|
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 ... |
25-488 |
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: 1040.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 25 TYKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDILRTPVSE 104
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 105 DMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 184
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 185 ICRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEF 264
Cdd:TIGR01040 161 ICRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 265 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 344
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 345 IPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 424
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401325 425 TPDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFPKEMLKRIPASILAEFYPRDS 488
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKS 464
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
22-486 |
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: 854.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 22 PRLTYKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDILRTP 101
Cdd:COG1156 2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 102 VSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEI 181
Cdd:COG1156 82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 182 AAQICRQAglvKLPGKSvlddhtDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTA 261
Cdd:COG1156 162 AAQIARQA---KVRGEE------EKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 262 AEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDI 341
Cdd:COG1156 233 AEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 342 THPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGE 421
Cdd:COG1156 313 THPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 401325 422 EALTPDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFPKEMLKRIPASILAEFYPR 486
Cdd:COG1156 393 EALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPK 457
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
26-487 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 821.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 26 YKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDILRTPVSED 105
Cdd:PRK04196 4 YRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 106 MLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 185
Cdd:PRK04196 84 MLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 186 CRQAglvKLPGKSvlddhtDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 265
Cdd:PRK04196 164 ARQA---KVLGEE------ENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 266 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPI 345
Cdd:PRK04196 235 AFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 346 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALT 425
Cdd:PRK04196 315 PDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401325 426 PDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFPKEMLKRIPASILAEFYPRD 487
Cdd:PRK04196 395 ERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKY 456
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
26-487 |
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: 701.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 26 YKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDILRTPVSED 105
Cdd:TIGR01041 2 YSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 106 MLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 185
Cdd:TIGR01041 82 MLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 186 CRQAglvKLPGKSvlddhtDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 265
Cdd:TIGR01041 162 ARQA---TVRGEE------SEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 266 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPI 345
Cdd:TIGR01041 233 AFEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 346 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALT 425
Cdd:TIGR01041 313 PDLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401325 426 PDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFPKEMLKRIPASILAEFYPRD 487
Cdd:TIGR01041 393 ERDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYHPKY 454
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
97-387 |
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: 624.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 97 ILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGL 176
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 177 PHNEIAAQICRQAGLVKlpgksvlddHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPR 256
Cdd:cd01135 81 PHNELAAQIARQAGVVG---------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 257 LALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTM 336
Cdd:cd01135 152 MALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 401325 337 PNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIG 387
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
26-490 |
1.30e-119 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 357.42 E-value: 1.30e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 26 YKTVSGVNGPLVILdEVKFPKFAEIVQLRLADGTvRSGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEFTGDILRTPVSED 105
Cdd:PRK02118 5 YTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGI-STGDEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 106 MLGRVFNGSGKPIDKGPpILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 185
Cdd:PRK02118 82 LLGRRFNGSGKPIDGGP-ELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 186 CRQAglvklpgksvlddhtDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 265
Cdd:PRK02118 161 ALQA---------------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 266 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITHPI 345
Cdd:PRK02118 226 ALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHPV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 346 PDLTGYITEGQIYvdrqLHNRQIYPpvnvLPSLSRLMKSAIGEgMTRKDHSDVSN---QLYACYAIGKDVQAMkavvGEE 422
Cdd:PRK02118 305 PDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GFK 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 423 aLTPDDLLYLEFLTKFEKNFISQGnyENRTVFESLDIGWQLL-RIF-PKEMLkrIPASILAEFYPRDSRH 490
Cdd:PRK02118 372 -LSNWDEKLLKFSELFESRLMDLE--VNIPLEEALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKNCLH 436
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
152-379 |
1.96e-109 |
|
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: 323.15 E-value: 1.96e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 152 GISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvklpgksvLDDhtdnfAIVFAAMGVNMETARFFKQDFEEN 231
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA----------SAD-----VVVYALIGERGREVREFIEELLGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 232 GSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDL 311
Cdd:pfam00006 66 GALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401325 312 ATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLS 379
Cdd:pfam00006 145 ARLLERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
99-381 |
4.96e-107 |
|
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: 319.40 E-value: 4.96e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 99 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH 178
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 179 NEIAAQICRQAGlvklpgksvlddHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLA 258
Cdd:cd19476 81 TVLAMQLARNQA------------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 259 LTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPN 338
Cdd:cd19476 149 LTIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 401325 339 DDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRL 381
Cdd:cd19476 228 DDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 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 ... |
389-483 |
1.32e-61 |
|
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: 196.12 E-value: 1.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 389 GMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALTPDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFP 468
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 401325 469 KEMLKRIPASILAEF 483
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
99-381 |
2.66e-45 |
|
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: 159.26 E-value: 2.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 99 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLph 178
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 179 neiaaqicrqaglvklpGKSVL----DDHTDNFAIVFAAMGvnmETAR----FFKQDFEENGsMENVCLFLNLANDPTIE 250
Cdd:cd01136 79 -----------------GKSTLlgmiARNTDADVNVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 251 RIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQ 330
Cdd:cd01136 138 RVRAAYTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 401325 331 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRL 381
Cdd:cd01136 215 FYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
28-382 |
3.92e-42 |
|
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: 155.19 E-value: 3.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 28 TVSGVNGPLVildEVKFPKFA--EIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEFTGDILRTPVSED 105
Cdd:COG1157 22 RVTRVVGLLI---EAVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 106 MLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSR--IypEEMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaa 183
Cdd:COG1157 98 LLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSG-------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 184 qicrqaglVklpGKSVL----DDHTDNFAIVFAAMGvnmETAR----FFKQDFEENGsMENVCLFLNLANDPTIERIITP 255
Cdd:COG1157 168 --------V---GKSTLlgmiARNTEADVNVIALIG---ERGRevreFIEDDLGEEG-LARSVVVVATSDEPPLMRLRAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 256 RLALTAAEFLAYQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQI- 331
Cdd:COG1157 233 YTATAIAEYFRDQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAFy 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 401325 332 PILTmPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 382
Cdd:COG1157 307 TVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
94-385 |
1.60e-39 |
|
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: 149.46 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 94 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 173
Cdd:TIGR00962 90 TGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 174 aglphneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERII 253
Cdd:TIGR00962 170 -------------RQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 254 TPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRNGSI 328
Cdd:TIGR00962 237 APYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKGGGSL 312
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 401325 329 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSA 385
Cdd:TIGR00962 313 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
64-464 |
3.23e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 147.65 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 64 QVLEVSGSKAVVQVFEGTSGIDAkNTLCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPiLAEDFLDIQGQPINPWSRI 143
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGLRC-GQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLTRQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 144 YPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICrqaglvklpgksvldDHTDNFAIVFAAMGV-NMETAR 222
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC---------------ADSAADVMVLALIGErGREVRE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 223 FFKQDFEENGSMENVcLFLNLANDPTIERIITPRLALTAAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRG 302
Cdd:PRK06820 207 FLEQVLTPEARARTV-VVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 303 FPGYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 382
Cdd:PRK06820 285 FPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 383 KSAIGEGmtRKDHSDVSNQLYACYaigKDVQAMKAVvgEEALTPDDLLYLEFLTKFE--KNFISQGNYENRTVFESLDIG 460
Cdd:PRK06820 363 PQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEHL 435
|
....
gi 401325 461 WQLL 464
Cdd:PRK06820 436 AQVV 439
|
|
| 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 ... |
25-96 |
3.19e-38 |
|
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: 133.71 E-value: 3.19e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401325 25 TYKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGD 96
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
46-413 |
1.92e-37 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 142.58 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 46 KFAEIVQLRLADGTVR-SGQVLEVSGSKAVVQVFEGTSGIDAkNTLCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPI 124
Cdd:PRK06936 43 RIGELCYLRNPDNSLSlQAEVIGFAQHQALLTPLGEMYGISS-NTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 125 LAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvklpgksvlddHT 204
Cdd:PRK06936 122 EPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIR---------------SA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 205 DNFAIVFAAMGV-NMETARFFKQDFEENGsMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSY 283
Cdd:PRK06936 187 EVDVTVLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 284 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQL 363
Cdd:PRK06936 265 ARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKL 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 401325 364 HNRQIYPPVNVLPSLSRLMKSAIGegmtrKDHSDVSNQLYACYAIGKDVQ 413
Cdd:PRK06936 343 AAANHYPAIDVLRSASRVMNQIVS-----KEHKTWAGRLRELLAKYEEVE 387
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-380 |
1.43e-34 |
|
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: 130.76 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 97 ILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAagl 176
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 177 phneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPR 256
Cdd:cd01132 78 ----------RQTGKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 257 LALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRNGSITQI 331
Cdd:cd01132 148 AGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 401325 332 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSR 380
Cdd:cd01132 224 PIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
98-388 |
1.17e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 131.73 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 98 LRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLP 177
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 178 HNEIAAQICRQAglvKLPGKsvlddhtdnfaiVFAAMGvnmETARFFKQDFEEN--GSMENVCLFLNLANDPTIERIITP 255
Cdd:PRK08472 170 KSTLMGMIVKGC---LAPIK------------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 256 RLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRnGSITQIPILT 335
Cdd:PRK08472 232 FCAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVL 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 401325 336 MPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGE 388
Cdd:PRK08472 310 VEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
96-468 |
5.67e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 127.54 E-value: 5.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 96 DILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAG 175
Cdd:PRK05688 99 DTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 176 LphneiaaqicrqaglvklpGKSVLDDHTDNFA----IVFAAMGV-NMETARFFKQDFEENGSMENVCLfLNLANDPTIE 250
Cdd:PRK05688 179 V-------------------GKSVLLGMMTRFTeadiIVVGLIGErGREVKEFIEHILGEEGLKRSVVV-ASPADDAPLM 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 251 RIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQ 330
Cdd:PRK05688 239 RLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 331 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIG-EGMTRKDHsdvSNQLYACYAIG 409
Cdd:PRK05688 318 FYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQS 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 401325 410 KDVQAMKAVVgeEALTPDDLLYLEFLTKFEKnFISQGNYENRTVFESLDigwQLLRIFP 468
Cdd:PRK05688 395 RDLISVGAYV--AGGDPETDLAIARFPHLVQ-FLRQGLRENVSLAQSRE---QLAAIFA 447
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
64-415 |
9.54e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 126.61 E-value: 9.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 64 QVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDiLRTPVSEDMLGRVFNGSGKPIDkGPPILAEDFLDIQGQPINPWSRI 143
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGLHCGQQVMALRRR-HQVPVGEALLGRVIDGFGRPLD-GRELPDVCWKDYDAMPPPAMVRQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 144 YPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICrqaglvKLPGKSVlddhtdnfaIVFAAMGVNMETARF 223
Cdd:PRK07594 134 PITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC------NAPDADS---------NVLVLIGERGREVRE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 224 FkQDFEENGSMENVCLFLNLAND-PTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRG 302
Cdd:PRK07594 199 F-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 303 FPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 382
Cdd:PRK07594 277 YPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF 354
|
330 340 350
....*....|....*....|....*....|...
gi 401325 383 KSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAM 415
Cdd:PRK07594 355 PVVTSH-----EHRQLAAILRRCLALYQEVELL 382
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
46-382 |
1.95e-31 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 125.65 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 46 KFAEIVQLRLADGTV-RSGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPI 124
Cdd:PRK09099 44 TLGELCELRQRDGTLlQRAEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 125 LAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaaqicrqaglvklpGKSVLddhT 204
Cdd:PRK09099 123 DCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGV-------------------GKSTL---M 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 205 DNFAI-------VFAAMGV-NMETARFFKQDFEENGsMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVI 276
Cdd:PRK09099 181 GMFARgtqcdvnVIALIGErGREVREFIELILGEDG-MARSVVVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 277 LTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQ 356
Cdd:PRK09099 259 MDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGH 336
|
330 340
....*....|....*....|....*.
gi 401325 357 IYVDRQLHNRQIYPPVNVLPSLSRLM 382
Cdd:PRK09099 337 MILSREIAARNQYPAIDVLGSLSRVM 362
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
94-385 |
2.05e-31 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 126.23 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 94 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 173
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 174 aglphneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERII 253
Cdd:CHL00059 150 -------------RQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 254 TPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRVEGR--NGSI 328
Cdd:CHL00059 217 APYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSQlgEGSM 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 401325 329 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSA 385
Cdd:CHL00059 293 TALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
25-445 |
6.43e-31 |
|
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: 124.45 E-value: 6.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 25 TYKTVSGVNGPLV-----------ILD--EVKFPKFAEI---VQLRLADGTVRSgqvLEVSGSKAVVQvfegtsGIDAKN 88
Cdd:TIGR01039 1 TKGKVVQVIGPVVdvefeqgelprIYNalKVQNRAESELtleVAQHLGDDTVRT---IAMGSTDGLVR------GLEVID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 89 TlceftGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKI 168
Cdd:TIGR01039 72 T-----GAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 169 PIFSAAGLphneiaaqicrqaglvklpGKSVL-DDHTDNFAI------VFAAMGVNMETARFFKQDFEENGSMENVCLFL 241
Cdd:TIGR01039 147 GLFGGAGV-------------------GKTVLiQELINNIAKehggysVFAGVGERTREGNDLYHEMKESGVIDKTALVY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 242 NLANDPTIERIITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrV 321
Cdd:TIGR01039 208 GQMNEPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--T 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 322 EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMK-SAIGEgmtrkDHSDVSN 400
Cdd:TIGR01039 286 STKTGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVAR 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 401325 401 QLYACYAIGKDVQAMKAVVGEEALTPDDLLYLEFLTKFEKnFISQ 445
Cdd:TIGR01039 361 GVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
25-385 |
2.11e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 122.80 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 25 TYKTVSGVngplvildeVKFPKFAEIVQLRLADGTVRsGQVLEVSGSKAVVQVFEgtSGIDAKNTLCEFTGDILRTPVSE 104
Cdd:PRK06002 36 SHYRVRGL---------SRFVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 105 DMLGRVFNGSGKPID-KGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaa 183
Cdd:PRK06002 104 SWKGRVINALGEPIDgLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGV------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 184 qicrqaglvklpGKSVL------DDHTDnfAIVFAAMGvnmETARFFKQDFEEN--GSMENVCLFLNLANDPTIERIITP 255
Cdd:PRK06002 177 ------------GKSTLlamlarADAFD--TVVIALVG---ERGREVREFLEDTlaDNLKKAVAVVATSDESPMMRRLAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 256 RLALTAAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILT 335
Cdd:PRK06002 240 LTATAIAEYFRDRGEN-VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 401325 336 MPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSA 385
Cdd:PRK06002 319 VDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
94-380 |
2.44e-29 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 120.41 E-value: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 94 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLdiqgqPINpwsRIYPEEM--------IQTGISAIDVMNSIARG 165
Cdd:PRK13343 91 TGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARR-----PLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 166 QKIPIFSAaglphneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLAN 245
Cdd:PRK13343 163 QRELIIGD-------------RQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEAS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 246 DPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRN 325
Cdd:PRK13343 230 DPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPEL 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 401325 326 --GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSR 380
Cdd:PRK13343 309 ggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
99-468 |
4.71e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 119.12 E-value: 4.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 99 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLph 178
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGV-- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 179 neiaaqicrqaglvklpGKSVL----DDHTDNFAIVFAAMGvnmETARFFKqDFeengsMENVCLFLNLANDPTIERI-- 252
Cdd:PRK07960 187 -----------------GKSVLlgmmARYTQADVIVVGLIG---ERGREVK-DF-----IENILGAEGRARSVVIAAPad 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 253 ITPRLALTAAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNG 326
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 327 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSdvSNQLYACY 406
Cdd:PRK07960 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQ--FKQLLSSF 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401325 407 AIGKDVQAmkavVGEEALTPDDLL--YLEFLTKFEKnFISQGNYENRTVFESLDigwQLLRIFP 468
Cdd:PRK07960 399 QRNRDLVS----VGAYAKGSDPMLdkAIALWPQLEA-FLQQGIFERADWEDSLQ---ALERIFP 454
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
101-411 |
7.11e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 118.16 E-value: 7.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 101 PVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNE 180
Cdd:PRK06793 92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 181 IAAQICRQA-------GLVKLPGKSVLDdhtdnfaivfaamgvnmetarFFKQDFEENGsMENVCLFLNLANDPTIERII 253
Cdd:PRK06793 172 LLGMIAKNAkadinviSLVGERGREVKD---------------------FIRKELGEEG-MRKSVVVVATSDESHLMQLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 254 TPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEgrNGSITQIP 332
Cdd:PRK06793 230 AAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQ--KGSITGIY 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401325 333 ILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEgmtrkDHSDVSNQLYACYAIGKD 411
Cdd:PRK06793 305 TVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
101-417 |
1.01e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 117.88 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 101 PVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphne 180
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGV---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 181 iaaqicrqaglvklpGKSVL----DDHTDNFAIVFAAMGvnmETARFFKQDFEE----NGSMENVCLFLNLANDPTIeRI 252
Cdd:PRK08972 174 ---------------GKSVLlgmmTRGTTADVIVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 253 ITPRLALTAAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIP 332
Cdd:PRK08972 235 KGCETATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 333 ILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEgmtrkDHSDVS---NQLYACYAIG 409
Cdd:PRK08972 314 TVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQN 388
|
....*...
gi 401325 410 KDVQAMKA 417
Cdd:PRK08972 389 RDLISIGA 396
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
78-411 |
3.90e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 116.36 E-value: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 78 FEGTSGIdAKNTLCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAID 157
Cdd:PRK07721 72 YTEVAEI-APGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAID 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 158 VMNSIARGQKIPIFSAAGLPHNEIAAQICRQaglvklpgksvlddhTDNFAIVFAAMGVN-METARFFKQDFEENGSMEN 236
Cdd:PRK07721 151 SLLTVGKGQRVGIFAGSGVGKSTLMGMIARN---------------TSADLNVIALIGERgREVREFIERDLGPEGLKRS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 237 VcLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 316
Cdd:PRK07721 216 I-VVVATSDQPALMRIKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 317 RAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEgmtrkDHS 396
Cdd:PRK07721 294 RTGTNA--SGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHK 366
|
330
....*....|....*...
gi 401325 397 DVSN---QLYACYAIGKD 411
Cdd:PRK07721 367 EAANrfrELLSTYQNSED 384
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
32-381 |
8.52e-27 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 112.40 E-value: 8.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 32 VNGPLV--ILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLcEFTGDILRTPVSEDMLGR 109
Cdd:PRK08149 13 IQGPIIeaELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTILSLIGNAQGLSRQVVL-KPTGKPLSVWVGEALLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 110 VFNGSGKPIDK-GPPILAEDF---LDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaaqi 185
Cdd:PRK08149 92 VLDPTGKIVERfDAPPTVGPIseeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAG---------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 186 CRQAGLVklpgkSVLDDHTDNFAIVFAAMGvnmETARF---FKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAA 262
Cdd:PRK08149 162 CGKTSLM-----NMLIEHSEADVFVIGLIG---ERGREvteFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 263 EFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRNGSITQIPILTMPNDDIT 342
Cdd:PRK08149 234 EYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESEEEP 310
|
330 340 350
....*....|....*....|....*....|....*....
gi 401325 343 HPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRL 381
Cdd:PRK08149 311 DPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
22-382 |
1.29e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 111.99 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 22 PRLTYKTVSGVNGPLVildEVKFPKFAEIVQLRLA----DGTVRSGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEFTGDI 97
Cdd:PRK08927 14 TLVIYGRVVAVRGLLV---EVAGPIHALSVGARIVvetrGGRPVPCEVVGFRGDRALLMPFGPLEGV-RRGCRAVIANAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 98 LRTPVSEDMLGRVFNGSGKPID-KGPpiLAEDFLD--IQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAA 174
Cdd:PRK08927 90 AAVRPSRAWLGRVVNALGEPIDgKGP--LPQGPVPypLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 175 GLphneiaaqicrqaglvklpGKSVL----DDHTDNFAIVFAAMGvnmETAR----FFKQDFEENGSMENVcLFLNLAND 246
Cdd:PRK08927 168 GV-------------------GKSVLlsmlARNADADVSVIGLIG---ERGRevqeFLQDDLGPEGLARSV-VVVATSDE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 247 PTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNG 326
Cdd:PRK08927 225 PALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEG 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 401325 327 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 382
Cdd:PRK08927 304 TITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
99-382 |
1.06e-24 |
|
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: 103.45 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 99 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQgQPINPWSRIYPE-EMIQTGISAIDVMNSIARGQKIPIFSAAGLp 177
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIH-REAPEFVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 178 hneiaaqicrqaglvklpGKSVL-DDHTDNFAI------VFAAMGVNMETARFFKQDFEENG-----SMENVCLFLNLAN 245
Cdd:cd01133 79 ------------------GKTVLiMELINNIAKahggysVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 246 DPTIERIITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRN 325
Cdd:cd01133 141 EPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST--KK 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 401325 326 GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 382
Cdd:cd01133 219 GSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
94-380 |
1.27e-24 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 106.69 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 94 TGDILRTPVSEDMLGRVFNGSGKPID-KGPpILAEDFLD--------IQGQPINpwsriypeEMIQTGISAIDVMNSIAR 164
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQPIDgKGP-IEATETRPverkapgvIDRKSVH--------EPLQTGIKAIDAMIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 165 GQKIPIfsaaglphneiaaqIC-RQAGlvklpgKS------VLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENV 237
Cdd:PRK09281 162 GQRELI--------------IGdRQTG------KTaiaidtIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 238 CLFLNLANDPTIERIITPRLALTAAEFLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLati 314
Cdd:PRK09281 222 IVVAATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL--- 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 401325 315 YERAGRV--EGRNGSITQIPIL-TMPNDdITHPIPdlTGY--ITEGQIYVDRQLHNRQIYPPVNVLPSLSR 380
Cdd:PRK09281 298 LERAAKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
56-407 |
2.05e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 105.36 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 56 ADGTVRSGQVLEVSGSKAVVQVFEGTSGI--DAKNTLCEFTGDILrtpVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQ 133
Cdd:PRK07196 47 VDETFIEAQVVGFDRDITYLMPFKHPGGVlgGARVFPSEQDGELL---IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 134 GQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaaqicrqaglvklpGKSVL----DDHTDNFAI 209
Cdd:PRK07196 124 LPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGV-------------------GKSVLlgmiTRYTQADVV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 210 VFAAMGV-NMETARFFKQDFEENGSMENVcLFLNLANDPTIERIITPRLALTAAEFlaYQCEKH-VLVILTDMSSYAEAL 287
Cdd:PRK07196 185 VVGLIGErGREVKEFIEHSLQAAGMAKSV-VVAAPADESPLMRIKATELCHAIATY--YRDKGHdVLLLVDSLTRYAMAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 288 REVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQ 367
Cdd:PRK07196 262 REIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAG 340
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 401325 368 IYPPVNVLPSLSRLMKSAIGegmtrKDHSDVSNQLYACYA 407
Cdd:PRK07196 341 HYPAIDISQSISRCMSQVIG-----SQQAKAASLLKQCYA 375
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
101-380 |
9.02e-24 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 103.45 E-value: 9.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 101 PVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNE 180
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 181 IAAQICRQAglvklpgKSVLDdhtdnfaiVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALT 260
Cdd:PRK05922 173 LLSTIAKGS-------KSTIN--------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 261 AAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQI-PILTMPNd 339
Cdd:PRK05922 238 IAEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYPN- 313
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 401325 340 ditHP--IPDLTGYITEGQIYVDRQlHNRQIYPPVNVLPSLSR 380
Cdd:PRK05922 314 ---HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
94-380 |
2.54e-23 |
|
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: 102.81 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 94 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLD--------IQGQPINpwsriypeEMIQTGISAIDVMNSIARG 165
Cdd:COG0056 91 TGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPverpapgvIDRQPVH--------EPLQTGIKAIDAMIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 166 QKipifsaaglphnEIaaqIC--RQAglvklpGKSVLddhtdnfAI-------------VFAAMGVNMETARFFKQDFEE 230
Cdd:COG0056 163 QR------------EL---IIgdRQT------GKTAI-------AIdtiinqkgkdvicIYVAIGQKASTVAQVVETLEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 231 NGSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YM 307
Cdd:COG0056 215 HGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 308 YTDLatiYERAGRV--EGRNGSITQIPIL-TMPNddithpipDLTGY-------ITEGQIYVDRQLHNRQIYPPVNVLPS 377
Cdd:COG0056 294 HSRL---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLS 362
|
...
gi 401325 378 LSR 380
Cdd:COG0056 363 VSR 365
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
106-380 |
1.15e-19 |
|
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: 89.17 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 106 MLGRVFNGSGKPIDkgppILAE---DFLDiQGQPINPW---------SRIYPEEMIQTGISAIDVMNSIARGqkipifSA 173
Cdd:cd01134 10 LLGSIFDGIQRPLE----VIAEtgsIFIP-RGVNVQRWpvrqprpvkEKLPPNVPLLTGQRVLDTLFPVAKG------GT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 174 AGLPhneiAAQICrqaglvklpGKSVLDDHTDNFA----IVFAAMG--------VNMEtarFFKQDFEENGS--MENVCL 239
Cdd:cd01134 79 AAIP----GPFGC---------GKTVISQSLSKWSnsdvVIYVGCGergnemaeVLEE---FPELKDPITGEslMERTVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 240 FLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 319
Cdd:cd01134 143 IANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAG 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401325 320 RVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPVNVLPSLSR 380
Cdd:cd01134 222 RVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
146-380 |
4.46e-19 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 90.03 E-value: 4.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 146 EEMIQTGISAIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFK 225
Cdd:PRK07165 124 NEQLYTGIIAIDLLIPIGKGQRELIIGD-------------RQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 226 QDFEENGSMENVCLFLNLANDPtIERIITPRLALTAAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG 305
Cdd:PRK07165 191 ETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMAHAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPG 267
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 401325 306 YMYTDLATIYERAGRVEGRNgSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSR 380
Cdd:PRK07165 268 DMFFAHSKLLERAGKFKNRK-TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
28-428 |
6.38e-17 |
|
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: 82.83 E-value: 6.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 28 TVSGVNGPLV-----------ILD--EVKFPKFAEI---VQLRLADGTVRSgqvleVSgskavvqvFEGTSGIdAKNTLC 91
Cdd:COG0055 7 KIVQVIGPVVdvefpegelpaIYNalEVENEGGGELvleVAQHLGDNTVRC-----IA--------MDSTDGL-VRGMEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 92 EFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPiNPWSRIYPE-EMIQTGISAIDVMNSIARGQKIPI 170
Cdd:COG0055 73 IDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPA-PPFEEQSTKtEILETGIKVIDLLAPYAKGGKIGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 171 FSAAG---------LPHNeIAAQicrQAGLVklpgksvlddhtdnfaiVFAAMGvnmETARF---FKQDFEENGSMENVC 238
Cdd:COG0055 152 FGGAGvgktvlimeLIHN-IAKE---HGGVS-----------------VFAGVG---ERTREgndLYREMKESGVLDKTA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 239 LFLNLANDPTIERIITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERA 318
Cdd:COG0055 208 LVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 319 GRVegRNGSITQIPILTMPNDDITHPIP-------DLTgyitegqIYVDRQLHNRQIYPPVNVLPSLSRLMKSAI-GEgm 390
Cdd:COG0055 288 TST--KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE-- 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 401325 391 trkDHSDVSN------QLYacyaigKDVQAMKAVVGEEALTPDD 428
Cdd:COG0055 357 ---EHYRVARevqrilQRY------KELQDIIAILGMDELSEED 391
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
47-390 |
1.00e-16 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 82.78 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 47 FAEIVQLRLADGTVRSGQV--LEVSGSKAVVQVFEGTSGIDAKNTLCefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPI 124
Cdd:PTZ00185 64 YNTIIMIQVSPTTFAAGLVfnLEKDGRIGIILMDNITEVQSGQKVMA--TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 125 LAEDFLDIQ--------GQPiNPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGLVKLPG 196
Cdd:PTZ00185 142 RSRALLESEqtlgkvdaGAP-NIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGD-------------RQTGKTSIAV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 197 KSVLDDHTDNFAI--------VFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQ 268
Cdd:PTZ00185 208 STIINQVRINQQIlsknavisIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 269 cEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GRNG-SITQIPILTMPNDDITHPIP 346
Cdd:PTZ00185 288 -GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKGGgSVTALPIVETLSNDVTAYIV 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 401325 347 DLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGM 390
Cdd:PTZ00185 367 TNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
28-433 |
1.88e-16 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 82.14 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 28 TVSGVNGPLVILDEVKFPKFAEIVQ---LRLAdgtvrsGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEFTGDilrtPVSE 104
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVRvgeEGLI------GEIIRIEGDKATIQVYEETSGI-KPGEPVEFTGE----PLSV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 105 D----MLGRVFNGSGKPIDKgppiLAE---DFL------------------------------DIQGQ------------ 135
Cdd:PRK04192 75 ElgpgLLGSIFDGIQRPLDE----LAEksgDFLergvyvpaldrekkweftptvkvgdkveagDILGTvqetpsiehkim 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 136 -PINP-------------------------------------W---------SRIYPEEMIQTGISAIDVMNSIARGQK- 167
Cdd:PRK04192 151 vPPGVsgtvkeivsegdytvddtiavlededgegveltmmqkWpvrrprpykEKLPPVEPLITGQRVIDTFFPVAKGGTa 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 168 -IP-IFSAaglphneiaaqicrqaglvklpGKSVLDDHTDNFA----IVFAAMG--VN-M-ETARFFKQ--DFEENGS-M 234
Cdd:PRK04192 231 aIPgPFGS----------------------GKTVTQHQLAKWAdadiVIYVGCGerGNeMtEVLEEFPEliDPKTGRPlM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 235 ENVCLFLNLANDPTIER---IITprlALTAAEF---LAYqcekHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMY 308
Cdd:PRK04192 289 ERTVLIANTSNMPVAAReasIYT---GITIAEYyrdMGY----DVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 309 TDLATIYERAGRVE---GRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSrLMKSA 385
Cdd:PRK04192 362 SRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQ 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 401325 386 IGEGMTRKDHSDVS---NQLYACYAIGKDVQAMKAVVGEEALTPDDLLYLE 433
Cdd:PRK04192 441 VAPWWEENVDPDWRelrDEAMDLLQREAELQEIVRLVGPDALPEEDRLILE 491
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
234-379 |
3.72e-16 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 81.61 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 234 MENVCLFLNLANDPTIERIITPRLALTAAEF---LAYQcekhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 310
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYfrdMGYD----VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASK 792
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401325 311 LATIYERAGRV-----EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLS 379
Cdd:PRK14698 793 LAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
51-445 |
1.56e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 78.93 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 51 VQLRLADGTVRSgqvleVSGSkAVVQVFEGTSGIDakntlcefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFL 130
Cdd:CHL00060 61 VQQLLGNNRVRA-----VAMS-ATDGLMRGMEVID--------TGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 131 diqgqPINpwsRIYPE--------EMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaaqicrqaglvklpGKSVL-D 201
Cdd:CHL00060 127 -----PIH---RSAPAfiqldtklSIFETGIKVVDLLAPYRRGGKIGLFGGAGV-------------------GKTVLiM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 202 DHTDNFA------IVFAAMG----------VNMETARFFKqdfEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 265
Cdd:CHL00060 180 ELINNIAkahggvSVFGGVGertregndlyMEMKESGVIN---EQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 266 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRNGSITQIPILTMPNDDITHPI 345
Cdd:CHL00060 257 RDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITST--KEGSITSIQAVYVPADDLTDPA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 346 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAI-GEgmtrkDHSDVSN------QLYacyaigKDVQAMKAV 418
Cdd:CHL00060 335 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----EHYETAQrvkqtlQRY------KELQDIIAI 403
|
410 420
....*....|....*....|....*..
gi 401325 419 VGEEALTPDDLLYLEFLTKFEkNFISQ 445
Cdd:CHL00060 404 LGLDELSEEDRLTVARARKIE-RFLSQ 429
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
29-95 |
1.33e-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: 1.33e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 29 VSGVNGPLVILD--EVKFPKFAEIVQLRLAD-GTVRSGQVLEVSGSKAVVQVFEGTSGIDaKNTLCEFTG 95
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, ... |
395-465 |
4.95e-10 |
|
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: 55.53 E-value: 4.95e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 401325 395 HSDVSNQLYACYAIGKDVQAMKAVVGEEALTPDDLLYLEFLTKFEKnFISQGNYENRTVFESLDIGWQLLR 465
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, ... |
26-96 |
3.18e-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: 53.47 E-value: 3.18e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401325 26 YKTVSGVNGPLVILDEVKFPKFAEIVQLRLADG---TVRSGQVLEVSGSKAVVQVFEGTSGIDAKnTLCEFTGD 96
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLSRG-ALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
32-119 |
2.85e-05 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 46.94 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 32 VNGPLVILDEVKFPKFAEIVqlRLAD-GTVrsGQVLEVSGSKAVVQVFEGTSGIDAKNTLcEFTGDILRTPVSEDMLGRV 110
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVV--RVGElGLI--GEIIRLEGDKAVIQVYEETAGLKPGEPV-EGTGSSLSVELGPGLLTSI 84
|
....*....
gi 401325 111 FNGSGKPID 119
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 ... |
28-84 |
2.36e-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: 2.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 401325 28 TVSGVNGPLVILDEVKFPKFAEIV---QLRLAdgtvrsGQVLEVSGSKAVVQVFEGTSGI 84
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELVrvgEEGLI------GEIIRLEGDKATIQVYEETSGL 56
|
|
| |
