|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-401 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 961.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 1 LGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSI 80
Cdd:CHL00060 65 LGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLSI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 81 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEENIS 160
Cdd:CHL00060 145 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 161 ESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGT 240
Cdd:CHL00060 225 ESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGS 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 241 LQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGQEHYETA 320
Cdd:CHL00060 305 LQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 321 QGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIKGFQLILSGDLDA 400
Cdd:CHL00060 385 QRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDG 464
|
.
gi 28188339 401 L 401
Cdd:CHL00060 465 L 465
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-401 |
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: 845.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 1 LGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSI 80
Cdd:COG0055 50 LGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 81 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINeenis 160
Cdd:COG0055 130 LETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD----- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 161 esKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGT 240
Cdd:COG0055 205 --KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 241 LQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGQEHYETA 320
Cdd:COG0055 283 LQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 321 QGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIKGFQLILSGDLDA 400
Cdd:COG0055 363 REVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDD 442
|
.
gi 28188339 401 L 401
Cdd:COG0055 443 L 443
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-401 |
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: 753.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 1 LGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSI 80
Cdd:TIGR01039 47 LGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 81 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINeenis 160
Cdd:TIGR01039 127 LETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID----- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 161 esKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGT 240
Cdd:TIGR01039 202 --KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 241 LQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGQEHYETA 320
Cdd:TIGR01039 280 LQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 321 QGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIKGFQLILSGDLDA 400
Cdd:TIGR01039 360 RGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDH 439
|
.
gi 28188339 401 L 401
Cdd:TIGR01039 440 L 440
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
31-309 |
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: 584.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 31 SVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 110
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 111 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEENISesKVALVYGQMNEPPGARMRVGLTALTMAE 190
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGLS--KVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 191 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGSITSIQAVYVPADDLTDPA 270
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 28188339 271 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 309
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
1-399 |
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: 537.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 1 LGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSI 80
Cdd:TIGR03305 42 LDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 81 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEenis 160
Cdd:TIGR03305 122 FETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 161 eskVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGT 240
Cdd:TIGR03305 198 ---TVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 241 LQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGQEHYETA 320
Cdd:TIGR03305 275 LEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLA 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28188339 321 QGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIKGFQLILSGDLD 399
Cdd:TIGR03305 355 REVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLERFLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQ 433
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
31-306 |
3.32e-133 |
|
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: 382.57 E-value: 3.32e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 31 SVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 110
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 111 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVineenisESKVALVYGQMNEPPGARMRVGLTALTMAE 190
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 191 YFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTK--EGSITSIQAVYVPADDLTD 268
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 28188339 269 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 306
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
84-304 |
1.04e-86 |
|
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: 261.91 E-value: 1.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 84 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESKVIneeniseSK 163
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 164 VALVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQE 243
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28188339 244 RITSTKE--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 304
Cdd:pfam00006 150 RAGRVKGkgGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
311-401 |
1.27e-63 |
|
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: 199.24 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 311 IVGQEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLIETIKGF 390
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90
....*....|.
gi 28188339 391 QLILSGDLDAL 401
Cdd:cd18110 81 KEILDGEYDDL 91
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
3-366 |
6.15e-62 |
|
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: 205.65 E-value: 6.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 3 DNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQ---LDTKLs 79
Cdd:COG1157 63 GDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 80 ifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN----------IAkahggvsvfggvgERTREGNDlYMEmk 149
Cdd:COG1157 142 --DTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNteadvnvialIG-------------ERGREVRE-FIE-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 150 esKVINEENISESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG 229
Cdd:COG1157 204 --DDLGEEGLARSVV--VVATSDEPPLMRLRAAYTATAIAEYFRDQGK-NVLLLMDSLTRFAMAQREIGLAAGEPPATRG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 230 YQPTLSTEMGTLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMLQ 308
Cdd:COG1157 279 YPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISrVMPD 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28188339 309 pwIVGQEHYETAQGVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 366
Cdd:COG1157 359 --IVSPEHRALARRLRRLLARYEENEDLIRI-GayqpgsdpeLDE-------AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
31-304 |
1.26e-55 |
|
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: 183.92 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 31 SVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 110
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 111 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYMEmkesKVINEENISESkvALVYGQMNEPPGARMRVGLTALTMAE 190
Cdd:cd01136 81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGLKRS--VLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 191 YFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGSITSIQAVYVPADDLTDPA 270
Cdd:cd01136 151 YFRDQGK-KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....
gi 28188339 271 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 304
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
12-365 |
3.23e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 166.91 E-value: 3.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 12 SATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDElGPVDSTITLPIHRSAPafTQLDTKL--SIFETGIKVVD 89
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPP--SPLTRQPieQMLTTGIRAID 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 90 LLAPYRRGGKIGLFGGAGVGKTVLIMELInniAKAHGGVSVFGGVGERTREGNDlYMEmkesKVINEEniSESKVALVYG 169
Cdd:PRK06820 156 GILSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVRE-FLE----QVLTPE--ARARTVVVVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 170 QMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTK 249
Cdd:PRK06820 226 TSDRPALERLKGLSTATTIAEYFRDRGK-KVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 250 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVKQTLQR 329
Cdd:PRK06820 305 RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLAC 383
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 28188339 330 YKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 365
Cdd:PRK06820 384 YQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
16-365 |
1.10e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 165.70 E-value: 1.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 16 GLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQ---LDTKLSifeTGIKVVDLLA 92
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 93 PYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREgndlYMEMKESKvINEENISESkvALVYGQMN 172
Cdd:PRK06936 158 TCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKA--VLVVATSD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 173 EPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGS 252
Cdd:PRK06936 228 RPSMERAKAGFVATSIAEYFRDQGKR-VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 253 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQTLQRYKE 332
Cdd:PRK06936 307 ITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350
....*....|....*....|....*....|....*..
gi 28188339 333 LQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 365
Cdd:PRK06936 386 VELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
11-367 |
1.84e-46 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 164.78 E-value: 1.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 11 MSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTIT----LPIHRSAPAFTQLDTKLSIFETGIK 86
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGPiseeRVIDVAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 87 VVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYMEMKESKvineeniSESKVAL 166
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS-------RREKCVL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 167 VYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERIT 246
Cdd:PRK08149 211 VYATSDFSSVDRCNAALVATTVAEYFRDQGK-RVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 247 STKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQT 326
Cdd:PRK08149 290 ATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAFRKL 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 28188339 327 LQRYKELQDIIAiLG---LDELSEEDRlTVARARKIERFLSQPF 367
Cdd:PRK08149 369 LTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDV 410
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
15-366 |
3.13e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 159.16 E-value: 3.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 15 DGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQ---LDTKLSifeTGIKVVDLL 91
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 92 APYRRGGKIGLFGGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEMkeskVINEENISESKV 164
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMGMFargtqcdVNVIA----------LIGERGREVRE-FIEL----ILGEDGMARSVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 165 alVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQER 244
Cdd:PRK09099 223 --VCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 245 ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVK 324
Cdd:PRK09099 300 AGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLR 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 28188339 325 QTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQP 366
Cdd:PRK09099 379 QLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
3-365 |
7.13e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 155.66 E-value: 7.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 3 DNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPV--------DSTITLPIHRsAPAFTQL 74
Cdd:PRK05688 74 GDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMkaedwvpmDGPTINPLNR-HPISEPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 75 DTklsifetGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREgndlymeMKE--SK 152
Cdd:PRK05688 153 DV-------GIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVVGLIG--ERGRE-------VKEfiEH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 153 VINEENISESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQP 232
Cdd:PRK05688 216 ILGEEGLKRSVV--VASPADDAPLMRLRAAMYCTRIAEYFRDKGK-NVLLLMDSLTRFAQAQREIALAIGEPPATKGYPP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 233 TLSTEMGTLQERITSTKEG--SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPW 310
Cdd:PRK05688 293 SVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQ 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 28188339 311 IVGQEHYETAQGVKQTLQRYKELQDIIAI----LGLDelsEEDRLTVARARKIERFLSQ 365
Cdd:PRK05688 372 VVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
16-339 |
1.21e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 154.86 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 16 GLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHrsAPAFTQLDTKlSIFE---TGIKVVDLLA 92
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 93 PYRRGGKIGLFGGAGVGKTVLI-MELINNIAKAhggvSVFGGVGERTREgndlymeMKE--SKVINEENISESKValVYG 169
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGRE-------VKEfiEEILGEEGRARSVV--VAA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 170 QMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERIT--S 247
Cdd:PRK08972 225 PADTSPLMRLKGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 248 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVKQTL 327
Cdd:PRK08972 304 PGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVY 382
|
330
....*....|..
gi 28188339 328 QRYKELQDIIAI 339
Cdd:PRK08972 383 SLYQQNRDLISI 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
30-365 |
4.41e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 152.92 E-value: 4.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 30 LSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 109
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 110 KTVLiMELINNIAKAhgGVSVFGGVGERTRE---------GNDLymemkESKVINEENISESKVALVYGqmneppgarmr 180
Cdd:PRK08472 170 KSTL-MGMIVKGCLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYG----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 181 vGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTK-EGSITSIQAV 259
Cdd:PRK08472 231 -AFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 260 YVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQTLQRYKELQDIIAI 339
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350
....*....|....*....|....*....|.
gi 28188339 340 ----LGLD-ELSEedrlTVARARKIERFLSQ 365
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
40-341 |
4.61e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 150.53 E-value: 4.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 40 GRIFNVLGEPVDELGPVDS-TITLPIHRSAPAF---TQLDTKlsiFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIM 115
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAmtrARVETG---LRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 116 ELinniAKA-HGGVSVFGGVGERTREgndlYMEMKESKVINeeniSESKVALVYGQMNEPPGARMRVGLTALTMAEYFRD 194
Cdd:PRK06002 184 ML----ARAdAFDTVVIALVGERGRE----VREFLEDTLAD----NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 195 VNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKE--GSITSIQAVYVPADDLTDPAPA 272
Cdd:PRK06002 252 RG-ENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVAD 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 273 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ-PWIVGQEhyETAQGVKQTLQRYKELQDIIAILG 341
Cdd:PRK06002 331 SIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARhAWTPEQR--KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
26-339 |
6.40e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 149.87 E-value: 6.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 26 TGAPLSVPVGEATLGRIFNVLGEPVD--ELGPVDSTItlPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLF 103
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDgsALPKGLAPV--STDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 104 GGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEmkesKVINEENISESKValVYGQMNEPPG 176
Cdd:PRK07721 165 AGSGVGKSTLMGMIarntsadLNVIA----------LIGERGREVRE-FIE----RDLGPEGLKRSIV--VVATSDQPAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 177 ARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGSITSI 256
Cdd:PRK07721 228 MRIKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 257 QAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVKQTLQRYKELQDI 336
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDL 385
|
...
gi 28188339 337 IAI 339
Cdd:PRK07721 386 INI 388
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
14-365 |
3.49e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 147.82 E-value: 3.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 14 TDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELG--------PVDSTitlPIHrsapAFTQLDTKlSIFETGI 85
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAeniplqkiKLDAP---PIH----AFEREEIT-DVFETGI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 86 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGvgERTREGNDLYmemkeSKVINEENISESKVa 165
Cdd:PRK06793 145 KSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKADINVISLVG--ERGREVKDFI-----RKELGEEGMRKSVV- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 166 lVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAvGYQPTLSTEMGTLQERI 245
Cdd:PRK06793 216 -VVATSDESHLMQLRAAKLATSIAEYFRDQGN-NVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 246 TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQ 325
Cdd:PRK06793 293 GKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRK 371
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 28188339 326 TLQRYKElQDIIAILGLDELSEEDRLTVARARKIE---RFLSQ 365
Cdd:PRK06793 372 ILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
7-365 |
1.36e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 146.66 E-value: 1.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 7 RAVSM--SATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPV-DSTITLPIHRSAP---AFTQLDTKLsi 80
Cdd:PRK08927 65 RALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPpahSRARVGEPL-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 81 fETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAhggVSVFGGVGERTREGNDLYMEmkeskVINEENIS 160
Cdd:PRK08927 143 -DLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQD-----DLGPEGLA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 161 ESKValVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGT 240
Cdd:PRK08927 214 RSVV--VVATSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 241 LQERI--TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPWIVGQEHY 317
Cdd:PRK08927 291 LLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSrTM--PGCNDPEEN 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 28188339 318 ETAQGVKQTLQRYKELQDIIAI----LGLDelSEEDRlTVARARKIERFLSQ 365
Cdd:PRK08927 369 PLVRRARQLMATYADMEELIRLgayrAGSD--PEVDE-AIRLNPALEAFLRQ 417
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
12-339 |
3.26e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 134.31 E-value: 3.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 12 SATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDEL----GPVDSTITLPihrsAPAFTQLDTKLSIFeTGIKV 87
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 88 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFGGVGERTREGNDLYmemkeSKVINEEniSESKVALV 167
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGREVREFI-----DFTLSEE--TRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 168 YGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITS 247
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 248 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVKQTL 327
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330
....*....|..
gi 28188339 328 QRYKELQDIIAI 339
Cdd:PRK07594 374 ALYQEVELLIRI 385
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
16-389 |
8.39e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 133.48 E-value: 8.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 16 GLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITL-----PIH--RSAPAFTQLDTklsifetGIKVV 88
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLqqqlpQIHplQRRAVDTPLDV-------GVNAI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 89 DLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREGNDLYmemkeSKVINEENISESkvALVY 168
Cdd:PRK07196 147 NGLLTIGKGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGLIG--ERGREVKEFI-----EHSLQAAGMAKS--VVVA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 169 GQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERI-TS 247
Cdd:PRK07196 217 APADESPLMRIKATELCHAIATYYRDKGH-DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 248 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMLQpwIVGQEHYETAQGVKQT 326
Cdd:PRK07196 296 SGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISrCMSQ--VIGSQQAKAASLLKQC 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28188339 327 LQRYKELQDIIA----ILGLDELSEEdrlTVARARKIERFLSQPffvaevfTGSPGKYVSLIETIKG 389
Cdd:PRK07196 374 YADYMAIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQE-------VGHPALFSASVEQLTG 430
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
32-368 |
1.69e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 124.51 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 32 VPVGEATLGRIFNVLGEPVDELGPVDSTITLPIhrSAPAFTQLD-TKLS-IFETGIKVVDLLAPYRRGGKIGLFGGAGVG 109
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFNPLQrTPIEhVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 110 KTVLiMELINNIAKAHGGVSVFGGvgERTREGNDlYMEmkesKVINEENISESKValVYGQMNEPPGARMRVGLTALTMA 189
Cdd:PRK07960 188 KSVL-LGMMARYTQADVIVVGLIG--ERGREVKD-FIE----NILGAEGRARSVV--IAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 190 EYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITS--TKEGSITSIQAVYVPADDLT 267
Cdd:PRK07960 258 EDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 268 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQTLQRYKELQDIIAI----LGLD 343
Cdd:PRK07960 337 DPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTA-LIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSD 415
|
330 340
....*....|....*....|....*
gi 28188339 344 ELSEEdrlTVARARKIERFLSQPFF 368
Cdd:PRK07960 416 PMLDK---AIALWPQLEAFLQQGIF 437
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
29-308 |
1.39e-26 |
|
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: 107.69 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 29 PLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV 108
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 109 GKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESkviNEENISESKVALVYGQMNEPPGARMRVGLTALTM 188
Cdd:cd01135 81 PHNELAAQIARQ-AGVVGSEENFAIVFAAMGVTMEEARFFKDD---FEETGALERVVLFLNLANDPTIERIITPRMALTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 189 AEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQER--ITSTKEGSITSIQAVYVPADDL 266
Cdd:cd01135 157 AEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDDI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 28188339 267 TDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 308
Cdd:cd01135 237 THPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
9-394 |
1.95e-26 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 109.99 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 9 VSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSIFETGIKVV 88
Cdd:PRK05922 69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 89 DLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYMEMkeskviNEENISESKVALV 167
Cdd:PRK05922 149 DAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQ------HKEGLAAQRTIII 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 168 YGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITS 247
Cdd:PRK05922 218 ASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 248 TKEGSITSIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQPWIVgQEHYETAQGVK 324
Cdd:PRK05922 297 NDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSARQLAL-PHHYAAAEELR 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28188339 325 QTLQRYKELQDIIAiLGLDELSEEDRLTvaRARK----IERFLSQPFfvaevftgspGKYVSLIETIKGFQLIL 394
Cdd:PRK05922 371 SLLKAYHEALDIIQ-LGAYVPGQDAHLD--RAVKllpsIKQFLSQPL----------SSYCALHNTLKQLEALL 431
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
14-367 |
4.70e-26 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 109.15 E-value: 4.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 14 TDGLM-RGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSA--PA-------FTQldtklsifeT 83
Cdd:PRK04196 59 TTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------T 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 84 GIKVVDLLAPYRRGGKIGLFGGAGVgktvlimelinniakAHggvsvfggvgertregNDLYMEM-KESKVINEenisES 162
Cdd:PRK04196 130 GISAIDGLNTLVRGQKLPIFSGSGL---------------PH----------------NELAAQIaRQAKVLGE----EE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 163 KVALVYGQM------------------------------NEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQ 212
Cdd:PRK04196 175 NFAVVFAAMgitfeeanffmedfeetgalersvvflnlaDDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 213 AGSEVSALLGRMPSAVGYQPTLSTEMGTLQER--ITSTKEGSITSIQAVYVPADDLTDPAPattfahlDAT-------TV 283
Cdd:PRK04196 255 ALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 284 LSRGLAAKGIYPAVDPLDSTSTMLQPWIvGQEHY-ETAQGVKQTL----QRYKELQDIIAILGLDELSEEDRLTVARARK 358
Cdd:PRK04196 328 LSRELHRKGIYPPIDVLPSLSRLMKDGI-GEGKTrEDHKDVANQLyaayARGKDLRELAAIVGEEALSERDRKYLKFADA 406
|
410
....*....|
gi 28188339 359 IE-RFLSQPF 367
Cdd:PRK04196 407 FErEFVNQGF 416
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-304 |
1.77e-25 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 107.69 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 1 LGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSI 80
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 81 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESKVIN 155
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 156 -----EENISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 230
Cdd:PRK13343 208 vietlREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 231 qP---------------TLSTEMGTlqeritstkeGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYP 295
Cdd:PRK13343 287 -PgdifylhsrlleraaKLSPELGG----------GSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRP 355
|
....*....
gi 28188339 296 AVDPLDSTS 304
Cdd:PRK13343 356 AVDVGLSVS 364
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
26-365 |
1.98e-22 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 98.64 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 26 TGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITL-----PIHRSAPAFTQldtklSIFETGIKVVDLLAPYRRGGKI 100
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLdingqPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 101 GLFGGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGN------DLYMEMKESKVIN---EENISESKVALVYGQM 171
Cdd:TIGR01040 145 PIFSAAGLPHN----EIAAQICRQAGLVKLPTKDVHDGHEDNfaivfaAMGVNMETARFFKqdfEENGSMERVCLFLNLA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 172 NEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERI--TSTK 249
Cdd:TIGR01040 221 NDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 250 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWI-VGQEHYETAQGVKQTLQ 328
Cdd:TIGR01040 301 NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgEGMTRKDHSDVSNQLYA 380
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 28188339 329 RY---KELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 365
Cdd:TIGR01040 381 CYaigKDVQAMKAVVGEEALSSEDLLYLEFLDKFEKnFIAQ 421
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
29-304 |
7.36e-22 |
|
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: 94.56 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 29 PLSVPVGEATLGRIFNVLGEPVDELGPVDS--------TITLPIHRSAPAFTQLDTKLsIFETGIKVVDLLAPYRRGGKI 100
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGSifiprgvnVQRWPVRQPRPVKEKLPPNV-PLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 101 GLFGGAGVGKTVlimeLINNIAK-AHGGVSVFGGVGERTREGNDLYMEMKESKV-INEENISEsKVALVYGQMNEPPGAR 178
Cdd:cd01134 80 AIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGERGNEMAEVLEEFPELKDpITGESLME-RTVLIANTSNMPVAAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 179 MRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERI-------TSTKEG 251
Cdd:cd01134 155 EASIYTGITIAEYFRDMGY-NVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 28188339 252 SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 304
Cdd:cd01134 234 SVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
184-394 |
6.10e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 94.85 E-value: 6.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 184 TALTMAEYFRDvnkQ--DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQER----IT-STKEGSITSI 256
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 257 QAVYVPADDLTDPapaTTFAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQPWI---VGQEHYETAQGVKQTL 327
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPWWeenVDPDWRELRDEAMDLL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28188339 328 QRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQPFFvAEVFTgspgkYVSLIETIKGFQLIL 394
Cdd:PRK04192 465 QREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQNAF-DPVDT-----YCPPEKQYEMLKLIL 526
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
136-390 |
1.14e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 91.24 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 136 ERTREGNDLYMEMKESKVINEENISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGS 215
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 216 EVSALLGRMPSAVGYQPTLSTEMGTLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 288
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 289 AAKGIYPAVDPLDSTS---TMLQPWI---VGQEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ER 361
Cdd:PRK14698 851 ARRRHFPAINWLTSYSlyvDAVKDWWhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250 260
....*....|....*....|....*....
gi 28188339 362 FLSQPFFVAEVFTGSPGKYVSLIETIKGF 390
Cdd:PRK14698 931 YLQQDAFDEVDTYCPPEKQVTMMRVLLNF 959
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
316-385 |
7.44e-19 |
|
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: 80.18 E-value: 7.44e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 316 HYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLIE 385
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
30-304 |
3.85e-17 |
|
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: 80.68 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 30 LSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 109
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 110 KTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESKVINEENISESKVALVY-----GQMNEPPGARM 179
Cdd:cd01132 82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 180 RVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGY--------QPTLSTEMGtlqeri 245
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlhsrllerAAKLSDELG------ 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 28188339 246 tstkEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 304
Cdd:cd01132 217 ----GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
3-225 |
8.39e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 78.95 E-value: 8.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 3 DNkVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTQldtKLSIFE 82
Cdd:PRK09281 69 DN-VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 83 ---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESKVI 154
Cdd:PRK09281 145 plqTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN------------------QKGKDVIciyvaIGQKASTVA 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28188339 155 NEENISESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMP 225
Cdd:PRK09281 207 QVVRKLEEHGAMEYtivvaATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
14-274 |
6.69e-13 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 69.68 E-value: 6.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 14 TDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDElGPvdSTITLPIHRSAPAFTQLDTKL--SIFETGIKVVDLL 91
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDG-GP--ELEGEPIEIGGPSVNPVKRIVprEMIRTGIPMIDVF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 92 APYRRGGKIGLFGGAGVGKTVLIMElINNIAKAHGGVSVFGGVGertregNDLYMEMKESKvinEENISESKVALVYGQM 171
Cdd:PRK02118 135 NTLVESQKIPIFSVSGEPYNALLAR-IALQAEADIIILGGMGLT------FDDYLFFKDTF---ENAGALDRTVMFIHTA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 172 NEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKE- 250
Cdd:PRK02118 205 SDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDg 284
|
250 260
....*....|....*....|....
gi 28188339 251 GSITSIQAVYVPADDLTDPAPATT 274
Cdd:PRK02118 285 GSITIIAVTTMPGDDVTHPVPDNT 308
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
1-30 |
1.47e-12 |
|
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: 62.53 E-value: 1.47e-12
10 20 30
....*....|....*....|....*....|
gi 28188339 1 LGDNKVRAVSMSATDGLMRGMDVIDTGAPL 30
Cdd:cd18115 47 LGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
1-298 |
9.80e-11 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 63.06 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 1 LGDNKVRAVSMSatDGLM--RGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDSTITLPIHRSAPAFTqldTKL 78
Cdd:CHL00059 45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 79 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGND---LYMEM--KE 150
Cdd:CHL00059 120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 151 SKVINEENISESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMP 225
Cdd:CHL00059 182 SSVAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 226 SAVGY--------------QPTLSTEMGtlqeritstkEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAK 291
Cdd:CHL00059 261 GREAYpgdvfylhsrllerAAKLSSQLG----------EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNA 330
|
....*..
gi 28188339 292 GIYPAVD 298
Cdd:CHL00059 331 GIRPAIN 337
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
3-298 |
6.60e-08 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 54.66 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 3 DNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPV---------------DELGPVDSTITLPIHRS 67
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 68 APAFTQLdtklsifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGErtregndLYME 147
Cdd:PTZ00185 168 PVNYNLL--------TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVIS-------IYVS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 148 MKE--SKVINEENISESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFiDNIFRFVQAGSEVSAL 220
Cdd:PTZ00185 233 IGQrcSNVARIHRLLRSYGALRYttvmaATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVY-DDLSKQAVAYRQISLL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 221 LGRMPSAVGYQPTLSTEMGTLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPA 296
Cdd:PTZ00185 312 LRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPA 391
|
..
gi 28188339 297 VD 298
Cdd:PTZ00185 392 VN 393
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
1-27 |
6.18e-05 |
|
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: 40.61 E-value: 6.18e-05
10 20
....*....|....*....|....*..
gi 28188339 1 LGDNKVRAVSMSATDGLMRGMDVIDTG 27
Cdd:pfam02874 43 LGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| 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 ... |
331-365 |
3.55e-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: 39.34 E-value: 3.55e-04
10 20 30
....*....|....*....|....*....|....*.
gi 28188339 331 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 365
Cdd:cd18112 22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
|
|
| 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 ... |
327-365 |
1.13e-03 |
|
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: 38.14 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 28188339 327 LQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 365
Cdd:cd18111 12 LQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
96-224 |
1.22e-03 |
|
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: 39.28 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28188339 96 RGGKIGLFGGAGVGKTVLIMELINNIAKAHggvsvfggvgertregndlymemKESKVINEENISE---SKVALVYGQMN 172
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG-----------------------GGVIYIDGEDILEevlDQLLLIIVGGK 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 28188339 173 EPPGARMRVGLTALTMAEYFRdvnkqDVLLFIDNIFRFVQAGSEVSALLGRM 224
Cdd:smart00382 58 KASGSGELRLRLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
312-366 |
2.21e-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: 36.26 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28188339 312 VGQEHYETAQGVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 366
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
|
|
| |
