|
Name |
Accession |
Description |
Interval |
E-value |
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
40-504 |
0e+00 |
|
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: 1005.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 40 TYRTVCSVNGPLVVLDQVKFAQYAEIVNFTLPNGTQRSGQVLEVSGTKAIVQVFEGTSGIDAQKTTCEFTGDILRTPVSE 119
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 120 DMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 199
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 200 ICRQAGLVKKS-KAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEF 278
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 279 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHP 358
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 359 IPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEAL 438
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28603772 439 TSEDLLYLEFLQKFEKKFINQGPYEKRSVFESLDLGWKLLRTFPKEMLKRIPQNIIDEFFSREGAP 504
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSAD 466
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
37-503 |
0e+00 |
|
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 440770 [Multi-domain] Cd Length: 462 Bit Score: 827.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 37 PRITYRTVCSVNGPLVVLDQVKFAQYAEIVNFTLPNGTQRSGQVLEVSGTKAIVQVFEGTSGIDAQKTTCEFTGDILRTP 116
Cdd:COG1156 2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 117 VSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNEI 196
Cdd:COG1156 82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 197 AAQICRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTA 276
Cdd:COG1156 162 AAQIARQAKVRGE--------EEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 277 EFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDIT 356
Cdd:COG1156 234 EYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDIT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 357 HPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEE 436
Cdd:COG1156 314 HPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28603772 437 ALTSEDLLYLEFLQKFEKKFINQGPYEKRSVFESLDLGWKLLRTFPKEMLKRIPQNIIDEFFSREGA 503
Cdd:COG1156 394 ALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRA 460
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
38-503 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 800.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 38 RITYRTVCSVNGPLVVLDQVKFAQYAEIVNFTLPNGTQRSGQVLEVSGTKAIVQVFEGTSGIDAQKTTCEFTGDILRTPV 117
Cdd:PRK04196 1 LKEYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 118 SEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNEIA 197
Cdd:PRK04196 81 SEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 198 AQICRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAE 277
Cdd:PRK04196 161 AQIARQAKVLGE--------EENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 278 FLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITH 357
Cdd:PRK04196 233 YLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 358 PIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEA 437
Cdd:PRK04196 313 PIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28603772 438 LTSEDLLYLEFLQKFEKKFINQGPYEKRSVFESLDLGWKLLRTFPKEMLKRIPQNIIDEFFSREGA 503
Cdd:PRK04196 393 LSERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRG 458
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
41-497 |
0e+00 |
|
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity with eukaryotic and prokaryotic V-type (H+)-ATPases. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 200071 [Multi-domain] Cd Length: 458 Bit Score: 686.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 41 YRTVCSVNGPLVVLDQVKFAQYAEIVNFTLPNGTQRSGQVLEVSGTKAIVQVFEGTSGIDAQKTTCEFTGDILRTPVSED 120
Cdd:TIGR01041 2 YSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 121 MLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 200
Cdd:TIGR01041 82 MLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 201 CRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLA 280
Cdd:TIGR01041 162 ARQATVRGE--------ESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 281 YQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIP 360
Cdd:TIGR01041 234 FEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 361 DLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTS 440
Cdd:TIGR01041 314 DLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 28603772 441 EDLLYLEFLQKFEKKFINQGPYEKRSVFESLDLGWKLLRTFPKEMLKRIPQNIIDEF 497
Cdd:TIGR01041 394 RDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKY 450
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
112-401 |
0e+00 |
|
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: 609.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 112 ILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGL 191
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 192 PHNEIAAQICRQAGLVKkskavldyHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRL 271
Cdd:cd01135 81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 272 ALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMP 351
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 28603772 352 NDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 401
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
38-501 |
6.66e-120 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 359.35 E-value: 6.66e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 38 RITYRTVCSVNGPLVVLdQVKFAQYAEIVNFTLPNGTqRSGQVLEVSGTKAIVQVFEGTSGI--DAQKTtceFTGDILRT 115
Cdd:PRK02118 2 QKIYTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGIstGDEVV---FLGRPMQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 116 PVSEDMLGRVFNGSGKPIDKGPVVMAEDfLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNE 195
Cdd:PRK02118 77 TYSESLLGRRFNGSGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 196 IAAQICRQAglvkkskavldyhdDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTT 275
Cdd:PRK02118 156 LLARIALQA--------------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 276 AEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrGGSITQIPILTMPNDDI 355
Cdd:PRK02118 222 AEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 356 THPIPDLTGFITEGQIYvdrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRKDHGDVSN---QLYACYAIGKDVQAMkav 432
Cdd:PRK02118 301 THPVPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM--- 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28603772 433 vGEEaLTSEDLLYLEFLQKFEKKFINQG---PYEkrsvfESLDLGWKLL-RTF-PKEMLkrIPQNIIDEFFSRE 501
Cdd:PRK02118 369 -GFK-LSNWDEKLLKFSELFESRLMDLEvniPLE-----EALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKN 433
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
167-393 |
5.46e-105 |
|
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: 312.75 E-value: 5.46e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 167 GISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGlvkkskavldyHDdnfAIVFAAMGVNMETARFFKSDFEQNG 246
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS-----------AD---VVVYALIGERGREVREFIEELLGSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 247 TMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 326
Cdd:pfam00006 67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28603772 327 TIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 393
Cdd:pfam00006 146 RLLERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
114-395 |
5.69e-103 |
|
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: 309.77 E-value: 5.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPH 193
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 194 NEIAAQICRQAglvKKSKAvldyhddnFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLAL 273
Cdd:cd19476 81 TVLAMQLARNQ---AKAHA--------GVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 274 TTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPND 353
Cdd:cd19476 150 TIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 28603772 354 DITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:cd19476 229 DLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| 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 ... |
403-497 |
3.46e-62 |
|
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: 198.04 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 403 GMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKKFINQGPYEKRSVFESLDLGWKLLRTFP 482
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 28603772 483 KEMLKRIPQNIIDEF 497
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
114-395 |
1.91e-41 |
|
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: 149.25 E-value: 1.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPH 193
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 194 NEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETAR----FFKSDFEQNGtMGNVCLFLNLANDPTIERIITP 269
Cdd:cd01136 81 STLLGMIAR--------------NTDADVNVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 270 RLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILT 349
Cdd:cd01136 143 YTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 28603772 350 MPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:cd01136 220 VEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
64-399 |
2.49e-38 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 146.76 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 64 EIVNFtlPNGTQRSGQVLEVSGTKAIVqvFEGTSGIdAQKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVmAE 142
Cdd:TIGR00962 50 ELIEF--EGGVQGIALNLEEDSVGAVI--MGDYSDI-REGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDgKGPID-SD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 143 DFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGlvKKSKAV---LDYHDD 219
Cdd:TIGR00962 124 EFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGD-------------RQTG--KTAVAIdtiINQKDS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 220 NFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAE 299
Cdd:TIGR00962 189 DVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 300 ALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVD 374
Cdd:TIGR00962 268 AYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 344
|
330 340
....*....|....*....|....*
gi 28603772 375 RQLHNRQIYPPINVLPSLSRLMKSA 399
Cdd:TIGR00962 345 SDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| ATP-synt_V_A-type_beta_N |
cd18118 |
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 ... |
40-111 |
1.85e-36 |
|
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core, that is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex which 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: 349742 [Multi-domain] Cd Length: 72 Bit Score: 129.47 E-value: 1.85e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28603772 40 TYRTVCSVNGPLVVLDQVKFAQYAEIVNFTLPNGTQRSGQVLEVSGTKAIVQVFEGTSGIDAQKTTCEFTGD 111
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
64-396 |
2.55e-35 |
|
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: 136.70 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 64 EIVNFTLPNGTQRSGQVLEVSGTKAIVQVFEGTSGIdAQKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAED 143
Cdd:COG1157 42 ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 144 FLDINGQPINPHDR--IypEEMIETGISPIDVMNSIARGQKIPIFSAAG------LphneiaAQICRQA-------GLV- 207
Cdd:COG1157 121 RRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL------GMIARNTeadvnviALIg 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 208 -------------------KKSkavldyhddnfaIVFAAmgvnmeTarffkSDfeqngtmgnvclflnlanDPTIERIIT 268
Cdd:COG1157 193 ergrevrefieddlgeeglARS------------VVVVA------T-----SD------------------EPPLMRLRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 269 PRLALTTAEFLAYQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQI 345
Cdd:COG1157 232 AYTATAIAEYFRDQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAF 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 28603772 346 -PILTmPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:COG1157 306 yTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
79-478 |
1.35e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 134.94 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 79 QVLEVSGTKAIVQVFEGTSGIDAQKTTcEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINPHDRI 158
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGLRCGQWV-TPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 159 YPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETARFF 238
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA--------------DSAADVMVLALIG---ERGREV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 239 KSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLALTTAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRR 315
Cdd:PRK06820 205 REFLEQVLTpeaRARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 316 GFPGYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:PRK06820 284 SFPPSVFANLPRLLERTGNSDR--GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 396 MKSAIGEGmtRKDHGDVSNQLYACYaigKDVQAMKAVvgEEALTSEDLLYLEFLQKFE--KKFINQGPYEKRSVFESLDL 473
Cdd:PRK06820 362 MPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEH 434
|
....*
gi 28603772 474 GWKLL 478
Cdd:PRK06820 435 LAQVV 439
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
109-396 |
6.02e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 133.34 E-value: 6.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 109 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSA 188
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 189 AGLPHNEIAAQICRQAglvkkskavldyhdDNFAIVFAAMGV-NMETARFFKSDFEQNGtMGNVCLFLNLANDPTIERII 267
Cdd:PRK06936 171 AGGGKSTLLASLIRSA--------------EVDVTVLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 268 TPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRGGSITQIPI 347
Cdd:PRK06936 236 AGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYT 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 28603772 348 LTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:PRK06936 313 VLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVM 361
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
113-402 |
2.13e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 128.65 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 113 LRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLP 192
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 193 HNEIAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQN--GTMGNVCLFLNLANDPTIERIITPR 270
Cdd:PRK08472 170 KSTLMGMI------VKGCLAPIK--------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGAF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 271 LALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILTM 350
Cdd:PRK08472 233 CAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLV 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 28603772 351 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGE 402
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
112-394 |
1.04e-31 |
|
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: 123.05 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 112 ILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP-INPHDRIYpeEMIETGISPIDVMNSIARGQKIPIFSAa 189
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDgKGPIQTKERRRVESKAPgIIPRQSVN--EPLQTGIKAIDSLIPIGRGQRELIIGD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 190 glphneiaaqicRQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERI 266
Cdd:cd01132 78 ------------RQTG--KTAIAIdtiINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 267 ITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGS 341
Cdd:cd01132 144 LAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGS 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 28603772 342 ITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:cd01132 220 LTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
79-402 |
2.20e-29 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 120.06 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 79 QVLEVSGTKAIVQVFEGTSGIdaqktTCEFTGDILR----TPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINP 154
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGL-----HCGQQVMALRrrhqVPVGEALLGRVIDGFGRPLDGRELPDVC-WKDYDAMPPPA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 155 HDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyhDDNfaiVFAAMGVNMET 234
Cdd:PRK07594 130 MVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA-----------DSN---VLVLIGERGRE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 235 ARFFkSDFEQNGTMGNVCLFLNLAND-PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPG 313
Cdd:PRK07594 196 VREF-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 314 RRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 393
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLS 351
|
....*....
gi 28603772 394 RLMKSAIGE 402
Cdd:PRK07594 352 RVFPVVTSH 360
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
111-433 |
3.53e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 119.84 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 111 DILRTPVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAA 189
Cdd:PRK05688 99 DTGRLPMGMSMLGRVLDGAGRALDgKGPM-KAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 190 GLphneiaaqicrqaglvkkSKAVLDYHDDNFA----IVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIER 265
Cdd:PRK05688 178 GV------------------GKSVLLGMMTRFTeadiIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 266 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQI 345
Cdd:PRK05688 240 LRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 346 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG-EGMTRKDHgdvSNQLYACYAIGK 424
Cdd:PRK05688 319 YTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQSR 395
|
....*....
gi 28603772 425 DVQAMKAVV 433
Cdd:PRK05688 396 DLISVGAYV 404
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
25-399 |
5.60e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 119.33 E-value: 5.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 25 HVQAVTRNYIThprityrtvcsVNGplvvldQVKFAQYAEIVNFTLPNGTQRsGQVLEVSGTKAIVQVFEgtSGIDAQKT 104
Cdd:PRK06002 29 TVSEVTASHYR-----------VRG------LSRFVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFE--PRIEIGLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 105 TCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKI 183
Cdd:PRK06002 89 DAVFRKGPLRIRPDPSWKGRVINALGEPIDgLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 184 PIFSAAGlphneiaaqicrqaglVKKSK--AVLDYHDDNFAIVFAAMGVNMETARFFKSDfeqngTMGNvclflNLANDP 261
Cdd:PRK06002 169 GIFAGSG----------------VGKSTllAMLARADAFDTVVIALVGERGREVREFLED-----TLAD-----NLKKAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 262 TI---------ERIITPRLALTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERA 332
Cdd:PRK06002 223 AVvatsdespmMRRLAPLTATAIAEYFRDRGEN-VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERA 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28603772 333 GRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 399
Cdd:PRK06002 302 GPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
96-394 |
1.07e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 118.86 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 96 TSGIDAQkTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFldingqpinPHDRIYPEEM--------IET 166
Cdd:PRK13343 79 TADILAG-TEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDgGGPLQATARR---------PLERPAPAIIerdfvtepLQT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 167 GISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQicrqaglvkkskAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNG 246
Cdd:PRK13343 149 GIKVVDALIPIGRGQRELIIGDRQTGKTAIAID------------AIINQKDSDVICVYVAIGQKASAVARVIETLREHG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 247 TMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 326
Cdd:PRK13343 217 ALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHS 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 327 TIYERAGRV--EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:PRK13343 296 RLLERAAKLspELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
114-469 |
6.97e-28 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 116.04 E-value: 6.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPH 193
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 194 NEIAAQICR--QAGLvkkskavldyhddnfaIVFAAMGvnmETARFFKsDFEQN--GTMGnvclflnLANDPTIERI--I 267
Cdd:PRK07960 189 SVLLGMMARytQADV----------------IVVGLIG---ERGREVK-DFIENilGAEG-------RARSVVIAAPadV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 268 TPRLALTTAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGS 341
Cdd:PRK07960 242 SPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 342 ITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKdhgdVSN--QLYAC 419
Cdd:PRK07960 322 ITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR----VRQfkQLLSS 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 28603772 420 YAIGKDVQAmkavVGEEALTSEDLL--YLEFLQKFEkKFINQGPYEkRSVFE 469
Cdd:PRK07960 398 FQRNRDLVS----VGAYAKGSDPMLdkAIALWPQLE-AFLQQGIFE-RADWE 443
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
40-468 |
1.26e-27 |
|
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: 115.20 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 40 TYRTVCSVNGPLVvldQVKFAQYA--EIVNFTLPNGTQRSGQVLEVSG------TKAIVqvFEGTSGIdAQKTTCEFTGD 111
Cdd:TIGR01039 1 TKGKVVQVIGPVV---DVEFEQGElpRIYNALKVQNRAESELTLEVAQhlgddtVRTIA--MGSTDGL-VRGLEVIDTGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 112 ILRTPVSEDMLGRVFNGSGKPID-KGPvVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAG 190
Cdd:TIGR01039 75 PISVPVGKETLGRIFNVLGEPIDeKGP-IPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 191 LPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERI 266
Cdd:TIGR01039 154 VGKTvliqELINNIAKEHGGYS---------------VFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 267 ITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRGGSITQIP 346
Cdd:TIGR01039 219 RVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKTGSITSVQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 347 ILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrkDHGDVSNQLYACYAIGKD 425
Cdd:TIGR01039 297 AVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQILQRYKE 371
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 28603772 426 VQAMKAVVGEEALTSEDLLYLEFLQKFEkKFINQgPYEKRSVF 468
Cdd:TIGR01039 372 LQDIIAILGMDELSEEDKLTVERARRIQ-RFLSQ-PFFVAEVF 412
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
109-399 |
1.92e-27 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 115.06 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 109 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP-INPHDRIYpeEMIETGISPIDVMNSIARGQKIPIF 186
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDgKGEISASESRLIESPAPgIISRRSVY--EPLQTGLIAIDSMIPIGRGQRELII 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 187 SAaglphneiaaqicRQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTI 263
Cdd:CHL00059 148 GD-------------RQTG--KTAVATdtiLNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPAT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 264 ERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRVEGR-- 338
Cdd:CHL00059 213 LQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSQlg 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28603772 339 GGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 399
Cdd:CHL00059 289 EGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
107-484 |
4.27e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 113.66 E-value: 4.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 107 EFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIF 186
Cdd:PRK07721 85 EATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 187 SAAGLPHNEIAAQICRQaglvkkSKAVLDyhddnfaiVFAAMGVN-METARFFKSDFEQNGTMGNVcLFLNLANDPTIER 265
Cdd:PRK07721 165 AGSGVGKSTLMGMIARN------TSADLN--------VIALIGERgREVREFIERDLGPEGLKRSI-VVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 266 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrgGSITQI 345
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS--GSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 346 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSN---QLYACYAi 422
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQ- 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28603772 423 gkdvqamkavvgeealTSEDLLYL------------EFLQKFEK--KFINQGPYEKRSVFESLDlgwKLLRTFPKE 484
Cdd:PRK07721 381 ----------------NSEDLINIgaykrgssreidEAIQFYPQiiSFLKQGTDEKATFEESIQ---ALLSLFGKG 437
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
116-425 |
6.75e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 112.76 E-value: 6.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 116 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNE 195
Cdd:PRK06793 92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 196 IAAQICRQAglvkksKAvldyhDDNFAIVFAAMGvnMETARFFKSDFEQNGTMGNVcLFLNLANDPTIERIITPRLALTT 275
Cdd:PRK06793 172 LLGMIAKNA------KA-----DINVISLVGERG--REVKDFIRKELGEEGMRKSV-VVVATSDESHLMQLRAAKLATSI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 276 AEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDD 354
Cdd:PRK06793 238 AEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQK--GSITGIYTVLVDGDD 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28603772 355 ITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSNQLYACYAIGKD 425
Cdd:PRK06793 313 LNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
60-396 |
1.46e-26 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 112.17 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 60 AQYAEIVNFTLPNGT--QRsGQVLEVSGTKAIVQVFEGTSGIdAQKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGP 137
Cdd:PRK09099 43 VTLGELCELRQRDGTllQR-AEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 138 VVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyh 217
Cdd:PRK09099 121 PLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQC----------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 218 DDNFAIVFAAMGvnMETARFFKSDFEQNGtMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSY 297
Cdd:PRK09099 190 DVNVIALIGERG--REVREFIELILGEDG-MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 298 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQL 377
Cdd:PRK09099 266 ARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREI 343
|
330
....*....|....*....
gi 28603772 378 HNRQIYPPINVLPSLSRLM 396
Cdd:PRK09099 344 AARNQYPAIDVLGSLSRVM 362
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
32-395 |
8.46e-25 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 106.62 E-value: 8.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 32 NYITHPRityrtvcSVNGPLV--VLDQVKFAQYAEIvnftlpngtQRSGQVLEVSGtKAIVQVFEGTSGI-----DAQKT 104
Cdd:PRK08149 5 QRLAHPL-------RIQGPIIeaELPDVAIGEICEI---------RAGWHSNEVIA-RAQVVGFQRERTIlsligNAQGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 105 TCEF----TGDILRTPVSEDMLGRVFNGSGKPIDK--GPVVMAEDF--LDINGQPINPHDRIYPEEMIETGISPIDVMNS 176
Cdd:PRK08149 68 SRQVvlkpTGKPLSVWVGEALLGAVLDPTGKIVERfdAPPTVGPISeeRVIDVAPPSYAERRPIREPLITGVRAIDGLLT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 177 IARGQKIPIFSAAGLPHNEIAAQICRQAglvkkskavldyHDDNFAIvfaamGVNMETARF---FKSDFEQNGTMGNVCL 253
Cdd:PRK08149 148 CGVGQRMGIFASAGCGKTSLMNMLIEHS------------EADVFVI-----GLIGERGREvteFVESLRASSRREKCVL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 254 FLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 333
Cdd:PRK08149 211 VYATSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPG 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28603772 334 RVegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:PRK08149 290 AT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
60-394 |
4.08e-23 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 102.45 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 60 AQYAEIVNFtlPNGTQrsGQV--LEVSGTKAIV-----QVFEGTsgidaqktTCEFTGDILRTPVSEDMLGRVFNGSGKP 132
Cdd:PRK09281 47 VMAGELLEF--PGGVY--GIAlnLEEDNVGAVIlgdyeDIKEGD--------TVKRTGRILEVPVGEALLGRVVNPLGQP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 133 ID-KGPVVmAEDFLDIngqpinphDRIYP--------EEMIETGISPIDVMNSIARGQKIPIfsaaglphneiaaqIC-R 202
Cdd:PRK09281 115 IDgKGPIE-ATETRPV--------ERKAPgvidrksvHEPLQTGIKAIDAMIPIGRGQRELI--------------IGdR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 203 QAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFL 279
Cdd:PRK09281 172 QTG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 280 AYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPIL-TMPND 353
Cdd:PRK09281 250 MDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTALPIIeTQAGD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 28603772 354 dITHPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:PRK09281 326 -VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
101-452 |
4.51e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 101.51 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 101 AQKTTCEFTGDILrtpVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIAR 179
Cdd:PRK07196 79 ARVFPSEQDGELL---IGDSWLGRVINGLGEPLDgKGQL-GGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 180 GQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAN 259
Cdd:PRK07196 155 GQRVGLMAGSGVGKSVLLGMITR--------------YTQADVVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPAD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 260 DPTIERIITPRLALTTAEFlaYQCEKH-VLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGr 338
Cdd:PRK07196 221 ESPLMRIKATELCHAIATY--YRDKGHdVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG- 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 339 GGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGegmtrKDHGDVSNQLYA 418
Cdd:PRK07196 298 NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIG-----SQQAKAASLLKQ 372
|
330 340 350
....*....|....*....|....*....|....*...
gi 28603772 419 CYAIGKDVQAMKA----VVGEEALTSEDLLYLEFLQKF 452
Cdd:PRK07196 373 CYADYMAIKPLIPlggyVAGADPMADQAVHYYPAITQF 410
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
116-431 |
1.47e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 100.16 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 116 PVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHN 194
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDgLGPI-YTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 195 EIAAQICRqaglvkKSKAVLdyhddnfaIVFAAMGvnmETARFFKSDFEQ----NGTMGNVCLFLNLANDPTIeRIITPR 270
Cdd:PRK08972 177 VLLGMMTR------GTTADV--------IVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 271 LALTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTM 350
Cdd:PRK08972 239 TATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 351 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVS---NQLYACYAIGKDVQ 427
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDLI 392
|
....
gi 28603772 428 AMKA 431
Cdd:PRK08972 393 SIGA 396
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
37-396 |
7.54e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 98.13 E-value: 7.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 37 PRITYRTVCSVNGPLVVLDQVKFAQY--AEIVNFTLPNGTQRSgQVLEVSGTKAIVQVFEGTSGIdAQKTTCEFTGDILR 114
Cdd:PRK08927 14 TLVIYGRVVAVRGLLVEVAGPIHALSvgARIVVETRGGRPVPC-EVVGFRGDRALLMPFGPLEGV-RRGCRAVIANAAAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 115 TPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGlph 193
Cdd:PRK08927 92 VRPSRAWLGRVVNALGEPIDgKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSG--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 194 neiaaqicrqaglVKKSK--AVLDYHDDNFAIVFAAMGvnmETAR----FFKSDFEQNGTMGNVcLFLNLANDPTIERII 267
Cdd:PRK08927 169 -------------VGKSVllSMLARNADADVSVIGLIG---ERGRevqeFLQDDLGPEGLARSV-VVVATSDEPALMRRQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 268 TPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPI 347
Cdd:PRK08927 232 AAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFT 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 28603772 348 LTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:PRK08927 311 VLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
114-396 |
1.70e-21 |
|
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: 94.21 E-value: 1.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPinPH-DRIYPE-EMIETGISPIDVMNSIARGQKIPIFSAAG- 190
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA--PEfVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 191 --------LPHNeIAAqicRQAGLVkkskavldyhddnfaiVFAAMGvnmETAR--------FFKSDFEQNGTMGNVCLF 254
Cdd:cd01133 79 gktvlimeLINN-IAK---AHGGYS----------------VFAGVG---ERTRegndlyheMKESGVINLDGLSKVALV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 255 LNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 334
Cdd:cd01133 136 YGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITS 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28603772 335 VegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:cd01133 216 T--KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
116-394 |
3.54e-21 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 95.74 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 116 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNE 195
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 196 IAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLA 272
Cdd:PRK05922 173 LLSTI------AKGSKSTIN--------VIALIG---ERGREVREYIEQHKEglaAQRTIIIASPAHETAPTKVIAGRAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 273 LTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrGGSITQI-PILTMP 351
Cdd:PRK05922 236 MTIAEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYP 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 28603772 352 NdditHP--IPDLTGFITEGQIYVDRQlHNRQIYPPINVLPSLSR 394
Cdd:PRK05922 313 N----HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
60-394 |
9.13e-21 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 95.11 E-value: 9.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 60 AQYAEIVNFtlPNGTQrsGQVL-----EVsgtkAIVqVFEGTSGIDA-QKTTCefTGDILRTPVSEDMLGRVFNGSGKPI 133
Cdd:COG0056 47 AMAGELLEF--PGGVY--GMALnleedNV----GVV-LLGDYEGIKEgDTVKR--TGRILSVPVGEALLGRVVDPLGRPI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 134 D-KGPVVmAEDFLDIngqpinphDRIYP--------EEMIETGISPIDVMNSIARGQKipifsaaglphnEIaaqIC--R 202
Cdd:COG0056 116 DgKGPIE-AEERRPV--------ERPAPgvidrqpvHEPLQTGIKAIDAMIPIGRGQR------------EL---IIgdR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 203 QAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFL 279
Cdd:COG0056 172 QTG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 280 AYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDD 354
Cdd:COG0056 250 MDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTALPIIETQAGD 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 28603772 355 ITHPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:COG0056 326 VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
118-420 |
8.56e-18 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 86.18 E-value: 8.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 118 SEDMLGRVFNGSGKPI-DKGPVVMAEDFLDINGQPIN-PHD---RIYPEEMIETGISPIDVMNSIARGQKIPIFSAaglp 192
Cdd:PRK07165 76 SKEYFGKIIDIDGNIIyPEAQNPLSKKFLPNTSSIFNlAHGlmtVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGD---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 193 hneiaaqicRQAGlvKKSKA---VLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPtIERIITP 269
Cdd:PRK07165 152 ---------RQTG--KTHIAlntIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYLAP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 270 RLALTTAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILT 349
Cdd:PRK07165 220 YVAMAHAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNR-KTITALPILQ 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28603772 350 MPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLmKSAIGEGMTRKDHGDVsNQLYACY 420
Cdd:PRK07165 297 TVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRT-GSSVQSKTITKVAGEI-SKIYRAY 365
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
248-394 |
9.59e-18 |
|
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: 83.39 E-value: 9.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 248 MGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLAT 327
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28603772 328 IYERAGRVE-----GRGGSITQIPILTMPNDDITHPIPDLTGFITegQIY--VDRQLHNRQIYPPINVLPSLSR 394
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
62-404 |
7.05e-16 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 80.47 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 62 YAEIVNFTLPNGTQRSGQV--LEVSGTKAIVQVFEGTSGIDAQKTTCefTGDILRTPVSEDMLGRVFNGSGKPIDKGPVV 139
Cdd:PTZ00185 64 YNTIIMIQVSPTTFAAGLVfnLEKDGRIGIILMDNITEVQSGQKVMA--TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 140 MAEDFLD-------INGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSAAGLPHNEIA-AQICRQaglVKKSK 211
Cdd:PTZ00185 142 RSRALLEseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvSTIINQ---VRINQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 212 AVLDyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVIL 291
Cdd:PTZ00185 219 QILS--KNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNR-GRHCLCVY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 292 TDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GRGG-SITQIPILTMPNDDITHPIPDLTGFITEG 369
Cdd:PTZ00185 296 DDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKGGgSVTALPIVETLSNDVTAYIVTNVISITDG 375
|
330 340 350
....*....|....*....|....*....|....*
gi 28603772 370 QIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 404
Cdd:PTZ00185 376 QIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
248-393 |
3.09e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 78.91 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 248 MGNVCLFLNLANDPTIERIITPRLALTTAEF---LAYQcekhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 324
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYfrdMGYD----VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASK 792
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28603772 325 LATIYERAGRV-----EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 393
Cdd:PRK14698 793 LAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
109-468 |
6.34e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 77.00 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 109 TGDILRTPVSEDMLGRVFNGSGKPIDK-GPVVMAEDFldingqPINPHDRIYPE-----EMIETGISPIDVMNSIARGQK 182
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTS------PIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 183 IPIFSAAGLPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMG--------VNMETaRFFKSDFEQNGTMGN 250
Cdd:CHL00060 164 IGLFGGAGVGKTvlimELINNIAKAHGGVS---------------VFGGVGertregndLYMEM-KESGVINEQNIAESK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 251 VCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 330
Cdd:CHL00060 228 VALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 331 RAGRVegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmtrkdhg 410
Cdd:CHL00060 308 RITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRI---------- 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28603772 411 dVSNQLYAC----------YaigKDVQAMKAVVGEEALTSEDLLYLEFLQKFEkKFINQgPYEKRSVF 468
Cdd:CHL00060 376 -VGEEHYETaqrvkqtlqrY---KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ-PFFVAEVF 437
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
43-450 |
2.51e-14 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 75.59 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 43 TVCSVNGPLVVLDQVKFAQYAEIVNFtlpnGTQR-SGQVLEVSGTKAIVQVFEGTSGIdAQKTTCEFTGDilrtPVSED- 120
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVRV----GEEGlIGEIIRIEGDKATIQVYEETSGI-KPGEPVEFTGE----PLSVEl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 121 ---MLGRVFNGSGKPIDK--------------------------------GPVVMAEDFL-----------------DIN 148
Cdd:PRK04192 77 gpgLLGSIFDGIQRPLDElaeksgdflergvyvpaldrekkweftptvkvGDKVEAGDILgtvqetpsiehkimvppGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 149 G---------------------------------------QPINPHDRIYPEEMIETGISPIDVMNSIARGQK--IPIFS 187
Cdd:PRK04192 157 GtvkeivsegdytvddtiavlededgegveltmmqkwpvrRPRPYKEKLPPVEPLITGQRVIDTFFPVAKGGTaaIPGPF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 188 AAG---LPHneiaaQICRQAglvkkskavldyhdDNFAIVFAAMGvnmetarffksdfEQNGTMGNV------------- 251
Cdd:PRK04192 237 GSGktvTQH-----QLAKWA--------------DADIVIYVGCG-------------ERGNEMTEVleefpelidpktg 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 252 -------CLFLNLANDPTIER---IITprlALTTAEF---LAYqcekHVLVILTDMSSYAEALREVSAAREEVPGRRGFP 318
Cdd:PRK04192 285 rplmertVLIANTSNMPVAAReasIYT---GITIAEYyrdMGY----DVLLMADSTSRWAEALREISGRLEEMPGEEGYP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 319 GYMYTDLATIYERAGRVE---GRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSrL 395
Cdd:PRK04192 358 AYLASRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-L 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28603772 396 MKSAIGEGMTRK---DHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLE--------FLQ 450
Cdd:PRK04192 437 YLDQVAPWWEENvdpDWRELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEvarliredFLQ 502
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
109-442 |
5.48e-14 |
|
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: 73.97 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 109 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHDRIYPEEMIETGISPIDVMNSIARGQKIPIFSA 188
Cdd:COG0055 75 TGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 189 AG---------LPHNeIAAQicrQAGLVkkskavldyhddnfaiVFAAMGvnmETARF---FKSDFEQNGTMGNVCLFLN 256
Cdd:COG0055 155 AGvgktvlimeLIHN-IAKE---HGGVS----------------VFAGVG---ERTREgndLYREMKESGVLDKTALVFG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 257 LANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVe 336
Cdd:COG0055 212 QMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITST- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 337 gRGGSITQIPILTMPNDDITHPIP-------DLTgfitegqIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkD 408
Cdd:COG0055 291 -KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE-----E 357
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 28603772 409 HGDVSN------QLYacyaigKDVQAMKAVVGEEALTSED 442
Cdd:COG0055 358 HYRVARevqrilQRY------KELQDIIAILGMDELSEED 391
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
44-110 |
1.61e-10 |
|
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: 56.78 E-value: 1.61e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 44 VCSVNGPLVVLDQVKFAQYAEIVNFTLP---NGTQRSGQVLEVSGTKAIVQVFEGTSGIDaQKTTCEFTG 110
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVElveFGSLVLGEVLNLGGDKVRVQVFGGTSGLS-RGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
409-479 |
4.72e-08 |
|
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: 50.14 E-value: 4.72e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28603772 409 HGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEkKFINQGPYEKRSVFESLDLGWKLLR 479
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLE-EFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
41-111 |
9.57e-08 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 49.23 E-value: 9.57e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28603772 41 YRTVCSVNGPLVVLDQVKFAQYAEIVNFTLPNG---TQRSGQVLEVSGTKAIVQVFEGTSGIDaQKTTCEFTGD 111
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLS-RGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
44-134 |
1.94e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 44.24 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 44 VCSVNGPLVVLDQVKFAQYAEIVNFtlpNGTQRSGQVLEVSGTKAIVQVFEGTSGIDAQKTTcEFTGDILRTPVSEDMLG 123
Cdd:PRK14698 7 IIRVTGPLVIADGMKGAKMYEVVRV---GELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPV-EGTGSSLSVELGPGLLT 82
|
90
....*....|.
gi 28603772 124 RVFNGSGKPID 134
Cdd:PRK14698 83 SIYDGIQRPLE 93
|
|
| ATP-synt_V_A-type_alpha_N |
cd18119 |
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of ... |
43-99 |
2.10e-03 |
|
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex 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: 349743 [Multi-domain] Cd Length: 67 Bit Score: 36.73 E-value: 2.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28603772 43 TVCSVNGPLVVLDQVKFAQYAEIV---NFTLPngtqrsGQVLEVSGTKAIVQVFEGTSGI 99
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELVrvgEEGLI------GEIIRLEGDKATIQVYEETSGL 56
|
|
| |
