|
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 ... |
40-503 |
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: 1015.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 40 TYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSE 119
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 120 DMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 199
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 200 ICRQAGLVKKS-KAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEF 278
Cdd:TIGR01040 161 ICRQAGLVKLPtKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 279 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHP 358
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 359 IPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEAL 438
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109103298 439 TSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 503
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
|
|
| 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: 839.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 37 PRVTYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTP 116
Cdd:COG1156 2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 117 VSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEI 196
Cdd:COG1156 82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 197 AAQICRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTA 276
Cdd:COG1156 162 AAQIARQAKVRGE--------EEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 277 EFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDIT 356
Cdd:COG1156 234 EYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDIT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 357 HPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEE 436
Cdd:COG1156 314 HPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109103298 437 ALTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 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: 809.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 38 RVTYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPV 117
Cdd:PRK04196 1 LKEYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 118 SEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIA 197
Cdd:PRK04196 81 SEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 198 AQICRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAE 277
Cdd:PRK04196 161 AQIARQAKVLGE--------EENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 278 FLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITH 357
Cdd:PRK04196 233 YLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 358 PIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEA 437
Cdd:PRK04196 313 PIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109103298 438 LTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFYSREGA 503
Cdd:PRK04196 393 LSERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRG 458
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
41-498 |
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: 693.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 41 YRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSED 120
Cdd:TIGR01041 2 YSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 121 MLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 200
Cdd:TIGR01041 82 MLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 201 CRQAGLVKKskavldyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLA 280
Cdd:TIGR01041 162 ARQATVRGE--------ESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 281 YQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIP 360
Cdd:TIGR01041 234 FEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 361 DLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTS 440
Cdd:TIGR01041 314 DLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 109103298 441 EDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFPKEMLKRIPQAVIDEFY 498
Cdd:TIGR01041 394 RDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYH 451
|
|
| 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: 612.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 112 ILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGL 191
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 192 PHNEIAAQICRQAGLVKkskavldyHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRL 271
Cdd:cd01135 81 PHNELAAQIARQAGVVG--------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 272 ALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMP 351
Cdd:cd01135 153 ALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 109103298 352 NDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG 401
Cdd:cd01135 233 NDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
38-501 |
1.06e-119 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 358.58 E-value: 1.06e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 38 RVTYRTVCSVNGPLVVLdRVKFAQYAEIVHFTLPDGTqRSGQVLEVAGTKAIVQVFEGTSGI--DARKTtceFTGDILRT 115
Cdd:PRK02118 2 QKIYTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGIstGDEVV---FLGRPMQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 116 PVSEDMLGRVFNGSGKPIDKGPVVMAEDfLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 195
Cdd:PRK02118 77 TYSESLLGRRFNGSGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 196 IAAQICRQAglvkkskavldyhdDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTT 275
Cdd:PRK02118 156 LLARIALQA--------------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 276 AEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrGGSITQIPILTMPNDDI 355
Cdd:PRK02118 222 AEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 356 THPIPDLTGFITEGQIYvdrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRKDHGDVSN---QLYACYAIGKDVQAMkav 432
Cdd:PRK02118 301 THPVPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM--- 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109103298 433 vGEEaLTSEDLLYLEFLQKFEKNFINQG---PYEnrsvfESLDLGWKLL-RIF-PKEMLkrIPQAVIDEFYSRE 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 |
7.24e-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: 312.37 E-value: 7.24e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 167 GISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGlvkkskavldyHDdnfAIVFAAMGVNMETARFFKSDFEQNG 246
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQAS-----------AD---VVVYALIGERGREVREFIEELLGSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 247 TMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLA 326
Cdd:pfam00006 67 ALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109103298 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 |
1.39e-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: 311.31 E-value: 1.39e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPH 193
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 194 NEIAAQICRQAglvKKSKAvldyhddnFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLAL 273
Cdd:cd19476 81 TVLAMQLARNQ---AKAHA--------GVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 274 TTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPND 353
Cdd:cd19476 150 TIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 109103298 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 |
6.67e-64 |
|
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: 202.66 E-value: 6.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 403 GMTRKDHGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRIFP 482
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 109103298 483 KEMLKRIPQAVIDEF 497
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
114-395 |
4.31e-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: 148.48 E-value: 4.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPH 193
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 194 NEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETAR----FFKSDFEQNGtMGNVCLFLNLANDPTIERIITP 269
Cdd:cd01136 81 STLLGMIAR--------------NTDADVNVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVRAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 270 RLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILT 349
Cdd:cd01136 143 YTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVL 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 109103298 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 |
4.09e-37 |
|
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: 143.30 E-value: 4.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 64 EIVHFtlPDGTQRSGQVLEVAGTKAIVqvFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KGPVVmAE 142
Cdd:TIGR00962 50 ELIEF--EGGVQGIALNLEEDSVGAVI--MGDYSDI-REGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDgKGPID-SD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 143 DFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGlvKKSKAV---LDYHDD 219
Cdd:TIGR00962 124 EFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGD-------------RQTG--KTAVAIdtiINQKDS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 220 NFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAE 299
Cdd:TIGR00962 189 DVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 300 ALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVD 374
Cdd:TIGR00962 268 AYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLE 344
|
330 340
....*....|....*....|....*
gi 109103298 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 |
1.99e-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: 1.99e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109103298 40 TYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGD 111
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
64-396 |
4.78e-36 |
|
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: 139.01 E-value: 4.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 64 EIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAED 143
Cdd:COG1157 42 ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 144 FLDINGQPINPHSR--IypEEMIQTGISPIDVMNSIARGQKIPIFSAAG------LphneiaAQICRQA-------GLV- 207
Cdd:COG1157 121 RRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL------GMIARNTeadvnviALIg 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 208 -------------------KKSkavldyhddnfaIVFAAmgvnmeTarffkSDfeqngtmgnvclflnlanDPTIERIIT 268
Cdd:COG1157 193 ergrevrefieddlgeeglARS------------VVVVA------T-----SD------------------EPPLMRLRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 269 PRLALTTAEFLAYQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQI 345
Cdd:COG1157 232 AYTATAIAEYFRDQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAF 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 109103298 346 -PILTmPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:COG1157 306 yTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
79-478 |
4.81e-35 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 136.48 E-value: 4.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 79 QVLEVAGTKAIVQVFEGTSGIDARKTTcEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINPHSRI 158
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGLRCGQWV-TPLGHMHQVQVGADLAGRILDGLGAPIDGGPPLTGQ-WRELDCPPPSPLTRQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 159 YPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAMGvnmETARFF 238
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA--------------DSAADVMVLALIG---ERGREV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 239 KSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLALTTAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRR 315
Cdd:PRK06820 205 REFLEQVLTpeaRARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 316 GFPGYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:PRK06820 284 SFPPSVFANLPRLLERTGNSDR--GSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 396 MKSAIGEGmtRKDHGDVSNQLYACYaigKDVQAMKAVvgEEALTSEDLLYLEFLQKFE--KNFINQGPYENRSVFESLDL 473
Cdd:PRK06820 362 MPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEH 434
|
....*
gi 109103298 474 GWKLL 478
Cdd:PRK06820 435 LAQVV 439
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
109-396 |
2.37e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 134.49 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 109 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSA 188
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 189 AGLPHNEIAAQICRQAglvkkskavldyhdDNFAIVFAAMGV-NMETARFFKSDFEQNGtMGNVCLFLNLANDPTIERII 267
Cdd:PRK06936 171 AGGGKSTLLASLIRSA--------------EVDVTVLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAK 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 268 TPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRGGSITQIPI 347
Cdd:PRK06936 236 AGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYT 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 109103298 348 LTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:PRK06936 313 VLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVM 361
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
112-394 |
3.25e-32 |
|
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: 124.59 E-value: 3.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 112 ILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP-INPHSRIYpeEMIQTGISPIDVMNSIARGQKIPIFSAa 189
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDgKGPIQTKERRRVESKAPgIIPRQSVN--EPLQTGIKAIDSLIPIGRGQRELIIGD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 190 glphneiaaqicRQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERI 266
Cdd:cd01132 78 ------------RQTG--KTAIAIdtiINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 267 ITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGS 341
Cdd:cd01132 144 LAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGS 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 109103298 342 ITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:cd01132 220 LTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
113-402 |
3.97e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 127.88 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 113 LRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLP 192
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 193 HNEIAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQN--GTMGNVCLFLNLANDPTIERIITPR 270
Cdd:PRK08472 170 KSTLMGMI------VKGCLAPIK--------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGAF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 271 LALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILTM 350
Cdd:PRK08472 233 CAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLV 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 109103298 351 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGE 402
Cdd:PRK08472 311 EGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
79-402 |
1.37e-29 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 120.83 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 79 QVLEVAGTKAIVQVFEGTSGIdarktTCEFTGDILR----TPVSEDMLGRVFNGSGKPIDKGPVVMAEdFLDINGQPINP 154
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGL-----HCGQQVMALRrrhqVPVGEALLGRVIDGFGRPLDGRELPDVC-WKDYDAMPPPA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 155 HSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyhDDNfaiVFAAMGVNMET 234
Cdd:PRK07594 130 MVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA-----------DSN---VLVLIGERGRE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 235 ARFFkSDFEQNGTMGNVCLFLNLAND-PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPG 313
Cdd:PRK07594 196 VREF-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 314 RRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 393
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLS 351
|
....*....
gi 109103298 394 RLMKSAIGE 402
Cdd:PRK07594 352 RVFPVVTSH 360
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
111-471 |
3.30e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 119.84 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 111 DILRTPVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAA 189
Cdd:PRK05688 99 DTGRLPMGMSMLGRVLDGAGRALDgKGPM-KAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 190 GLphneiaaqicrqaglvkkSKAVLDYHDDNFA----IVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIER 265
Cdd:PRK05688 178 GV------------------GKSVLLGMMTRFTeadiIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 266 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQI 345
Cdd:PRK05688 240 LRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 346 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIG-EGMTRKDHgdvSNQLYACYAIGK 424
Cdd:PRK05688 319 YTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQSR 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 109103298 425 DVQAMKAVV-GEEALTSEDLLYLEFLQKfeknFINQGPYENRSVFESL 471
Cdd:PRK05688 396 DLISVGAYVaGGDPETDLAIARFPHLVQ----FLRQGLRENVSLAQSR 439
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
109-399 |
5.50e-29 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 119.68 E-value: 5.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 109 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQP--InphSRIYPEEMIQTGISPIDVMNSIARGQKIPI 185
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDgKGEISASESRLIESPAPgiI---SRRSVYEPLQTGLIAIDSMIPIGRGQRELI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 186 FSAaglphneiaaqicRQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPT 262
Cdd:CHL00059 147 IGD-------------RQTG--KTAVATdtiLNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 263 IERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRVEGR- 338
Cdd:CHL00059 212 TLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSQl 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109103298 339 -GGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 399
Cdd:CHL00059 288 gEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
58-399 |
6.98e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 118.95 E-value: 6.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 58 KFAQYAEIVHFTLPDGTQRsGQVLEVAGTKAIVQVFEgtSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID-KG 136
Cdd:PRK06002 45 RFVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPIDgLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 137 PVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGlphneiaaqicrqaglVKKSK--AVL 214
Cdd:PRK06002 122 PLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSG----------------VGKSTllAML 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 215 DYHDDNFAIVFAAMGVNMETARFFKSDfeqngTMGNvclflNLANDPTI---------ERIITPRLALTTAEFLAYQCEK 285
Cdd:PRK06002 186 ARADAFDTVVIALVGERGREVREFLED-----TLAD-----NLKKAVAVvatsdespmMRRLAPLTATAIAEYFRDRGEN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 286 hVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGF 365
Cdd:PRK06002 256 -VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRG 334
|
330 340 350
....*....|....*....|....*....|....
gi 109103298 366 ITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSA 399
Cdd:PRK06002 335 TLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
60-396 |
8.58e-29 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 118.33 E-value: 8.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 60 AQYAEIVHFTLPDGT--QRsGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGP 137
Cdd:PRK09099 43 VTLGELCELRQRDGTllQR-AEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 138 VVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLvkkskavldyh 217
Cdd:PRK09099 121 PLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQC----------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 218 DDNfaiVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSY 297
Cdd:PRK09099 190 DVN---VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 298 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQL 377
Cdd:PRK09099 266 ARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREI 343
|
330
....*....|....*....
gi 109103298 378 HNRQIYPPINVLPSLSRLM 396
Cdd:PRK09099 344 AARNQYPAIDVLGSLSRVM 362
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
109-394 |
1.30e-28 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 118.86 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 109 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFldingqPINphsRIYPEEM--------IQTGISPIDVMNSIAR 179
Cdd:PRK13343 91 TGRVLEVPVGDGLLGRVIDPLGRPLDgGGPLQATARR------PLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 180 GQKIPIFSAAGLPHNEIAAQicrqaglvkkskAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAN 259
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIAID------------AIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEAS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 260 DPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRV--EG 337
Cdd:PRK13343 230 DPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLspEL 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 109103298 338 RGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:PRK13343 309 GGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
101-482 |
6.28e-28 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 116.04 E-value: 6.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 101 ARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARG 180
Cdd:PRK07960 96 ARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 181 QKIPIFSAAGLPHNEIAAQICR--QAGLvkkskavldyhddnfaIVFAAMGvnmETARFFKsDFEQN--GTMGnvclfln 256
Cdd:PRK07960 176 QRMGLFAGSGVGKSVLLGMMARytQADV----------------IVVGLIG---ERGREVK-DFIENilGAEG------- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 257 LANDPTIERI--ITPRLALTTAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATI 328
Cdd:PRK07960 229 RARSVVIAAPadVSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPAL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 329 YERAGRVEGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKd 408
Cdd:PRK07960 309 VERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR- 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109103298 409 hgdVSN--QLYACYAIGKDVQAmkavVGEEALTSEDLL--YLEFLQKFEKnFINQGPYEnRSVFEslDLGWKLLRIFP 482
Cdd:PRK07960 388 ---VRQfkQLLSSFQRNRDLVS----VGAYAKGSDPMLdkAIALWPQLEA-FLQQGIFE-RADWE--DSLQALERIFP 454
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
40-459 |
6.28e-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: 113.28 E-value: 6.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 40 TYRTVCSVNGPLVvldRVKFAQYA--EIVHFTLPDGTQRSGQVLEVAG------TKAIVqvFEGTSGIdARKTTCEFTGD 111
Cdd:TIGR01039 1 TKGKVVQVIGPVV---DVEFEQGElpRIYNALKVQNRAESELTLEVAQhlgddtVRTIA--MGSTDGL-VRGLEVIDTGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 112 ILRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFldingqPINPHSRIYPE-----EMIQTGISPIDVMNSIARGQKIPI 185
Cdd:TIGR01039 75 PISVPVGKETLGRIFNVLGEPIDeKGPIPAKERW------PIHRKAPSFEEqstkvEILETGIKVIDLLAPYAKGGKIGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 186 FSAAGLPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDP 261
Cdd:TIGR01039 149 FGGAGVGKTvliqELINNIAKEHGGYS---------------VFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 262 TIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRGGS 341
Cdd:TIGR01039 214 PGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKTGS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 342 ITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrkDHGDVSNQLYACY 420
Cdd:TIGR01039 292 ITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQIL 366
|
410 420 430
....*....|....*....|....*....|....*....
gi 109103298 421 AIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKnFINQ 459
Cdd:TIGR01039 367 QRYKELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
107-425 |
1.52e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 111.74 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 107 EFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIF 186
Cdd:PRK07721 85 EATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 187 SAAGLPHNEIAAQICRQaglvkkSKAVLDyhddnfaiVFAAMGVN-METARFFKSDFEQNGTMGNVcLFLNLANDPTIER 265
Cdd:PRK07721 165 AGSGVGKSTLMGMIARN------TSADLN--------VIALIGERgREVREFIERDLGPEGLKRSI-VVVATSDQPALMR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 266 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrgGSITQI 345
Cdd:PRK07721 230 IKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS--GSITAF 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 346 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSN---QLYACYAI 422
Cdd:PRK07721 307 YTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQN 381
|
...
gi 109103298 423 GKD 425
Cdd:PRK07721 382 SED 384
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
116-425 |
1.57e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 111.99 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 116 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 195
Cdd:PRK06793 92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 196 IAAQICRQAglvkksKAvldyhDDNFAIVFAAMGvnMETARFFKSDFEQNGTMGNVcLFLNLANDPTIERIITPRLALTT 275
Cdd:PRK06793 172 LLGMIAKNA------KA-----DINVISLVGERG--REVKDFIRKELGEEGMRKSV-VVVATSDESHLMQLRAAKLATSI 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 276 AEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEGrgGSITQIPILTMPNDD 354
Cdd:PRK06793 238 AEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQK--GSITGIYTVLVDGDD 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109103298 355 ITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVSNQLYACYAIGKD 425
Cdd:PRK06793 313 LNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
32-395 |
2.71e-24 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 105.08 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 32 NYITHPRvtyrtvcSVNGPLV--VLDRVKFAQYAEIvhftlpdgtQRSGQVLEVAGtKAIVQVFEGTSGI-----DARKT 104
Cdd:PRK08149 5 QRLAHPL-------RIQGPIIeaELPDVAIGEICEI---------RAGWHSNEVIA-RAQVVGFQRERTIlsligNAQGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 105 TCEF----TGDILRTPVSEDMLGRVFNGSGKPIDK--GPVVMAEDF--LDINGQPINPHSRIYPEEMIQTGISPIDVMNS 176
Cdd:PRK08149 68 SRQVvlkpTGKPLSVWVGEALLGAVLDPTGKIVERfdAPPTVGPISeeRVIDVAPPSYAERRPIREPLITGVRAIDGLLT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 177 IARGQKIPIFSAAGLPHNEIAAQICRQAglvkkskavldyHDDNFAIvfaamGVNMETARF---FKSDFEQNGTMGNVCL 253
Cdd:PRK08149 148 CGVGQRMGIFASAGCGKTSLMNMLIEHS------------EADVFVI-----GLIGERGREvteFVESLRASSRREKCVL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 254 FLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 333
Cdd:PRK08149 211 VYATSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPG 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109103298 334 RVegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRL 395
Cdd:PRK08149 290 AT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
37-396 |
8.51e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 103.91 E-value: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 37 PRVTYRTVCSVNGPLV----VLDRVKFAQYAEIVHFtlpDGTQRSGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDI 112
Cdd:PRK08927 14 TLVIYGRVVAVRGLLVevagPIHALSVGARIVVETR---GGRPVPCEVVGFRGDRALLMPFGPLEGV-RRGCRAVIANAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 113 LRTPVSEDMLGRVFNGSGKPID-KGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGl 191
Cdd:PRK08927 90 AAVRPSRAWLGRVVNALGEPIDgKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSG- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 192 phneiaaqicrqaglVKKSK--AVLDYHDDNFAIVFAAMGvnmETAR----FFKSDFEQNGTMGNVcLFLNLANDPTIER 265
Cdd:PRK08927 169 ---------------VGKSVllSMLARNADADVSVIGLIG---ERGRevqeFLQDDLGPEGLARSV-VVVATSDEPALMR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 266 IITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQI 345
Cdd:PRK08927 230 RQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGL 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 109103298 346 PILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:PRK08927 309 FTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
109-394 |
3.58e-23 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 102.45 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 109 TGDILRTPVSEDMLGRVFNGSGKPID-KGPVVmAEDFLDIN----G----QPINphsriypeEMIQTGISPIDVMNSIAR 179
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQPIDgKGPIE-ATETRPVErkapGvidrKSVH--------EPLQTGIKAIDAMIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 180 GQKIPIfsaaglphneiaaqIC-RQAGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFL 255
Cdd:PRK09281 162 GQRELI--------------IGdRQTG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 256 NLANDPTIERIITPRLALTTAEFLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERA 332
Cdd:PRK09281 226 ATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERA 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109103298 333 GRV--EGRGGSITQIPIL-TMPNDdITHPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:PRK09281 302 AKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
116-431 |
4.88e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 101.70 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 116 PVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHN 194
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDgLGPI-YTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 195 EIAAQICRqaglvkKSKAVLdyhddnfaIVFAAMGvnmETARFFKSDFEQ----NGTMGNVCLFLNLANDPTIeRIITPR 270
Cdd:PRK08972 177 VLLGMMTR------GTTADV--------IVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 271 LALTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTM 350
Cdd:PRK08972 239 TATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 351 PNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHGDVS---NQLYACYAIGKDVQ 427
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDLI 392
|
....
gi 109103298 428 AMKA 431
Cdd:PRK08972 393 SIGA 396
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
72-452 |
4.99e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 101.51 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 72 DGTQRSGQVLEVAGTKAIVQVFEGTSGI--DARKTTCEFTGDILrtpVSEDMLGRVFNGSGKPID-KGPVvMAEDFLDIN 148
Cdd:PRK07196 48 DETFIEAQVVGFDRDITYLMPFKHPGGVlgGARVFPSEQDGELL---IGDSWLGRVINGLGEPLDgKGQL-GGSTPLQQQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 149 GQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvkkskavldyHDDNFAIVFAAM 228
Cdd:PRK07196 124 LPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITR--------------YTQADVVVVGLI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 229 GVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFlaYQCEKH-VLVILTDMSSYAEALREVSAA 307
Cdd:PRK07196 190 GERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATY--YRDKGHdVLLLVDSLTRYAMAQREIALS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 308 REEVPGRRGFPGYMYTDLATIYERAGRVEGrGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPIN 387
Cdd:PRK07196 268 LGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAID 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109103298 388 VLPSLSRLMKSAIGegmtrKDHGDVSNQLYACYAIGKDVQAMKA----VVGEEALTSEDLLYLEFLQKF 452
Cdd:PRK07196 347 ISQSISRCMSQVIG-----SQQAKAASLLKQCYADYMAIKPLIPlggyVAGADPMADQAVHYYPAITQF 410
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
116-394 |
7.25e-22 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 98.05 E-value: 7.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 116 PVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNE 195
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 196 IAAQIcrqaglVKKSKAVLDyhddnfaiVFAAMGvnmETARFFKSDFEQNGT---MGNVCLFLNLANDPTIERIITPRLA 272
Cdd:PRK05922 173 LLSTI------AKGSKSTIN--------VIALIG---ERGREVREYIEQHKEglaAQRTIIIASPAHETAPTKVIAGRAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 273 LTTAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrGGSITQI-PILTMP 351
Cdd:PRK05922 236 MTIAEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYP 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 109103298 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 |
2.41e-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: 97.03 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 60 AQYAEIVHFtlPDGTQrsGQVL-----EVAgtkaiVQVFEGTSGIDArKTTCEFTGDILRTPVSEDMLGRVFNGSGKPID 134
Cdd:COG0056 47 AMAGELLEF--PGGVY--GMALnleedNVG-----VVLLGDYEGIKE-GDTVKRTGRILSVPVGEALLGRVVDPLGRPID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 135 -KGPVVmAEDFLDING--------QPINphsriypeEMIQTGISPIDVMNSIARGQKipifsaaglphnEIaaqIC--RQ 203
Cdd:COG0056 117 gKGPIE-AEERRPVERpapgvidrQPVH--------EPLQTGIKAIDAMIPIGRGQR------------EL---IIgdRQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 204 AGlvKKSKAV---LDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLA 280
Cdd:COG0056 173 TG--KTAIAIdtiINQKGKDVICIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 281 YQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRGGSITQIPILTMPNDDI 355
Cdd:COG0056 251 DQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTALPIIETQAGDV 326
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 109103298 356 THPIPdlTGF--ITEGQIYVDRQLHNRQIYPPINVLPSLSR 394
Cdd:COG0056 327 SAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
114-396 |
1.46e-20 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 91.51 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 114 RTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPinPH-SRIYPE-EMIQTGISPIDVMNSIARGQKIPIFSAAG- 190
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA--PEfVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 191 --------LPHNeIAAqicRQAGLVkkskavldyhddnfaiVFAAMGvnmETAR--------FFKSDFEQNGTMGNVCLF 254
Cdd:cd01133 79 gktvlimeLINN-IAK---AHGGYS----------------VFAGVG---ERTRegndlyheMKESGVINLDGLSKVALV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 255 LNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 334
Cdd:cd01133 136 YGQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITS 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109103298 335 VegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLM 396
Cdd:cd01133 216 T--KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
130-420 |
6.54e-18 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 86.57 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 130 GKPID-KGPVVMAEDFLDINGQPINPHSRIYP-----------EEMIQTGISPIDVMNSIARGQKIPIFSAaglphneia 197
Cdd:PRK07165 81 GKIIDiDGNIIYPEAQNPLSKKFLPNTSSIFNlahglmtvktlNEQLYTGIIAIDLLIPIGKGQRELIIGD--------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 198 aqicRQAGlvKKSKA---VLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPtIERIITPRLALT 274
Cdd:PRK07165 152 ----RQTG--KTHIAlntIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 275 TAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRgGSITQIPILTMPNDD 354
Cdd:PRK07165 225 HAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNR-KTITALPILQTVDND 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109103298 355 ITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLmKSAIGEGMTRKDHGDVsNQLYACY 420
Cdd:PRK07165 302 ITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSRT-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 |
8.98e-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: 83.78 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 248 MGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLAT 327
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109103298 328 IYERAGRVE-----GRGGSITQIPILTMPNDDITHPIPDLTGFITegQIY--VDRQLHNRQIYPPINVLPSLSR 394
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
109-404 |
2.06e-16 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 82.01 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 109 TGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLD-------INGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQ 181
Cdd:PTZ00185 111 TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTRSRALLEseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQ 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 182 KIPIFSAAGLPHNEIA-AQICRQaglVKKSKAVLDyhDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLAND 260
Cdd:PTZ00185 191 RELIVGDRQTGKTSIAvSTIINQ---VRINQQILS--KNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 261 PTIERIITPRLALTTAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GRG 339
Cdd:PTZ00185 266 PAGLQYLAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKG 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109103298 340 G-SITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 404
Cdd:PTZ00185 345 GgSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
248-393 |
2.18e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 79.30 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 248 MGNVCLFLNLANDPTIERIITPRLALTTAEFlaYQCEKHVLVILTDMSS-YAEALREVSAAREEVPGRRGFPGYMYTDLA 326
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEY--FRDMGYDVALMADSTSrWAEALREISGRLEEMPGEEGYPAYLASKLA 794
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109103298 327 TIYERAGRV-----EGRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLS 393
Cdd:PRK14698 795 EFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
109-459 |
7.24e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 77.00 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 109 TGDILRTPVSEDMLGRVFNGSGKPIDK-GPVVMAEDFldingqPINPHSRIYPE-----EMIQTGISPIDVMNSIARGQK 182
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGPVDTRTTS------PIHRSAPAFIQldtklSIFETGIKVVDLLAPYRRGGK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 183 IPIFSAAGLPHN----EIAAQICRQAGLVKkskavldyhddnfaiVFAAMG--------VNMETaRFFKSDFEQNGTMGN 250
Cdd:CHL00060 164 IGLFGGAGVGKTvlimELINNIAKAHGGVS---------------VFGGVGertregndLYMEM-KESGVINEQNIAESK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 251 VCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 330
Cdd:CHL00060 228 VALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 331 RAGRVegRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIgegmtrkdhg 410
Cdd:CHL00060 308 RITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRI---------- 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 109103298 411 dVSNQLYAC----------YaigKDVQAMKAVVGEEALTSEDLLYLEFLQKFEkNFINQ 459
Cdd:CHL00060 376 -VGEEHYETaqrvkqtlqrY---KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 429
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
43-450 |
7.32e-14 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 74.05 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 43 TVCSVNGPLVVLDRVKFAQYAEIVHFtlpdGTQR-SGQVLEVAGTKAIVQVFEGTSGIdARKTTCEFTGDilrtPVSED- 120
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVRV----GEEGlIGEIIRIEGDKATIQVYEETSGI-KPGEPVEFTGE----PLSVEl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 121 ---MLGRVFNG-----------SGKPIDKG---------------PVVMAEDFL---DINGQ-------------PINPH 155
Cdd:PRK04192 77 gpgLLGSIFDGiqrpldelaekSGDFLERGvyvpaldrekkweftPTVKVGDKVeagDILGTvqetpsiehkimvPPGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 156 SRI----------------------------------------------YPEEMIQTGISPIDVMNSIARGQK--IPIFS 187
Cdd:PRK04192 157 GTVkeivsegdytvddtiavlededgegveltmmqkwpvrrprpykeklPPVEPLITGQRVIDTFFPVAKGGTaaIPGPF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 188 AAG---LPHneiaaQICRQAglvkkskavldyhdDNFAIVFAAMGvnmetarffksdfEQNGTMGNV------------- 251
Cdd:PRK04192 237 GSGktvTQH-----QLAKWA--------------DADIVIYVGCG-------------ERGNEMTEVleefpelidpktg 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 252 -------CLFLNLANDPTIER---IITprlALTTAEF---LAYqcekHVLVILTDMSSYAEALREVSAAREEVPGRRGFP 318
Cdd:PRK04192 285 rplmertVLIANTSNMPVAAReasIYT---GITIAEYyrdMGY----DVLLMADSTSRWAEALREISGRLEEMPGEEGYP 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 319 GYMYTDLATIYERAGRVE---GRGGSITQIPILTMPNDDITHPIPDLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSrL 395
Cdd:PRK04192 358 AYLASRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-L 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 109103298 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 ... |
43-442 |
9.11e-13 |
|
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: 70.12 E-value: 9.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 43 TVCSVNGPlvVLDrVKFAQYA-----EIVHFTLPDGTQRsgqVLEVA-----GT-KAIVqvFEGTSGIdARKTTCEFTGD 111
Cdd:COG0055 7 KIVQVIGP--VVD-VEFPEGElpaiyNALEVENEGGGEL---VLEVAqhlgdNTvRCIA--MDSTDGL-VRGMEVIDTGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 112 ILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAG- 190
Cdd:COG0055 78 PISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 191 --------LPHNeIAAQicrQAGLVkkskavldyhddnfaiVFAAMGvnmETARF---FKSDFEQNGTMGNVCLFLNLAN 259
Cdd:COG0055 158 gktvlimeLIHN-IAKE---HGGVS----------------VFAGVG---ERTREgndLYREMKESGVLDKTALVFGQMN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 260 DPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRG 339
Cdd:COG0055 215 EPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITST--KK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 340 GSITQIPILTMPNDDITHPIP-------DLTgfitegqIYVDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHGD 411
Cdd:COG0055 293 GSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE-----EHYR 360
|
410 420 430
....*....|....*....|....*....|....*..
gi 109103298 412 VSN------QLYacyaigKDVQAMKAVVGEEALTSED 442
Cdd:COG0055 361 VARevqrilQRY------KELQDIIAILGMDELSEED 391
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
44-110 |
1.45e-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: 57.17 E-value: 1.45e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 44 VCSVNGPLVVLDRVKFAQYAE--IVHFTLPD-GTQRSGQVLEVAGTKAIVQVFEGTSGIDaRKTTCEFTG 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 |
1.11e-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: 51.68 E-value: 1.11e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109103298 409 HGDVSNQLYACYAIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKnFINQGPYENRSVFESLDLGWKLLR 479
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPETIEDTLEKLYPIKE 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 |
3.93e-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: 50.39 E-value: 3.93e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109103298 41 YRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDG---TQRSGQVLEVAGTKAIVQVFEGTSGIDaRKTTCEFTGD 111
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLS-RGALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
44-134 |
3.50e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 43.47 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 44 VCSVNGPLVVLDRVKFAQYAEIVHFtlpDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTcEFTGDILRTPVSEDMLG 123
Cdd:PRK14698 7 IIRVTGPLVIADGMKGAKMYEVVRV---GELGLIGEIIRLEGDKAVIQVYEETAGLKPGEPV-EGTGSSLSVELGPGLLT 82
|
90
....*....|.
gi 109103298 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 |
2.96e-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: 36.35 E-value: 2.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 109103298 43 TVCSVNGPLVVLDRVKFAQYAEIV---HFTLPdgtqrsGQVLEVAGTKAIVQVFEGTSGI 99
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELVrvgEEGLI------GEIIRLEGDKATIQVYEETSGL 56
|
|
| |
