|
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 ... |
22-488 |
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: 962.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 22 EYRTVSAVNGPLIILQNVKSPRFAEIVNVTLGDGSVRRGQVLEINQDKAVVQIFEGTTGIDNKKTVCQFTGEILKTPVSL 101
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 102 DMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQ 181
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 182 ICRQVCLVSTCTLVKRSGKdEEDFAIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRLALTFAE 261
Cdd:TIGR01040 161 ICRQAGLVKLPTKDVHDGH-EDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 262 YLAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILTMPNDDITH 341
Cdd:TIGR01040 240 YLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 342 PIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYAAYAMGKDALAMRAVVGVEA 421
Cdd:TIGR01040 320 PIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEA 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1352831 422 LSQEDLLYLEFHDKFERRFVNQGAYERRDIYTSLDMAWDLLRIFPVQMLRRIPEKILQEYYHRTSNY 488
Cdd:TIGR01040 400 LSSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSAD 466
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
19-484 |
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: 847.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 19 PRLEYRTVSAVNGPLIILQNVKSPRFAEIVNVTLGDGSVRRGQVLEINQDKAVVQIFEGTTGIDNKKTVCQFTGEILKTP 98
Cdd:COG1156 2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 99 VSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEV 178
Cdd:COG1156 82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 179 AAQICRQVclvstctlvkRSGKDEEDFAIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRLALT 258
Cdd:COG1156 162 AAQIARQA----------KVRGEEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 259 FAEYLAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILTMPNDD 338
Cdd:COG1156 232 AAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 339 ITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYAAYAMGKDALAMRAVVG 418
Cdd:COG1156 312 ITHPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1352831 419 VEALSQEDLLYLEFHDKFERRFVNQGAYERRDIYTSLDMAWDLLRIFPVQMLRRIPEKILQEYYHR 484
Cdd:COG1156 392 EEALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPK 457
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
22-489 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 821.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 22 EYRTVSAVNGPLIILQNVKSPRFAEIVNVTLGDGSVRRGQVLEINQDKAVVQIFEGTTGIDNKKTVCQFTGEILKTPVSL 101
Cdd:PRK04196 3 EYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 102 DMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQ 181
Cdd:PRK04196 83 DMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 182 ICRQVclvstctlvkRSGKDEEDFAIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRLALTFAE 261
Cdd:PRK04196 163 IARQA----------KVLGEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 262 YLAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILTMPNDDITH 341
Cdd:PRK04196 233 YLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 342 PIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYAAYAMGKDALAMRAVVGVEA 421
Cdd:PRK04196 313 PIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352831 422 LSQEDLLYLEFHDKFERRFVNQGAYERRDIYTSLDMAWDLLRIFPVQMLRRIPEKILQEYYHRTSNYE 489
Cdd:PRK04196 393 LSERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRGKE 460
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
22-482 |
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: 708.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 22 EYRTVSAVNGPLIILQNVKSPRFAEIVNVTLGDGSVRRGQVLEINQDKAVVQIFEGTTGIDNKKTVCQFTGEILKTPVSL 101
Cdd:TIGR01041 1 EYSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 102 DMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQ 181
Cdd:TIGR01041 81 DMLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 182 ICRQVCLVStctlvkrsgkDEEDFAIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRLALTFAE 261
Cdd:TIGR01041 161 IARQATVRG----------EESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 262 YLAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILTMPNDDITH 341
Cdd:TIGR01041 231 YLAFEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITH 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 342 PIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYAAYAMGKDALAMRAVVGVEA 421
Cdd:TIGR01041 311 PIPDLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352831 422 LSQEDLLYLEFHDKFERRFVNQGAYERRDIYTSLDMAWDLLRIFPVQMLRRIPEKILQEYY 482
Cdd:TIGR01041 391 LSERDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYH 451
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
94-385 |
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: 610.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 94 ILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGL 173
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 174 PHNEVAAQICRQVCLVstctlvkrsgKDEEDFAIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITP 253
Cdd:cd01135 81 PHNELAAQIARQAGVV----------GSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 254 RLALTFAEYLAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILT 333
Cdd:cd01135 151 RMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILT 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1352831 334 MPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIG 385
Cdd:cd01135 231 MPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
23-482 |
9.23e-122 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 363.58 E-value: 9.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 23 YRTVSAVNGPLIILQnVKSPRFAEIVNVTLGDGSvRRGQVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGEILKTPVSLD 102
Cdd:PRK02118 5 YTKITDITGNVITVE-AEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGISTGDEV-VFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 103 MLGRVFNGSGKPIDGGPPILPEAyLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQI 182
Cdd:PRK02118 82 LLGRRFNGSGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 183 CRQVclvstctlvkrsgkdEEDFaIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRLALTFAEY 262
Cdd:PRK02118 161 ALQA---------------EADI-IILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 263 LAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGrPGSITQLPILTMPNDDITHP 342
Cdd:PRK02118 225 FALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 343 IPDLTGYITEEQIYldrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRKDHSDVSN---QLYAAYAMGKDALAMravvGV 419
Cdd:PRK02118 304 VPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GF 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352831 420 EaLSQEDLLYLEFHDKFERRF----VNQgayerrDIYTSLDMAWDLL-RIF-PVQMLrrIPEKILQEYY 482
Cdd:PRK02118 371 K-LSNWDEKLLKFSELFESRLmdleVNI------PLEEALDLGWKILaQCFhPEEVG--IKEQLIDKYW 430
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
149-377 |
6.01e-110 |
|
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: 324.69 E-value: 6.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 149 GISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQICRQvclvstctlvkrSGKDeedfAIVFAAMGVNMETARFFRQDFEE 228
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQ------------ASAD----VVVYALIGERGREVREFIEELLG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 229 NGAMERVTLFLNLANDPTIERIITPRLALTFAEYLAYeKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTD 308
Cdd:pfam00006 65 SGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1352831 309 LATIYERAGRVEGRPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLS 377
Cdd:pfam00006 144 LARLLERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
96-379 |
3.79e-108 |
|
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: 322.48 E-value: 3.79e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 96 KTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPH 175
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 176 NEVAAQICRQVclvstctlvkrsgKDEEDFAIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRL 255
Cdd:cd19476 81 TVLAMQLARNQ-------------AKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 256 ALTFAEYLAYEkGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILTMP 335
Cdd:cd19476 148 GLTIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTP 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1352831 336 NDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRL 379
Cdd:cd19476 227 GDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 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 ... |
387-481 |
5.34e-56 |
|
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: 181.48 E-value: 5.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 387 GMTRKDHSDVSNQLYAAYAMGKDALAMRAVVGVEALSQEDLLYLEFHDKFERRFVNQGAYERRDIYTSLDMAWDLLRIFP 466
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 1352831 467 VQMLRRIPEKILQEY 481
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
96-379 |
4.02e-47 |
|
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: 164.27 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 96 KTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPH 175
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 176 NEVAAQICRQVclvstctlvkrsgkdEEDfAIVFAAMGvnmETAR----FFRQDFEENGaMERVTLFLNLANDPTIERII 251
Cdd:cd01136 81 STLLGMIARNT---------------DAD-VNVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLLRVR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 252 TPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRveGRPGSITQLPI 331
Cdd:cd01136 141 AAYTATAIAEYFR-DQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYT 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1352831 332 LTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRL 379
Cdd:cd01136 218 VLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
25-463 |
2.31e-45 |
|
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: 164.43 E-value: 2.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 25 TVSAVNGPLIIlqnVKSPRFA--EIVNVTLGDGSVRRGQVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGEILKTPVSLD 102
Cdd:COG1157 22 RVTRVVGLLIE---AVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARV-VPTGRPLSVPVGDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 103 MLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAG------Lphn 176
Cdd:COG1157 98 LLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 177 evaAQICRQvclvSTCTLVkrsgkdeedfaiVFAAMGvnmETAR----FFRQDFEENGaMER-----VTlflnlANDPTI 247
Cdd:COG1157 175 ---GMIARN----TEADVN------------VIALIG---ERGRevreFIEDDLGEEG-LARsvvvvAT-----SDEPPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 248 ERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGrpGSIT 327
Cdd:COG1157 227 MRLRAAYTATAIAEYFR-DQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGK--GSIT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 328 QlpILT--MPNDDITHPIPD-----LTGYiteeqIYLDRQLHNRQIYPPINVLPSLSRLMkSAIgegmTRKDHSDVSN-- 398
Cdd:COG1157 304 A--FYTvlVEGDDMNDPIADavrgiLDGH-----IVLSRKLAERGHYPAIDVLASISRVM-PDI----VSPEHRALARrl 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352831 399 -QLYA------------AYAMGKDALAMRAVvgvealsqedllylEFHDKFErRFVNQGAYERrdiyTSLDMAWDLLR 463
Cdd:COG1157 372 rRLLAryeenedlirigAYQPGSDPELDEAI--------------ALIPAIE-AFLRQGMDER----VSFEESLAQLA 430
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
58-383 |
4.80e-41 |
|
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: 154.08 E-value: 4.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 58 RRGQVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGEILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQ 137
Cdd:TIGR00962 58 VQGIALNLEEDSVGAVIMGDYSDIREGSTV-KRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVI 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 138 SRTYPEEMFETGISSIDVMNSIARGQKiPLFSGAglphnevaaqicRQVCLVSTC--TLVKRSGKDeedFAIVFAAMGVN 215
Cdd:TIGR00962 137 ERKSVHEPLQTGIKAIDAMIPIGRGQR-ELIIGD------------RQTGKTAVAidTIINQKDSD---VYCIYVAIGQK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 216 METARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRLALTFAEYLAYEkGKHVLVILTDMSAYADALREVSAAREEV 295
Cdd:TIGR00962 201 ASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 296 PGRRGYPG---YMYTDLatiYERAGRV--EGRPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPI 370
Cdd:TIGR00962 280 PGREAFPGdvfYLHSRL---LERAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAI 356
|
330
....*....|...
gi 1352831 371 NVLPSLSRLMKSA 383
Cdd:TIGR00962 357 NVGLSVSRVGGAA 369
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
91-455 |
5.68e-40 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 149.90 E-value: 5.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 91 TGEILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSG 170
Cdd:PRK06936 91 TGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 171 AGLPHNEVAAQICR----QVCLVStctLVKRSGKdeedfaivfaamgvnmETARFFRQDFEENGaMERVTLFLNLANDPT 246
Cdd:PRK06936 171 AGGGKSTLLASLIRsaevDVTVLA---LIGERGR----------------EVREFIESDLGEEG-LRKAVLVVATSDRPS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 247 IERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGrvEGRPGSI 326
Cdd:PRK06936 231 MERAKAGFVATSIAEYFR-DQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 327 TQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIGegmtrKDHSDVSNQL------ 400
Cdd:PRK06936 308 TALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVS-----KEHKTWAGRLrellak 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352831 401 YA---------AYAMGKDALAMRAVVGVEALsqedllylefhdkfeRRFVNQGAYERRDIYTSL 455
Cdd:PRK06936 383 YEevelllqigEYQKGQDKEADQAIERIGAI---------------RGFLRQGTHELSHFNETL 431
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
59-462 |
1.25e-37 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 143.42 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 59 RGQVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGEILKTPVSLDMLGRVFNGSGKPIDGGPPiLPEAYLDIQGQPINPQS 138
Cdd:PRK06820 62 LAEVVSIEQEMALLSPFASSDGLRCGQWV-TPLGHMHQVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 139 RTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQICrqvclvstctlvkrSGKDEEdfAIVFAAMGvnmET 218
Cdd:PRK06820 140 RQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC--------------ADSAAD--VMVLALIG---ER 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 219 ARFFRQDFEEN---GAMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEV 295
Cdd:PRK06820 201 GREVREFLEQVltpEARARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 296 PGRRGYPGYMYTDLATIYERAGRVEgrPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPS 375
Cdd:PRK06820 280 PAAGSFPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAAS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 376 LSRLMKSAIGEGmtRKDHSDVSNQLYAAYamgkDALAMRAVVGvEALSQEDllyLEFHDKFER-----RFVNQGAYERRD 450
Cdd:PRK06820 358 VSRIMPQIVSAG--QLAMAQKLRRMLACY----QEIELLVRVG-EYQAGED---LQADEALQRypaicAFLQQDHSETAH 427
|
410
....*....|..
gi 1352831 451 IYTSLDMAWDLL 462
Cdd:PRK06820 428 LETTLEHLAQVV 439
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
41-409 |
1.65e-37 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 142.90 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 41 SPRFAEIVNVTLGDGSVRR-GQVLEINQDKAVVQIFEGTTGID-NKKTVCQFTGeiLKTPVSLDMLGRVFNGSGKPIDGG 118
Cdd:PRK08472 36 NPSVGDIVKIESSDNGKEClGMVVVIEKEQFGISPFSFIEGFKiGDKVFISKEG--LNIPVGRNLLGRVVDPLGRPIDGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 119 PPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGlphnevaaqicrqvclVSTCTLVKRS 198
Cdd:PRK08472 114 GAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSG----------------VGKSTLMGMI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 199 GKDEEDFAIVFAAMGvnmETARFFRQDFEEN--GAMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILT 276
Cdd:PRK08472 178 VKGCLAPIKVVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK-NQGLDVLFIMD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 277 DMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRpGSITQLPILTMPNDDITHPIPDLTGYITEEQIY 356
Cdd:PRK08472 254 SVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLVEGDDMSDPIADQSRSILDGHIV 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1352831 357 LDRQLHNRQIYPPINVLPSLSRLMKSAIGegmtrKDHSDVSNQLYAAYAMGKD 409
Cdd:PRK08472 333 LSRELTDFGIYPPINILNSASRVMNDIIS-----PEHKLAARKFKRLYSLLKE 380
|
|
| 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 ... |
22-93 |
3.94e-37 |
|
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: 131.01 E-value: 3.94e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352831 22 EYRTVSAVNGPLIILQNVKSPRFAEIVNVTLGDGSVRRGQVLEINQDKAVVQIFEGTTGIDNKKTVCQFTGE 93
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
43-463 |
1.08e-36 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 140.67 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 43 RFAEIVNVTLGDGSV-RRGQVLEINQDKAVVQIFEGTTGIDNKKTVCQFtGEILKTPVSLDMLGRVFNGSGKPIDGGPPI 121
Cdd:PRK09099 44 TLGELCELRQRDGTLlQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGL-GRPLSVPVGPALLGRVIDGLGEPIDGGGPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 122 LPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQICRQV-CLVSTCTLVKRSGK 200
Cdd:PRK09099 123 DCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTqCDVNVIALIGERGR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 201 deedfaivfaamgvnmETARFFRQDFEENGaMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSA 280
Cdd:PRK09099 203 ----------------EVREFIELILGEDG-MARSVVVCATSDRSSIERAKAAYVATAIAEYFR-DRGLRVLLMMDSLTR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 281 YADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRveGRPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQ 360
Cdd:PRK09099 265 FARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSRE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 361 LHNRQIYPPINVLPSLSRLMKSAIGEGMTR---------KDHSDVSNQL-YAAYAMGKDALAMRAVVGVEALsqedllyl 430
Cdd:PRK09099 343 IAARNQYPAIDVLGSLSRVMPQVVPREHVQaagrlrqllAKHREVETLLqVGEYRAGSDPVADEAIAKIDAI-------- 414
|
410 420 430
....*....|....*....|....*....|...
gi 1352831 431 efhdkfeRRFVNQgayeRRDIYTSLDMAWDLLR 463
Cdd:PRK09099 415 -------RDFLSQ----RTDEYSDPDATLAALA 436
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-378 |
2.20e-36 |
|
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: 135.76 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 94 ILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKiPLFSGAgl 173
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQR-ELIIGD-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 174 phnevaaqicRQV--CLVSTCTLVKRSGKDeedFAIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERII 251
Cdd:cd01132 78 ----------RQTgkTAIAIDTIINQKGKK---VYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 252 TPRLALTFAEYLAYeKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRV--EGRPGSI 326
Cdd:cd01132 145 APYAGCAMGEYFRD-NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSL 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1352831 327 TQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSR 378
Cdd:cd01132 221 TALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
26-443 |
3.29e-36 |
|
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: 139.85 E-value: 3.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 26 VSAVNGPLI--ILQNVKSPRFAEIVNVTLGDGSVrrgQVLEINQ---DKAVVQIFEGTTGIDNKKTVCQFTGEILKTPVS 100
Cdd:TIGR01039 5 VVQVIGPVVdvEFEQGELPRIYNALKVQNRAESE---LTLEVAQhlgDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 101 LDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGlphneVAA 180
Cdd:TIGR01039 82 KETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAG-----VGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 181 QICRQvclvstcTLVKRSGKDEEDFAiVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRLALTFA 260
Cdd:TIGR01039 157 TVLIQ-------ELINNIAKEHGGYS-VFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 261 EYLAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGrpGSITQLPILTMPNDDIT 340
Cdd:TIGR01039 229 EYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKT--GSITSVQAVYVPADDLT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 341 HPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrkDHSDVSNQLYAAYAMGKDALAMRAVVGV 419
Cdd:TIGR01039 307 DPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQILQRYKELQDIIAILGM 381
|
410 420
....*....|....*....|....
gi 1352831 420 EALSQEDLLYLEFHDKFErRFVNQ 443
Cdd:TIGR01039 382 DELSEEDKLTVERARRIQ-RFLSQ 404
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
98-417 |
4.43e-35 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 136.40 E-value: 4.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 98 PVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGlphne 177
Cdd:PRK05688 104 PMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTG----- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 178 vaaqicrqvclVSTCTLVKRSGKDEEDFAIVFAAMGVN-METARFFRQDFEENGaMERVTLFLNLANDPTIERIITPRLA 256
Cdd:PRK05688 179 -----------VGKSVLLGMMTRFTEADIIVVGLIGERgREVKEFIEHILGEEG-LKRSVVVASPADDAPLMRLRAAMYC 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 257 LTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILTMPN 336
Cdd:PRK05688 247 TRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVLSEG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 337 DDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIG-EGMTRKDHsdvSNQLYAAYAMGKDALAMRA 415
Cdd:PRK05688 326 DDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQSRDLISVGA 402
|
..
gi 1352831 416 VV 417
Cdd:PRK05688 403 YV 404
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
98-415 |
6.56e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 132.90 E-value: 6.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 98 PVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNE 177
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 178 VAAQICR----QVCLVStctLVKRSGKdeedfaivfaamgvnmETARFFRQDFEENGAMERVTLFLNLANDPTIeRIITP 253
Cdd:PRK08972 178 LLGMMTRgttaDVIVVG---LVGERGR----------------EVKEFIEEILGEEGRARSVVVAAPADTSPLM-RLKGC 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 254 RLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILT 333
Cdd:PRK08972 238 ETATTIAEYFR-DQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 334 MPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHSDVS---NQLYAAYAMGKDA 410
Cdd:PRK08972 317 TEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDL 391
|
....*
gi 1352831 411 LAMRA 415
Cdd:PRK08972 392 ISIGA 396
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
61-416 |
3.06e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 130.84 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 61 QVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGEILKTPVSLDMLGRVFNGSGKPIDGGPpiLPEA-YLDIQGQPINPQSR 139
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGLHCGQQV-MALRRRHQVPVGEALLGRVIDGFGRPLDGRE--LPDVcWKDYDAMPPPAMVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 140 TYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQICRQV-CLVSTCTLVKRSGKdeedfaivfaamgvnmET 218
Cdd:PRK07594 133 QPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPdADSNVLVLIGERGR----------------EV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 219 ARFFRQDFEENgAMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGR 298
Cdd:PRK07594 197 REFIDFTLSEE-TRKRCVIVVATSDRPALERVRALFVATTIAEFFR-DNGKRVVLLADSLTRYARAAREIALAAGETAVS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 299 RGYPGYMYTDLATIYERAGRveGRPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSR 378
Cdd:PRK07594 275 GEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSR 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1352831 379 LMKSAIGE-----GMTRKDHSDVSNQL-----YAAYAMGKDALAMRAV 416
Cdd:PRK07594 353 VFPVVTSHehrqlAAILRRCLALYQEVellirIGEYQRGVDTDTDKAI 400
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
61-400 |
3.72e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 130.48 E-value: 3.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 61 QVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGEILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRT 140
Cdd:PRK06793 56 EVIAIEKENNMLLPFEQTEKVCYGDSV-TLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFERE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 141 YPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQICRQV-CLVSTCTLVKRSGKDEEDfaivfaamgvnmeta 219
Cdd:PRK06793 135 EITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAkADINVISLVGERGREVKD--------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 220 rFFRQDFEENGaMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPgRR 299
Cdd:PRK06793 200 -FIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFR-DQGNNVLLMMDSVTRFADARRSVDIAVKELP-IG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 300 GYPGYMYTDLATIYERAGRVEGrpGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRL 379
Cdd:PRK06793 276 GKTLLMESYMKKLLERSGKTQK--GSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRI 353
|
330 340
....*....|....*....|.
gi 1352831 380 MKSAIGEgmtrkDHSDVSNQL 400
Cdd:PRK06793 354 MEEIVSP-----NHWQLANEM 369
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
53-383 |
5.84e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 130.50 E-value: 5.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 53 GDGSVRRGQVLEINQDKAVVQIFEGTTGIDNKKTVcqftgeILKTPVSL----DMLGRVFNGSGKPIDGGPPILP-EAYL 127
Cdd:PRK06002 57 ADGGTHLGEVVRVDPDGVTVKPFEPRIEIGLGDAV------FRKGPLRIrpdpSWKGRVINALGEPIDGLGPLAPgTRPM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 128 DIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGlphnevaaqicrqvclVSTCTLVKR-SGKDEEDfA 206
Cdd:PRK06002 131 SIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSG----------------VGKSTLLAMlARADAFD-T 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 207 IVFAAMGvnmETARFFRQDFEEN--GAMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADA 284
Cdd:PRK06002 194 VVIALVG---ERGREVREFLEDTlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFR-DRGENVLLIVDSVTRFAHA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 285 LREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNR 364
Cdd:PRK06002 270 AREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQ 349
|
330
....*....|....*....
gi 1352831 365 QIYPPINVLPSLSRLMKSA 383
Cdd:PRK06002 350 GRYPAVDPLASISRLARHA 368
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
91-462 |
7.98e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 129.84 E-value: 7.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 91 TGEILKTPVSLDMLGRVFNGSGKPIDGGPpiLPE--AYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLF 168
Cdd:PRK07721 87 TGKPLEVKVGSGLIGQVLDALGEPLDGSA--LPKglAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 169 SGAGLPHNEVAAQICRQVCL-VSTCTLVKRSGKdeedfaivfaamgvnmETARFFRQDFEENGaMERVTLFLNLANDPTI 247
Cdd:PRK07721 165 AGSGVGKSTLMGMIARNTSAdLNVIALIGERGR----------------EVREFIERDLGPEG-LKRSIVVVATSDQPAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 248 ERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGrpGSIT 327
Cdd:PRK07721 228 MRIKGAYTATAIAEYFR-DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS--GSIT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 328 QLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrkDHSDVSN---QLYAAY 404
Cdd:PRK07721 305 AFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTY 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352831 405 AMGKDALAMRAVvgVEALSQEDLLYLEFHDKFErRFVNQGAYERRDIYTSLDMAWDLL 462
Cdd:PRK07721 380 QNSEDLINIGAY--KRGSSREIDEAIQFYPQII-SFLKQGTDEKATFEESIQALLSLF 434
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
91-383 |
1.36e-31 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 127.00 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 91 TGEILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKiPLFSG 170
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR-ELIIG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 171 AglphnevaaqicRQV--CLVSTCTLVKRSGkdeEDFAIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIE 248
Cdd:CHL00059 149 D------------RQTgkTAVATDTILNQKG---QNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 249 RIITPRLALTFAEYLAYeKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRVEGR--P 323
Cdd:CHL00059 214 QYLAPYTGAALAEYFMY-RGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSQlgE 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 324 GSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSA 383
Cdd:CHL00059 290 GSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
98-467 |
2.50e-31 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 125.67 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 98 PVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGlphne 177
Cdd:PRK07960 111 PLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSG----- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 178 vaaqicrqvclVSTCTLVKRSGKDEEDFAIVFAAMGvnmETARFFRqDFEEN--GA--MERVTLFLNLANDPTIERIITP 253
Cdd:PRK07960 186 -----------VGKSVLLGMMARYTQADVIVVGLIG---ERGREVK-DFIENilGAegRARSVVIAAPADVSPLLRMQGA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 254 RLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILT 333
Cdd:PRK07960 251 AYATRIAEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 334 MPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSdvSNQLYAAYAMGKDALAm 413
Cdd:PRK07960 330 TEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQ--FKQLLSSFQRNRDLVS- 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1352831 414 ravVGVEALSQEDLL--YLEFHDKFErRFVNQGAYERrdiyTSLDMAWDLLR-IFPV 467
Cdd:PRK07960 407 ---VGAYAKGSDPMLdkAIALWPQLE-AFLQQGIFER----ADWEDSLQALErIFPT 455
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
58-378 |
6.15e-31 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 125.41 E-value: 6.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 58 RRGQVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGEILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGqpINPQ 137
Cdd:PRK13343 59 SRGFAFNLEEELVGAVLLDDTADILAGTEV-RRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLER--PAPA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 138 --SRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQicrqvclvstcTLVKRSGKDeedFAIVFAAMGVN 215
Cdd:PRK13343 136 iiERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAID-----------AIINQKDSD---VICVYVAIGQK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 216 METARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEV 295
Cdd:PRK13343 202 ASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFR-DQGQDALIVYDDLSKHAAAYRELSLLLRRP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 296 PGRRGYPGYMYTDLATIYERAGRV--EGRPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVL 373
Cdd:PRK13343 281 PGREAYPGDIFYLHSRLLERAAKLspELGGGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVG 360
|
....*
gi 1352831 374 PSLSR 378
Cdd:PRK13343 361 LSVSR 365
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
54-445 |
1.17e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 117.68 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 54 DGSVRRGQVLEINQDKAVVQIFEGTTGIDNKKTV--CQFTGEILktpVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQG 131
Cdd:PRK07196 48 DETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVfpSEQDGELL---IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 132 QPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQICRQVclvstctlvkrsgkdEEDFAIVFAA 211
Cdd:PRK07196 125 PQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYT---------------QADVVVVGLI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 212 MGVNMETARFFRQDFEENGaMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAA 291
Cdd:PRK07196 190 GERGREVKEFIEHSLQAAG-MAKSVVVAAPADESPLMRIKATELCHAIATYYR-DKGHDVLLLVDSLTRYAMAQREIALS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 292 REEVPGRRGYPGYMYTDLATIYERAGRVEGrPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPIN 371
Cdd:PRK07196 268 LGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAID 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1352831 372 VLPSLSRLMKSAIGegmtrKDHSDVSNQL---YAAYAMGKDALAMRAVV-GVEALSQEDLLYLEFHDKFERRFVNQGA 445
Cdd:PRK07196 347 ISQSISRCMSQVIG-----SQQAKAASLLkqcYADYMAIKPLIPLGGYVaGADPMADQAVHYYPAITQFLRQEVGHPA 419
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
59-379 |
6.09e-28 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 115.48 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 59 RGQVLEINQDKAVVQIFEGTTGIdNKKTVCQFTGEILKTPVSLDMLGRVFNGSGK---PIDGGPPILPEA-YLDIQGQPI 134
Cdd:PRK08149 45 RAQVVGFQRERTILSLIGNAQGL-SRQVVLKPTGKPLSVWVGEALLGAVLDPTGKiveRFDAPPTVGPISeERVIDVAPP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 135 NPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGlphnevaaqiCRQVCLVSTctLVKRSGKDeedfaiVFAaMGV 214
Cdd:PRK08149 124 SYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAG----------CGKTSLMNM--LIEHSEAD------VFV-IGL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 215 NMETARF---FRQDFEENGAMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAA 291
Cdd:PRK08149 185 IGERGREvteFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFR-DQGKRVVLFIDSMTRYARALRDVALA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 292 REEVPGRRGYPGYMYTDLATIYERAGRVegRPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPIN 371
Cdd:PRK08149 264 AGELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAID 341
|
....*...
gi 1352831 372 VLPSLSRL 379
Cdd:PRK08149 342 VLKSVSRV 349
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
96-380 |
1.64e-27 |
|
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: 111.16 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 96 KTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQP--INPQSRTYpeEMFETGISSIDVMNSIARGQKIPLFSGAG- 172
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREApeFVELSTEQ--EILETGIKVVDLLAPYAKGGKIGLFGGAGv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 173 --------LPHNeVAaqicrqvclvstctlVKRSGKDeedfaiVFAAMGVNMETARFFRQDFEENG-----AMERVTLFL 239
Cdd:cd01133 79 gktvlimeLINN-IA---------------KAHGGYS------VFAGVGERTREGNDLYHEMKESGvinldGLSKVALVY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 240 NLANDPTIERIITPRLALTFAEYLAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRV 319
Cdd:cd01133 137 GQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352831 320 EGrpGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLM 380
Cdd:cd01133 217 KK--GSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
98-378 |
2.18e-27 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 114.23 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 98 PVSLDMLGRVFNGSGKPIDGGPPiLPEAYLD-IQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFS--GAGlp 174
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQ-LPKTHLKpLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSepGSG-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 175 hnevaaqicrQVCLVSTCTLVKRSGKDeedfaiVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITPR 254
Cdd:PRK05922 170 ----------KSSLLSTIAKGSKSTIN------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 255 LALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEgrPGSITQL-PILT 333
Cdd:PRK05922 234 AAMTIAEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILH 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1352831 334 MPNdditHP--IPDLTGYITEEQIYLDRQlHNRQIYPPINVLPSLSR 378
Cdd:PRK05922 311 YPN----HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
23-380 |
3.31e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 113.54 E-value: 3.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 23 YRTVSAVNGPLIilqNVKSPRFAEIV----NVTLGDGSVRRGQVLEINQDKAVVQIFEGTTGIDNKKTVCqFTGEILKTP 98
Cdd:PRK08927 18 YGRVVAVRGLLV---EVAGPIHALSVgariVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAV-IANAAAAVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 99 VSLDMLGRVFNGSGKPIDGGPPIL--PEAYLdIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHN 176
Cdd:PRK08927 94 PSRAWLGRVVNALGEPIDGKGPLPqgPVPYP-LRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 177 EVAAQICRQV-CLVSTCTLVKRSGKdeedfaivfaamgvnmETARFFRQDFEENGaMERVTLFLNLANDPTIERIITPRL 255
Cdd:PRK08927 173 VLLSMLARNAdADVSVIGLIGERGR----------------EVQEFLQDDLGPEG-LARSVVVVATSDEPALMRRQAAYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 256 ALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPGSITQLPILTMP 335
Cdd:PRK08927 236 TLAIAEYFR-DQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLVD 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1352831 336 NDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLM 380
Cdd:PRK08927 315 GDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
91-378 |
1.02e-25 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 110.15 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 91 TGEILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLD--------IQGQPINpqsrtypeEMFETGISSIDVMNSIARG 162
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPverkapgvIDRKSVH--------EPLQTGIKAIDAMIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 163 QkiplfsgaglphnevaaqicRQvclvstctLV---KRSGK-----DeedfAI----------VFAAMGVNMETARFFRQ 224
Cdd:PRK09281 163 Q--------------------RE--------LIigdRQTGKtaiaiD----TIinqkgkdvicIYVAIGQKASTVAQVVR 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 225 DFEENGAMERVTLFLNLANDPTIERIITPRLALTFAEYLAYeKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPG- 303
Cdd:PRK09281 211 KLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGd 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 304 --YMYTDLatiYERAGRV--EGRPGSITQLPIL-TMPNDdITHPIPdlTGY--ITEEQIYLDRQLHNRQIYPPINVLPSL 376
Cdd:PRK09281 290 vfYLHSRL---LERAAKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISV 363
|
..
gi 1352831 377 SR 378
Cdd:PRK09281 364 SR 365
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
91-378 |
2.11e-25 |
|
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: 108.97 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 91 TGEILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLD--------IQGQPINpqsrtypeEMFETGISSIDVMNSIARG 162
Cdd:COG0056 91 TGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPverpapgvIDRQPVH--------EPLQTGIKAIDAMIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 163 QkiplfsgaglphnevaaqicRQvclvstctLV---KRSGK-----DeedfAI----------VFAAMGVNMETARFFRQ 224
Cdd:COG0056 163 Q--------------------RE--------LIigdRQTGKtaiaiD----TIinqkgkdvicIYVAIGQKASTVAQVVE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 225 DFEENGAMERVTLFLNLANDPTIERIITPRLALTFAEYLAYeKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPG- 303
Cdd:COG0056 211 TLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGd 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 304 --YMYTDLatiYERAGRV--EGRPGSITQLPIL-TMPNddithpipDLTGY-------ITEEQIYLDRQLHNRQIYPPIN 371
Cdd:COG0056 290 vfYLHSRL---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAIN 358
|
....*..
gi 1352831 372 VLPSLSR 378
Cdd:COG0056 359 VGLSVSR 365
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
91-426 |
1.60e-23 |
|
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: 103.25 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 91 TGEILKTPVSLDMLGRVFNGSGKPIDGGPPILPEAYLDIQGQPINPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSG 170
Cdd:COG0055 75 TGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 171 AG---------LPHNeVAAQicrqvclvstctlvkRSGKDeedfaiVFAAMGvnmETAR----FFRqDFEENGAMERVTL 237
Cdd:COG0055 155 AGvgktvlimeLIHN-IAKE---------------HGGVS------VFAGVG---ERTRegndLYR-EMKESGVLDKTAL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 238 FLNLANDPTIERIITPRLALTFAEYLAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAG 317
Cdd:COG0055 209 VFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERIT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 318 RVEGrpGSITQLPILTMPNDDITHPIP-------DLTgyiteeqIYLDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmt 389
Cdd:COG0055 289 STKK--GSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE--- 356
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1352831 390 rkDHSDVSN---QLYAAYAMGKDALAMravVGVEALSQED 426
Cdd:COG0055 357 --EHYRVARevqRILQRYKELQDIIAI---LGMDELSEED 391
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
103-378 |
1.39e-21 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 94.56 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 103 MLGRVFNGSGKPI----DGGPPILPEAyLDIQGQPINpQSRTY-----PEEMFETGISSIDVMNSIARGQK--IPLFSGA 171
Cdd:cd01134 10 LLGSIFDGIQRPLeviaETGSIFIPRG-VNVQRWPVR-QPRPVkeklpPNVPLLTGQRVLDTLFPVAKGGTaaIPGPFGC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 172 GlphNEVAAQicrqvclvstcTLVKRSGKDeedfAIVFAAMGVN-METARFFRqDFEE-------NGAMERVTLFLNLAN 243
Cdd:cd01134 88 G---KTVISQ-----------SLSKWSNSD----VVIYVGCGERgNEMAEVLE-EFPElkdpitgESLMERTVLIANTSN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 244 DPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVE--- 320
Cdd:cd01134 149 MPVAAREASIYTGITIAEYFR-DMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRclg 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1352831 321 --GRPGSITQLPILTMPNDDITHPIPDLTGYITeeQIY--LDRQLHNRQIYPPINVLPSLSR 378
Cdd:cd01134 228 spGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
232-465 |
9.27e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 93.16 E-value: 9.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 232 MERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLAT 311
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 312 IYERAGRV-----EGRPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAige 386
Cdd:PRK14698 796 FYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAV--- 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 387 gmtrKD--HSDVSNQLYAAYAMGKDALAMRA-------VVGVEALSQEDLLYLEFHDKFERRFVNQGAYERRDIYTSLDM 457
Cdd:PRK14698 873 ----KDwwHKNVDPEWKAMRDKAMELLQKEAelqeivrIVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEK 948
|
....*...
gi 1352831 458 AWDLLRIF 465
Cdd:PRK14698 949 QVTMMRVL 956
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
33-443 |
1.08e-18 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 88.56 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 33 LIILQNVKSPrfAEIVNVT------LGDGSVRrgqvleinqdkAVVqiFEGTTGIDNKKTVCQfTGEILKTPVSLDMLGR 106
Cdd:CHL00060 42 ALVVKGRDTA--GQEINVTcevqqlLGNNRVR-----------AVA--MSATDGLMRGMEVID-TGAPLSVPVGGATLGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 107 VFNGSGKPIDGGPPILPEAYLDI-QGQPINPQSRTYPEeMFETGISSIDVMNSIARGQKIPLFSGAGLPHN----EVAAQ 181
Cdd:CHL00060 106 IFNVLGEPVDNLGPVDTRTTSPIhRSAPAFIQLDTKLS-IFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTvlimELINN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 182 ICRQVCLVStctlvkrsgkdeedfaiVFAamGVNMETarffRQDF-------------EENGAMERVTLFLNLANDPTIE 248
Cdd:CHL00060 185 IAKAHGGVS-----------------VFG--GVGERT----REGNdlymemkesgvinEQNIAESKVALVYGQMNEPPGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 249 RIITPRLALTFAEYLAYEKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVegRPGSITQ 328
Cdd:CHL00060 242 RMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITST--KEGSITS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 329 LPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRLMKSAI-GEgmtrkDHSDVSNQLYAAYAMG 407
Cdd:CHL00060 320 IQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----EHYETAQRVKQTLQRY 394
|
410 420 430
....*....|....*....|....*....|....*.
gi 1352831 408 KDALAMRAVVGVEALSQEDLLYLEFHDKFErRFVNQ 443
Cdd:CHL00060 395 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 429
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
44-388 |
1.98e-18 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 88.17 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 44 FAEIVNVTLGDGSVRRGQVLEINQDKAV-VQIFEGTTGIDNKKTVCQfTGEILKTPVSLDMLGRVFNGSGKPIDGGPPIL 122
Cdd:PTZ00185 64 YNTIIMIQVSPTTFAAGLVFNLEKDGRIgIILMDNITEVQSGQKVMA-TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLTR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 123 PEAYLDIQ--------GQPiNPQSRTYPEEMFETGISSIDVMNSIARGQKIPLFSGAGLPHNEVAAQICRQVCLVSTCTL 194
Cdd:PTZ00185 143 SRALLESEqtlgkvdaGAP-NIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVSTIINQVRINQQIL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 195 VKRSgkdeedFAIVFAAMGVNMETARFFRQDFEENGAMERVTLFLNLANDPTIERIITPRLALTFAEYLAyEKGKHVLVI 274
Cdd:PTZ00185 222 SKNA------VISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFM-NRGRHCLCV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 275 LTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVE-GRPG-SITQLPILTMPNDDITHPIPDLTGYITE 352
Cdd:PTZ00185 295 YDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKGGgSVTALPIVETLSNDVTAYIVTNVISITD 374
|
330 340 350
....*....|....*....|....*....|....*.
gi 1352831 353 EQIYLDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 388
Cdd:PTZ00185 375 GQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
25-465 |
2.00e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 88.30 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 25 TVSAVNGPLIILQNVKSPRFAEIVNVtlgdGSVR-RGQVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGEilktPVSLD- 102
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVRV----GEEGlIGEIIRIEGDKATIQVYEETSGIKPGEPV-EFTGE----PLSVEl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 103 ---MLGRVFNGSGKPID--------------------------------------GG------------------PP--- 120
Cdd:PRK04192 77 gpgLLGSIFDGIQRPLDelaeksgdflergvyvpaldrekkweftptvkvgdkveAGdilgtvqetpsiehkimvPPgvs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 121 -----ILPE-AY-----------LDIQGQPIN-----P--QSRTY-----PEEMFETGISSIDVMNSIARGQK--IPLFS 169
Cdd:PRK04192 157 gtvkeIVSEgDYtvddtiavledEDGEGVELTmmqkwPvrRPRPYkeklpPVEPLITGQRVIDTFFPVAKGGTaaIPGPF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 170 GAG---LPHnevaaqicrqvclvstcTLVKRSGKDeedfAIVFAAMGvnmEtarffR--------QDFEE-------NGA 231
Cdd:PRK04192 237 GSGktvTQH-----------------QLAKWADAD----IVIYVGCG---E-----RgnemtevlEEFPElidpktgRPL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 232 MERVTLFLNLANDPTIER---IITprlALTFAEYlaY-EKGKHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYT 307
Cdd:PRK04192 288 MERTVLIANTSNMPVAAReasIYT---GITIAEY--YrDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLAS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 308 DLATIYERAGRVE---GRPGSITQLPILTMPNDDITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSrLMKSAI 384
Cdd:PRK04192 363 RLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQV 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 385 GEGMTRKDHSDVSNqlYAAYAM-----GKDALAMRAVVGVEALSQEDLLYLEFHDKFERRFVNQGAYERRDIYTSLDMAW 459
Cdd:PRK04192 442 APWWEENVDPDWRE--LRDEAMdllqrEAELQEIVRLVGPDALPEEDRLILEVARLIREDFLQQNAFDPVDTYCPPEKQY 519
|
....*.
gi 1352831 460 DLLRIF 465
Cdd:PRK04192 520 EMLKLI 525
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
112-404 |
1.05e-17 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 85.80 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 112 GKPID-GGPPILPEAYLDIQ-----------GQPINPQSRTYPEEMFETGISSIDVMNSIARGQK--IPLFSGAGLPHNE 177
Cdd:PRK07165 81 GKIIDiDGNIIYPEAQNPLSkkflpntssifNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRelIIGDRQTGKTHIA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 178 VAAQIcrqvclvstctlvkrsGKDEEDFAIVFAAMGVNMETARFFRQDFEENGAMERvTLFLNLANDPTIERIITPRLAL 257
Cdd:PRK07165 161 LNTII----------------NQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKN-TIIIDAPSTSPYEQYLAPYVAM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 258 TFAEYLAYEKgkHVLVILTDMSAYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRPgSITQLPILTMPND 337
Cdd:PRK07165 224 AHAENISYND--DVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK-TITALPILQTVDN 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 338 DITHPIPDLTGYITEEQIYLDRQLHNRQIYPPINVLPSLSRlmksaIGEGMTRKDHSDVS---NQLYAAY 404
Cdd:PRK07165 301 DITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR-----TGSSVQSKTITKVAgeiSKIYRAY 365
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
26-92 |
9.36e-11 |
|
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: 57.55 E-value: 9.36e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 26 VSAVNGPLIILQNV--KSPRFAEIVNVTLGD-GSVRRGQVLEINQDKAVVQIFEGTTGIDnKKTVCQFTG 92
Cdd:pfam02874 1 IVQVIGPVVDVEFGigRLPGLLNALEVELVEfGSLVLGEVLNLGGDKVRVQVFGGTSGLS-RGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
23-93 |
1.40e-09 |
|
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: 54.24 E-value: 1.40e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1352831 23 YRTVSAVNGPLIILQNVKSPRFAEIVNVTLGDGS---VRRGQVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGE 93
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGNnetVLKAEVIGFRGDRAILQLFESTRGLSRGALV-EPTGR 73
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
393-463 |
1.52e-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: 51.29 E-value: 1.52e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1352831 393 HSDVSNQLYAAYAMGKDALAMRAVVGVEALSQEDLLYLEFHDKFeRRFVNQGAYERRDIYTSLDMAWDLLR 463
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRL-EEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
29-116 |
4.39e-04 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 43.09 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1352831 29 VNGPLIILQNVKSPRFAEIVNV-TLGdgsvRRGQVLEINQDKAVVQIFEGTTGIDNKKTVcQFTGEILKTPVSLDMLGRV 107
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVVRVgELG----LIGEIIRLEGDKAVIQVYEETAGLKPGEPV-EGTGSSLSVELGPGLLTSI 84
|
....*....
gi 1352831 108 FNGSGKPID 116
Cdd:PRK14698 85 YDGIQRPLE 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 ... |
25-81 |
8.51e-04 |
|
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: 37.89 E-value: 8.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1352831 25 TVSAVNGPLIILQNVKSPRFAEIVNVtlgdGSVRR-GQVLEINQDKAVVQIFEGTTGI 81
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELVRV----GEEGLiGEIIRLEGDKATIQVYEETSGL 56
|
|
| |
