58 IAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 81 DLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFAGVGERTREGNDLYAEMKESGVIveknlsdSKVALVY 160
Cdd:COG0055 138 DLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVL-------DKTALVF 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 161 GQMNEPPGARMRVALTALTMAEYFRDVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITST 240
Cdd:COG0055 211 GQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITST 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 241 KDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPWIVGEKHYEKAQSVKKTLQ 320
Cdd:COG0055 291 KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQ 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4519356 321 RYKELQDIIAILGLDELSEEDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVSLA 376
Cdd:COG0055 371 RYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLE 426
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-376 |
0e+00 |
|
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: 741.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 1 VSMNPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDLDTRLSIFETGIKVV 80
Cdd:TIGR01039 55 IAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 81 DLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFAGVGERTREGNDLYAEMKESGVIveknlsdSKVALVY 160
Cdd:TIGR01039 135 DLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVI-------DKTALVY 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 161 GQMNEPPGARMRVALTALTMAEYFRDVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITST 240
Cdd:TIGR01039 208 GQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITST 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 241 KDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPWIVGEKHYEKAQSVKKTLQ 320
Cdd:TIGR01039 288 KTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQ 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4519356 321 RYKELQDIIAILGLDELSEEDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVSLA 376
Cdd:TIGR01039 368 RYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLK 423
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
24-301 |
0e+00 |
|
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: 604.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 24 VPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDLDTRLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 103
Cdd:cd01133 2 VPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 104 VLIMELINNIAKAHGGVSVFAGVGERTREGNDLYAEMKESGVIVEKNLSdsKVALVYGQMNEPPGARMRVALTALTMAEY 183
Cdd:cd01133 82 VLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGLS--KVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 184 FRDVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKDGSITSIQAVYVPADDLTDPAP 263
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 4519356 264 ATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQP 301
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
1-376 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.
Pssm-ID: 132348 [Multi-domain] Cd Length: 449 Bit Score: 541.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 1 VSMNPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDLDTRLSIFETGIKVV 80
Cdd:TIGR03305 50 IALTPTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 81 DLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFAGVGERTREGNDLYAEMKESGVIveknlsDSKVaLVY 160
Cdd:TIGR03305 130 DVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVL------DNTV-MVF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 161 GQMNEPPGARMRVALTALTMAEYFRDVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITST 240
Cdd:TIGR03305 203 GQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 241 KDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPWIVGEKHYEKAQSVKKTLQ 320
Cdd:TIGR03305 283 SDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLA 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 4519356 321 RYKELQDIIAILGLDELSEEDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVSLA 376
Cdd:TIGR03305 363 QYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQPFFTTEQFTGMKGKTVSLE 418
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
24-298 |
5.62e-134 |
|
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: 383.73 E-value: 5.62e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 24 VPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDLDTRLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKT 103
Cdd:cd19476 2 VPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 104 VLIMELINNIAKAHGGVSVFAGVGERTREGNDLYAEMKESGVIveknlsdSKVALVYGQMNEPPGARMRVALTALTMAEY 183
Cdd:cd19476 82 VLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAM-------ERTVVVANTANDPPGARMRVPYTGLTIAEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 184 FRDvNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKD--GSITSIQAVYVPADDLTDP 261
Cdd:cd19476 155 FRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDggGSITAIPAVSTPGDDLTDP 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 4519356 262 APATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTM 298
Cdd:cd19476 234 IPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
76-296 |
8.81e-98 |
|
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: 289.26 E-value: 8.81e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 76 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFAGVGERTREGNDLYAEMKESGVIveknlsdSK 155
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 156 VALVYGQMNEPPGARMRVALTALTMAEYFRDvNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQE 235
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4519356 236 RITSTKD--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTS 296
Cdd:pfam00006 150 RAGRVKGkgGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
5-358 |
6.77e-67 |
|
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: 217.59 E-value: 6.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 5 PTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVD---LDTRLsifETGIKVVD 81
Cdd:COG1157 73 DLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL---DTGVRAID 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 82 LLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHggVSVFAGVGERTRE-----GNDLYAE-MKESGVIVEKnlSDsk 155
Cdd:COG1157 150 GLLTVGRGQRIGIFAGSGVGKSTLLGMIARN-TEAD--VNVIALIGERGREvrefiEDDLGEEgLARSVVVVAT--SD-- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 156 valvygqmnEPPGARMRVALTALTMAEYFRDVNKqDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQE 235
Cdd:COG1157 223 ---------EPPLMRLRAAYTATAIAEYFRDQGK-NVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 236 RITSTKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTS-TMLQpwIVGEKHYEKAQS 314
Cdd:COG1157 293 RAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISrVMPD--IVSPEHRALARR 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 4519356 315 VKKTLQRYKELQDIIAIlG---------LDElseedrlIVARARKIERFLSQP 358
Cdd:COG1157 371 LRRLLARYEENEDLIRI-GayqpgsdpeLDE-------AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
24-296 |
2.77e-60 |
|
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: 195.47 E-value: 2.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 24 VPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPafvDLDTRLSI---FETGIKVVDLLAPYRRGGKIGLFGGAGV 100
Cdd:cd01136 2 IPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPP---NPLKRAPIeqpLPTGVRAIDGLLTCGEGQRIGIFAGSGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 101 GKTVLIMELINNIAKAhggVSVFAGVGERTREGNDLyaemkesgviVEKNLSD---SKVALVYGQMNEPPGARMRVALTA 177
Cdd:cd01136 79 GKSTLLGMIARNTDAD---VNVIALIGERGREVREF----------IEKDLGEeglKRSVLVVATSDESPLLRVRAAYTA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 178 LTMAEYFRDVNKqDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKDGSITSIQAVYVPADD 257
Cdd:cd01136 146 TAIAEYFRDQGK-KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDD 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 4519356 258 LTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTS 296
Cdd:cd01136 225 FNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
303-376 |
1.90e-52 |
|
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) 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 beta subunit of ATP synthase is catalytic.
Pssm-ID: 349745 [Multi-domain] Cd Length: 108 Bit Score: 169.58 E-value: 1.90e-52
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4519356 303 IVGEKHYEKAQSVKKTLQRYKELQDIIAILGLDELSEEDRLIVARARKIERFLSQPFFVAEVFTGSPGKYVSLA 376
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLK 74
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
3-359 |
3.57e-50 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 173.64 E-value: 3.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 3 MNPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVE----ETLPIHRKAPAFVDldtRLSI---FET 75
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVgpisEERVIDVAPPSYAE---RRPIrepLIT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 76 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFAGVGERTREGNDLYAEMKESGviveknlSDSK 155
Cdd:PRK08149 138 GVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS-------RREK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 156 VALVYGQMNEPPGARMRVALTALTMAEYFRDVNKqDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQE 235
Cdd:PRK08149 208 CVLVYATSDFSSVDRCNAALVATTVAEYFRDQGK-RVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 236 RITSTKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPwIVGEKHYEKAQSV 315
Cdd:PRK08149 287 RPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAF 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 4519356 316 KKTLQRYKELQDIIAiLG---LDELSEEDRLIVARArKIERFLSQPF 359
Cdd:PRK08149 366 RKLLTRLEELQLFID-LGeyrRGENADNDRAMDKRP-ALEAFLKQDV 410
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
22-357 |
2.08e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 171.79 E-value: 2.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 22 LAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDLDTRLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 101
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 102 KTVLiMELINNIAKAHggVSVFAGVGERTRE---------GNDLyaemkESGVIVEKNLSDSKVALVYGqmneppgarmr 172
Cdd:PRK08472 170 KSTL-MGMIVKGCLAP--IKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYG----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 173 vALTALTMAEYFRDVNKqDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKD-GSITSIQAV 251
Cdd:PRK08472 231 -AFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGkGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 252 YVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPwIVGEKHYEKAQSVKKTLQRYKELQDIIAI 331
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350
....*....|....*....|....*....|.
gi 4519356 332 ----LGLD-ELSEEdrliVARARKIERFLSQ 357
Cdd:PRK08472 388 gayqKGNDkELDEA----ISKKEFMEQFLKQ 414
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
18-331 |
4.28e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 168.75 E-value: 4.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 18 TGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDLDTRLSIFETGIKVVDLLAPYRRGGKIGLFGG 97
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 98 AGVGKTVLiMELINNIAKAHggVSVFAGVGERTREgndlyaeMKEsgvIVEKNLSD---SKVALVYGQMNEPPGARMRVA 174
Cdd:PRK07721 167 SGVGKSTL-MGMIARNTSAD--LNVIALIGERGRE-------VRE---FIERDLGPeglKRSIVVVATSDQPALMRIKGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 175 LTALTMAEYFRDvNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKDGSITSIQAVYVP 254
Cdd:PRK07721 234 YTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVD 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4519356 255 ADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLqPWIVGEKHYEKAQSVKKTLQRYKELQDIIAI 331
Cdd:PRK07721 313 GDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
6-357 |
5.26e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 168.45 E-value: 5.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 6 TEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEeTLPIHRKAPAFVDLDTRLSIFETGIKVVDLLAP 85
Cdd:PRK06820 81 SDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQPIEQMLTTGIRAIDGILS 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 86 YRRGGKIGLFGGAGVGKTVLIMELInniAKAHGGVSVFAGVGERTREgndlyaeMKEsgvIVEKNLSD---SKVALVYGQ 162
Cdd:PRK06820 160 CGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGRE-------VRE---FLEQVLTPearARTVVVVAT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 163 MNEPPGARMRVALTALTMAEYFRDVNKqDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKD 242
Cdd:PRK06820 227 SDRPALERLKGLSTATTIAEYFRDRGK-KVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 243 GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLqPWIVGEKHYEKAQSVKKTLQRY 322
Cdd:PRK06820 306 GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACY 384
|
330 340 350
....*....|....*....|....*....|....*....
gi 4519356 323 KELQDIIAI----LGLDELSEEdrlIVARARKIERFLSQ 357
Cdd:PRK06820 385 QEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
7-357 |
1.36e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 167.24 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 7 EGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVdldTRLSI---FETGIKVVDLL 83
Cdd:PRK06936 80 YGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPM---SRRLIetpLSLGVRVIDGL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 84 APYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFAGVGERTREgndlyaeMKEsgvIVEKNLSD---SKVALVY 160
Cdd:PRK06936 157 LTCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE-------VRE---FIESDLGEeglRKAVLVV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 161 GQMNEPPGARMRVALTALTMAEYFRDVNKQdVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITST 240
Cdd:PRK06936 224 ATSDRPSMERAKAGFVATSIAEYFRDQGKR-VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 241 KDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPwIVGEKHYEKAQSVKKTLQ 320
Cdd:PRK06936 303 DKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLA 381
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 4519356 321 RYKELQDIIAI----LGLDELSEEdrlIVARARKIERFLSQ 357
Cdd:PRK06936 382 KYEEVELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
4-357 |
1.26e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 164.38 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 4 NPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFN----VLGEPVDNMGLVKVE-ETLPIHrkapAFvDLDTRLSIFETGIK 78
Cdd:PRK06793 71 EQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSangeVLNEEAENIPLQKIKlDAPPIH----AF-EREEITDVFETGIK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 79 VVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHggVSVFAGVGERTREGND-LYAEMKESGViveknlsdSKVA 157
Cdd:PRK06793 146 SIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKAD--INVISLVGERGREVKDfIRKELGEEGM--------RKSV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 158 LVYGQMNEPPGARMRVALTALTMAEYFRDVNKqDVLFFVDNIFRFVQAGAEVSALLGRMPSAvGYQPTLATEMGGLQERI 237
Cdd:PRK06793 215 VVVATSDESHLMQLRAAKLATSIAEYFRDQGN-NVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 238 TSTKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPwIVGEKHYEKAQSVKK 317
Cdd:PRK06793 293 GKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRK 371
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 4519356 318 TLQRYKElQDIIAILGLDELSEEDRLIVARARKIE---RFLSQ 357
Cdd:PRK06793 372 ILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
32-333 |
2.97e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 161.32 E-value: 2.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 32 GRIFNVLGEPVDNMG-LVKVEETLPIHRKAPAFVdldTRLSI---FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIM 107
Cdd:PRK06002 107 GRVINALGEPIDGLGpLAPGTRPMSIDATAPPAM---TRARVetgLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 108 ELinniAKAHG-GVSVFAGVGERTREgndlYAEMkesgviVEKNLSD--SKVALVYGQMNEPPGARMRVALTALTMAEYF 184
Cdd:PRK06002 184 ML----ARADAfDTVVIALVGERGRE----VREF------LEDTLADnlKKAVAVVATSDESPMMRRLAPLTATAIAEYF 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 185 RDVNkQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKD--GSITSIQAVYVPADDLTDPA 262
Cdd:PRK06002 250 RDRG-ENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPV 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4519356 263 PATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQ-PWIVGEKhyEKAQSVKKTLQRYKELQDIIAILG 333
Cdd:PRK06002 329 ADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARhAWTPEQR--KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
5-331 |
3.89e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 158.32 E-value: 3.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 5 PTE---GLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKApafVDLDTRLSIFE---TGIK 78
Cdd:PRK08972 75 PIEelrGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPP---INPLSRRPITEpldVGVR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 79 VVDLLAPYRRGGKIGLFGGAGVGKTVLI-MELINNIAKahggVSVFAGVGERTREgndlyaeMKEsgvIVEKNLSD---S 154
Cdd:PRK08972 152 AINAMLTVGKGQRMGLFAGSGVGKSVLLgMMTRGTTAD----VIVVGLVGERGRE-------VKE---FIEEILGEegrA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 155 KVALVYGQMNEPPGARMRVALTALTMAEYFRDVNkQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQ 234
Cdd:PRK08972 218 RSVVVAAPADTSPLMRLKGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALV 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 235 ERIT--STKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDpLESTSTMLQPWIVGEKHYEKA 312
Cdd:PRK08972 297 ERAGngGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAID-IEASISRVMPMVISEEHLEAM 375
|
330
....*....|....*....
gi 4519356 313 QSVKKTLQRYKELQDIIAI 331
Cdd:PRK08972 376 RRVKQVYSLYQQNRDLISI 394
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
7-358 |
3.34e-43 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 155.70 E-value: 3.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 7 EGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPafvDLDTRLSI---FETGIKVVDLL 83
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPP---DPMSRRMVeapLPTGVRIVDGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 84 APYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFAGVGERTREGNDlYAEMkesgVIVEKNLSDSKValVYGQM 163
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMGMFARG---TQCDVNVIALIGERGREVRE-FIEL----ILGEDGMARSVV--VCATS 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 164 NEPPGARMRVALTALTMAEYFRDVNKQdVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKDG 243
Cdd:PRK09099 228 DRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 244 SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLqPWIVGEKHYEKAQSVKKTLQRYK 323
Cdd:PRK09099 307 SITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHR 385
|
330 340 350
....*....|....*....|....*....|....*....
gi 4519356 324 ELQDIIAI----LGLDELSEEdrlIVARARKIERFLSQP 358
Cdd:PRK09099 386 EVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
7-331 |
8.17e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 152.19 E-value: 8.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 7 EGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIhrkAPAFVDLDTRLSIFET---GIKVVDLL 83
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPM---DGPTINPLNRHPISEPldvGIRSINGL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 84 APYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHggVSVFAGVGERTREgndlyaeMKE--SGVIVEKNLSDSKValVYG 161
Cdd:PRK05688 163 LTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEAD--IIVVGLIGERGRE-------VKEfiEHILGEEGLKRSVV--VAS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 162 QMNEPPGARMRVALTALTMAEYFRDVNKqDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTK 241
Cdd:PRK05688 231 PADDAPLMRLRAAMYCTRIAEYFRDKGK-NVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 242 DG--SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDpLESTSTMLQPWIVGEKHYEKAQSVKKTL 319
Cdd:PRK05688 310 PGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAID-IEASISRVMPQVVDPEHLRRAQRFKQLW 388
|
330
....*....|..
gi 4519356 320 QRYKELQDIIAI 331
Cdd:PRK05688 389 SRYQQSRDLISV 400
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
5-331 |
2.40e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 147.79 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 5 PTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKV----EETLPihrkAPAFVdldtRLSIFE---TGI 77
Cdd:PRK07594 72 STIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRELPDVcwkdYDAMP----PPAMV----RQPITQplmTGI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 78 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFAGVGERTREGNDLyaemkesgviVEKNLSDS--- 154
Cdd:PRK07594 144 RAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGREVREF----------IDFTLSEEtrk 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 155 KVALVYGQMNEPPGARMRVALTALTMAEYFRDVNKQdVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQ 234
Cdd:PRK07594 211 RCVIVVATSDRPALERVRALFVATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 235 ERITSTKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLqPWIVGEKHYEKAQS 314
Cdd:PRK07594 290 ERTGMGEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAI 368
|
330
....*....|....*..
gi 4519356 315 VKKTLQRYKELQDIIAI 331
Cdd:PRK07594 369 LRRCLALYQEVELLIRI 385
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
5-357 |
4.94e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 147.05 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 5 PTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMG-LVKVEETLPIhRKAPAFVDLDTRLSI-FETGIKVVDL 82
Cdd:PRK08927 73 PLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGpLPQGPVPYPL-RAPPPPAHSRARVGEpLDLGVRALNT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 83 LAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAhggVSVFAGVGERTRE-----GNDLYAE-MKESGVIVEKnlSDskv 156
Cdd:PRK08927 152 FLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEgLARSVVVVAT--SD--- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 157 alvygqmnEPPGARMRVALTALTMAEYFRDvNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQER 236
Cdd:PRK08927 224 --------EPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLER 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 237 I--TSTKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTS-TMlqPWIVGEKHYEKAQ 313
Cdd:PRK08927 295 AgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSrTM--PGCNDPEENPLVR 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 4519356 314 SVKKTLQRYKELQDIIAI----LGLDelSEEDRLIvARARKIERFLSQ 357
Cdd:PRK08927 373 RARQLMATYADMEELIRLgayrAGSD--PEVDEAI-RLNPALEAFLRQ 417
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
8-357 |
1.67e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 137.33 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 8 GLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETL-----PIH--RKAPAFVDLDTrlsifetGIKVV 80
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLqqqlpQIHplQRRAVDTPLDV-------GVNAI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 81 DLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHggVSVFAGVGERTREGNDLYAE-MKESGViveknlsdSKVALV 159
Cdd:PRK07196 147 NGLLTIGKGQRVGLMAGSGVGKSVL-LGMITRYTQAD--VVVVGLIGERGREVKEFIEHsLQAAGM--------AKSVVV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 160 YGQMNEPPGARMRVALTALTMAEYFRDVNKqDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERI-T 238
Cdd:PRK07196 216 AAPADESPLMRIKATELCHAIATYYRDKGH-DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgN 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 239 STKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTS-TMLQpwIVGEKHYEKAQSVKK 317
Cdd:PRK07196 295 SSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISrCMSQ--VIGSQQAKAASLLKQ 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 4519356 318 TLQRYKELQDIIA----ILGLDELSEEdrlIVARARKIERFLSQ 357
Cdd:PRK07196 373 CYADYMAIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQ 413
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
6-359 |
1.59e-33 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 129.56 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 6 TEGLM-RGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIH--------RKAPA-FVdldtrlsifET 75
Cdd:PRK04196 59 TTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINgapinpvaREYPEeFI---------QT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 76 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVS----VFAGVGERTREGNDLYAEMKESGVIveknl 151
Cdd:PRK04196 130 GISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQIARQ-AKVLGEEEnfavVFAAMGITFEEANFFMEDFEETGAL----- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 152 sdSKVALVYGQMNEPPGARM---RVALTAltmAEYFRDVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLAT 228
Cdd:PRK04196 204 --ERSVVFLNLADDPAIERIltpRMALTA---AEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 229 EMGGLQER--ITSTKDGSITSIQAVYVPADDLTDPAPattfahlDAT-------TVLSRNLAAKGIYPAVDPLESTSTML 299
Cdd:PRK04196 279 DLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIVLSRELHRKGIYPPIDVLPSLSRLM 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4519356 300 QPWIVGEKHYEKAQSVKKTL----QRYKELQDIIAILGLDELSEEDRLIVARARKIE-RFLSQPF 359
Cdd:PRK04196 352 KDGIGEGKTREDHKDVANQLyaayARGKDLRELAAIVGEEALSERDRKYLKFADAFErEFVNQGF 416
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
21-300 |
2.69e-31 |
|
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: 120.02 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 21 PLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIH--------RKAPAfvdldtrlSIFETGIKVVDLLAPYRRGGKI 92
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINgppinpvaRIYPE--------EMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 93 GLFGGAGVGKTVLIMELINNiAKAHGGVS----VFAGVGERTREGNDLYAEMKESGVIveknlsdSKVALVYGQMNEPPG 168
Cdd:cd01135 73 PIFSGSGLPHNELAAQIARQ-AGVVGSEEnfaiVFAAMGVTMEEARFFKDDFEETGAL-------ERVVLFLNLANDPTI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 169 ARMRVALTALTMAEYFRDVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQER--ITSTKDGSIT 246
Cdd:cd01135 145 ERIITPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSIT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 4519356 247 SIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQ 300
Cdd:cd01135 225 QIPILTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
24-360 |
3.42e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 122.97 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 24 VPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHrkAPAFVDLD-TRLS-IFETGIKVVDLLAPYRRGGKIGLFGGAGVG 101
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGALI--TPPFNPLQrTPIEhVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 102 KTVLiMELINNIAKAHggVSVFAGVGERTREGND-----LYAEMKESGVIVEKNLSDSkvalvygqmnepPGARMRVALT 176
Cdd:PRK07960 188 KSVL-LGMMARYTQAD--VIVVGLIGERGREVKDfieniLGAEGRARSVVIAAPADVS------------PLLRMQGAAY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 177 ALTMAEYFRDvNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERITSTKD--GSITSIQAVYVP 254
Cdd:PRK07960 253 ATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISggGSITAFYTVLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 255 ADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDpLESTSTMLQPWIVGEKHYEKAQSVKKTLQRYKELQDIIAI--- 331
Cdd:PRK07960 332 GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAID-IEASISRAMTALIDEQHYARVRQFKQLLSSFQRNRDLVSVgay 410
|
330 340 350
....*....|....*....|....*....|
gi 4519356 332 -LGLDELSeeDRLIvARARKIERFLSQPFF 360
Cdd:PRK07960 411 aKGSDPML--DKAI-ALWPQLEAFLQQGIF 437
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
1-359 |
1.18e-30 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 121.16 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 1 VSMNPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNmglvkvEETLPIHRKAPAFVDLDTRLS------IFE 74
Cdd:PRK05922 69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDG------KEQLPKTHLKPLFSSPPSPMSrqpiqeIFP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 75 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFAGVGERTREGNDlYAEMKESGviveknLSD 153
Cdd:PRK05922 143 TGIKAIDAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQHKEG------LAA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 154 SKVALVYGQMNEPPGARMRVALTALTMAEYFRDvNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGL 233
Cdd:PRK05922 212 QRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 234 QERITSTKDGSITSIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRNLAAkgiyPAVDPLESTSTMLQPWIVgEKHYE 310
Cdd:PRK05922 291 TERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSARQLAL-PHHYA 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 4519356 311 KAQSVKKTLQRYKELQDIIAI----LGLD-ELSEEDRLIVArarkIERFLSQPF 359
Cdd:PRK05922 365 AAEELRSLLKAYHEALDIIQLgayvPGQDaHLDRAVKLLPS----IKQFLSQPL 414
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
73-357 |
1.68e-26 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 110.64 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 73 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLImeliNNIAK-AHGGVSVFAGVGERtreGNdlyaEMKEsgVIVE--- 148
Cdd:PRK04192 211 LITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQ----HQLAKwADADIVIYVGCGER---GN----EMTE--VLEEfpe 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 149 -------KNLSDSKVaLVYGQMNEPPGARMRVALTALTMAEYFRDVNkQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVG 221
Cdd:PRK04192 278 lidpktgRPLMERTV-LIANTSNMPVAAREASIYTGITIAEYYRDMG-YDVLLMADSTSRWAEALREISGRLEEMPGEEG 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 222 YQPTLATEMGGLQER----IT-STKDGSITSIQAVYVPADDLTDPapaTTFAHLDATTV---LSRNLAAKGIYPAVDPLE 293
Cdd:PRK04192 356 YPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLT 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4519356 294 STS---TMLQPWI---VGEKHYEKAQSVKKTLQRYKELQDIIAILGLDELSEEDRLIVARARKI-ERFLSQ 357
Cdd:PRK04192 433 SYSlylDQVAPWWeenVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-296 |
4.86e-26 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 108.85 E-value: 4.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 1 VSMNPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDLDTRLSIFETGIKVV 80
Cdd:PRK13343 74 VLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 81 DLLAPYRRGGKIGLFGGAGVGKTVLIMELInnIAKAHGGV-SVFAGVGERTREGNDLYAEMKESGvivekNLSDSKValV 159
Cdd:PRK13343 154 DALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDViCVYVAIGQKASAVARVIETLREHG-----ALEYTTV--V 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 160 YGQMNEPPGARMRVALTALTMAEYFRDvNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYqP--------------- 224
Cdd:PRK13343 225 VAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY-Pgdifylhsrlleraa 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4519356 225 TLATEMGGlqeritstkdGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTS 296
Cdd:PRK13343 303 KLSPELGG----------GSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVS 364
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
21-296 |
2.93e-25 |
|
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: 103.42 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 21 PLAVPVGKVTLGRIFNVLGEPVDNMGLVK--------------VEETLPIHRKAPAFVDLdtrlsifETGIKVVDLLAPY 86
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGsifiprgvnvqrwpVRQPRPVKEKLPPNVPL-------LTGQRVLDTLFPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 87 RRGGKIGLFGGAGVGKTVlimeLINNIAK-AHGGVSVFAGVGERtreGNDLYAEMKE----SGVIVEKNLSDsKVALVYG 161
Cdd:cd01134 74 AKGGTAAIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGER---GNEMAEVLEEfpelKDPITGESLME-RTVLIAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 162 QMNEPPGARMRVALTALTMAEYFRDVNKqDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERI---- 237
Cdd:cd01134 146 TSNMPVAAREASIYTGITIAEYFRDMGY-NVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvr 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4519356 238 ---TSTKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTS 296
Cdd:cd01134 225 clgSPGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
18-357 |
9.86e-23 |
|
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: 99.03 E-value: 9.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 18 TGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETL-----PIHRKAPAFVDldtrlSIFETGIKVVDLLAPYRRGGKI 92
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLdingqPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 93 GLFGGAGVGKTvlimELINNIAKAHGGVSvfagvgertREGNDLYAEMKESGVIV------------------EKNLSDS 154
Cdd:TIGR01040 145 PIFSAAGLPHN----EIAAQICRQAGLVK---------LPTKDVHDGHEDNFAIVfaamgvnmetarffkqdfEENGSME 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 155 KVALVYGQMNEPPGARMRVALTALTMAEYFRDVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQ 234
Cdd:TIGR01040 212 RVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIY 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 235 ERI--TSTKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTSTMLQPWIvGEKHYEKA 312
Cdd:TIGR01040 292 ERAgrVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEGMTRKD 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 4519356 313 QS-VKKTL-QRY---KELQDIIAILGLDELSEEDRLIVARARKIER-FLSQ 357
Cdd:TIGR01040 371 HSdVSNQLyACYaigKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
120-369 |
9.57e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 94.32 E-value: 9.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 120 VSVFAGVGERTREGNDLYAEM-KESGVIVEKNLSDSKVaLVYGQMNEPPGARMRVALTALTMAEYFRDVNkQDVLFFVDN 198
Cdd:PRK14698 684 VVIYIGCGERGNEMTDVLEEFpKLKDPKTGKPLMERTV-LIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADS 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 199 IFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQER----ITSTKD---GSITSIQAVYVPADDLTDPAPATTFAHLD 271
Cdd:PRK14698 762 TSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERagrvVTLGSDyrvGSVSVIGAVSPPGGDFSEPVVQNTLRVVK 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 272 ATTVLSRNLAAKGIYPAVDPLESTS---TMLQPWI---VGEKHYEKAQSVKKTLQRYKELQDIIAILGLDELSEEDRLIV 345
Cdd:PRK14698 842 VFWALDADLARRRHFPAINWLTSYSlyvDAVKDWWhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAIL 921
|
250 260
....*....|....*....|....*
gi 4519356 346 ARARKI-ERFLSQPFFvAEVFTGSP 369
Cdd:PRK14698 922 LVARMLrEDYLQQDAF-DEVDTYCP 945
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
22-296 |
6.25e-20 |
|
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: 88.38 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 22 LAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDldtRLSIFE---TGIKVVDLLAPYRRGGKIGLFGGA 98
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIP---RQSVNEplqTGIKAIDSLIPIGRGQRELIIGDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 99 GVGKTVLIMELINNiAKAHGGVSVFAGVGERTREGNDLYAEMKESGVIveknlsdSKVALVYGQMNEPPGARMRVALTAL 178
Cdd:cd01132 79 QTGKTAIAIDTIIN-QKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAM-------EYTIVVAATASDPAPLQYLAPYAGC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 179 TMAEYFRDvNKQDVLFFVDNIFRFVQAGAEVSALLGR------MPSAVGYqptLATEmggLQERITSTKD----GSITSI 248
Cdd:cd01132 151 AMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFY---LHSR---LLERAAKLSDelggGSLTAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 4519356 249 QAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVDPLESTS 296
Cdd:cd01132 224 PIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
1-217 |
4.10e-18 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 85.50 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 1 VSMNPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVDldtRLSIFE---TGI 77
Cdd:PRK09281 74 VILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHEplqTGI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 78 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFAGVGErtregndlyaemKESGV--IVEKnLSDsk 155
Cdd:PRK09281 151 KAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN-QKGKDVICIYVAIGQ------------KASTVaqVVRK-LEE-- 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4519356 156 valvYGQM----------NEPPGARMRVALTALTMAEYFRDvNKQDVLFFVDNIFRfvQAGA--EVSALLGRMP 217
Cdd:PRK09281 215 ----HGAMeytivvaataSDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSK--QAVAyrQLSLLLRRPP 281
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
308-371 |
5.40e-18 |
|
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: 77.48 E-value: 5.40e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4519356 308 HYEKAQSVKKTLQRYKELQDIIAILGLDELSEEDRLIVARARKIERFLSQPFFVAEVFTGSPGK 371
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
6-266 |
3.97e-17 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 82.39 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 6 TEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETL-------PIHRKAPAfvdldtrlSIFETGIK 78
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDGGPELEGEPIEiggpsvnPVKRIVPR--------EMIRTGIP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 79 VVDLLAPYRRGGKIGLFGGAGVGKTVLIMelinNIA-KAHGGVSVFAGVGERtregNDLYAEMKESgviVEKNLSDSKVA 157
Cdd:PRK02118 130 MIDVFNTLVESQKIPIFSVSGEPYNALLA----RIAlQAEADIIILGGMGLT----FDDYLFFKDT---FENAGALDRTV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 158 LVYGQMNEPPGARMRVALTALTMAEYFRDVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLATEMGGLQERI 237
Cdd:PRK02118 199 MFIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKA 278
|
250 260 270
....*....|....*....|....*....|
gi 4519356 238 TSTKD-GSITSIQAVYVPADDLTDPAPATT 266
Cdd:PRK02118 279 VDFEDgGSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
7-290 |
1.06e-13 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 71.92 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 7 EGLM--RGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVDNMGLVKVEETLPIHRKAPAFVdldTRLSIFE---TGIKVVD 81
Cdd:CHL00059 57 DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRRSVYEplqTGLIAID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 82 LLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFAGVGERTREGNDLYAEMKESG-----VIVEKNlSDSKV 156
Cdd:CHL00059 134 SMIPIGRGQRELIIGDRQTGKTAVATDTILN-QKGQNVICVYVAIGQKASSVAQVVTTLQERGameytIVVAET-ADSPA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 157 ALVYgqmneppgarmrVA-LTALTMAEYFRdVNKQDVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYqP----------- 224
Cdd:CHL00059 212 TLQY------------LApYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY-Pgdvfylhsrll 277
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 225 ----TLATEMGGlqeritstkdGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVD 290
Cdd:CHL00059 278 eraaKLSSQLGE----------GSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAIN 337
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
3-290 |
1.45e-10 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 62.75 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 3 MNPTEGLMRGMDVLDTGKPLAVPVGKVTLGRIFNVLGEPVD------NMGLVKVEETL-PIHRKAPAFVDLDTRLSIFET 75
Cdd:PTZ00185 96 MDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPvglltrSRALLESEQTLgKVDAGAPNIVSRSPVNYNLLT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 76 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN-------IAKAHGGVSVFAGVGERTREGNDLYAEMKESGVIVE 148
Cdd:PTZ00185 176 GFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINqvrinqqILSKNAVISIYVSIGQRCSNVARIHRLLRSYGALRY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 149 KNLSDSKVAlvygqmnEPPGARMRVALTALTMAEYFRDVNKQdVLFFVDNIFRFVQAGAEVSALLGRMPSAVGYQPTLAT 228
Cdd:PTZ00185 256 TTVMAATAA-------EPAGLQYLAPYSGVTMGEYFMNRGRH-CLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFY 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4519356 229 EMGGLQERIT----STKDGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRNLAAKGIYPAVD 290
Cdd:PTZ00185 328 LHSRLLERAAmlspGKGGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVN 393
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
1-22 |
6.82e-06 |
|
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) 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, 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 beta subunit of ATP synthase is catalytic.
Pssm-ID: 349739 [Multi-domain] Cd Length: 76 Bit Score: 43.66 E-value: 6.82e-06
10 20
....*....|....*....|..
gi 4519356 1 VSMNPTEGLMRGMDVLDTGKPL 22
Cdd:cd18115 55 IAMDSTDGLVRGMEVIDTGAPI 76
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
88-216 |
1.65e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.29 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 88 RGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFAgvGERTREGNDLYAEmkesgviveknlsdskvaLVYGQMNEPP 167
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID--GEDILEEVLDQLL------------------LIIVGGKKAS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 4519356 168 GARMRVALTALTMAEYFRdvnkQDVLFFvDNIFRFVQAGAEVSALLGRM 216
Cdd:smart00382 61 GSGELRLRLALALARKLK----PDVLIL-DEITSLLDAEQEALLLLLEE 104
|
|
| ATP-synt_V_A-type_beta_C |
cd18112 |
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ... |
323-357 |
1.50e-04 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the 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 Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 40.49 E-value: 1.50e-04
10 20 30
....*....|....*....|....*....|....*.
gi 4519356 323 KELQDIIAILGLDELSEEDRLIVARARKIE-RFLSQ 357
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
78-333 |
2.66e-04 |
|
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: 42.19 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 78 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFAG-VGERTREGNDlyaeMKESGviveknlsdsKV 156
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSV----------KG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 157 ALVYGQMNEPPGARMRVALTALTMAEyfRDV-NKQDVLFFVDNIFRFVQAGAEVSALLGRMPSavgyqptlatemGGLQ- 234
Cdd:cd01128 71 EVVASTFDEPPERHVQVAEMVIEKAK--RLVeHGKDVVILLDSITRLARAYNTVVPSSGKTLS------------GGVDa 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 235 ------ERITST-----KDGSITSIQAVYVP----ADDLtdpapatTFAHLDAT----TVLSRNLAAKGIYPAVDPLESt 295
Cdd:cd01128 137 nalhkpKRFFGAarnieEGGSLTIIATALVDtgsrMDEV-------IFEEFKGTgnmeLVLDRKLAEKRIFPAIDILKS- 208
|
250 260 270
....*....|....*....|....*....|....*...
gi 4519356 296 STMLQPWIVGEKHYEKAQSVKKTLQRYKELQDIIAILG 333
Cdd:cd01128 209 GTRKEELLLTPEELQKIWLLRRILSPMDPIEAMEFLLK 246
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
319-357 |
7.46e-04 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the 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 Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 38.52 E-value: 7.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 4519356 319 LQRYKELQDIIAILGLDELSEEDRLIVARARKI-ERFLSQ 357
Cdd:cd18111 12 LQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
304-358 |
2.75e-03 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 35.87 E-value: 2.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4519356 304 VGEKHYEKAQSVKKTLQRYKELQDIIAIlG---------LDElseedrlIVARARKIERFLSQP 358
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
58-360 |
3.17e-03 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 39.57 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 58 RKAPAF---VDLDTRLSIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFAGVGERTR 131
Cdd:PRK07165 106 NTSSIFnlaHGLMTVKTLNEqlyTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIALNTIIN-QKNTNVKCIYVAIGQKRE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 132 EGNDLYAEMKESGVIVEKNLSDSKVALVYGQMNEPpgarmrvaLTALTMAEYFRdvNKQDVLFFVD------NIFRfvqa 205
Cdd:PRK07165 185 NLSRIYETLKEHDALKNTIIIDAPSTSPYEQYLAP--------YVAMAHAENIS--YNDDVLIVFDdltkhaNIYR---- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 206 gaEVSALLGR------MPSAVGYQPTlatemgGLQERITSTKDG-SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSR 278
Cdd:PRK07165 251 --EIALLTNKpvgkeaFPGDMFFAHS------KLLERAGKFKNRkTITALPILQTVDNDITSLISSNIISITDGQIVTSS 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4519356 279 NLAAKGIYPAVDPLESTSTMLQPwiVGEKHYEK-AQSVKKTLQRYKElQDIIAILGLDeLSEEDRLIVARARKIERFLSQ 357
Cdd:PRK07165 323 DLFASGKLPAIDIDLSVSRTGSS--VQSKTITKvAGEISKIYRAYKR-QLKLSMLDYD-LNKETSDLLFKGKMIEKMFNQ 398
|
...
gi 4519356 358 PFF 360
Cdd:PRK07165 399 KGF 401
|
|
| |
