|
Name |
Accession |
Description |
Interval |
E-value |
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
1-402 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 965.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 1 LLGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLS 80
Cdd:CHL00060 64 LLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAPAFIQLDTKLS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 81 IFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEENI 160
Cdd:CHL00060 144 IFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 161 SESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMG 240
Cdd:CHL00060 224 AESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 241 TLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGQEHYET 320
Cdd:CHL00060 304 SLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYET 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 321 AQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLVETIKGFQLILSGDLD 400
Cdd:CHL00060 384 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELD 463
|
..
gi 37543303 401 AL 402
Cdd:CHL00060 464 GL 465
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
2-402 |
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: 847.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 2 LGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSI 81
Cdd:COG0055 50 LGDNTVRCIAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 82 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINeenis 161
Cdd:COG0055 130 LETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLD----- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 162 esKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGT 241
Cdd:COG0055 205 --KTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 242 LQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGQEHYETA 321
Cdd:COG0055 283 LQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVA 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 322 QGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLVETIKGFQLILSGDLDA 401
Cdd:COG0055 363 REVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDD 442
|
.
gi 37543303 402 L 402
Cdd:COG0055 443 L 443
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
1-402 |
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: 756.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 1 LLGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLS 80
Cdd:TIGR01039 46 HLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 81 IFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINeeni 160
Cdd:TIGR01039 126 ILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVID---- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 161 sesKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMG 240
Cdd:TIGR01039 202 ---KTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 241 TLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGQEHYET 320
Cdd:TIGR01039 279 ELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 321 AQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLVETIKGFQLILSGDLD 400
Cdd:TIGR01039 359 ARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYD 438
|
..
gi 37543303 401 AL 402
Cdd:TIGR01039 439 HL 440
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
32-310 |
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: 584.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 32 SVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 111
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 112 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEENISesKVALVYGQMNEPPGARMRVGLTALTMAE 191
Cdd:cd01133 81 TVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINLDGLS--KVALVYGQMNEPPGARARVALTGLTMAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 192 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGSITSIQAVYVPADDLTDPA 271
Cdd:cd01133 159 YFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPA 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 37543303 272 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP 310
Cdd:cd01133 239 PATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
2-400 |
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: 538.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 2 LGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSI 81
Cdd:TIGR03305 42 LDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVGKPTLSRMFDVFGNTIDRREPPKDVEWRSVHQAPPTLTRRSSKSEV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 82 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEenis 161
Cdd:TIGR03305 122 FETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLLTEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDN---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 162 eskVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGT 241
Cdd:TIGR03305 198 ---TVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVLLLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 242 LQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGQEHYETA 321
Cdd:TIGR03305 275 LEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSASLVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLA 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 37543303 322 QGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLVETIKGFQLILSGDLD 400
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 ... |
32-307 |
3.89e-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: 3.89e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 32 SVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 111
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 112 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESKVineenisESKVALVYGQMNEPPGARMRVGLTALTMAE 191
Cdd:cd19476 81 TVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGA-------MERTVVVANTANDPPGARMRVPYTGLTIAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 192 YFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTK--EGSITSIQAVYVPADDLTD 269
Cdd:cd19476 154 YFRD-NGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKdgGGSITAIPAVSTPGDDLTD 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 37543303 270 PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTM 307
Cdd:cd19476 233 PIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
85-305 |
7.12e-87 |
|
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: 262.68 E-value: 7.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 85 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKahgGVSVFGGVGERTREGNDLYMEMKESKVIneeniseSK 164
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGAL-------KR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 165 VALVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQE 244
Cdd:pfam00006 71 TVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37543303 245 RITSTKE--GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 305
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 ... |
312-402 |
5.27e-64 |
|
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: 200.01 E-value: 5.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 312 IVGQEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLVETIKGF 391
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90
....*....|.
gi 37543303 392 QLILSGDLDAL 402
Cdd:cd18110 81 KEILDGEYDDL 91
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
4-367 |
1.85e-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: 206.81 E-value: 1.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 4 DNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQ---LDTKLs 80
Cdd:COG1157 63 GDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLErarITEPL- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 81 ifETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINN----------IAkahggvsvfggvgERTREGNDlYMEmk 150
Cdd:COG1157 142 --DTGVRAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNteadvnvialIG-------------ERGREVRE-FIE-- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 151 esKVINEENISESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG 230
Cdd:COG1157 204 --DDLGEEGLARSVV--VVATSDEPPLMRLRAAYTATAIAEYFRDQGK-NVLLLMDSLTRFAMAQREIGLAAGEPPATRG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 231 YQPTLSTEMGTLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMLQ 309
Cdd:COG1157 279 YPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISrVMPD 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37543303 310 pwIVGQEHYETAQGVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 367
Cdd:COG1157 359 --IVSPEHRALARRLRRLLARYEENEDLIRI-GayqpgsdpeLDE-------AIALIPAIEAFLRQG 415
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
32-305 |
6.69e-56 |
|
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: 184.69 E-value: 6.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 32 SVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 111
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 112 TVLIMELINNiAKAhgGVSVFGGVGERTREGNDlYMEmkesKVINEENISESkvALVYGQMNEPPGARMRVGLTALTMAE 191
Cdd:cd01136 81 STLLGMIARN-TDA--DVNVIALIGERGREVRE-FIE----KDLGEEGLKRS--VLVVATSDESPLLRVRAAYTATAIAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 192 YFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGSITSIQAVYVPADDLTDPA 271
Cdd:cd01136 151 YFRDQGK-KVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPI 229
|
250 260 270
....*....|....*....|....*....|....
gi 37543303 272 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 305
Cdd:cd01136 230 ADEVRSILDGHIVLSRRLAERGHYPAIDVLASIS 263
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
17-366 |
4.79e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 169.16 E-value: 4.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 17 GLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQ---LDTKLSifeTGIKVVDLLA 93
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSrrlIETPLS---LGVRVIDGLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 94 PYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREgndlYMEMKESKvINEENISESkvALVYGQMN 173
Cdd:PRK06936 158 TCGEGQRMGIFAAAGGGKSTLLASLIRS---AEVDVTVLALIGERGRE----VREFIESD-LGEEGLRKA--VLVVATSD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 174 EPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGS 253
Cdd:PRK06936 228 RPSMERAKAGFVATSIAEYFRDQGKR-VLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 254 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQTLQRYKE 333
Cdd:PRK06936 307 ITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-IVSKEHKTWAGRLRELLAKYEE 385
|
330 340 350
....*....|....*....|....*....|....*..
gi 37543303 334 LQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 366
Cdd:PRK06936 386 VELLLQIgeyqKGQDKEADQ---AIERIGAIRGFLRQ 419
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
13-366 |
8.39e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 168.45 E-value: 8.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 13 SATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDElGPVDATTTFPIHRSAPafTQLDTKL--SIFETGIKVVD 90
Cdd:PRK06820 79 ASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDG-GPPLTGQWRELDCPPP--SPLTRQPieQMLTTGIRAID 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 91 LLAPYRRGGKIGLFGGAGVGKTVLIMELInniAKAHGGVSVFGGVGERTREGNDlYMEmkesKVINEEniSESKVALVYG 170
Cdd:PRK06820 156 GILSCGEGQRIGIFAAAGVGKSTLLGMLC---ADSAADVMVLALIGERGREVRE-FLE----QVLTPE--ARARTVVVVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 171 QMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTK 250
Cdd:PRK06820 226 TSDRPALERLKGLSTATTIAEYFRDRGK-KVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSD 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 251 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVKQTLQR 330
Cdd:PRK06820 305 RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLAC 383
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 37543303 331 YKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQ 366
Cdd:PRK06820 384 YQEIELLVRVgeyqAGEDLQADE---ALQRYPAICAFLQQ 420
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
12-368 |
8.03e-47 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 165.55 E-value: 8.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 12 MSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHR----SAPAFTQLDTKLSIFETGIK 87
Cdd:PRK08149 61 IGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERFDAPPTVGPISEERvidvAPPSYAERRPIREPLITGVR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 88 VVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakAHGGVSVFGGVGERTREGNDLYMEMKESKvineeniSESKVAL 167
Cdd:PRK08149 141 AIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEH---SEADVFVIGLIGERGREVTEFVESLRASS-------RREKCVL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 168 VYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERIT 247
Cdd:PRK08149 211 VYATSDFSSVDRCNAALVATTVAEYFRDQGK-RVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 248 STKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQT 327
Cdd:PRK08149 290 ATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-VTDPKHRQLAAAFRKL 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 37543303 328 LQRYKELQDIIAiLG---LDELSEEDRlTVARARKIERFLSQPF 368
Cdd:PRK08149 369 LTRLEELQLFID-LGeyrRGENADNDR-AMDKRPALEAFLKQDV 410
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
16-367 |
2.03e-44 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 159.55 E-value: 2.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 16 DGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQ---LDTKLSifeTGIKVVDLL 92
Cdd:PRK09099 81 GGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSrrmVEAPLP---TGVRIVDGL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 93 APYRRGGKIGLFGGAGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEMkeskVINEENISESKV 165
Cdd:PRK09099 158 MTLGEGQRMGIFAPAGVGKSTLMGMFargtqcdVNVIA----------LIGERGREVRE-FIEL----ILGEDGMARSVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 166 alVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQER 245
Cdd:PRK09099 223 --VCATSDRSSIERAKAAYVATAIAEYFRDRGLR-VLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLER 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 246 ITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVK 325
Cdd:PRK09099 300 AGMGETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLR 378
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 37543303 326 QTLQRYKELQDIIAI----LGLDELSEEdrlTVARARKIERFLSQP 367
Cdd:PRK09099 379 QLLAKHREVETLLQVgeyrAGSDPVADE---AIAKIDAIRDFLSQR 421
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
4-366 |
2.24e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 156.81 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 4 DNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPV--------DATTTFPIHRsAPAFTQL 75
Cdd:PRK05688 74 GDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMkaedwvpmDGPTINPLNR-HPISEPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 76 DTklsifetGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREgndlymeMKE--SK 153
Cdd:PRK05688 153 DV-------GIRSINGLLTVGRGQRLGLFAGTGVGKSVL-LGMMTRFTEADIIVVGLIG--ERGRE-------VKEfiEH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 154 VINEENISESKValVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQP 233
Cdd:PRK05688 216 ILGEEGLKRSVV--VASPADDAPLMRLRAAMYCTRIAEYFRDKGK-NVLLLMDSLTRFAQAQREIALAIGEPPATKGYPP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 234 TLSTEMGTLQERITSTKEG--SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPW 311
Cdd:PRK05688 293 SVFAKLPKLVERAGNAEPGggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQ 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 37543303 312 IVGQEHYETAQGVKQTLQRYKELQDIIAI----LGLDelsEEDRLTVARARKIERFLSQ 366
Cdd:PRK05688 372 VVDPEHLRRAQRFKQLWSRYQQSRDLISVgayvAGGD---PETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
31-366 |
3.54e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 156.00 E-value: 3.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 31 LSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 110
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 111 KTVLiMELINNIAKAhgGVSVFGGVGERTRE---------GNDLymemkESKVINEENISESKVALVYGqmneppgarmr 181
Cdd:PRK08472 170 KSTL-MGMIVKGCLA--PIKVVALIGERGREipefieknlGGDL-----ENTVIVVATSDDSPLMRKYG----------- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 182 vGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTK-EGSITSIQAV 260
Cdd:PRK08472 231 -AFCAMSVAEYFKNQGL-DVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 261 YVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQTLQRYKELQDIIAI 340
Cdd:PRK08472 309 LVEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMND-IISPEHKLAARKFKRLYSLLKENEVLIRI 387
|
330 340 350
....*....|....*....|....*....|.
gi 37543303 341 ----LGLD-ELSEedrlTVARARKIERFLSQ 366
Cdd:PRK08472 388 gayqKGNDkELDE----AISKKEFMEQFLKQ 414
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
17-340 |
6.71e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 155.63 E-value: 6.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 17 GLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHrsAPAFTQLDTKlSIFE---TGIKVVDLLA 93
Cdd:PRK08972 81 GVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRH--SPPINPLSRR-PITEpldVGVRAINAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 94 PYRRGGKIGLFGGAGVGKTVLI-MELINNIAKAhggvSVFGGVGERTREgndlymeMKE--SKVINEENISESKValVYG 170
Cdd:PRK08972 158 TVGKGQRMGLFAGSGVGKSVLLgMMTRGTTADV----IVVGLVGERGRE-------VKEfiEEILGEEGRARSVV--VAA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 171 QMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERIT--S 248
Cdd:PRK08972 225 PADTSPLMRLKGCETATTIAEYFRDQG-LNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGngG 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 249 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVKQTL 328
Cdd:PRK08972 304 PGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVY 382
|
330
....*....|..
gi 37543303 329 QRYKELQDIIAI 340
Cdd:PRK08972 383 SLYQQNRDLISI 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
27-340 |
4.68e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 152.95 E-value: 4.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 27 TGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGG 106
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 107 AGVGKTVLIMEL-------INNIAkahggvsvfgGVGERTREGNDlYMEmkesKVINEENISESKValVYGQMNEPPGAR 179
Cdd:PRK07721 167 SGVGKSTLMGMIarntsadLNVIA----------LIGERGREVRE-FIE----RDLGPEGLKRSIV--VVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 180 MRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGSITSIQA 259
Cdd:PRK07721 230 IKGAYTATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 260 VYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVKQTLQRYKELQDIIA 339
Cdd:PRK07721 309 VLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLIN 387
|
.
gi 37543303 340 I 340
Cdd:PRK07721 388 I 388
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
15-366 |
8.14e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 149.74 E-value: 8.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 15 TDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELG--------PVDATttfPIHrsapAFTQLDTKlSIFETGI 86
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAeniplqkiKLDAP---PIH----AFEREEIT-DVFETGI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 87 KVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiAKAHGGVSVFGGvgERTREGNDLYmemkeSKVINEENISESKVa 166
Cdd:PRK06793 145 KSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKADINVISLVG--ERGREVKDFI-----RKELGEEGMRKSVV- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 167 lVYGQMNEPPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAvGYQPTLSTEMGTLQERI 246
Cdd:PRK06793 216 -VVATSDESHLMQLRAAKLATSIAEYFRDQGN-NVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 247 TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQ 326
Cdd:PRK06793 293 GKTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEE-IVSPNHWQLANEMRK 371
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 37543303 327 TLQRYKElQDIIAILGLDELSEEDRLTVARARKIE---RFLSQ 366
Cdd:PRK06793 372 ILSIYKE-NELYFKLGTIQENAENAYIFECKNKVEginTFLKQ 413
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
41-342 |
9.74e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 149.76 E-value: 9.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 41 GRIFNVLGEPVDELGPVDA-TTTFPIHRSAPAF---TQLDTKlsiFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIM 116
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPgTRPMSIDATAPPAmtrARVETG---LRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 117 ELinniAKA-HGGVSVFGGVGERTREgndlYMEMKESKVINeeniSESKVALVYGQMNEPPGARMRVGLTALTMAEYFRD 195
Cdd:PRK06002 184 ML----ARAdAFDTVVIALVGERGRE----VREFLEDTLAD----NLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 196 VNkQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKE--GSITSIQAVYVPADDLTDPAPA 273
Cdd:PRK06002 252 RG-ENVLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEggGSITGIFSVLVDGDDHNDPVAD 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 274 TTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ-PWIVGQEhyETAQGVKQTLQRYKELQDIIAILG 342
Cdd:PRK06002 331 SIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARhAWTPEQR--KLVSRLKSMIARFEETRDLRLIGG 398
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
8-366 |
9.51e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 147.05 E-value: 9.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 8 RAVSM--SATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPV-DATTTFPIHRSAP---AFTQLDTKLsi 81
Cdd:PRK08927 65 RALLMpfGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVVNALGEPIDGKGPLpQGPVPYPLRAPPPpahSRARVGEPL-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 82 fETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAhggVSVFGGVGERTREGNDLYMEmkeskVINEENIS 161
Cdd:PRK08927 143 -DLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD---VSVIGLIGERGREVQEFLQD-----DLGPEGLA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 162 ESKValVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGT 241
Cdd:PRK08927 214 RSVV--VVATSDEPALMRRQAAYLTLAIAEYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 242 LQERI--TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMlqPWIVGQEHY 318
Cdd:PRK08927 291 LLERAgpGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSrTM--PGCNDPEEN 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 37543303 319 ETAQGVKQTLQRYKELQDIIAI----LGLDelSEEDRlTVARARKIERFLSQ 366
Cdd:PRK08927 369 PLVRRARQLMATYADMEELIRLgayrAGSD--PEVDE-AIRLNPALEAFLRQ 417
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
17-390 |
4.49e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 134.25 E-value: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 17 GLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTtfPIHRSAPAFTQLDTKL--SIFETGIKVVDLLAP 94
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST--PLQQQLPQIHPLQRRAvdTPLDVGVNAINGLLT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 95 YRRGGKIGLFGGAGVGKTVLiMELINNIAKAHGGVSVFGGvgERTREGNDLYmemkeSKVINEENISESkvALVYGQMNE 174
Cdd:PRK07196 152 IGKGQRVGLMAGSGVGKSVL-LGMITRYTQADVVVVGLIG--ERGREVKEFI-----EHSLQAAGMAKS--VVVAAPADE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 175 PPGARMRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERI-TSTKEGS 253
Cdd:PRK07196 222 SPLMRIKATELCHAIATYYRDKGH-DVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 254 ITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS-TMLQpwIVGQEHYETAQGVKQTLQRYK 332
Cdd:PRK07196 301 MTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISrCMSQ--VIGSQQAKAASLLKQCYADYM 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37543303 333 ELQDIIA----ILGLDELSEEdrlTVARARKIERFLSQPffvaevfTGSPGKYVSLVETIKG 390
Cdd:PRK07196 379 AIKPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQE-------VGHPALFSASVEQLTG 430
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
13-340 |
4.64e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 133.92 E-value: 4.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 13 SATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDEL----GPVDATTTFPihrsAPAFTQLDTKLSIFeTGIKV 88
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRelpdVCWKDYDAMP----PPAMVRQPITQPLM-TGIRA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 89 VDLLAPYRRGGKIGLFGGAGVGKTVLIMELINniaKAHGGVSVFGGVGERTREGNDLYmemkeSKVINEEniSESKVALV 168
Cdd:PRK07594 146 IDSVATCGEGQRVGIFSAPGVGKSTLLAMLCN---APDADSNVLVLIGERGREVREFI-----DFTLSEE--TRKRCVIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 169 YGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITS 248
Cdd:PRK07594 216 VATSDRPALERVRALFVATTIAEFFRDNGKR-VVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 249 TKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLqPWIVGQEHYETAQGVKQTL 328
Cdd:PRK07594 295 GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCL 373
|
330
....*....|..
gi 37543303 329 QRYKELQDIIAI 340
Cdd:PRK07594 374 ALYQEVELLIRI 385
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
33-369 |
1.84e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 124.51 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 33 VPVGEATLGRIFNVLGEPVDELGPVDATTTFPIhrSAPAFTQLD-TKLS-IFETGIKVVDLLAPYRRGGKIGLFGGAGVG 110
Cdd:PRK07960 110 LPLGPALLGRVLDGSGKPLDGLPAPDTGETGAL--ITPPFNPLQrTPIEhVLDTGVRAINALLTVGRGQRMGLFAGSGVG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 111 KTVLiMELINNIAKAHGGVSVFGGvgERTREGNDlYMEmkesKVINEENISESKValVYGQMNEPPGARMRVGLTALTMA 190
Cdd:PRK07960 188 KSVL-LGMMARYTQADVIVVGLIG--ERGREVKD-FIE----NILGAEGRARSVV--IAAPADVSPLLRMQGAAYATRIA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 191 EYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITS--TKEGSITSIQAVYVPADDLT 268
Cdd:PRK07960 258 EDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGDDQQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 269 DPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPwIVGQEHYETAQGVKQTLQRYKELQDIIAI----LGLD 344
Cdd:PRK07960 337 DPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTA-LIDEQHYARVRQFKQLLSSFQRNRDLVSVgayaKGSD 415
|
330 340
....*....|....*....|....*
gi 37543303 345 ELSEEdrlTVARARKIERFLSQPFF 369
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 ... |
30-309 |
8.43e-27 |
|
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: 108.08 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 30 PLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV 109
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 110 GKTVLIMELINNiAKAHGGVSVFGGVGERTREGNDLYMEMKESkviNEENISESKVALVYGQMNEPPGARMRVGLTALTM 189
Cdd:cd01135 81 PHNELAAQIARQ-AGVVGSEENFAIVFAAMGVTMEEARFFKDD---FEETGALERVVLFLNLANDPTIERIITPRMALTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 190 AEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQER--ITSTKEGSITSIQAVYVPADDL 267
Cdd:cd01135 157 AEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPILTMPNDDI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 37543303 268 TDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ 309
Cdd:cd01135 237 THPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMK 278
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
10-395 |
1.05e-26 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 110.76 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 10 VSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSIFETGIKVV 89
Cdd:PRK05922 69 MSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 90 DLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDlYMEMkeskviNEENISESKVALV 168
Cdd:PRK05922 149 DAFLTLGKGQRIGVFSEPGSGKS----SLLSTIAKgSKSTINVIALIGERGREVRE-YIEQ------HKEGLAAQRTIII 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 169 YGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITS 248
Cdd:PRK05922 218 ASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGN 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 249 TKEGSITSIQAV-YVP--ADDLTDPAPATTFAHLDATTVlSRGLAAkgiyPAVDPLDSTSTMLQPWIVgQEHYETAQGVK 325
Cdd:PRK05922 297 NDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHFFLTPQ-GKALAS----PPIDILTSLSRSARQLAL-PHHYAAAEELR 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37543303 326 QTLQRYKELQDIIAiLGLDELSEEDRLTvaRARK----IERFLSQPFfvaevftgspGKYVSLVETIKGFQLIL 395
Cdd:PRK05922 371 SLLKAYHEALDIIQ-LGAYVPGQDAHLD--RAVKllpsIKQFLSQPL----------SSYCALHNTLKQLEALL 431
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
2-305 |
7.33e-26 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 108.85 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 2 LGDNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSI 81
Cdd:PRK13343 66 LEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 82 FETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESKVIN 156
Cdd:PRK13343 146 LQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAIIN------------------QKDSDVIcvyvaIGQKASAVAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 157 -----EENISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGY 231
Cdd:PRK13343 208 vietlREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 232 qP---------------TLSTEMGTlqeritstkeGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYP 296
Cdd:PRK13343 287 -PgdifylhsrlleraaKLSPELGG----------GSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRP 355
|
....*....
gi 37543303 297 AVDPLDSTS 305
Cdd:PRK13343 356 AVDVGLSVS 364
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
15-368 |
3.23e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 106.83 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 15 TDGLM-RGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSA--PA-------FTQldtklsifeT 84
Cdd:PRK04196 59 TTGLDlKDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPinPVareypeeFIQ---------T 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 85 GIKVVDLLAPYRRGGKIGLFGGAGVgktvlimelinniakAHggvsvfggvgertregNDLYMEM-KESKVINEenisES 163
Cdd:PRK04196 130 GISAIDGLNTLVRGQKLPIFSGSGL---------------PH----------------NELAAQIaRQAKVLGE----EE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 164 KVALVYGQM------------------------------NEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQ 213
Cdd:PRK04196 175 NFAVVFAAMgitfeeanffmedfeetgalersvvflnlaDDPAIERILTPRMALTAAEYLAFEKGMHVLVILTDMTNYCE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 214 AGSEVSALLGRMPSAVGYQPTLSTEMGTLQER--ITSTKEGSITSIQAVYVPADDLTDPAPattfahlDAT-------TV 284
Cdd:PRK04196 255 ALREISAAREEVPGRRGYPGYMYTDLATIYERagRIKGKKGSITQIPILTMPDDDITHPIP-------DLTgyitegqIV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 285 LSRGLAAKGIYPAVDPLDSTSTMLQPWIvGQEHY-ETAQGVKQTL----QRYKELQDIIAILGLDELSEEDRLTVARARK 359
Cdd:PRK04196 328 LSRELHRKGIYPPIDVLPSLSRLMKDGI-GEGKTrEDHKDVANQLyaayARGKDLRELAAIVGEEALSERDRKYLKFADA 406
|
410
....*....|
gi 37543303 360 IE-RFLSQPF 368
Cdd:PRK04196 407 FErEFVNQGF 416
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
27-366 |
1.19e-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: 99.41 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 27 TGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTF-----PIHRSAPAFTQldtklSIFETGIKVVDLLAPYRRGGKI 101
Cdd:TIGR01040 70 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLdingqPINPYARIYPE-----EMIQTGISAIDVMNSIARGQKI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 102 GLFGGAGVGKTvlimELINNIAKAHGGVSVFGGVGERTREGN------DLYMEMKESKVIN---EENISESKVALVYGQM 172
Cdd:TIGR01040 145 PIFSAAGLPHN----EIAAQICRQAGLVKLPTKDVHDGHEDNfaivfaAMGVNMETARFFKqdfEENGSMERVCLFLNLA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 173 NEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERI--TSTK 250
Cdd:TIGR01040 221 NDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 251 EGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWI-VGQEHYETAQGVKQTLQ 329
Cdd:TIGR01040 301 NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgEGMTRKDHSDVSNQLYA 380
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 37543303 330 RY---KELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 366
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 ... |
30-305 |
7.74e-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: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 30 PLSVPVGEATLGRIFNVLGEPVDELGPVDA--------TTTFPIHRSAPAFTQLDTKLsIFETGIKVVDLLAPYRRGGKI 101
Cdd:cd01134 1 PLSVELGPGLLGSIFDGIQRPLEVIAETGSifiprgvnVQRWPVRQPRPVKEKLPPNV-PLLTGQRVLDTLFPVAKGGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 102 GLFGGAGVGKTVlimeLINNIAK-AHGGVSVFGGVGERTREGNDLYMEMKESKV-INEENISEsKVALVYGQMNEPPGAR 179
Cdd:cd01134 80 AIPGPFGCGKTV----ISQSLSKwSNSDVVIYVGCGERGNEMAEVLEEFPELKDpITGESLME-RTVLIANTSNMPVAAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 180 MRVGLTALTMAEYFRDVNKqDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERI-------TSTKEG 252
Cdd:cd01134 155 EASIYTGITIAEYFRDMGY-NVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAgrvrclgSPGREG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 37543303 253 SITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 305
Cdd:cd01134 234 SVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYS 286
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
185-366 |
6.52e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 94.85 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 185 TALTMAEYFRDvnkQ--DVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQER----IT-STKEGSITSI 257
Cdd:PRK04192 311 TGITIAEYYRD---MgyDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTII 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 258 QAVYVPADDLTDPapaTTFAHLDATTV---LSRGLAAKGIYPAVDPLDSTS---TMLQPWI---VGQEHYETAQGVKQTL 328
Cdd:PRK04192 388 GAVSPPGGDFSEP---VTQNTLRIVKVfwaLDAELADRRHFPAINWLTSYSlylDQVAPWWeenVDPDWRELRDEAMDLL 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 37543303 329 QRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 366
Cdd:PRK04192 465 QREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
137-391 |
1.12e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 91.24 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 137 ERTREGNDLYMEMKESKVINEENISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNkQDVLLFIDNIFRFVQAGS 216
Cdd:PRK14698 692 ERGNEMTDVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFRDMG-YDVALMADSTSRWAEALR 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 217 EVSALLGRMPSAVGYQPTLSTEMGTLQERI-------TSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGL 289
Cdd:PRK14698 771 EISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 290 AAKGIYPAVDPLDSTS---TMLQPWI---VGQEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ER 362
Cdd:PRK14698 851 ARRRHFPAINWLTSYSlyvDAVKDWWhknVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLVARMLrED 930
|
250 260
....*....|....*....|....*....
gi 37543303 363 FLSQPFFVAEVFTGSPGKYVSLVETIKGF 391
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, ... |
317-386 |
3.43e-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: 80.95 E-value: 3.43e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 317 HYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLVE 386
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 ... |
31-305 |
1.25e-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: 82.22 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 31 LSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG 110
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 111 KTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESKVINEENISESKVALVY-----GQMNEPPGARM 180
Cdd:cd01132 82 KTAIAIDTIIN------------------QKGKKVYciyvaIGQKRSTVAQIVKTLEEHGAMEYtivvaATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 181 RVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGR------MPSAVGY--------QPTLSTEMGtlqeri 246
Cdd:cd01132 144 LAPYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRppgreaYPGDVFYlhsrllerAAKLSDELG------ 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 37543303 247 tstkEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTS 305
Cdd:cd01132 217 ----GGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVS 271
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
4-226 |
5.48e-16 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 79.34 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 4 DNkVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTQldtKLSIFE 83
Cdd:PRK09281 69 DN-VGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPVERKAPGVID---RKSVHE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 84 ---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGNDLY-----MEMKESKVI 155
Cdd:PRK09281 145 plqTGIKAIDAMIPIGRGQRELIIGDRQTGKTAIAIDTIIN------------------QKGKDVIciyvaIGQKASTVA 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37543303 156 NEENISESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDvNKQDVLLFIDNIFRFVQAGSEVSALLGRMP 226
Cdd:PRK09281 207 QVVRKLEEHGAMEYtivvaATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPP 281
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
15-275 |
2.59e-13 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 70.83 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 15 TDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVD-------ELGPVDATTTFPIHRSAPAftqldtklSIFETGIK 87
Cdd:PRK02118 58 TRGISTGDEVVFLGRPMQVTYSESLLGRRFNGSGKPIDggpelegEPIEIGGPSVNPVKRIVPR--------EMIRTGIP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 88 VVDLLAPYRRGGKIGLFGGAGVGKTVLIMElINNIAKAHGGVSVFGGVGertregNDLYMEMKESKvinEENISESKVAL 167
Cdd:PRK02118 130 MIDVFNTLVESQKIPIFSVSGEPYNALLAR-IALQAEADIIILGGMGLT------FDDYLFFKDTF---ENAGALDRTVM 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 168 VYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERIT 247
Cdd:PRK02118 200 FIHTASDPPVECLLVPDMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAV 279
|
250 260
....*....|....*....|....*....
gi 37543303 248 STKE-GSITSIQAVYVPADDLTDPAPATT 275
Cdd:PRK02118 280 DFEDgGSITIIAVTTMPGDDVTHPVPDNT 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 ... |
1-31 |
7.08e-13 |
|
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: 63.30 E-value: 7.08e-13
10 20 30
....*....|....*....|....*....|.
gi 37543303 1 LLGDNKVRAVSMSATDGLMRGMDVIDTGAPL 31
Cdd:cd18115 46 HLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
2-299 |
3.74e-11 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 64.60 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 2 LGDNKVRAVSMSatDGLM--RGMDVIDTGAPLSVPVGEATLGRIFNVLGEPVDELGPVDATTTFPIHRSAPAFTqldTKL 79
Cdd:CHL00059 45 LESNNVGVVLMG--DGLMiqEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGII---SRR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 80 SIFE---TGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNiakahggvsvfggvgertREGND---LYMEM--KE 151
Cdd:CHL00059 120 SVYEplqTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILN------------------QKGQNvicVYVAIgqKA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 152 SKVINEENISESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRdVNKQDVLLFIDNIFRFVQAGSEVSALLGRMP 226
Cdd:CHL00059 182 SSVAQVVTTLQERGAMEYtivvaETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 227 SAVGY--------------QPTLSTEMGtlqeritstkEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAK 292
Cdd:CHL00059 261 GREAYpgdvfylhsrllerAAKLSSQLG----------EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNA 330
|
....*..
gi 37543303 293 GIYPAVD 299
Cdd:CHL00059 331 GIRPAIN 337
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
4-299 |
2.63e-08 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 55.82 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 4 DNKVRAVSMSATDGLMRGMDVIDTGAPLSVPVGEATLGRIFNVLGEPV---------------DELGPVDATTTFPIHRS 68
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVpvglltrsralleseQTLGKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 69 APAFTQLdtklsifeTGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGErtregndLYME 148
Cdd:PTZ00185 168 PVNYNLL--------TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQILSKNAVIS-------IYVS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 149 MKE--SKVINEENISESKVALVY-----GQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFiDNIFRFVQAGSEVSAL 221
Cdd:PTZ00185 233 IGQrcSNVARIHRLLRSYGALRYttvmaATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVY-DDLSKQAVAYRQISLL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 222 LGRMPSAVGYQPTLSTEMGTLQERITSTKE----GSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPA 297
Cdd:PTZ00185 312 LRRPPGREAYPGDVFYLHSRLLERAAMLSPgkggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPA 391
|
..
gi 37543303 298 VD 299
Cdd:PTZ00185 392 VN 393
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
2-28 |
6.25e-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: 6.25e-05
10 20
....*....|....*....|....*..
gi 37543303 2 LGDNKVRAVSMSATDGLMRGMDVIDTG 28
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 ... |
332-366 |
3.53e-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: 3.53e-04
10 20 30
....*....|....*....|....*....|....*.
gi 37543303 332 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 366
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 ... |
328-366 |
1.01e-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: 1.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 37543303 328 LQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 366
Cdd:cd18111 12 LQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
97-225 |
1.01e-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: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37543303 97 RGGKIGLFGGAGVGKTVLIMELINNIAKAHggvsvfggvgertregndlymemKESKVINEENISE---SKVALVYGQMN 173
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG-----------------------GGVIYIDGEDILEevlDQLLLIIVGGK 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 37543303 174 EPPGARMRVGLTALTMAEYFRdvnkqDVLLFIDNIFRFVQAGSEVSALLGRM 225
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 ... |
313-367 |
2.18e-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: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 37543303 313 VGQEHYETAQGVKQTLQRYKELQDIIAIlG---------LDElseedrlTVARARKIERFLSQP 367
Cdd:pfam18269 1 VSPEHLQAARRLRELLATYQENEDLIRI-GayqagsdpeIDE-------AIAKRPAINAFLRQG 56
|
|
| |
